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98		<h2>GZNL's Respiratory Data Centre, GZNL-RDC</h2>
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100		  <h1>Ribocentre</h1>
101		</div>
102		<p>A database of ribozymes</p>
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310  <h1 id="publications">Publications</h1>
311
312<blockquote>
313  <font size="4">List of all the articles of Ribozyme.<font><br />
314</font></font>
315</blockquote>
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377	  <table id="mytable" class="table-style1" cellspacing="0" width="100%">
378<thead>
379  <tr>
380    <th>Year</th>
381    <th>Author</th>
382    <th>Title</th>
383    <th>Ribozyme name</th>
384    <th>Description</th>
385    <th>Journal</th>
386  </tr>
387</thead>
388  <tr>
389    <td>2004</td>
390    <td>Adams, P. L., M. R. Stahley, A. B. Kosek, J. Wang and S. A. Strobel </td>
391    <td>Crystal structure of a self-splicing group I intron with both exons.</td>
392    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
393    <td>Crystal structure of <em>Azoarcus</em> group I intron with both exons</td>
394    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15175762" target="_blank"><b> Nature 430 (6995): 45-50.</b></a></td>
395  </tr>
396  <tr>
397    <td>2004</td>
398    <td>Guo, F., A. R. Gooding and T. R. Cech </td>
399    <td>Structure of the <em>Tetrahymena</em> ribozyme: base triple sandwich and metal ion at the  active site.</td>
400    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
401    <td>Crystal structure of an active <em>Tetrahymena</em> ribozyme</td>
402    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15525509" target="_blank"><b> Mol Cell 16 (3): 351-62.</b></a></td>
403  </tr>
404  <tr>
405    <td>2005</td>
406    <td>Golden, B. L., H. Kim and E. Chase </td>
407    <td>Crystal structure of a phage Twort group I ribozyme-product complex.</td>
408    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
409    <td>Crystal structure of  phage Twort group I ribozyme-product complex</td>
410    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15580277" target="_blank"><b> Nat Struct Mol Biol 12 (1): 82-9.</b></a></td>
411  </tr>
412  <tr>
413    <td>2005</td>
414    <td>Stahley, M. R. and S. A. Strobel </td>
415    <td>Structural evidence for a two-metal-ion mechanism of group I intron splicing.</td>
416    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
417    <td>Crystal structure of a catalytically active <em>Azoarcus</em> group I intron splicing intermediate</td>
418    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16141079" target="_blank"><b> Science 309 (5740): 1587-90.</b></a></td>
419  </tr>
420  <tr>
421    <td>2021</td>
422    <td>Su, Z., K. Zhang, K. Kappel, S. Li, M. Z. Palo, G. D. Pintilie, R. Rangan, B. Luo, Y. Wei, R. Das and W. Chiu </td>
423    <td>Cryo-EM structures of full-length <em>Tetrahymena</em> ribozyme at 3.1 A resolution.</td>
424    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
425    <td>Cryo-EM structures of full-length <em>Tetrahymena</em> ribozyme</td>
426    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/34381213" target="_blank"><b> Nature 596 (7873): 603-607.</b></a></td>
427  </tr>
428  <tr>
429    <td>1989</td>
430    <td>Williamson, C. L., N. M. Desai and J. M. Burke </td>
431    <td>Compensatory mutations demonstrate that P8 and P6 are RNA secondary structure elements important for processing of a group I intron.</td>
432    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
433    <td>Verify the existence and importance of P6, P8</td>
434    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2915927" target="_blank"><b> Nucleic Acids Res 17 (2): 675-89.</b></a></td>
435  </tr>
436  <tr>
437    <td>1989</td>
438    <td>Doudna, J. A., B. P. Cormack and J. W. Szostak </td>
439    <td>RNA structure, not sequence, determines the 5' splice-site specificity of a group I intron.</td>
440    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
441    <td>Conserved UG is an important recognition element for determining guanosine attack sites</td>
442    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2678103" target="_blank"><b> Proc Natl Acad Sci U S A 86 (19): 7402-6.</b></a></td>
443  </tr>
444  <tr>
445    <td>1989</td>
446    <td>Flor, P. J., J. B. Flanegan and T. R. Cech </td>
447    <td>A conserved base pair within helix P4 of the <em>Tetrahymena</em> ribozyme helps to form the tertiary structure required for self-splicing.</td>
448    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
449    <td>The conserved base pair C109-G212 in P4 contributes to the tertiary structure required for self-splicing</td>
450    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2684642" target="_blank"><b> EMBO J 8 (11): 3391-9.</b></a></td>
451  </tr>
452  <tr>
453    <td>1982</td>
454    <td>Kruger, K., P. J. Grabowski, A. J. Zaug, J. Sands, D. E. Gottschling and T. R. Cech </td>
455    <td>Self-splicing RNA: autoexcision and autocyclization of the ribosomal RNA intervening sequence of <em>Tetrahymena</em>
455.</td>
456    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
457    <td>Discovery</td>
458    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/6297754" target="_blank"><b> Cell 31 (1): 147-57.</b></a></td>
459  </tr>
460  <tr>
461    <td>1982</td>
462    <td>Davies, R. W., R. B. Waring, J. A. Ray, T. A. Brown and C. Scazzocchio </td>
463    <td>Making ends meet: a model for RNA splicing in fungal mitochondria.</td>
464    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
465    <td>Determination of shared secondary structure</td>
466    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/6757759" target="_blank"><b> Nature 300 (5894): 719-24.</b></a></td>
467  </tr>
468  <tr>
469    <td>1986</td>
470    <td>Zaug, A. J. and T. R. Cech </td>
471    <td>The intervening sequence RNA of <em>Tetrahymena</em> is an enzyme.</td>
472    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
473    <td>The intervening sequence RNA of <em>Tetrahymena</em> is an enzyme</td>
474    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/3941911" target="_blank"><b> Science 231 (4737): 470-5.</b></a></td>
475  </tr>
476  <tr>
477    <td>1988</td>
478    <td>Price, J. V. and T. R. Cech </td>
479    <td>Determinants of the 3' splice site for self-splicing of the <em>Tetrahymena</em> pre-rRNA.</td>
480    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
481    <td>ωG is closely related to the choice of 3' splice site</td>
482    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/3209068" target="_blank"><b> Genes Dev 2 (11): 1439-47.</b></a></td>
483  </tr>
484  <tr>
485    <td>1990</td>
486    <td>Michel, F. and E. Westhof </td>
487    <td>Modelling of the three-dimensional architecture of group I catalytic introns based on comparative sequence analysis.</td>
488    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
489    <td>3D models of  group I intron based on comparative sequence analysis</td>
490    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2258934" target="_blank"><b> J Mol Biol 216 (3): 585-610.</b></a></td>
491  </tr>
492  <tr>
493    <td>1996</td>
494    <td>Cate, J. H., A. R. Gooding, E. Podell, K. Zhou, B. L. Golden, C. E. Kundrot, T. R. Cech and J. A. Doudna </td>
495    <td>Crystal structure of a group I ribozyme domain: principles of RNA packing.</td>
496    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
497    <td>Crystal structure of <em>Tetrahymena</em> P4-P6 domain</td>
498    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8781224" target="_blank"><b> Science 273 (5282): 1678-85.</b></a></td>
499  </tr>
500  <tr>
501    <td>1998</td>
502    <td>Golden, B. L., A. R. Gooding, E. R. Podell and T. R. Cech </td>
503    <td>A preorganized active site in the crystal structure of the <em>Tetrahymena</em> ribozyme.</td>
504    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
505    <td>Crystal structure of an engineered, active <em>Tetrahymena</em> ribozyme at 5.0 Å resolution</td>
506    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9841391" target="_blank"><b> Science 282 (5387): 259-64.</b></a></td>
507  </tr>
508  <tr>
509    <td>2011</td>
510    <td>Benz-Moy, T. L. and D. Herschlag </td>
511    <td>Structure-function analysis from the outside in: long-range tertiary contacts in  RNA exhibit distinct catalytic roles.</td>
512    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
513    <td>Long-range tertiary contacts in RNA exhibit distinct catalytic roles</td>
514    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21815635" target="_blank"><b> Biochemistry 50 (40): 8733-55.</b></a></td>
515  </tr>
516  <tr>
517    <td>2022</td>
518    <td>Liu, D., F. A. Thelot, J. A. Piccirilli, M. Liao and P. Yin </td>
519    <td>Sub-3-A cryo-EM structure of RNA enabled by engineered homomeric self-assembly.</td>
520    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron</b></a></td>
521    <td><em>Tetrahymena</em> group I intron at 2.98-Å resolution overall (2.85 Å for the core)</td>
522    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/35501384" target="_blank"><b> Nat Methods 19 (5): 576-585.</b></a></td>
523  </tr>
524  <tr>
525    <td>1994</td>
526    <td>
526Damberger, S. H. and R. R. Gutell </td>
527    <td>A comparative database of group I intron structures.</td>
528    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron </b></a></td>
529    <td>Comparative database</td>
530    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7937050" target="_blank"><b> Nucleic Acids Res 22 (17): 3508-10.</b></a></td>
531  </tr>
532  <tr>
533    <td>2008</td>
534    <td>Zhou, Y., C. Lu, Q. J. Wu, Y. Wang, Z. T. Sun, J. C. Deng and Y. Zhang </td>
535    <td>GISSD: Group I Intron Sequence and Structure Database.</td>
536    <td><a href="https://www.ribocentre.org/docs/groupI.html" target="_blank"><b> Group I self-splicing intron </b></a></td>
537    <td>Sequence and structure database</td>
538    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/17942415" target="_blank"><b> Nucleic Acids Res 36 (Database issue): D31-7.</b></a></td>
539  </tr>
540  <tr>
541    <td>2009</td>
542    <td>Vicens, Q. and T. R. Cech </td>
543    <td>A natural ribozyme with 3',5' RNA ligase activity.</td>
544    <td><a href="https://www.ribocentre.org/docs/nature-ribozyme.html" target="_blank"><b>A natural ribozyme with 3',5' RNA ligase activity</b></a></td>
545    <td>Discovery</td>
546    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/19125157" target="_blank"><b> Nat Chem Biol 5(2): 97-9.</b></a></td>
547  </tr>
548  <tr>
549    <td>2004</td>
550    <td>J. Proudfoot and A. Akoulitchev </td>
551    <td>Autocatalytic RNA cleavage in the human beta-globin pre-mRNA promotes transcription termination.</td>
552    <td><a href="https://www.ribocentre.org/docs/CoTC.html" target="_blank"><b>CoTC ribozyme(Beta-globin co-transcriptional cleavage ribozyme)</b></a></td>
553    <td>Discovery that the CoTC process in the human beta-globin gene involves an RNA self-cleaving activity</td>
554    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15565159" target="_blank"><b> Nature 432(7016): 526-530.</b></a></td>
555  </tr>
556  <tr>
557    <td>2006</td>
558    <td>Salehi-Ashtiani, K., A. Luptak, A. Litovchick and J. W. Szostak </td>
559    <td>A genomewide search for ribozymes reveals an HDV-like sequence in the human CPEB3 gene.</td>
560    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>CPEB3 ribozyme</b></a></td>
561    <td>A HDV-like sequence in the human CPEB3 gene</td>
562    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16990549" target="_blank"><b> Science 313 (5794): 1788-92.</b></a></td>
563  </tr>
564  <tr>
565    <td>2014</td>
566    <td>Skilandat, M., M. Rowinska-Zyrek and R. K. Sigel </td>
567    <td>Solution structure and metal ion binding sites of the human CPEB3 ribozyme's P4 domain.</td>
568    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>CPEB3 ribozyme</b></a></td>
569    <td>NMR solution structure of CPEB3 ribozyme's P4 domain</td>
570    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/24652468" target="_blank"><b> J Biol Inorg Chem 19 (6): 903-12.</b></a></td>
571  </tr>
572  <tr>
573    <td>2016</td>
574    <td>Skilandat, M., M. Rowinska-Zyrek and R. K. Sigel </td>
575    <td>Secondary structure confirmation and localization of Mg2+ ions in the mammalian CPEB3 ribozyme.</td>
576    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>CPEB3 ribozyme</b></a></td>
577    <td>NMR studies confirm secondary structure and Mg2+ location in CPEB3 ribozyme </td>
578    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26966151" target="_blank"><b> RNA 22 (5): 750-63.</b></a></td>
579  </tr>
580  <tr>
581    <td>2021</td>
582    <td>Bendixsen, D. P., T. B. Pollock, G. Peri and E. J. Hayden </td>
583    <td>Experimental Resurrection of Ancestral Mammalian CPEB3 Ribozymes Reveals Deep Functional Conservation.</td>
584    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>CPEB3 ribozyme</b></a></td>
585    <td>The functional conservation of CPEB3 ribozyme in mammalian evolution</td>
586    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/33720319" target="_blank"><b> Mol Biol Evol 38 (7): 2843-2853.</b></a></td>
587  </tr>
588  <tr>
589    <td>2014</td>
590    <td>Meyer, M., H. Nielsen, V. Olieric, P. Roblin, S. D. Johansen, E. Westhof and B. Masquida </td>
591    <td>Speciation of a group I intron into a lariat capping ribozyme.</td>
592    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
593    <td>Crystal structures of the precleavage and postcleavage lariat-capping ribozymes</td>
594    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/24821772" target="_blank"><b>
594 Proc Natl Acad Sci U S A 111(21): 7659-7664.</b></a></td>
595  </tr>
596  <tr>
597    <td>2002</td>
598    <td>Johansen, S., C. Einvik and H. Nielsen </td>
599    <td>DiGIR1 and NaGIR1: naturally occurring group I-like ribozymes with unique core organization and evolved biological role.</td>
600    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
601    <td>REVIEW</td>
602    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/12458083" target="_blank"><b> Biochimie 84(9): 905-912.</b></a></td>
603  </tr>
604  <tr>
605    <td>2002</td>
606    <td>Vader, A., S. Johansen and H. Nielsen </td>
607    <td>The group I-like ribozyme DiGIR1 mediates alternative processing of pre-rRNA transcripts in Didymium iridis.</td>
608    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
609    <td>DiGIR1 mediates alternative processing of pre-rRNA transcripts in Didymium iridis</td>
610    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/12444968" target="_blank"><b> Eur J Biochem 269(23): 5804-5812.</b></a></td>
611  </tr>
612  <tr>
613    <td>2014</td>
614    <td>Tang, Y., H. Nielsen, B. Masquida, P. P. Gardner and S. D. Johansen </td>
615    <td>Molecular characterization of a new member of the lariat capping twin-ribozyme introns.</td>
616    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
617    <td>Molecular characterization of a new member of the lariat capping twin-ribozyme introns</td>
618    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25342998" target="_blank"><b> Mob DNA 5: 25.</b></a></td>
619  </tr>
620  <tr>
621    <td>2021</td>
622    <td>Pietschmann, M., G. Tempel, M. Halladjian, N. Krogh and H. Nielsen </td>
623    <td>Use of a Lariat Capping Ribozyme to Study Cap Function In Vivo.</td>
624    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
625    <td>Use of a lariat capping ribozyme to study cap function in vivo</td>
626    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32712925" target="_blank"><b> Methods Mol Biol 2167: 271-285.</b></a></td>
627  </tr>
628  <tr>
629    <td>1994</td>
630    <td>Johansen, S. and V. M. Vogt </td>
631    <td>An intron in the nuclear ribosomal DNA of Didymium iridis codes for a group I ribozyme and a novel ribozyme that cooperate in self-splicing.</td>
632    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
633    <td>Sequence discovered</td>
634    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8124711" target="_blank"><b> Cell 76(4): 725-734.</b></a></td>
635  </tr>
636  <tr>
637    <td>1995</td>
638    <td>Decatur, W. A., C. Einvik, S. Johansen and V. M. Vogt </td>
639    <td>Two group I ribozymes with different functions in a nuclear rDNA intron.</td>
640    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
641    <td>Catalytic RNA element renamed as the group I-like ribozyme, GIR1</td>
642    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7556099" target="_blank"><b> EMBO J 14(18): 4558-4568.</b></a></td>
643  </tr>
644  <tr>
645    <td>2005</td>
646    <td>Nielsen, H., E. Westhof and S. Johansen </td>
647    <td>An mRNA is capped by a 2', 5' lariat catalyzed by a group I-like ribozyme.</td>
648    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
649    <td>GIR1 makes tiny lariats</td>
650    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16141078" target="_blank"><b> Science 309(5740): 1584-1587.</b></a></td>
651  </tr>
652  <tr>
653    <td>2008</td>
654    <td>eckert, B., H. Nielsen, C. Einvik, S. D. Johansen, E. Westhof and B. Masquida </td>
655    <td>Molecular modelling of the GIR1 branching ribozyme gives new insight into evolution of structurally related ribozymes.</td>
656    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
657    <td>Molecular modelling of the GIR1 branching ribozyme</td>
658    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/18219270" target="_blank"><b> EMBO J 27(4): 667-678.</b></a></td>
659  </tr>
660  <tr>
661    <td>2017</td>
662    <td>Krogh, N., M. Pietschmann, M. Schmid, T. H. Jensen and H. Nielsen </td>
663    <td>Lariat capping as a tool to manipulate the 5' end of individual yeast mRNA species in vivo.</td>
664    <td><a href="https://www.ribocentre.org/docs/LC-ribozyme.html" target="_blank"><b>Lariat capping ribozyme</b></a></td>
665    <td>Lariat capping as a tool to manipulate the 5' end of mRNA</td>
666    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28159804" target="_blank"><b> RNA 23(5): 683-695.</b></a></td>
667  </tr>
668  <tr>
669    <td>2006</td>
670    <td>Klein, D. and A. Ferré-D'Amaré </td>
671    <td>Structural basis of glmS ribozyme activation by glucosamine-6-phosphate.</td>
672    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
673    <td>Crystal structure</td>
674    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16990543" target="_blank"><b> Science (New York, N.Y.) 313(5794): 1752-1756.</b></a></td>
675  </tr>
676  <tr>
677    <td>2007</td>
678    <td>Cochrane, J., S. Lipchock and S. Strobel </td>
679    <td>Structural investigation of the GlmS ribozyme bound to Its catalytic cofactor.</td>
680    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
681    <td>Crystal structure</td>
682    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/17196404" target="_blank"><b> Chemistry &amp; biology 14(1): 97-105.</b></a></td>
683  </tr>
684  <tr>
685    <td>2007</td>
686    <td>Klein, D., M. Been and A. Ferré-D'Amaré </td>
687    <td>Essential role of an active-site guanine in glmS ribozyme catalysis.</td>
688    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
689    <td>Essential role of an active-site guanine G40 in glmS ribozyme catalysis</td>
690    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/17990888" target="_blank"><b> Journal of the American Chemical Society 129(48): 14858-14859.</b></a></td>
691  </tr>
692  <tr>
693    <td>2017</td>
694    <td>Schüller, A., D. Matzner, C. Lünse, V. Wittmann, C. Schumacher, S. Unsleber, H. Brötz-Oesterhelt, C. Mayer, G. Bierbaum and G. Mayer </td>
695    <td>Activation of the glmS Ribozyme Confers Bacterial Growth Inhibition.</td>
696    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
697    <td>GlcN6P cofactor play a variety of catalytic roles in glmS ribozyme</td>
698    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28012261" target="_blank"><b> Chembiochem : a European journal of chemical biology 18(5): 435-440.</b></a></td>
699  </tr>
700  <tr>
701    <td>
7012004</td>
702    <td>Winkler, W., A. Nahvi, A. Roth, J. Collins and R. Breaker </td>
703    <td>Control of gene expression by a natural metabolite-responsive ribozyme.</td>
704    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
705    <td>Discovery,Secondary structure</td>
706    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15029187" target="_blank"><b> Nature 428(6980): 281-286.</b></a></td>
707  </tr>
708  <tr>
709    <td>2006</td>
710    <td>Soukup, G. </td>
711    <td>Core requirements for glmS ribozyme self-cleavage reveal a putative pseudoknot structure.</td>
712    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
713    <td>Pseudoknot structure</td>
714    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16464827" target="_blank"><b> Nucleic acids research 34(3): 968-975.</b></a></td>
715  </tr>
716  <tr>
717    <td>2007</td>
718    <td>Collins, J., I. Irnov, S. Baker and W. Winkler </td>
719    <td>Mechanism of mRNA destabilization by the glmS ribozyme.</td>
720    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
721    <td>Mechanism of mRNA destabilization by the glms ribozyme</td>
722    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/18079181" target="_blank"><b> Genes &amp; development 21(24): 3356-3368.</b></a></td>
723  </tr>
724  <tr>
725    <td>2009</td>
726    <td>Cochrane, J., S. Lipchock, K. Smith and S. Strobel </td>
727    <td>Structural and chemical basis for glucosamine 6-phosphate binding and activation of the glmS ribozyme.</td>
728    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
729    <td>Chemical Mechanism</td>
730    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/19228039" target="_blank"><b> Biochemistry 48(15): 3239-3246.</b></a></td>
731  </tr>
732  <tr>
733    <td>2010</td>
734    <td>Ferré-D'Amaré, A. </td>
735    <td>The glmS ribozyme: use of a small molecule coenzyme by a gene-regulatory RNA.</td>
736    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
737    <td>Use of a small molecule coenzyme by a gene-regulatory RNA</td>
738    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/20822574" target="_blank"><b> Quarterly reviews of biophysics 43(4): 423-447.</b></a></td>
739  </tr>
740  <tr>
741    <td>2010</td>
742    <td>Klawuhn, K., J. Jansen, J. Souchek, G. Soukup and J. Soukup </td>
743    <td>Analysis of metal ion dependence in glmS ribozyme self-cleavage and coenzyme binding.</td>
744    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
745    <td>The role of Mg2+ in active sites</td>
746    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21108273" target="_blank"><b> Chembiochem : a European journal of chemical biology 11(18): 2567-2571.</b></a></td>
747  </tr>
748  <tr>
749    <td>2011</td>
750    <td>Watson, P. and M. Fedor </td>
751    <td>The glmS riboswitch integrates signals from activating and inhibitory metabolites in vivo.</td>
752    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
753    <td>The glmS riboswitch integrates signals from activating and inhibitory metabolites in vivo</td>
754    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21317896" target="_blank"><b> Nature structural &amp; molecular biology 18(3): 359-363.</b></a></td>
755  </tr>
756  <tr>
757    <td>2011</td>
758    <td>McCown, P., A. Roth and R. Breaker </td>
759    <td>An expanded collection and refined consensus model of glmS ribozymes.</td>
760    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
761    <td>An expanded collection and refined consensus model of glmS ribozymes</td>
762    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21367971" target="_blank"><b> RNA (New York, N.Y.) 17(4): 728-736.</b></a></td>
763  </tr>
764  <tr>
765    <td>2012</td>
766    <td>Viladoms, J. and M. Fedor </td>
767    <td>The glmS ribozyme cofactor is a general acid-base catalyst.</td>
768    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
769    <td>The glmS ribozyme cofactor is a general acid-base catalyst</td>
770    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/23113700" target="_blank"><b> Journal of the American Chemical Society 134(46): 19043-19049.</b></a></td>
771  </tr>
772  <tr>
773    <td>2013</td>
774    <td>Lau, M. W. L. and A. R. Ferré-D Amaré</td>
775    <td>An in vitro evolved glmS ribozyme has the wild-type fold but loses coenzyme dependence.</td>
776    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
777    <td>An in vitro evolved glmS ribozyme has the wild-type fold but loses coenzyme dependence</td>
778    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/24096303" target="_blank"><b> Journal of the American Chemical Society 134(46): 19043-19049.</b></a></td>
779  </tr>
780  <tr>
781    <td>2017</td>
782    <td>
782Bingaman, J., S. Zhang, D. Stevens, N. Yennawar, S. Hammes-Schiffer and P. Bevilacqua </td>
783    <td>The GlcN6P cofactor plays multiple catalytic roles in the glmS ribozyme.</td>
784    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
785    <td>GlcN6P cofactor play a variety of catalytic roles in glmS ribozyme</td>
786    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28192411" target="_blank"><b> Nature chemical biology 13(4): 439-445.</b></a></td>
787  </tr>
788  <tr>
789    <td>2018</td>
790    <td>Cruz-Bustos, T., S. Ramakrishnan, C. Cordeiro, M. Ahmed and R. Docampo </td>
791    <td>A Riboswitch-based Inducible Gene Expression System for Trypanosoma brucei.</td>
792    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
793    <td>The glmS ribozyme could be used as a tool to study essential genes in T. brucei</td>
794    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29265590" target="_blank"><b> The Journal of eukaryotic microbiology 65(3): 412-421.</b></a></td>
795  </tr>
796  <tr>
797    <td>2020</td>
798    <td>Andreasson, J., A. Savinov, S. Block and W. Greenleaf </td>
799    <td>Comprehensive sequence-to-function mapping of cofactor-dependent RNA catalysis in the glmS ribozyme.</td>
800    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
801    <td>Comprehensive sequence-to-function mapping of cofactor-dependent RNA catalysis in the glmS ribozyme</td>
802    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32245964" target="_blank"><b> Nature communications 11(1): 1663.</b></a></td>
803  </tr>
804  <tr>
805    <td>2021</td>
806    <td>Traykovska, M., K. Popova and R. Penchovsky </td>
807    <td>Targeting glmS Ribozyme with Chimeric Antisense Oligonucleotides for Antibacterial Drug Development.</td>
808    <td><a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><b>GlmS ribozyme</b></a></td>
809    <td>The glmS ribozyme is a very suitable target for antibacterial drug development with antisense oligonucleotides</td>
810    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/34734706" target="_blank"><b> ACS synthetic biology 10(11): 3167-3176.</b></a></td>
811  </tr>
812  <tr>
813    <td>1980</td>
814    <td>Halbreich, A., P. Pajot, M. Foucher, C. Grandchamp and P. Slonimski </td>
815    <td>A pathway of cytochrome b mRNA processing in yeast mitochondria: specific splicing steps and an intron-derived circular DNA.</td>
816    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
817    <td>"Circular" introns were found to splice out from a mitochondrial gene</td>
818    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/6986990" target="_blank"><b>  Cell 19 (2): 321-9.</b></a></td>
819  </tr>
820  <tr>
821    <td>1982</td>
822    <td>Michel, F., A. Jacquier and B. Dujon </td>
823    <td>Comparison of fungal mitochondrial introns reveals extensive homologies in RNA secondary structure.</td>
824    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
825    <td>First secondary structure model by comparative sequence analysis</td>
826    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/6817818" target="_blank"><b>  Biochimie 64 (10): 867-81.</b></a></td>
827  </tr>
828  <tr>
829    <td>1986</td>
830    <td>van der Veen, R., A. C. Arnberg, G. van der Horst, L. Bonen, H. F. Tabak and L. A. Grivell </td>
831    <td>Excised group II introns in yeast mitochondria are lariats and can be formed by self-splicing in vitro.</td>
832    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
833    <td>Group II introns form a lariat by self-splicing in vivo</td>
834    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2417726" target="_blank"><b>  Cell 44 (2): 225-34.</b></a></td>
835  </tr>
836  <tr>
837    <td>1986</td>
838    <td>Peebles, C. L., P. S. Perlman, K. L. Mecklenburg, M. L. Petrillo, J. H. Tabor, K. A. Jarrell and H. L. Cheng </td>
839    <td>A self-splicing RNA excises an intron lariat.</td>
840    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
841    <td>Group II introns form a lariat by self-splicing in vivo</td>
842    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/3510741" target="_blank"><b> Cell 44 (2): 213-23.</b></a></td>
843  </tr>
844  <tr>
845    <td>1994</td>
846    <td>Chanfreau, G. and A. Jacquier </td>
847    <td>Catalytic site components common to both splicing steps of a group II intron.</td>
848    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
849    <td>Common catalytic site to both splicing steps.</td>
850    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31348888" target="_blank"><b> Cell 178 (3): 612-623.e12.</b></a></td>
851  </tr>
852  <tr>
853    <td>1995</td>
854    <td>Peebles, C. L., M. Zhang, P. S. Perlman and J. S. Franzen </td>
855    <td>Catalytically critical nucleotide in domain 5 of a group II intron.</td>
856    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
857    <td>Catalytically critical nucleotide in domain 5 </td>
858    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7538669" target="_blank"><b> Proc Natl Acad Sci U S A 92 (10): 4422-6.</b></a></td>
859  </tr>
860  <tr>
861    <td>1995</td>
862    <td>Boulanger, S. C., S. M. Belcher, U. Schmidt, S. D. Dib-Hajj, T. Schmidt and P. S. Perlman </td>
863    <td>Studies of point mutants define three essential paired nucleotides in the domain  5 substructure of a group II intron.</td>
864    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
865    <td>Three essential paired nucleotides in the domain  5</td>
866    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7623838" target="_blank"><b> Mol Cell Biol 15 (8): 4479-88.</b></a></td>
867  </tr>
868  <tr>
869    <td>1996</td>
870    <td>Schmidt, U., M. Podar, U. Stahl and P. S. Perlman </td>
871    <td>Mutations of the two-nucleotide bulge of D5 of a group II intron block splicing in vitro and in vivo: phenotypes and suppressor mutations.</td>
872    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
873    <td>Two-nucleotide bulge in D5 are important</td>
874    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8903346" target="_blank"><b> RNA 2 (11): 1161-72.</b></a></td>
875  </tr>
876  <tr>
877    <td>1996</td>
878    <td>Abramovitz, D. L., R. A. Friedman and A. M. Pyle </td>
879    <td>Catalytic role of 2'-hydroxyl groups within a group II intron active site.</td>
880    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
881    <td>Eight hydroxyl groups in D5 are the key to activity</td>
882    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8596912" target="_blank"><b> Science 271 (5254): 1410-3.</b></a></td>
883  </tr>
884  <tr>
885    <td>1997</td>
886    <td>Costa, M., E. Deme, A. Jacquier and F. Michel </td>
887    <td>Multiple tertiary interactions involving domain II of group II self-splicing introns.</td>
888    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
889    <td>D2 stabilizes the ribozyme core and controls the location of D6 and branching sites</td>
890    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9126835" target="_blank"><b> J Mol Biol 267 (3): 520-36.</b></a></td>
891  </tr>
892  <tr>
893    <td>2000</td>
894    <td>Boudvillain, M., A. de Lencastre and A. M. Pyle </td>
895    <td>A tertiary interaction that links active-site domains to the 5' splice site of a  group II intron.</td>
896    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
897    <td>Demonstration of tertiary interactions linking the catalytically critical regions of D1 to D5 and anchoring them at the 5' splice site</td>
898    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10917534" target="_blank"><b> Nature 406 (6793): 315-8.</b></a></td>
899  </tr>
900  <tr>
901    <td>2002</td>
902    <td>Zhang, L. and J. A. Doudna </td>
903    <td>Structural insights into group II intron catalysis and branch-site selection.</td>
904    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
905    <td>Crystal structures of 70-nucleotide RNAs of yeast ai5γ D5 and D6 (3 Å
905)</td>
906    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11859154" target="_blank"><b> Science 295 (5562): 2084-8.</b></a></td>
907  </tr>
908  <tr>
909    <td>2005</td>
910    <td>Fedorova, O. and A. M. Pyle </td>
911    <td>Linking the group II intron catalytic domains: tertiary contacts and structural features of domain 3.</td>
912    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
913    <td>D3 is a functional group important for catalytic activity, and the interaction of D3 and D5 promotes catalysis</td>
914    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16252007" target="_blank"><b> EMBO J 24 (22): 3906-16.</b></a></td>
915  </tr>
916  <tr>
917    <td>2005</td>
918    <td>de Lencastre, A., S. Hamill and A. M. Pyle </td>
919    <td>A single active-site region for a group II intron.</td>
920    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
921    <td>Single active-site region for group II intron catalysis</td>
922    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15980867" target="_blank"><b>  Nat Struct Mol Biol 12 (7): 626-7.</b></a></td>
923  </tr>
924  <tr>
925    <td>2007</td>
926    <td>Fedorova, O. and N. Zingler </td>
927    <td>Group II introns: structure, folding and splicing mechanism.</td>
928    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
929    <td>Review: splicing mechanism</td>
930    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/17570818" target="_blank"><b> Biol Chem 388 (7): 665-78.</b></a></td>
931  </tr>
932  <tr>
933    <td>2008</td>
934    <td>Toor, N., K. S. Keating, S. D. Taylor and A. M. Pyle </td>
935    <td>Crystal structure of a self-spliced group II intron.</td>
936    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
937    <td>The first 3D structure of the <em>Oceanobacillus iheyensis</em> group IIC intron</td>
938    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/18388288" target="_blank"><b> Science 320 (5872): 77-82.</b></a></td>
939  </tr>
940  <tr>
941    <td>2010</td>
942    <td>Pyle, A. M. </td>
943    <td>The tertiary structure of group II introns: implications for biological function  and evolution.</td>
944    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
945    <td>Common tertiary structure of the catalytic core</td>
946    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/20446804" target="_blank"><b> Crit Rev Biochem Mol Biol 45 (3): 215-32.</b></a></td>
947  </tr>
948  <tr>
949    <td>2012</td>
950    <td>Marcia, M. and A. M. Pyle </td>
951    <td>Visualizing group II intron catalysis through the stages of splicing.</td>
952    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
953    <td>Crystal structures of a group II intron at different stages of catalysis.</td>
954    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/23101623" target="_blank"><b>  Cell 151 (3): 497-507.</b></a></td>
955  </tr>
956  <tr>
957    <td>2014</td>
958    <td>Robart, A. R., R. T. Chan, J. K. Peters, K. R. Rajashankar and N. Toor </td>
959    <td>Crystal structure of a eukaryotic group II intron lariat.</td>
960    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
961    <td>Crystal structure of the intronic lariat form of eukaryotic group IIB</td>
962    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25252982" target="_blank"><b> Nature 514 (7521): 193-7.</b></a></td>
963  </tr>
964  <tr>
965    <td>2016</td>
966    <td>Qu, G., P. S. Kaushal, J. Wang, H. Shigematsu, C. L. Piazza, R. K. Agrawal, M. Belfort and H. W. Wang </td>
967    <td>Structure of a group II intron in complex with its reverse transcriptase.</td>
968    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
969    <td>Cryo-EM structures of a group Ⅱ intron in complex with its maturase</td>
970    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27136327" target="_blank"><b>  Nat Struct Mol Biol 23 (6): 549-57.</b></a></td>
971  </tr>
972  <tr>
973    <td>2017</td>
974    <td>Zhao, C. and A. M. Pyle </td>
975    <td>Structural Insights into the Mechanism of Group II Intron Splicing.</td>
976    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
977    <td>Review: Structural insights into the splicing mechanism</td>
978    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28438387" target="_blank"><b> Trends Biochem Sci 42 (6): 470-482.</b></a></td>
979  </tr>
980  <tr>
981    <td>2019</td>
982    <td>Haack, D. B., X. Yan, C. Zhang, J. Hingey, D. Lyumkis, T. S. Baker and N. Toor </td>
983    <td>Cryo-EM Structures of a Group II Intron Reverse Splicing into DNA.</td>
984    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
985    <td>Cryo-EM structures of a group II intron reverse splicing into DNA</td>
986    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31348888" target="_blank"><b> Cell 178 (3): 612-623.e12.</b></a></td>
987  </tr>
988  <tr>
989    <td>2020</td>
990    <td>Liu, N., X. Dong, C. Hu, J. Zeng, J. Wang, J. Wang, H. W. Wang and M. Belfort </td>
991    <td>Exon and protein positioning in a pre-catalytic group II intron RNP primed for splicing.</td>
992    <td><a href="https://www.ribocentre.org/docs/groupII.html" target="_blank"><b>Group II self-splicing intron</b></a></td>
993    <td>Two cryo-EM structures of group II intron RNPs  in their pre-catalytic state</td>
994    <td>
994<a href="https://www.ncbi.nlm.nih.gov/pubmed/33021674" target="_blank"><b> Nucleic Acids Res 48 (19): 11185-11198.</b></a></td>
995  </tr>
996  <tr>
997    <td>2002</td>
998    <td>Rupert, P., A. Massey, S. Sigurdsson and A. Ferré-D'Amaré </td>
999    <td>Transition state stabilization by a catalytic RNA.</td>
1000    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1001    <td>Crystal structure</td>
1002    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/12376595" target="_blank"><b> Science (New York, N.Y.) 298(5597): 1421-1424.</b></a></td>
1003  </tr>
1004  <tr>
1005    <td>2006</td>
1006    <td>Salter, J., J. Krucinska, S. Alam, V. Grum-Tokars and J. Wedekind </td>
1007    <td>Water in the active site of an all-RNA hairpin ribozyme and effects of Gua8 base variants on the geometry of phosphoryl transfer.</td>
1008    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1009    <td>Crystal structure</td>
1010    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16411744" target="_blank"><b> Biochemistry 45(3): 686-700.</b></a></td>
1011  </tr>
1012  <tr>
1013    <td>1997</td>
1014    <td>Hampel, A. and J. Cowan </td>
1015    <td>A unique mechanism for RNA catalysis: the role of metal cofactors in hairpin ribozyme cleavage.</td>
1016    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1017    <td>Chemical Mechanism</td>
1018    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9263639" target="_blank"><b> Chemistry &amp; biology 4(7): 513-517.</b></a></td>
1019  </tr>
1020  <tr>
1021    <td>1998</td>
1022    <td>Shippy, R., A. Siwkowski and A. Hampel </td>
1023    <td>Mutational analysis of loops 1 and 5 of the hairpin ribozyme.</td>
1024    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1025    <td>Loops 1 and 5 of the hairpin ribozyme</td>
1026    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9425078" target="_blank"><b> Biochemistry 37(2): 564-570.</b></a></td>
1027  </tr>
1028  <tr>
1029    <td>2001</td>
1030    <td>Rupert, P. and A. Ferré-D'Amaré </td>
1031    <td>Crystal structure of a hairpin ribozyme-inhibitor complex with implications for catalysis.</td>
1032    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1033    <td>Crystal structure</td>
1034    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11298439" target="_blank"><b> Nature 410(6830): 780-786.</b></a></td>
1035  </tr>
1036  <tr>
1037    <td>1986</td>
1038    <td>Buzayan, J. M., W. L. Gerlach and G. Bruening </td>
1039    <td>Non-enzymatic cleavage and ligation of RNAs complementary to a plant virus satellite RNA.</td>
1040    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1041    <td>Discovery</td>
1042    <td><a href="https://www.nature.com/articles/323349a0" target="_blank"><b> Nature.</b></a></td>
1043  </tr>
1044  <tr>
1045    <td>1993</td>
1046    <td>Berzal-Herranz, A., S. Joseph, B. Chowrira, S. Butcher and J. Burke </td>
1047    <td>Essential nucleotide sequences and secondary structure elements of the hairpin ribozyme.</td>
1048    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1049    <td>Sequence/Secondary structure</td>
1050    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8508779" target="_blank"><b> The EMBO journal 12(6): 2567-2573.</b></a></td>
1051  </tr>
1052  <tr>
1053    <td>2001</td>
1054    <td>Pinard, R., K. Hampel, J. Heckman, D. Lambert, P. Chan, F. Major and J. Burke </td>
1055    <td>Functional involvement of G8 in the hairpin ribozyme cleavage mechanism.</td>
1056    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1057    <td>Essential role of an active-site G8 in hairpin ribozyme catalysis</td>
1058    <td>
1058<a href="https://www.ncbi.nlm.nih.gov/pubmed/11707414" target="_blank"><b> The EMBO journal 20(22): 6434-6442.</b></a></td>
1059  </tr>
1060  <tr>
1061    <td>2005</td>
1062    <td>Kuzmin, Y., C. Da Costa, J. Cottrell and M. Fedor </td>
1063    <td>Role of an active site adenine in hairpin ribozyme catalysis.</td>
1064    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1065    <td>Essential role of an active-site A38 in hairpin ribozyme catalysis</td>
1066    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15907933" target="_blank"><b> Journal of molecular biology 349(5): 989-1010.</b></a></td>
1067  </tr>
1068  <tr>
1069    <td>2012</td>
1070    <td>Kath-Schorr, S., T. Wilson, N. Li, J. Lu, J. Piccirilli and D. Lilley </td>
1071    <td>General acid-base catalysis mediated by nucleobases in the hairpin ribozyme.</td>
1072    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1073    <td>Catalytic mechanism</td>
1074    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/22958171" target="_blank"><b> Journal of the American Chemical Society 134(40): 16717-16724.</b></a></td>
1075  </tr>
1076  <tr>
1077    <td>2019</td>
1078    <td>Hieronymus, R. and S. Müller </td>
1079    <td>Engineering of hairpin ribozyme variants for RNA recombination and splicing.</td>
1080    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1081    <td>Engineering of hairpin ribozyme variants</td>
1082    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30941784" target="_blank"><b> Annals of the New York Academy of Sciences 1447(1): 135-143.</b></a></td>
1083  </tr>
1084  <tr>
1085    <td>2021</td>
1086    <td>Song, E., E. Jiménez, H. Lin, K. Le Vay, R. Krishnamurthy and H. Mutschler </td>
1087    <td>Prebiotically Plausible RNA Activation Compatible with Ribozyme-Catalyzed Ligation.</td>
1088    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1089    <td>Situ activation of RNA substrates under reaction conditions amenable to catalysis by the hairpin ribozyme</td>
1090    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/33128282" target="_blank"><b> Angewandte Chemie (International ed. in English) 60(6): 2952-2957.</b></a></td>
1091  </tr>
1092  <tr>
1093    <td>2021</td>
1094    <td>Weinberg, C., V. Olzog, I. Eckert and Z. Weinberg </td>
1095    <td>Identification of over 200-fold more hairpin ribozymes than previously known in diverse circular RNAs.</td>
1096    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1097    <td>Expand the number of natural hairpin ribozymes</td>
1098    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/34096583" target="_blank"><b> Nucleic acids research 49(11): 6375-6388.</b></a></td>
1099  </tr>
1100  <tr>
1101    <td>2022</td>
1102    <td>Lee, B., U. Neri, C. Oh, P. Simmonds and E. Koonin </td>
1103    <td>ViroidDB: a database of viroids and viroid-like circular RNAs.</td>
1104    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1105    <td>ViroidDB: a database of viroids and viroid-like circular RNAs</td>
1106    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/34751403" target="_blank"><b> Nucleic acids research 50: D432-D438.</b></a></td>
1107  </tr>
1108  <tr>
1109    <td>2022</td>
1110    <td>Hieronymus, R., J. Zhu and S. Müller </td>
1111    <td>RNA self-splicing by engineered hairpin ribozyme variants.</td>
1112    <td><a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><b>Hairpin ribozyme</b></a></td>
1113    <td>Engineering of hairpin ribozyme variants</td>
1114    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/34928378" target="_blank"><b> Nucleic acids research 50(1): 368-377.</b></a></td>
1115  </tr>
1116  <tr>
1117    <td>1994</td>
1118    <td>Pley, H. W., K. M. Flaherty and D. B. McKay </td>
1119    <td>Three-dimensional structure of a hammerhead ribozyme.</td>
1120    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1121    <td>Crystal structure of type III HHR</td>
1122    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7969422" target="_blank"><b> Nature 372(6501): 68-74.</b></a></td>
1123  </tr>
1124  <tr>
1125    <td>2008</td>
1126    <td>Chi, Y. I., M. Martick, M. Lares, R. Kim, W. G. Scott and S. H. Kim </td>
1127    <td>Capturing hammerhead ribozyme structures in action by modulating general base catalysis.</td>
1128    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1129    <td>Crystal structure </td>
1130    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/18834200" target="_blank"><b> PLoS Biol 6(9): e234.</b></a></td>
1131  </tr>
1132  <tr>
1133    <td>2014</td>
1134    <td>Schultz, E. P., E. E. Vasquez and W. G. Scott </td>
1135    <td>Structural and catalytic effects of an invariant purine substitution in the hammerhead ribozyme: implications for the mechanism of acid-base catalysis.</td>
1136    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1137    <td>Specific base catalysis mechanism</td>
1138    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25195740" target="_blank"><b>
1138 Acta Crystallogr D Biol Crystallogr 70(Pt 9): 2256-2263.</b></a></td>
1139  </tr>
1140  <tr>
1141    <td>2006</td>
1142    <td>Martick, M. and W. G. Scott </td>
1143    <td>Tertiary contacts distant from the active site prime a ribozyme for catalysis.</td>
1144    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1145    <td>Crystal structure of typeⅠ HHR</td>
1146    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16859740" target="_blank"><b> Cell 126(2): 309-320.</b></a></td>
1147  </tr>
1148  <tr>
1149    <td>2013</td>
1150    <td>Anderson, M., E. P. Schultz, M. Martick and W. G. Scott </td>
1151    <td>Active-site monovalent cations revealed in a 1.55-Å-resolution hammerhead ribozyme structure.</td>
1152    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1153    <td>Crystal structure</td>
1154    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/23711504" target="_blank"><b> J Mol Biol 425(20): 3790-3798.</b></a></td>
1155  </tr>
1156  <tr>
1157    <td>1986</td>
1158    <td>Prody, G. A., J. T. Bakos, J. M. Buzayan, I. R. Schneider and G. Bruening </td>
1159    <td>Autolytic Processing of Dimeric Plant Virus Satellite RNA.</td>
1160    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1161    <td>Discovery</td>
1162    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/17833317" target="_blank"><b> Science 231(4745): 1577-1580.</b></a></td>
1163  </tr>
1164  <tr>
1165    <td>2015</td>
1166    <td>Weinberg, Z., P. B. Kim, T. H. Chen, S. Li, K. A. Harris, C. E. Lünse and R. R. Breaker </td>
1167    <td>New classes of self-cleaving ribozymes revealed by comparative genomics analysis.</td>
1168    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1169    <td>Discover variants of typeⅠHHR  </td>
1170    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26167874" target="_blank"><b> Nat Chem Biol 11(8): 606-610.</b></a></td>
1171  </tr>
1172  <tr>
1173    <td>2017</td>
1174    <td>Lünse, C. E., Z. Weinberg and R. R. Breaker </td>
1175    <td>Numerous small hammerhead ribozyme variants associated with Penelope-like retrotransposons cleave RNA as dimers.</td>
1176    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1177    <td>Some variants form dimers to cleave RNA</td>
1178    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27858507" target="_blank"><b> RNA Biol 14(11): 1499-1507.</b></a></td>
1179  </tr>
1180  <tr>
1181    <td>2017</td>
1182    <td>Ren, A., R. Micura and D. J. Patel </td>
1183    <td>Structure-based mechanistic insights into catalysis by small self-cleaving ribozymes.</td>
1184    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1185    <td>Catalytic mechanism</td>
1186    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29107885" target="_blank"><b> Curr Opin Chem Biol 41: 71-83.</b></a></td>
1187  </tr>
1188  <tr>
1189    <td>2019</td>
1190    <td>Wilson, T. J., Y. Liu, N. S. Li, Q. Dai, J. A. Piccirilli and D. M. J. Lilley </td>
1191    <td>Comparison of the Structures and Mechanisms of the Pistol and Hammerhead Ribozymes.</td>
1192    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1193    <td>The structure is similar with the pistol ribozyme</td>
1194    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31017785" target="_blank"><b> J Am Chem Soc 141(19): 7865-7875.</b></a></td>
1195  </tr>
1196  <tr>
1197    <td>1986</td>
1198    <td>Hutchins, C. J., P. D. Rathjen, A. C. Forster and R. H. Symons </td>
1199    <td>Self-cleavage of plus and minus RNA transcripts of avocado sunblotch viroid.</td>
1200    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1201    <td>Discovery</td>
1202    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/3714492" target="_blank"><b> Nucleic Acids Research 14(9): 3627-3640.</b></a></td>
1203  </tr>
1204  <tr>
1205    <td>1986</td>
1206    <td>Hutchins, C. J., P. D. Rathjen, A. C. Forster and R. H. Symons </td>
1207    <td>Self-cleavage of plus and minus RNA transcripts of avocado sunblotch viroid.</td>
1208    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1209    <td>Secondary structure of type I HHR</td>
1210    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/3714492" target="_blank"><b> Nucleic Acids Research 14(9): 3627-3640.</b></a></td>
1211  </tr>
1212  <tr>
1213    <td>1987</td>
1214    <td>Forster, A. C. and R. H. Symons </td>
1215    <td>Self-cleavage of plus and minus RNAs of a virusoid and a structural model for the active sites.</td>
1216    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1217    <td>Secondary structure of type III HHR</td>
1218    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2436805" target="_blank"><b> Cell 49(2): 211-220.</b></a></td>
1219  </tr>
1220  <tr>
1221    <td>1991</td>
1222    <td>Pabón-Peña, L. M., Y. Zhang and L. M. Epstein </td>
1223    <td>Newt satellite 2 transcripts self-cleave by using an extended hammerhead structure.</td>
1224    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1225    <td>Internal loops are important</td>
1226    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/1944278" target="_blank"><b> Mol Cell Biol 11(12): 6109-6115.</b></a></td>
1227  </tr>
1228  <tr>
1229    <td>1998</td>
1230    <td>Murray, J. B., A. A. Seyhan, N. G. Walter, J. M. Burke and W. G. Scott </td>
1231    <td>The hammerhead, hairpin and VS ribozymes are catalytically proficient in monovalent cations alone.</td>
1232    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1233    <td>Dense positive charge is critical for catalysis</td>
1234    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9818150" target="_blank"><b> Chem Biol 5(10): 587-595.</b></a></td>
1235  </tr>
1236  <tr>
1237    <td>2005</td>
1238    <td>Han, J. and J. M. Burke </td>
1239    <td>
1239Model for general acid-base catalysis by the hammerhead ribozyme: pH-activity relationships of G8 and G12 variants at the putative active site.</td>
1240    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1241    <td>G8 and G12 is critical for catalysis</td>
1242    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15910000" target="_blank"><b> Biochemistry 44(21): 7864-7870.</b></a></td>
1243  </tr>
1244  <tr>
1245    <td>2005</td>
1246    <td>Han, J. and J. M. Burke </td>
1247    <td>Model for general acid-base catalysis by the hammerhead ribozyme: pH-activity relationships of G8 and G12 variants at the putative active site.</td>
1248    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1249    <td>Catalytic mechanism</td>
1250    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15910000" target="_blank"><b> Biochemistry 44(21): 7864-7870.</b></a></td>
1251  </tr>
1252  <tr>
1253    <td>2011</td>
1254    <td>Jimenez, R. M., E. Delwart and A. Lupták </td>
1255    <td>Structure-based search reveals hammerhead ribozymes in the human microbiome.</td>
1256    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1257    <td>Secondary structure of type II HHR</td>
1258    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21257745" target="_blank"><b> J Biol Chem 286(10): 7737-7743.</b></a></td>
1259  </tr>
1260  <tr>
1261    <td>2013</td>
1262    <td>Lee, T. S., K. Y. Wong, G. M. Giambasu and D. M. York </td>
1263    <td>Bridging the gap between theory and experiment to derive a detailed understanding of hammerhead ribozyme catalysis.</td>
1264    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1265    <td>Catalytic mechanism</td>
1266    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/24156941" target="_blank"><b> Prog Mol Biol Transl Sci 120: 25-91.</b></a></td>
1267  </tr>
1268  <tr>
1269    <td>2015</td>
1270    <td>O'Rourke, S. M., W. Estell and W. G. Scott </td>
1271    <td>Minimal Hammerhead Ribozymes with Uncompromised Catalytic Activity.</td>
1272    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1273    <td>Trans-Hoogsteen greatly enhances the activity of the minimal hammer ribozyme<br /> &nbsp;&nbsp;</td>
1274    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25981451" target="_blank"><b> J Mol Biol 427(14): 2340-2347.</b></a></td>
1275  </tr>
1276  <tr>
1277    <td>2017</td>
1278    <td>de la Peña, M. and A. Cervera </td>
1279    <td>Circular RNAs with hammerhead ribozymes encoded in eukaryotic genomes: The enemy at home.</td>
1280    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1281    <td>Found on some retrozyme sequences</td>
1282    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28448743" target="_blank"><b> RNA Biol 14(8): 985-991.</b></a></td>
1283  </tr>
1284  <tr>
1285    <td>2017</td>
1286    <td>Chen, H., T. J. Giese, B. L. Golden and D. M. York </td>
1287    <td>Divalent Metal Ion Activation of a Guanine General Base in the Hammerhead Ribozyme: Insights from Molecular Simulations.</td>
1288    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1289    <td>Mg2+ is critical for catalysis by activating G12</td>
1290    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28530384" target="_blank"><b> Biochemistry 56(24): 2985-2994.</b></a></td>
1291  </tr>
1292  <tr>
1293    <td>2018</td>
1294    <td>O'Rourke, S. M. and W. G. Scott </td>
1295    <td>Structural Simplicity and Mechanistic Complexity in the Hammerhead Ribozyme.</td>
1296    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1297    <td>Complex mechanism of enhancing activity</td>
1298    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30340787" target="_blank"><b> Prog Mol Biol Transl Sci 159: 177-202.</b></a></td>
1299  </tr>
1300  <tr>
1301    <td>2019</td>
1302    <td>You, M., J. L. Litke, R. Wu and S. R. Jaffrey </td>
1303    <td>Detection of Low-Abundance Metabolites in Live Cells Using an RNA Integrator.</td>
1304    <td><a href="https://www.ribocentre.org/docs/hammer.html" target="_blank"><b>Hammerhead ribozyme</b></a></td>
1305    <td>Composing RNA-based biosensor</td>
1306    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30773480" target="_blank"><b> Cell Chem Biol 26(4): 471-481.e473.</b></a></td>
1307  </tr>
1308  <tr>
1309    <td>2019</td>
1310    <td>Zheng, L., C. Falschlunger, K. Huang, E. Mairhofer, S. Yuan, J. Wang, D. J. Patel, R. Micura and A. Ren </td>
1311    <td>Hatchet ribozyme structure and implications for cleavage mechanism.</td>
1312    <td><a href="https://www.ribocentre.org/docs/Hatchet.html" target="_blank"><b>Hatchet ribozyme</b></a></td>
1313    <td>Crystal structure and cleavage mechanism</td>
1314    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31088965" target="_blank"><b> Proc Natl Acad Sci U S A 116(22): 10783-10791.</b></a></td>
1315  </tr>
1316  <tr>
1317    <td>2020</td>
1318    <td>Micura, R. and C. Hobartner </td>
1319    <td>Fundamental studies of functional nucleic acids: aptamers, riboswitches, ribozymes and DNAzymes.</td>
1320    <td><a href="https://www.ribocentre.org/docs/Hatchet.html" target="_blank"><b>Hatchet ribozyme</b></a></td>
1321    <td>Review about functional nucleic acids<br /> &nbsp;&nbsp;</td>
1322    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32944725" target="_blank"><b> Chem Soc Rev 49(20): 7331-7353.</b></a></td>
1323  </tr>
1324  <tr>
1325    <td>2015</td>
1326    <td>Weinberg, Z., P. B. Kim, T. H. Chen, S. Li, K. A. Harris, C. E. Lunse and R. R. Breaker </td>
1327    <td>
1327New classes of self-cleaving ribozymes revealed by comparative genomics analysis.</td>
1328    <td><a href="https://www.ribocentre.org/docs/Hatchet.html" target="_blank"><b>Hatchet ribozyme</b></a></td>
1329    <td>Discovery, Secondary structure</td>
1330    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26167874" target="_blank"><b> Nat Chem Biol 11(8): 606-10.</b></a></td>
1331  </tr>
1332  <tr>
1333    <td>2015</td>
1334    <td>Li, S., C. E. Lunse, K. A. Harris and R. R. Breaker </td>
1335    <td>Biochemical analysis of hatchet self-cleaving ribozymes.</td>
1336    <td><a href="https://www.ribocentre.org/docs/Hatchet.html" target="_blank"><b>Hatchet ribozyme</b></a></td>
1337    <td>Biochemical analysis of hatchet ribozyme</td>
1338    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26385510" target="_blank"><b> RNA 21(11): 1845-51.</b></a></td>
1339  </tr>
1340  <tr>
1341    <td>2018</td>
1342    <td>Gasser, C., J. Gebetsberger, M. Gebetsberger and R. Micura </td>
1343    <td>SHAPE probing pictures Mg2+-dependent folding of small self-cleaving ribozymes.</td>
1344    <td><a href="https://www.ribocentre.org/docs/Hatchet.html" target="_blank"><b>Hatchet ribozyme</b></a></td>
1345    <td>SHAPE probing of pre-catalytic folds of hatchet ribozyme</td>
1346    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29924364" target="_blank"><b> Nucleic Acids Res 46(14): 6983-6995.</b></a></td>
1347  </tr>
1348  <tr>
1349    <td>1997</td>
1350    <td>Kolk, M. H. </td>
1351    <td>The structure of the isolated, central hairpin of the HDV antigenomic ribozyme: novel structural features and similarity of the loop in the ribozyme and free in solution.</td>
1352    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1353    <td>NMR structure of the isolated central hairpin(Stem Loop Ⅲ)</td>
1354    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9218809" target="_blank"><b>
1354 The EMBO Journal 16(12): 3685-3692.</b></a></td>
1355  </tr>
1356  <tr>
1357    <td>1998</td>
1358    <td>Ferré-D'Amaré, A. R., K. Zhou and J. A. Doudna </td>
1359    <td>Crystal structure of a hepatitis delta virus ribozyme.</td>
1360    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1361    <td>Crystal structure</td>
1362    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9783582" target="_blank"><b> Nature 395(6702): 567-574.</b></a></td>
1363  </tr>
1364  <tr>
1365    <td>2004</td>
1366    <td>Ke, A., K. Zhou, F. Ding, J. H. Cate and J. A. Doudna </td>
1367    <td>A conformational switch controls hepatitis delta virus ribozyme catalysis.</td>
1368    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1369    <td>Precursor structures</td>
1370    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15141216" target="_blank"><b> Nature 429(6988): 201-205.</b></a></td>
1371  </tr>
1372  <tr>
1373    <td>2010</td>
1374    <td>Chen, J. H., R. Yajima, D. M. Chadalavada, E. Chase, P. C. Bevilacqua and B. L. Golden </td>
1375    <td>A 1.9 A crystal structure of the HDV ribozyme precleavage suggests both Lewis acid and general acid mechanisms contribute to phosphodiester cleavage.</td>
1376    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1377    <td>Precleavage structures</td>
1378    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/20677830" target="_blank"><b> Biochemistry 49(31): 6508-6518.</b></a></td>
1379  </tr>
1380  <tr>
1381    <td>1991</td>
1382    <td>Rosenstein, S. P. and M. D. Been </td>
1383    <td>Evidence that genomic and antigenomic RNA self-cleaving elements from hepatitis delta virus have similar secondary structures.</td>
1384    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1385    <td>Pseudoknot-like secondary structure</td>
1386    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/1923826" target="_blank"><b> Nucleic Acids Research 19(19): 5409-5416.</b></a></td>
1387  </tr>
1388  <tr>
1389    <td>2019</td>
1390    <td>Lilley, D. M. J. </td>
1391    <td>Classification of the nucleolytic ribozymes based upon catalytic mechanism.</td>
1392    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1393    <td>Review</td>
1394    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31489181 " target="_blank"><b> F1000Res 8.</b></a></td>
1395  </tr>
1396  <tr>
1397    <td>1988</td>
1398    <td>Kuo, M. Y., L. Sharmeen, G. Dinter-Gottlieb and J. Taylor </td>
1399    <td>Characterization of self-cleaving RNA sequences on the genome and antigenome of human hepatitis delta virus.</td>
1400    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1401    <td>Discovery</td>
1402    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/3184270" target="_blank"><b> J Virol 62(12): 4439-4444.</b></a></td>
1403  </tr>
1404  <tr>
1405    <td>1988</td>
1406    <td>Sharmeen, L., M. Y. Kuo, G. Dinter-Gottlieb and J. Taylor </td>
1407    <td>Antigenomic RNA of human hepatitis delta virus can undergo self-cleavage.</td>
1408    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1409    <td>Discovery</td>
1410    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2455816" target="_blank"><b> J Virol 62(8): 2674-2679.</b></a></td>
1411  </tr>
1412  <tr>
1413    <td>1989</td>
1414    <td>Wu, H. N., Y. J. Lin, F. P. Lin, S. Makino, M. F. Chang and M. M. Lai </td>
1415    <td>Human hepatitis delta virus RNA subfragments contain an autocleavage activity.</td>
1416    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1417    <td>Discovery</td>
1418    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2648383" target="_blank"><b> Proceedings of the National Academy of Sciences 86(6): 1831-1835.</b></a></td>
1419  </tr>
1420  <tr>
1421    <td>1990</td>
1422    <td>Perrotta, A. T. and M. D. Been </td>
1423    <td>The self-cleaving domain from the genomic RNA of hepatitis delta virus: sequence requirements and the effects of denaturant.</td>
1424    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1425    <td>
142584 nucleotides are required for rapid and efficient self-cleavage</td>
1426    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2263447" target="_blank"><b> Nucleic Acids Res 18(23): 6821-6827.</b></a></td>
1427  </tr>
1428  <tr>
1429    <td>1991</td>
1430    <td>Perrotta, A. T. and M. D. Been </td>
1431    <td>A pseudoknot-like structure required for efficient self-cleavage of hepatitis delta virus RNA.</td>
1432    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1433    <td>Pseudoknot-like secondary structure</td>
1434    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2011192" target="_blank"><b> Nature 350(6317): 434-436.</b></a></td>
1435  </tr>
1436  <tr>
1437    <td>1992</td>
1438    <td>Been, M. D., A. T. Perrotta and S. P. Rosenstein </td>
1439    <td>Secondary structure of the self-cleaving RNA of hepatitis delta virus: applications to catalytic RNA design.</td>
1440    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1441    <td>The P4 duplex can reduce the minimum size to about 65 nucleotides</td>
1442    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/1445917" target="_blank"><b> Biochemistry 31(47): 11843-11852.</b></a></td>
1443  </tr>
1444  <tr>
1445    <td>1993</td>
1446    <td>Suh, Y. A., P. K. Kumar, K. Taira and S. Nishikawa </td>
1447    <td>Self-cleavage activity of the genomic HDV ribozyme in the presence of various divalent metal ions.</td>
1448    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1449    <td>Nonspecifific divalent cations are required for self-cleavage</td>
1450    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8341602" target="_blank"><b> Nucleic Acids Res 21(14): 3277-3280.</b></a></td>
1451  </tr>
1452  <tr>
1453    <td>1996</td>
1454    <td>Ferre-D'Amare, A. R. and J. A. Doudna </td>
1455    <td>Use of cis- and trans-ribozymes to remove 5' and 3' heterogeneities from milligrams of in vitro transcribed RNA.</td>
1456    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1457    <td>Use of cis-delta ribozyme generated 3′homogeneous RNA ends</td>
1458    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8600468" target="_blank"><b> Nucleic Acids Res 24(5): 977-978</b></a></td>
1459  </tr>
1460  <tr>
1461    <td>2000</td>
1462    <td>Nakano, S., D. M. Chadalavada and P. C. Bevilacqua </td>
1463    <td>General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme.</td>
1464    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1465    <td>C75 acts as the general acid and ribozyme-bound hydrated metal hydroxide as the general base</td>
1466    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10688799" target="_blank"><b> Science 287(5457): 1493-1497.</b></a></td>
1467  </tr>
1468  <tr>
1469    <td>2005</td>
1470    <td>Das, S. R. and J. A. Piccirilli </td>
1471    <td>General acid catalysis by the hepatitis delta virus ribozyme.</td>
1472    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1473    <td>It is prooved that C75 acts as the general acid</td>
1474    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16407993" target="_blank"><b> Nat Chem Biol 1(1): 45-52.</b></a></td>
1475  </tr>
1476  <tr>
1477    <td>2015</td>
1478    <td>Weinberg, Z., P. B. Kim, T. H. Chen, S. Li, K. A. Harris, C. E. Lünse and R. R. Breaker </td>
1479    <td>New classes of self-cleaving ribozymes revealed by comparative genomics analysis.</td>
1480    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1481    <td>The HDV ribozyme variants were discovered</td>
1482    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26167874" target="_blank"><b> Nature Chemical Biology 11(8): 606-610.</b></a></td>
1483  </tr>
1484  <tr>
1485    <td>2015</td>
1486    <td>Koo, S. C., J. Lu, N. S. Li, E. Leung, S. R. Das, M. E. Harris and J. A. Piccirilli </td>
1487    <td>Transition State Features in the Hepatitis Delta Virus Ribozyme Reaction Revealed by Atomic Perturbations.</td>
1488    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1489    <td>Transition state features</td>
1490    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26125657" target="_blank"><b> J Am Chem Soc 137(28): 8973-8982.</b></a></td>
1491  </tr>
1492  <tr>
1493    <td>2016</td>
1494    <td>Lee, T. S., B. K. Radak, M. E. Harris and D. M. York </td>
1495    <td>A Two-Metal-Ion-Mediated Conformational Switching Pathway for HDV Ribozyme Activation.</td>
1496    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1497    <td>Dynamic reaction mechanism model with two Mg2+ ions</td>
1498    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27774349" target="_blank"><b> ACS Catal 6(3): 1853-1869.</b></a></td>
1499  </tr>
1500  <tr>
1501    <td>2019</td>
1502    <td>Yamagami, R., M. Kayedkhordeh, D. H. Mathews and P. C. Bevilacqua </td>
1503    <td>Design of highly active double-pseudoknotted ribozymes: a combined computational and experimental study.</td>
1504    <td><a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><b>HDV ribozyme</b></a></td>
1505    <td>Double-pseudoknot HDV can self-cleavge with the same mechanism as the WT ribozyme</td>
1506    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30462314" target="_blank"><b> Nucleic Acids Res 47(1): 29-42.</b></a></td>
1507  </tr>
1508  <tr>
1509    <td>2015</td>
1510    <td>Weinberg, Z., P. B. Kim, T. H. Chen, S. Li, K. A. Harris, C. E. Lunse and R. R. Breaker </td>
1511    <td>
1511New classes of self-cleaving ribozymes revealed by comparative genomics analysis.</td>
1512    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>HDV ribozyme variants</b></a></td>
1513    <td>HDV ribozyme variants in bacterial metagenomes and fungal genomes</td>
1514    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26167874" target="_blank"><b> Nat Chem Biol 11 (8): 606-10</b></a></td>
1515  </tr>
1516  <tr>
1517    <td>2017</td>
1518    <td>Li, S. and R. R. Breaker </td>
1519    <td>Identification of 15 candidate structured noncoding RNA motifs in fungi by comparative genomics.</td>
1520    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>HDV variants</b></a></td>
1521    <td>More HDV ribozyme variants in fungi</td>
1522    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29029611" target="_blank"><b> BMC Genomics 18 (1): 785.</b></a></td>
1523  </tr>
1524  <tr>
1525    <td>2009</td>
1526    <td>Webb, C. H., N. J. Riccitelli, D. J. Ruminski and A. Luptak </td>
1527    <td>Widespread occurrence of self-cleaving ribozymes.</td>
1528    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>HDV-like ribozymes</b></a></td>
1529    <td>HDV-like ribozymes in other species</td>
1530    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/19965505" target="_blank"><b> Science 326 (5955): 953.</b></a></td>
1531  </tr>
1532  <tr>
1533    <td>2011</td>
1534    <td>Webb, C. H. and A. Luptak </td>
1535    <td>HDV-like self-cleaving ribozymes.</td>
1536    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>HDV-like self-cleaving ribozymes</b></a></td>
1537    <td>A review of HDV-like self-cleaving ribozymes</td>
1538    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21734469" target="_blank"><b> RNA Biol 8 (5): 719-27.</b></a></td>
1539  </tr>
1540  <tr>
1541    <td>2021</td>
1542    <td>Chen, Y., F. Qi, F. Gao, H. Cao, D. Xu, K. Salehi-Ashtiani and P. Kapranov </td>
1543    <td>Hovlinc is a recently evolved class of ribozyme found in human lncRNA.</td>
1544    <td><a href="https://www.ribocentre.org/docs/Hovlinc.html" target="_blank"><b>Hovlinc ribozyme</b></a></td>
1545    <td>Discovery of Hovlinc ribozyme and its secondary structure</td>
1546    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/33753927" target="_blank"><b> Nature Chemical Biology 17 (5): 601-607.</b></a></td>
1547  </tr>
1548  <tr>
1549    <td>2011</td>
1550    <td>Sanchez-Luque, F. J., M. C. Lopez, F. Macias, C. Alonso and M. C. Thomas </td>
1551    <td>Identification of an hepatitis delta virus-like ribozyme at the mRNA 5'-end of the L1Tc retrotransposon from Trypanosoma cruzi.</td>
1552    <td><a href="https://www.ribocentre.org/docs/Hovlinc.html" target="_blank"><b>L1Tc ribozyme(L1TcRz)</b></a></td>
1553    <td>A HDV-like ribozyme in L1Tc mRNA</td>
1554    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21724615" target="_blank"><b> Nucleic Acids Res 39 (18): 8065-77.</b></a></td>
1555  </tr>
1556  <tr>
1557    <td>2006</td>
1558    <td>Salehi-Ashtiani, K., A. Luptak, A. Litovchick and J. W. Szostak </td>
1559    <td>A genomewide search for ribozymes reveals an HDV-like sequence in the human CPEB3 gene.</td>
1560    <td><a href="https://www.ribocentre.org/docs/Line1.html" target="_blank"><b>LINE1 ribozyme</b></a></td>
1561    <td>Discovery</td>
1562    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16990549" target="_blank"><b> Science 313(5794): 1788-1792.</b></a></td>
1563  </tr>
1564  <tr>
1565    <td>2016</td>
1566    <td>Ren, A., Vusurovic, N., Gebetsberger, J., Gao, P., Juen, M., Kreutz, C., Micura, R. &amp; Patel, D. J. </td>
1567    <td>Pistol ribozyme adopts a pseudoknot fold facilitating site-specific in-line cleavage. </td>
1568    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1569    <td>The pseudoknot fold facilitating sitespecific in-line cleavage</td>
1570    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27398999" target="_blank"><b>Nature Chemical Biology, 12, 702-8.</b></a></td>
1571  </tr>
1572  <tr>
1573    <td>2017</td>
1574    <td>Nguyen, L. A., Wang, J. &amp; Steitz, T. A. </td>
1575    <td>Crystal structure of Pistol, a class of self-cleaving ribozyme.</td>
1576    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1577    <td> Crystal structure of Pistol shows an evolutionarily conserved cleavage mechanism that is like other self-cleaving ribozymes</td>
1578    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28096403" target="_blank"><b>Proc Natl Acad Sci U S A, 114, 1021-6.</b></a></td>
1579  </tr>
1580  <tr>
1581    <td>2019</td>
1582    <td>Wilson, T. J., Y. Liu, N. S. Li, Q. Dai, J. A. Piccirilli and D. Lilley </td>
1583    <td>Comparison of the Structures and Mechanisms of the Pistol and Hammerhead Ribozymes.</td>
1584    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1585    <td>Comparison of the Structures and Mechanisms of the Pistol and Hammerhead Ribozymes</td>
1586    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31017785" target="_blank"><b> J Am Chem Soc 141(19): 7865-7875.</b></a></td>
1587  </tr>
1588  <tr>
1589    <td>2020</td>
1590    <td>Teplova, M., Falschlunger, C., Krasheninina, O., Egger, M., Ren, A., Patel, D. J. &amp; Micura, R. </td>
1591    <td>Crucial Roles of Two Hydrated Mg2+ Ions in Reaction Catalysis of the Pistol Ribozyme. </td>
1592    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1593    <td>Crucial Roles of Two Hydrated Mg2+ Ions in Reaction Catalysis</td>
1594    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31804735" target="_blank"><b>Angew Chem Int Ed Engl, 59, 2837-43.</b></a></td>
1595  </tr>
1596  <tr>
1597    <td>2017</td>
1598    <td>Kobori, S., K. Takahashi and Y. Yokobayashi </td>
1599    <td>
1599Deep Sequencing Analysis of Aptazyme Variants Based on a Pistol Ribozyme.</td>
1600    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1601    <td>Deep Sequencing Analysis of Aptazyme Variants Based on Pistol Ribozyme</td>
1602    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28398719" target="_blank"><b> ACS Synth Biol 6(7): 1283-1288.</b></a></td>
1603  </tr>
1604  <tr>
1605    <td>2020</td>
1606    <td>Micura, R. and C. Hobartner </td>
1607    <td>Fundamental studies of functional nucleic acids: aptamers, riboswitches, ribozymes and DNAzymes.</td>
1608    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1609    <td>Review about functional nucleic acids</td>
1610    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32944725" target="_blank"><b> Chem Soc Rev 49(20): 7331-7353.</b></a></td>
1611  </tr>
1612  <tr>
1613    <td>2021</td>
1614    <td>Mustafina, K., Y. Nomura, R. Rotrattanadumrong and Y. Yokobayashi </td>
1615    <td>Circularly-Permuted Pistol Ribozyme: A Synthetic Ribozyme Scaffold for Mammalian  Riboswitches.</td>
1616    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1617    <td>Pistol ribozyme used for Mammalian Riboswitches</td>
1618    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/34374523" target="_blank"><b> ACS Synth Biol 10(8): 2040-2048.</b></a></td>
1619  </tr>
1620  <tr>
1621    <td>2015</td>
1622    <td>Weinberg, Z., Kim, P. B., Chen, T. H., Li, S., Harris, K. A., Lunse, C. E. &amp; Breaker, R. R. </td>
1623    <td>New classes of self-cleaving ribozymes revealed by comparative genomics analysis.</td>
1624    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1625    <td>Discovery, Secondary structure</td>
1626    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26167874" target="_blank"><b> Nature Chemical Biology, 11, 606-10.</b></a></td>
1627  </tr>
1628  <tr>
1629    <td>2015</td>
1630    <td>Harris, K. A., C. E. Lunse, S. Li, K. I. Brewer and R. R. Breaker </td>
1631    <td>Biochemical analysis of pistol self-cleaving ribozymes.</td>
1632    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1633    <td>Biochemical analysis of pistol ribozyme</td>
1634    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26385507" target="_blank"><b> RNA 21(11): 1852-8.</b></a></td>
1635  </tr>
1636  <tr>
1637    <td>2017</td>
1638    <td>Neuner, S., C. Falschlunger, E. Fuchs, M. Himmelstoss, A. Ren, D. J. Patel and R. Micura </td>
1639    <td>Atom-Specific Mutagenesis Reveals Structural and Catalytic Roles for an Active-Site Adenosine and Hydrated Mg(2+) in Pistol Ribozymes.</td>
1640    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1641    <td>Structural and Catalytic Roles for an Active-Site Adenosine and Hydrated Mg(2+) in Pistol Ribozymes</td>
1642    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29098759" target="_blank"><b> Angew Chem Int Ed Engl 56(50): 15954-15958.</b></a></td>
1643  </tr>
1644  <tr>
1645    <td>2020</td>
1646    <td>Joseph, N. N., R. N. Roy and T. A. Steitz </td>
1647    <td>Molecular dynamics analysis of Mg(2+) -dependent cleavage of a pistol ribozyme reveals a fail-safe secondary ion for catalysis.</td>
1648    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1649    <td> Mg2+ -dependent cleavage of a pistol ribozyme reveals a fail-safe secondary ion for catalysis</td>
1650    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32091136" target="_blank"><b> J Comput Chem 41(14): 1345-1352.</b></a></td>
1651  </tr>
1652  <tr>
1653    <td>2021</td>
1654    <td>Lihanova, Y. and C. E. Weinberg </td>
1655    <td>Biochemical analysis of cleavage and ligation activities of the pistol ribozyme from Paenibacillus polymyxa.</td>
1656    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1657    <td>Biochemical analysis of cleavage and ligation activities of the pistol ribozyme from Paenibacillus polymyxa</td>
1658    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/33622172" target="_blank"><b> RNA Biol 18(11): 1858-1866.</b></a></td>
1659  </tr>
1660  <tr>
1661    <td>2022</td>
1662    <td>Ekesan, S. and D. M. York </td>
1663    <td>Who stole the proton? Suspect general base guanine found with a smoking gun in the pistol ribozyme.</td>
1664    <td><a href="https://www.ribocentre.org/docs/Pistol.html" target="_blank"><b>Pistol ribozyme</b></a></td>
1665    <td>new classical and combined quantum mechanical/molecular mechanical simulation of pistol ribozyme</td>
1666    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/35452066" target="_blank"><b> Org Biomol Chem.</b></a></td>
1667  </tr>
1668  <tr>
1669    <td>2010</td>
1670    <td>Eickbush, D. G. and T. H. Eickbush </td>
1671    <td>R2 retrotransposons encode a self-cleaving ribozyme for processing from an rRNA cotranscript.</td>
1672    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>R2 ribozyme</b></a></td>
1673    <td>A HDV-like ribozyme encoded by R2 retrotransposons</td>
1674    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/20421411" target="_blank"><b> Mol Cell Biol 30 (13): 3142-50.</b></a></td>
1675  </tr>
1676  <tr>
1677    <td>2011</td>
1678    <td>Ruminski, D. J., C. T. Webb, N. J. Riccitelli and A. Luptak </td>
1679    <td>Processing and translation initiation of non-long terminal repeat retrotransposons by hepatitis delta virus (HDV)-like self-cleaving ribozymes.</td>
1680    <td><a href="https://www.ribocentre.org/docs/HDV-like.html" target="_blank"><b>RT-associated ribozymes</b></a></td>
1681    <td>
1681More retrotransposons encode HDV-like ribozymes</td>
1682    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21994949" target="_blank"><b> J Biol Chem 286 (48): 41286-41295.</b></a></td>
1683  </tr>
1684  <tr>
1685    <td>2014</td>
1686    <td>Liu, Y., T. J. Wilson, S. A. McPhee and D. M. Lilley </td>
1687    <td>Crystal structure and mechanistic investigation of the twister ribozyme.</td>
1688    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1689    <td>Crystal structure of P1-type </td>
1690    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25038788" target="_blank"><b> Nat Chem Biol 10(9): 739-44.</b></a></td>
1691  </tr>
1692  <tr>
1693    <td>2014</td>
1694    <td>Eiler, D., J. Wang and T. A. Steitz </td>
1695    <td>Structural basis for the fast self-cleavage reaction catalyzed by the twister ribozyme.</td>
1696    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1697    <td>Crystal structure of P3-type </td>
1698    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25157168" target="_blank"><b> Proc Natl Acad Sci U S A 111(36): 13028-33.</b></a></td>
1699  </tr>
1700  <tr>
1701    <td>2014</td>
1702    <td>Ren, A., M. Kosutic, K. R. Rajashankar, M. Frener, T. Santner, E. Westhof, R. Micura and D. J. Patel </td>
1703    <td>In-line alignment and Mg(2)(+) coordination at the cleavage site of the env22 twister ribozyme.</td>
1704    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1705    <td>Crystal structure of P1-type </td>
1706    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25410397" target="_blank"><b> Nat Commun 5: 5534.</b></a></td>
1707  </tr>
1708  <tr>
1709    <td>2015</td>
1710    <td>Kosutic, M., S. Neuner, A. Ren, S. Flur, C. Wunderlich, E. Mairhofer, N. Vusurovic, J. Seikowski, K. Breuker, C. Hobartner, D. J. Patel, C. Kreutz and R. Micura </td>
1711    <td>A Mini-Twister Variant and Impact of Residues/Cations on the Phosphodiester Cleavage of this Ribozyme Class.</td>
1712    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1713    <td>Catalytic mechanism of Mini-Twister Variant</td>
1714    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26473980" target="_blank"><b> Angew Chem Int Ed Engl 54(50): 15128-15133.</b></a></td>
1715  </tr>
1716  <tr>
1717    <td>2016</td>
1718    <td>Wilson, T. J., Y. Liu, C. Domnick, S. Kath-Schorr and D. M. Lilley </td>
1719    <td>The Novel Chemical Mechanism of the Twister Ribozyme.</td>
1720    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1721    <td>Novel chemical Mechanism</td>
1722    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27153229" target="_blank"><b> J Am Chem Soc 138(19): 6151-62.</b></a></td>
1723  </tr>
1724  <tr>
1725    <td>2016</td>
1726    <td>Kobori, S. and Y. Yokobayashi </td>
1727    <td>High-Throughput Mutational Analysis of a Twister Ribozyme.</td>
1728    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1729    <td>High-Throughput Mutational Analysis of a Twister Ribozyme</td>
1730    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27461281" target="_blank"><b> Angew Chem Int Ed Engl 55(35): 10354-7.</b></a></td>
1731  </tr>
1732  <tr>
1733    <td>2017</td>
1734    <td>Vusurovic, N., Altman, R. B., Terry, D. S., Micura, R. &amp; Blanchard, S. C.</td>
1735    <td>Pseudoknot Formation Seeds the Twister Ribozyme Cleavage Reaction Coordinate.</td>
1736    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1737    <td>The role of pseudokno</td>
1738    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28598157" target="_blank"><b> J Am Chem Soc 139 (24): 8186-8193.</b></a></td>
1739  </tr>
1740  <tr>
1741    <td>2017</td>
1742    <td>Panja, S., B. Hua, D. Zegarra, T. Ha and S. A. Woodson </td>
1743    <td>Metals induce transient folding and activation of the twister ribozyme.</td>
1744    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1745    <td>Metals induce transient folding and activation of the twister ribozyme</td>
1746    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28825710" target="_blank"><b> Nat Chem Biol 13(10): 1109-1114.</b></a></td>
1747  </tr>
1748  <tr>
1749    <td>2018</td>
1750    <td>Messina, K. J. and P. C. Bevilacqua </td>
1751    <td>Cellular Small Molecules Contribute to Twister Ribozyme Catalysis.</td>
1752    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1753    <td>Cellular Small Molecules Contribute to Twister Ribozyme Catalysis</td>
1754    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30102530" target="_blank"><b> J Am Chem Soc 140(33): 10578-10582.</b></a></td>
1755  </tr>
1756  <tr>
1757    <td>2019</td>
1758    <td>Gaines, C. S., T. J. Giese and D. M. York </td>
1759    <td>Cleaning Up Mechanistic Debris Generated by Twister Ribozymes Using Computational RNA Enzymology.</td>
1760    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1761    <td>Cleaning Up Mechanistic Debris Generated by Twister Ribozymes Using Computational RNA Enzymology</td>
1762    <td>
1762<a href="https://www.ncbi.nlm.nih.gov/pubmed/31328021" target="_blank"><b> ACS Catal 9(7): 5803-5815.</b></a></td>
1763  </tr>
1764  <tr>
1765    <td>2019</td>
1766    <td>Lilley, D. </td>
1767    <td>Classification of the nucleolytic ribozymes based upon catalytic mechanism.</td>
1768    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1769    <td>Classification of the nucleolytic ribozymes based upon catalytic mechanism</td>
1770    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31489181" target="_blank"><b> F1000Res 8.</b></a></td>
1771  </tr>
1772  <tr>
1773    <td>2019</td>
1774    <td>Litke, J. L. and S. R. Jaffrey </td>
1775    <td>Highly efficient expression of circular RNA aptamers in cells using autocatalytic transcripts.</td>
1776    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1777    <td>Application for highly efficient express circular RNA aptamers </td>
1778    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30962542" target="_blank"><b> Nat Biotechnol 37(6): 667-675.</b></a></td>
1779  </tr>
1780  <tr>
1781    <td>2020</td>
1782    <td>Korman, A., H. Sun, B. Hua, H. Yang, J. N. Capilato, R. Paul, S. Panja, T. Ha, M. M. Greenberg and S. A. Woodson </td>
1783    <td>Light-controlled twister ribozyme with single-molecule detection resolves RNA function in time and space.</td>
1784    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1785    <td>Application for RNA function detection</td>
1786    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32430319" target="_blank"><b> Proc Natl Acad Sci U S A 117(22): 12080-12086.</b></a></td>
1787  </tr>
1788  <tr>
1789    <td>2014</td>
1790    <td>Roth, A., Z. Weinberg, A. G. Chen, P. B. Kim, T. D. Ames and R. R. Breaker </td>
1791    <td>A widespread self-cleaving ribozyme class is revealed by bioinformatics.</td>
1792    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1793    <td>Discovery, Secondary structure</td>
1794    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/24240507" target="_blank"><b> Nat Chem Biol 10(1): 56-60.</b></a></td>
1795  </tr>
1796  <tr>
1797    <td>2016</td>
1798    <td>Felletti, M., J. Stifel, L. A. Wurmthaler, S. Geiger and J. S. Hartig </td>
1799    <td>Twister ribozymes as highly versatile expression platforms for artificial riboswitches.</td>
1800    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1801    <td>Application:Twister ribozymes as highly versatile expression platforms for artificial riboswitches</td>
1802    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27670347" target="_blank"><b> Nat Commun 7: 12834.</b></a></td>
1803  </tr>
1804  <tr>
1805    <td>2016</td>
1806    <td>Gaines, C. S. and D. M. York </td>
1807    <td>Ribozyme Catalysis with a Twist: Active State of the Twister Ribozyme in Solution Predicted from Molecular Simulation.</td>
1808    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1809    <td>Active State of the Twister Ribozyme in Solution Predicted from Molecular Simulation</td>
1810    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26859432" target="_blank"><b> J Am Chem Soc 138(9): 3058-65.</b></a></td>
1811  </tr>
1812  <tr>
1813    <td>2017</td>
1814    <td>Gebetsberger, J. &amp; Micura, R.</td>
1815    <td>Unwinding the twister ribozyme: from structure to mechanism.</td>
1816    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1817    <td>Chemical Mechanism</td>
1818    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27863022" target="_blank"><b> Wiley Interdiscip Rev RNA 8 (3).</b></a></td>
1819  </tr>
1820  <tr>
1821    <td>2017</td>
1822    <td>Breaker, R. R. </td>
1823    <td>Mechanistic Debris Generated by Twister Ribozymes.</td>
1824    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1825    <td>Mechanistic Debris Generated by Twister Ribozymes</td>
1826    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28191925" target="_blank"><b> ACS Chem Biol 12(4): 886-891.</b></a></td>
1827  </tr>
1828  <tr>
1829    <td>2021</td>
1830    <td>Liu, G., H. Jiang, W. Sun, J. Zhang, D. Chen and A. Murchie </td>
1831    <td>The function of twister ribozyme variants in non-LTR retrotransposition in Sc
1831histosoma mansoni.</td>
1832    <td><a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><b>twister ribozyme</b></a></td>
1833    <td>The function of twister ribozyme variants in non-LTR retrotransposition</td>
1834    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/34551436" target="_blank"><b> Nucleic Acids Res 49(18): 10573-10588.</b></a></td>
1835  </tr>
1836  <tr>
1837    <td>2017</td>
1838    <td>Liu, Y., T. J. Wilson and D. Lilley </td>
1839    <td>The structure of a nucleolytic ribozyme that employs a catalytic metal ion.</td>
1840    <td><a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><b>twister-sister ribozyme</b></a></td>
1841    <td>Three-way junctional pre-catalytic structure </td>
1842    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28263963" target="_blank"><b> Nat Chem Biol 13(5): 508-513.</b></a></td>
1843  </tr>
1844  <tr>
1845    <td>2017</td>
1846    <td>Zheng, L., E. Mairhofer, M. Teplova, Y. Zhang, J. Ma, D. J. Patel, R. Micura and A. Ren </td>
1847    <td>Structure-based insights into self-cleavage by a four-way junctional twister-sister ribozyme.</td>
1848    <td><a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><b>twister-sister ribozyme</b></a></td>
1849    <td>Four-way junctional pre-catalytic structure </td>
1850    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29081514" target="_blank"><b> Nat Commun 8(1): 1180.</b></a></td>
1851  </tr>
1852  <tr>
1853    <td>2017</td>
1854    <td>Gaines, C. S. and D. M. York </td>
1855    <td>Model for the Functional Active State of the TS Ribozyme from Molecular Simulation.</td>
1856    <td><a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><b>twister-sister ribozyme</b></a></td>
1857    <td>Model for the Functional Active State of the TS Ribozyme</td>
1858    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28763583" target="_blank"><b> Angew Chem Int Ed Engl 56(43): 13392-13395.</b></a></td>
1859  </tr>
1860  <tr>
1861    <td>2019</td>
1862    <td>Lilley, D. </td>
1863    <td>Classification of the nucleolytic ribozymes based upon catalytic mechanism.</td>
1864    <td><a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><b>twister-sister ribozyme</b></a></td>
1865    <td>Classification of the nucleolytic ribozymes based upon catalytic mechanism</td>
1866    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31489181" target="_blank"><b> F1000Res 8.</b></a></td>
1867  </tr>
1868  <tr>
1869    <td>2019</td>
1870    <td>You, M., J. L. Litke, R. Wu and S. R. Jaffrey </td>
1871    <td>Detection of Low-Abundance Metabolites in Live Cells Using an RNA Integrator.</td>
1872    <td><a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><b>twister-sister ribozyme</b></a></td>
1873    <td>Application:twister sister ribozyme is used to detect Low-Abundance Mrtabolites</td>
1874    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30773480" target="_blank"><b> Cell Chem Biol 26(4): 471-481.e3.</b></a></td>
1875  </tr>
1876  <tr>
1877    <td>2020</td>
1878    <td>Micura, R. and C. Hobartner </td>
1879    <td>Fundamental studies of functional nucleic acids: aptamers, riboswitches, ribozymes and DNAzymes.</td>
1880    <td><a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><b>twister-sister ribozyme</b></a></td>
1881    <td>Review about functional nucleic acids<br /> &nbsp;&nbsp;</td>
1882    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32944725" target="_blank"><b> Chem Soc Rev 49(20): 7331-7353.</b></a></td>
1883  </tr>
1884  <tr>
1885    <td>2015</td>
1886    <td>Weinberg, Z., P. B. Kim, T. H. Chen, S. Li, K. A. Harris, C. E. Lunse and R. R. Breaker </td>
1887    <td>New classes of self-cleaving ribozymes revealed by comparative genomics analysis.</td>
1888    <td><a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><b>twister-sister ribozyme</b></a></td>
1889    <td>Discovery, Secondary structure</td>
1890    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26167874" target="_blank"><b> Nat Chem Biol 11(8): 606-10.</b></a></td>
1891  </tr>
1892  <tr>
1893    <td>2017</td>
1894    <td>Ren, A., R. Micura and D. J. Patel </td>
1895    <td>Structure-based mechanistic insights into catalysis by small self-cleaving ribozymes.</td>
1896    <td><a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><b>twister-sister ribozyme</b></a></td>
1897    <td>Structure-based mechanistic</td>
1898    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29107885" target="_blank"><b> Curr Opin Chem Biol 41: 71-83.</b></a></td>
1899  </tr>
1900  <tr>
1901    <td>2008</td>
1902    <td>Kolev, N. G., E. I. Hartland and P. W. Huber </td>
1903    <td>
1903A manganese-dependent ribozyme in the 3'-untranslated region of Xenopus Vg1 mRNA.</td>
1904    <td><a href="https://www.ribocentre.org/docs/Vg1.html" target="_blank"><b>Vg1 ribozyme</b></a></td>
1905    <td>Discovery that manganese-dependent ribozyme occurs naturally in the 3'-UTR of Vg1 and beta-actin mRNAs</td>
1906    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/18753150" target="_blank"><b> Nucleic Acids Res 36(17): 5530-5539.</b></a></td>
1907  </tr>
1908  <tr>
1909    <td>1990</td>
1910    <td>Saville, B. J. and R. A. Collins </td>
1911    <td>A site-specific self-cleavage reaction performed by a novel RNA in neurospora mitochondria.</td>
1912    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1913    <td>discovery</td>
1914    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/2160856" target="_blank"><b> Cell 61(4): 685-696.</b></a></td>
1915  </tr>
1916  <tr>
1917    <td>1995</td>
1918    <td>Beattie, T. L., J. E. Olive and R. A. Collins </td>
1919    <td>A secondary-structure model for the self-cleaving region of Neurospora VS RNA.</td>
1920    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1921    <td>secondary structure</td>
1922    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7753865" target="_blank"><b> Proc Natl Acad Sci U S A 92(10): 4686-4690.</b></a></td>
1923  </tr>
1924  <tr>
1925    <td>2001</td>
1926    <td>D.A. Lafontaine, D.G. Norman and D.M.J. Lilley  </td>
1927    <td>Structure, folding and activity of the VS ribozyme : Importance of the 2-3-6 helical junction  </td>
1928    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1929    <td>Importance of the 2-3-6 helical junction</td>
1930    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11250907" target="_blank"><b>EMBO J. 20 1415-1424 </b></a></td>
1931  </tr>
1932  <tr>
1933    <td>2001</td>
1934    <td>Lafontaine, D. A., T. J. Wilson, D. G. Norman and D. M. Lilley </td>
1935    <td>The A730 loop is an important component of the active site of the VS ribozyme.</td>
1936    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1937    <td>A730 loop is important</td>
1938    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11575922" target="_blank"><b> J Mol Biol 312(4): 663-674.</b></a></td>
1939  </tr>
1940  <tr>
1941    <td>2001</td>
1942    <td>Flinders, J. and T. Dieckmann </td>
1943    <td>A pH controlled conformational switch in the cleavage site of the VS ribozyme substrate RNA.</td>
1944    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1945    <td>NMR structure of the isolated substrate helix</td>
1946    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11350168" target="_blank"><b> J Mol Biol 308(4): 665-679.</b></a></td>
1947  </tr>
1948  <tr>
1949    <td>2002</td>
1950    <td>D.A. Lafontaine, D.G. Norman and D. M.J. Lilley </td>
1951    <td>The global structure of the VS ribozyme. </td>
1952    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1953    <td>The global structure of the VS ribozyme</td>
1954    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/12006498" target="_blank"><b>EMBO J. 21, 2461-2471 </b></a></td>
1955  </tr>
1956  <tr>
1957    <td>2002</td>
1958    <td>Lafontaine, D. A., T. J. Wilson, Z.-Y. Zhao and D. M. J. Lilley </td>
1959    <td>Functional Group Requirements in the Probable Active Site of the VS Ribozyme.</td>
1960    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1961    <td>A756 is critical for catalysis</td>
1962    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/12368096" target="_blank"><b> Journal of Molecular Biology 323(1): 23-34.</b></a></td>
1963  </tr>
1964  <tr>
1965    <td>2005</td>
1966    <td>Campbell, D. O. and P. Legault </td>
1967    <td>Nuclear magnetic resonance structure of the Varkud satellite ribozyme stem-loop V RNA and magnesium-ion binding from chemical-shift mapping.</td>
1968    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1969    <td>NMR structure of SL5</td>
1970    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/15766243" target="_blank"><b>
1970 Biochemistry 44(11): 4157-4170.</b></a></td>
1971  </tr>
1972  <tr>
1973    <td>2007</td>
1974    <td>Wilson, T. J., A. C. McLeod and D. M. Lilley </td>
1975    <td>A guanine nucleobase important for catalysis by the VS ribozyme.</td>
1976    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1977    <td>G638 is critical for catalysis</td>
1978    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/17464286" target="_blank"><b> EMBO J 26(10): 2489-2500.</b></a></td>
1979  </tr>
1980  <tr>
1981    <td>2008</td>
1982    <td>Lipfert, J., J. Ouellet, D. G. Norman, S. Doniach and D. M. Lilley </td>
1983    <td>The complete VS ribozyme in solution studied by small-angle X-ray scattering.</td>
1984    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1985    <td>SAXS-deriverd structure</td>
1986    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/18786398" target="_blank"><b> Structure 16(9): 1357-1367.</b></a></td>
1987  </tr>
1988  <tr>
1989    <td>2009</td>
1990    <td>J. Ouellet, M. Byrne and D. M. J. Lilley  </td>
1991    <td>Formation of an active site in trans by interaction of two complete Varkud Satellite ribozymes</td>
1992    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
1993    <td>The soixante-neuf experiment</td>
1994    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/19703941" target="_blank"><b>RNA 15, 1822-1826 </b></a></td>
1995  </tr>
1996  <tr>
1997    <td>2010</td>
1998    <td>Wilson, T. J., N. S. Li, J. Lu, J. K. Frederiksen, J. A. Piccirilli and D. M. Lilley </td>
1999    <td>Nucleobase-mediated general acid-base catalysis in the Varkud satellite ribozyme.</td>
2000    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
2001    <td>catalytic mechanism</td>
2002    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/20547881" target="_blank"><b> Proc Natl Acad Sci U S A 107(26): 11751-11756.</b></a></td>
2003  </tr>
2004  <tr>
2005    <td>2011</td>
2006    <td>T. J. Wilson and D. M. J. Lilley. </td>
2007    <td>Do the hairpin and VS ribozymes share a common catalytic mechanism based on general acid-base catalysis ? A critical assessment of available experimental data. </td>
2008    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
2009    <td>Detailed discussion of the chemical mechanism</td>
2010    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21173201" target="_blank"><b>RNA 17, 213-221 </b></a></td>
2011  </tr>
2012  <tr>
2013    <td>2011</td>
2014    <td>Desjardins, G., E. Bonneau, N. Girard, J. Boisbouvier and P. Legault </td>
2015    <td>NMR structure of the A730 loop of the Neurospora VS ribozyme: insights into the formation of the active site.</td>
2016    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
2017    <td>NMR structure of A730 loop</td>
2018    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21266483" target="_blank"><b> Nucleic Acids Res 39(10): 4427-4437.</b></a></td>
2019  </tr>
2020  <tr>
2021    <td>2014</td>
2022    <td>Bonneau, E. and P. Legault </td>
2023    <td>Nuclear magnetic resonance structure of the III-IV-V three-way junction from the Varkud satellite ribozyme and identification of magnesium-binding sites using paramagnetic relaxation enhancement.</td>
2024    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
2025    <td>NMR structure of the III-IV-V three-way junction</td>
2026    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25238589" target="_blank"><b> Biochemistry 53(39): 6264-6275.</b></a></td>
2027  </tr>
2028  <tr>
2029    <td>2015</td>
2030    <td>Bonneau, E., N. Girard, S. Lemieux and P. Legault </td>
2031    <td>The NMR structure of the II-III-VI three-way junction from the Neurospora VS ribozyme reveals a critical tertiary interaction and provides new insights into the global ribozyme structure.</td>
2032    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
2033    <td>NMR structure of the II-III-VI three-way junction</td>
2034    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26124200" target="_blank"><b> RNA 21(9): 1621-1632.</b></a></td>
2035  </tr>
2036  <tr>
2037    <td>2015</td>
2038    <td>Suslov, N. B., S. DasGupta, H. Huang, J. R. Fuller, D. M. Lilley, P. A. Rice and J. A. Piccirilli </td>
2039    <td>Crystal structure of the Varkud satellite ribozyme.</td>
2040    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
2041    <td>Crystal structure</td>
2042    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26414446" target="_blank"><b> Nat Chem Biol 11(11): 840-846.</b></a></td>
2043  </tr>
2044  <tr>
2045    <td>2017</td>
2046    <td>
2046DasGupta, S., N. B. Suslov and J. A. Piccirilli </td>
2047    <td>Structural Basis for Substrate Helix Remodeling and Cleavage Loop Activation in the Varkud Satellite Ribozyme.</td>
2048    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
2049    <td>Crystal structure</td>
2050    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28625058" target="_blank"><b> J Am Chem Soc 139(28): 9591-9597.</b></a></td>
2051  </tr>
2052  <tr>
2053    <td>2020</td>
2054    <td>Ganguly, A., B. P. Weissman, T. J. Giese, N. S. Li, S. Hoshika, S. Rao, S. A. Benner, J. A. Piccirilli and D. M. York </td>
2055    <td>Confluence of theory and experiment reveals the catalytic mechanism of the Varkud satellite ribozyme.</td>
2056    <td><a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><b>VS ribozyme</b></a></td>
2057    <td>Additional experiments to summarize the structure and function of VS ribozyme</td>
2058    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31959957" target="_blank"><b> Nat Chem 12(2): 193-201.</b></a></td>
2059  </tr>
2060  <tr>
2061    <td>1977</td>
2062    <td>Chow, L. T., R. E. Gelinas, T. R. Broker and R. J. Roberts </td>
2063    <td>An amazing sequence arrangement at the 5′ ends of adenovirus 2 messenger RNA.</td>
2064    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2065    <td>Splicing phenomenon found</td>
2066    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/902310" target="_blank"><b> Cell 12(1): 1-8.</b></a></td>
2067  </tr>
2068  <tr>
2069    <td>1983</td>
2070    <td>Mount, S. M., I. Pettersson, M. Hinterberger, A. Karmas and J. A. Steitz </td>
2071    <td>The U1 small nuclear RNA-protein complex selectively binds a 5' splice site in vitro.</td>
2072    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2073    <td>First isolation of spliceosome subunits</td>
2074    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/6190573" target="_blank"><b> Cell 33(2): 509-518.</b></a></td>
2075  </tr>
2076  <tr>
2077    <td>1985</td>
2078    <td>Frendewey, D. and W. Keller </td>
2079    <td>Stepwise assembly of a pre-mRNA splicing complex requires U-snRNPs and specific intron sequences.</td>
2080    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2081    <td>In vitro splicing experiment</td>
2082    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/3160483" target="_blank"><b> Cell 42(1): 355-367.</b></a></td>
2083  </tr>
2084  <tr>
2085    <td>1985</td>
2086    <td>Grabowski, P., S. Seiler and P. Sharp </td>
2087    <td>A multicomponent complex is involved in the splicing of messenger RNA precursors.</td>
2088    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2089    <td>In vitro splicing experiment</td>
2090    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/3160482" target="_blank"><b> Cell 42(1): 345-353.</b></a></td>
2091  </tr>
2092  <tr>
2093    <td>1992</td>
2094    <td>Madhani, H. D. and C. Guthrie </td>
2095    <td>A novel base-pairing interaction between U2 and U6 snRNAs suggests a mechanism for the catalytic activation of the spliceosome.</td>
2096    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2097    <td>Demonstrate a conserved base-pairing interaction between the U6 and U2 snRNAs that is mutually exclusive with the U4-U6 interaction</td>
2098    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/1423631" target="_blank"><b> Cell 71(5): 803-817.</b></a></td>
2099  </tr>
2100  <tr>
2101    <td>1993</td>
2102    <td>Steitz, T. A. and J. A. Steitz </td>
2103    <td>A general two-metal-ion mechanism for catalytic RNA.</td>
2104    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2105    <td>Proposed that the two phosphotransesterifications of splicing are catalyzed by a two-metal mechanism</td>
2106    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8341661" target="_blank"><b> Proc Natl Acad Sci U S A 90(14): 6498-6502.</b></a></td>
2107  </tr>
2108  <tr>
2109    <td>1997</td>
2110    <td>Sontheimer, E. J., S. Sun and J. A. Piccirilli </td>
2111    <td>Metal ion catalysis during splicing of premessenger RNA.</td>
2112    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>
2112Spliceosome</b></a></td>
2113    <td>Divalent metals stabilize the leaving group during each step of splicing</td>
2114    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9285595" target="_blank"><b> Nature 388(6644): 801-805.</b></a></td>
2115  </tr>
2116  <tr>
2117    <td>2000</td>
2118    <td>Yean, S. L., G. Wuenschell, J. Termini and R. J. Lin </td>
2119    <td>Metal-ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome.</td>
2120    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2121    <td>Metal-ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome</td>
2122    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11130730" target="_blank"><b> Nature 408(6814): 881-884.</b></a></td>
2123  </tr>
2124  <tr>
2125    <td>2001</td>
2126    <td>Valadkhan, S. and J. L. Manley </td>
2127    <td>Splicing-related catalysis by protein-free snRNAs.</td>
2128    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2129    <td>U2 and U6 can base-pair and fold in vitro into a structure that catalyzes reactions similar to the two steps of pre-mRNA splicing</td>
2130    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11607023" target="_blank"><b> Nature 413(6857): 701-707.</b></a></td>
2131  </tr>
2132  <tr>
2133    <td>2009</td>
2134    <td>Mefford, M. A. and J. P. Staley </td>
2135    <td>Evidence that U2/U6 helix I promotes both catalytic steps of pre-mRNA splicing and rearranges in between these steps.</td>
2136    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2137    <td>U2/U6 helix I promotes both catalytic steps of pre-mRNA splicing and rearranges in between these steps</td>
2138    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/19458033" target="_blank"><b> RNA 15(7): 1386-1397.</b></a></td>
2139  </tr>
2140  <tr>
2141    <td>2013</td>
2142    <td>Galej, W. P., C. Oubridge, A. J. Newman and K. Nagai </td>
2143    <td>Crystal structure of Prp8 reveals active site cavity of the spliceosome.</td>
2144    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2145    <td>provides crucial insights into the architecture of the spliceosome active site, and reinforces the notion that nuclear pre-mRNA splicing and group II intron splicing have a common origin.</td>
2146    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/23354046" target="_blank"><b> Nature 493(7434): 638-643.</b></a></td>
2147  </tr>
2148  <tr>
2149    <td>2013</td>
2150    <td>Fica, S. M., N. Tuttle, T. Novak, N. S. Li, J. Lu, P. Koodathingal, Q. Dai, J. P. Staley and J. A. Piccirilli </td>
2151    <td>RNA catalyses nuclear pre-mRNA splicing.</td>
2152    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2153    <td>Demonstrate that RNA mediates catalysis within the spliceosome.</td>
2154    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/ 24196718" target="_blank"><b> Nature 503(7475): 229-234.</b></a></td>
2155  </tr>
2156  <tr>
2157    <td>2015</td>
2158    <td>Yan, C., J. Hang, R. Wan, M. Huang, C. C. Wong and Y. Shi </td>
2159    <td>Structure of a yeast spliceosome at 3.6-angstrom resolution.</td>
2160    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2161    <td>S.p ILS, 3.6 Å<br /> &nbsp;&nbsp;The first atomic structure of the intact spliceosome</td>
2162    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26292707" target="_blank"><b> Science 349(6253): 1182-1191.</b></a></td>
2163  </tr>
2164  <tr>
2165    <td>2016</td>
2166    <td>Galej, W. P., M. E. Wilkinson, S. M. Fica, C. Oubridge, A. J. Newman and K. Nagai </td>
2167    <td>Cryo-EM structure of the spliceosome immediately after branching.</td>
2168    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2169    <td>The resolution of tri-snRNP, a complex during splice assembly, was increased to 5.9 angstroms</td>
2170    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27459055" target="_blank"><b> Nature 537(7619): 197-201.</b></a></td>
2171  </tr>
2172  <tr>
2173    <td>2016</td>
2174    <td>Wan, R., C. Yan, R. Bai, G. Huang and Y. Shi </td>
2175    <td>Structure of a yeast catalytic step I spliceosome at 3.4 A resolution.</td>
2176    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>
2176Spliceosome</b></a></td>
2177    <td>S.c C, 3.4 Å<br /> &nbsp;&nbsp;Active site after branching</td>
2178    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27445308" target="_blank"><b> Science 353(6302): 895-904.</b></a></td>
2179  </tr>
2180  <tr>
2181    <td>2016</td>
2182    <td>Wan, R., C. Yan, R. Bai, L. Wang, M. Huang, C. C. Wong and Y. Shi </td>
2183    <td>The 3.8 A structure of the U4/U6.U5 tri-snRNP: Insights into spliceosome assembly and catalysis.</td>
2184    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2185    <td>U4/U6.U5 tri-snRNP,3.8Å</td>
2186    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/26743623" target="_blank"><b> Science 351(6272): 466-475.</b></a></td>
2187  </tr>
2188  <tr>
2189    <td>2016</td>
2190    <td>Yan, C., R. Wan, R. Bai, G. Huang and Y. Shi </td>
2191    <td>Structure of a yeast activated spliceosome at 3.5 A resolution.</td>
2192    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2193    <td>B act , 3.5 Å<br /> &nbsp;&nbsp;Catalytic center is formed</td>
2194    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27445306" target="_blank"><b> Science 353(6302): 904-911.</b></a></td>
2195  </tr>
2196  <tr>
2197    <td>2017</td>
2198    <td>Yan, C., R. Wan, R. Bai, G. Huang and Y. Shi </td>
2199    <td>Structure of a yeast step II catalytically activated spliceosome.</td>
2200    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2201    <td>S.c C*, 4.0 Å</td>
2202    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27980089" target="_blank"><b> Science 355(6321): 149-155.</b></a></td>
2203  </tr>
2204  <tr>
2205    <td>2017</td>
2206    <td>Fica, S. M., C. Oubridge, W. P. Galej, M. E. Wilkinson, X. C. Bai, A. J. Newman and K. Nagai </td>
2207    <td>Structure of a spliceosome remodelled for exon ligation.</td>
2208    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2209    <td>S.c C*, 3.8 Å</td>
2210    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28076345" target="_blank"><b> Nature 542(7641): 377-380.</b></a></td>
2211  </tr>
2212  <tr>
2213    <td>2017</td>
2214    <td>Plaschka, C., P. C. Lin and K. Nagai </td>
2215    <td>Structure of a pre-catalytic spliceosome.</td>
2216    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2217    <td>S.c B, 7.2 (3.7) Å<br /> &nbsp;&nbsp;</td>
2218    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28530653" target="_blank"><b> Nature 546(7660): 617-621.</b></a></td>
2219  </tr>
2220  <tr>
2221    <td>2017</td>
2222    <td>Wan, R., C. Yan, R. Bai, J. Lei and Y. Shi </td>
2223    <td>Structure of an Intron Lariat Spliceosome from Saccharomyces cerevisiae.</td>
2224    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2225    <td>S.c ILS, 3.5 Å</td>
2226    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28919079" target="_blank"><b> Cell 171(1): 120-132 e112.</b></a></td>
2227  </tr>
2228  <tr>
2229    <td>2017</td>
2230    <td>Liu, S., X. Li, L. Zhang, J. Jiang, R. C. Hill, Y. Cui, K. C. Hansen, Z. H. Zhou and R. Zhao </td>
2231    <td>Structure of the yeast spliceosomal postcatalytic P complex.</td>
2232    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2233    <td>S.c P, 3.3 Å</td>
2234    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29146870" target="_blank"><b> Science 358(6368): 1278-1283.</b></a></td>
2235  </tr>
2236  <tr>
2237    <td>2017</td>
2238    <td>Bai, R., C. Yan, R. Wan, J. Lei and Y. Shi </td>
2239    <td>Structure of the Post-catalytic Spliceosome from Saccharomyces cerevisiae.</td>
2240    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2241    <td> &nbsp;&nbsp;S.c P, 3.6 Å</td>
2242    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29153833" target="_blank"><b> Cell 171(7): 1589-1598 e1588.</b></a></td>
2243  </tr>
2244  <tr>
2245    <td>2017</td>
2246    <td>Bertram, K., D. E. Agafonov, O. Dybkov, D. Haselbach, M. N. Leelaram, C. L. Will, H. Urlaub, B. Kastner, R. Luhrmann and H. Stark </td>
2247    <td>Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.</td>
2248    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>
2248Spliceosome</b></a></td>
2249    <td>C*, 5.9 Å<br /> &nbsp;&nbsp;</td>
2250    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28781166" target="_blank"><b> Cell 170(4): 701-713 e711.</b></a></td>
2251  </tr>
2252  <tr>
2253    <td>2017</td>
2254    <td>Zhang, X., C. Yan, J. Hang, L. I. Finci, J. Lei and Y. Shi </td>
2255    <td>An Atomic Structure of the Human Spliceosome.</td>
2256    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2257    <td>C*, 3.8 Å<br /> &nbsp;&nbsp; The first atomic model of human spliceosom</td>
2258    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28502770" target="_blank"><b> Cell 169(5): 918-929 e914.</b></a></td>
2259  </tr>
2260  <tr>
2261    <td>2017</td>
2262    <td>Bertram, K., D. E. Agafonov, W. T. Liu, O. Dybkov, C. L. Will, K. Hartmuth, H. Urlaub, B. Kastner, H. Stark and R. Luhrmann </td>
2263    <td>Cryo-EM structure of a human spliceosome activated for step 2 of splicing.</td>
2264    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2265    <td>B, 9.9 (4.5) Å<br /> &nbsp;&nbsp;</td>
2266    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28076346" target="_blank"><b> Nature 542(7641): 318-323.</b></a></td>
2267  </tr>
2268  <tr>
2269    <td>2018</td>
2270    <td>Bai, R., R. Wan, C. Yan, J. Lei and Y. Shi </td>
2271    <td>Structures of the fully assembled Saccharomyces cerevisiae spliceosome before activation.</td>
2272    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2273    <td>S.c pre–B, 3.3–4.6 Å<br /> &nbsp;&nbsp;S.c B, 3.9 Å</td>
2274    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29794219" target="_blank"><b> Science 360(6396): 1423-1429.</b></a></td>
2275  </tr>
2276  <tr>
2277    <td>2018</td>
2278    <td>Plaschka, C., P. C. Lin, C. Charenton and K. Nagai </td>
2279    <td>Prespliceosome structure provides insights into spliceosome assembly and regulation.</td>
2280    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2281    <td>S.c A, 4.9 (4.0) Å</td>
2282    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29995849" target="_blank"><b> Nature 559(7714): 419-422.</b></a></td>
2283  </tr>
2284  <tr>
2285    <td>2018</td>
2286    <td>Zhan, X., C. Yan, X. Zhang, J. Lei and Y. Shi </td>
2287    <td>Structure of a human catalytic step I spliceosome.</td>
2288    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2289    <td> C, 4.1 Å<br /> &nbsp;&nbsp;</td>
2290    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29301961" target="_blank"><b> Science 359(6375): 537-545.</b></a></td>
2291  </tr>
2292  <tr>
2293    <td>2018</td>
2294    <td>Haselbach, D., I. Komarov, D. E. Agafonov, K. Hartmuth, B. Graf, O. Dybkov, H. Urlaub, B. Kastner, R. Luhrmann and H. Stark </td>
2295    <td>Structure and Conformational Dynamics of the Human Spliceosomal B(act) Complex.</td>
2296    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2297    <td> Bact , 3.4 Å (core)<br /> &nbsp;&nbsp;</td>
2298    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/29361316" target="_blank"><b> Cell 172(3): 454-464 e411.</b></a></td>
2299  </tr>
2300  <tr>
2301    <td>2018</td>
2302    <td>Zhan, X., C. Yan, X. Zhang, J. Lei and Y. Shi </td>
2303    <td>Structures of the human pre-catalytic spliceosome and its precursor spliceosome.</td>
2304    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2305    <td> pre–B (5.7 Å) and B (3.8 Å)</td>
2306    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30315277" target="_blank"><b> Cell Res 28(12): 1129-1140.</b></a></td>
2307  </tr>
2308  <tr>
2309    <td>2019</td>
2310    <td>Wan, R., R. Bai, C. Yan, J. Lei and Y. Shi </td>
2311    <td>Structures of the Catalytically Activated Yeast Spliceosome Reveal the Mechanism of Branching.</td>
2312    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2313    <td>S.c B*, 2.9–3.8 Å<br /> &nbsp;&nbsp;Four distinct structures on two different substrates</td>
2314    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30879786" target="_blank"><b> Cell 177(2): 339-351 e313.</b></a></td>
2315  </tr>
2316  <tr>
2317    <td>2019</td>
2318    <td>Fica, S. M., C. Oubridge, M. E. Wilkinson, A. J. Newman and K. Nagai </td>
2319    <td>A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation.</td>
2320    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>
2320Spliceosome</b></a></td>
2321    <td>P, 3.3 Å<br /> &nbsp;&nbsp;</td>
2322    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30705154" target="_blank"><b> Science 363(6428): 710-714.</b></a></td>
2323  </tr>
2324  <tr>
2325    <td>2019</td>
2326    <td>Zhang, X., X. Zhan, C. Yan, W. Zhang, D. Liu, J. Lei and Y. Shi </td>
2327    <td>Structures of the human spliceosomes before and after release of the ligated exon.</td>
2328    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2329    <td>P (3.0 Å) and ILS (2.9 Å)<br /> &nbsp;&nbsp;</td>
2330    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30728453" target="_blank"><b> Cell Res 29(4): 274-285.</b></a></td>
2331  </tr>
2332  <tr>
2333    <td>2019</td>
2334    <td>Charenton, C., M. E. Wilkinson and K. Nagai </td>
2335    <td>Mechanism of 5' splice site transfer for human spliceosome activation.</td>
2336    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2337    <td>pre–B, 3.3 Å <br /> &nbsp;&nbsp;Mechanism of 5' splice site transfer for human spliceosome activation</td>
2338    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30975767" target="_blank"><b> Science 364(6438): 362-367.</b></a></td>
2339  </tr>
2340  <tr>
2341    <td>2019</td>
2342    <td>Wan, R., R. Bai, C. Yan, J. Lei and Y. Shi </td>
2343    <td>Structures of the Catalytically Activated Yeast Spliceosome Reveal the Mechanism of Branching.</td>
2344    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2345    <td>Mechanism of Branching</td>
2346    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30879786" target="_blank"><b> Cell 177(2): 339-351 e313.</b></a></td>
2347  </tr>
2348  <tr>
2349    <td>2020</td>
2350    <td>Zhang, Z., C. L. Will, K. Bertram, O. Dybkov, K. Hartmuth, D. E. Agafonov, R. Hofele, H. Urlaub, B. Kastner, R. Luhrmann and H. Stark </td>
2351    <td>Molecular architecture of the human 17S U2 snRNP.</td>
2352    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2353    <td>The structure of 17s U2 snRNP was analyzed and a complete molecular model of 17s U2 snRNP was obtained</td>
2354    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32494006" target="_blank"><b> Nature 583(7815): 310-313.</b></a></td>
2355  </tr>
2356  <tr>
2357    <td>2020</td>
2358    <td>Townsend, C., M. N. Leelaram, D. E. Agafonov, O. Dybkov, C. L. Will, K. Bertram, H. Urlaub, B. Kastner, H. Stark and R. Luhrmann </td>
2359    <td>Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation.</td>
2360    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2361    <td>Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation</td>
2362    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/33243851" target="_blank"><b> Science 370(6523).</b></a></td>
2363  </tr>
2364  <tr>
2365    <td>2021</td>
2366    <td>Bai, R., R. Wan, C. Yan, Q. Jia, J. Lei and Y. Shi </td>
2367    <td>Mechanism of spliceosome remodeling by the ATPase/helicase Prp2 and its coactivator Spp2.</td>
2368    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2369    <td>Mechanism of spliceosome remodeling by the ATPase/helicase Prp2 and its coactivator Spp2</td>
2370    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/33243853" target="_blank"><b> Science 371(6525).</b></a></td>
2371  </tr>
2372  <tr>
2373    <td>2022</td>
2374    <td>Tholen, J., M. Razew, F. Weis and W. P. Galej </td>
2375    <td>Structural basis of branch site recognition by the human spliceosome.</td>
2376    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2377    <td>A series of high-resolution (2.0-2.2 Å) U2 snRNP structures were identified</td>
2378    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/34822310" target="_blank"><b> Science 375(6576): 50-57.</b></a></td>
2379  </tr>
2380  <tr>
2381    <td>2019</td>
2382    <td>Yan, C., R. Wan and Y. Shi </td>
2383    <td>Molecular Mechanisms of pre-mRNA Splicing through Structural Biology of the Spliceosome.</td>
2384    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>
2384Spliceosome</b></a></td>
2385    <td>Review</td>
2386    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30602541" target="_blank"><b> Cold Spring Harb Perspect Biol 11(1).</b></a></td>
2387  </tr>
2388  <tr>
2389    <td>2020</td>
2390    <td>Wan, R., R. Bai, X. Zhan and Y. Shi </td>
2391    <td>How Is Precursor Messenger RNA Spliced by the Spliceosome?</td>
2392    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2393    <td>Review</td>
2394    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31815536" target="_blank"><b> Annu Rev Biochem 89: 333-358.</b></a></td>
2395  </tr>
2396  <tr>
2397    <td>2020</td>
2398    <td>Wilkinson, M. E., C. Charenton and K. Nagai </td>
2399    <td>RNA Splicing by the Spliceosome.</td>
2400    <td><a href="https://www.ribocentre.org/docs/Spliceosome.html" target="_blank"><b>Spliceosome</b></a></td>
2401    <td>Review</td>
2402    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31794245" target="_blank"><b> Annu Rev Biochem 89: 359-388.</b></a></td>
2403  </tr>
2404  <tr>
2405    <td>1975</td>
2406    <td>Fox, G. E. and C. R. Woese </td>
2407    <td>5S RNA secondary structure.</td>
2408    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2409    <td>Secondary structure of 5S RNA</td>
2410    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/808733" target="_blank"><b> Nature 256(5517): 505-7.</b></a></td>
2411  </tr>
2412  <tr>
2413    <td>1980</td>
2414    <td>Woese, C. R., L. J. Magrum, R. Gupta, R. B. Siegel, D. A. Stahl, J. Kop, N. Crawford, J. Brosius, R. Gutell, J. J. Hogan and H. F. Noller </td>
2415    <td>Secondary structure model for bacterial 16S ribosomal RNA: phylogenetic, enzymatic and chemical evidence.</td>
2416    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2417    <td>A secondary structure model of bacterial 16S rRNA</td>
2418    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/6159576" target="_blank"><b> Nucleic Acids Res 8 (10): 2275-93.</b></a></td>
2419  </tr>
2420  <tr>
2421    <td>1981</td>
2422    <td>Noller, H. F., J. Kop, V. Wheaton, J. Brosius, R. R. Gutell, A. M. Kopylov, F. Dohme, W. Herr, D. A. Stahl, R. Gupta and C. R. Waese </td>
2423    <td>Secondary structure model for 23S ribosomal RNA.</td>
2424    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2425    <td>Construction of 23S ribosomal RNA secondary structure model by comparing sequences</td>
2426    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7031608" target="_blank"><b> Nucleic Acids Res 9 (22): 6167-89.</b></a></td>
2427  </tr>
2428  <tr>
2429    <td>1991</td>
2430    <td>von Bohlen, K., I. Makowski, H. A. Hansen, H. Bartels, Z. Berkovitch-Yellin, A. Zaytzev-Bashan, S. Meyer, C. Paulke, F. Franceschi and A. Yonath </td>
2431    <td>Characterization and preliminary attempts for derivatization of crystals of large ribosomal subunits from Haloarcula marismortui diffracting to 3 A resolution.</td>
2432    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2433    <td>Preliminary analysis of the structure of the H. marismortui ribosomal 50 S subunit</td>
2434    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/1942063" target="_blank"><b> J Mol Biol 222 (1): 11-5.</b></a></td>
2435  </tr>
2436  <tr>
2437    <td>1993</td>
2438    <td>Szewczak, A. A., P. B. Moore, Y. L. Chang and I. G. Wool </td>
2439    <td>The conformation of the sarcin/ricin loop from 28S ribosomal RNA.</td>
2440    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2441    <td>NMR structure of sarcin/ricin loop in 28s rRNA</td>
2442    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/8415744" target="_blank"><b> Proc Natl Acad Sci U S A 90 (20): 9581-5.</b></a></td>
2443  </tr>
2444  <tr>
2445    <td>1995</td>
2446    <td>Samaha, R. R., R. Green and H. F. Noller </td>
2447    <td>A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome.</td>
2448    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2449    <td>G2252 and G2251 of the 23S rRNA P-loop are important</td>
2450    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7566085" target="_blank"><b> Nature 377 (6547): 309-14.</b></a></td>
2451  </tr>
2452  <tr>
2453    <td>1995</td>
2454    <td>Frank, J., J. Zhu, P. Penczek, Y. Li, S. Srivastava, A. Verschoor, M. Radermacher, R. Grassucci, R. K. Lata and R. K. Agrawal </td>
2455    <td>A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome.</td>
2456    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2457    <td>CryoEM structure of E. coli ribosomes (25 Å)</td>
2458    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/7630422" target="_blank"><b> Nature 376 (6539): 441-4.</b></a></td>
2459  </tr>
2460  <tr>
2461    <td>1998</td>
2462    <td>Ban, N., B. Freeborn, P. Nissen, P. Penczek, R. A. Grassucci, R. Sweet, J. Frank, P. B. Moore and T. A. Steitz </td>
2463    <td>A 9 A resolution X-ray crystallographic map of the large ribosomal subunit.</td>
2464    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2465    <td>9 Å resolution electron density map of the H. marismortui ribosome 50S subunit</td>
2466    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/9657144" target="_blank"><b> Cell 93 (7): 1105-15.</b></a></td>
2467  </tr>
2468  <tr>
2469    <td>1999</td>
2470    <td>Kim, D. F. and R. Green </td>
2471    <td>Base-pairing between 23S rRNA and tRNA in the ribosomal A site.</td>
2472    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2473    <td>G2553 is important</td>
2474    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10619032" target="_blank"><b> Mol Cell 4(5): 859-64.</b></a></td>
2475  </tr>
2476  <tr>
2477    <td>1999</td>
2478    <td>Clemons, W. J., J. L. May, B. T. Wimberly, J. P. McCutcheon, M. S. Capel and V. Ramakrishnan </td>
2479    <td>Structure of a bacterial 30S ribosomal subunit at 5.5 A resolution.</td>
2480    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2481    <td>Structure of the ribosomal 30S subunit of T.thermophilus (5.5 Å)</td>
2482    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10476960" target="_blank"><b> Nature 400 (6747): 833-40.</b></a></td>
2483  </tr>
2484  <tr>
2485    <td>1999</td>
2486    <td>Tocilj, A., F. Schlunzen, D. Janell, M. Gluhmann, H. A. Hansen, J. Harms, A. Bashan, H. Bartels, I. Agmon, F. Franceschi and A. Yonath </td>
2487    <td>The small ribosomal subunit from Thermus thermophilus at 4.5 A resolution: pattern fittings and the identification of a functional site.</td>
2488    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2489    <td>Structure of the ribosomal 30S subunit of T.thermophilus (4.5 Å)</td>
2490    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10588692" target="_blank"><b> Proc Natl Acad Sci U S A 96 (25): 14252-7.</b></a></td>
2491  </tr>
2492  <tr>
2493    <td>1999</td>
2494    <td>Cate, J. H., M. M. Yusupov, G. Z. Yusupova, T. N. Earnest and H. F. Noller </td>
2495    <td>X-ray crystal structures of 70S ribosome functional complexes.</td>
2496    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2497    <td>Crystal structures of the 70S ribosome functional complex (7.8 Å)</td>
2498    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10497122" target="_blank"><b> Science 285 (5436): 2095-104.</b></a></td>
2499  </tr>
2500  <tr>
2501    <td>2000</td>
2502    <td>Ban, N., P. Nissen, J. Hansen, P. B. Moore and T. A. Steitz </td>
2503    <td>The complete atomic structure of the large ribosomal subunit at 2.4 A resolution.</td>
2504    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2505    <td>Crystal structure of the large ribosomal subunit of H. marismortui (2.4 Å)</td>
2506    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10937989" target="_blank"><b> Science 289 (5481): 905-20</b></a></td>
2507  </tr>
2508  <tr>
2509    <td>2000</td>
2510    <td>Nissen, P., J. Hansen, N. Ban, P. B. Moore and T. A. Steitz </td>
2511    <td>The structural basis of ribosome activity in peptide bond synthesis.</td>
2512    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2513    <td>The ribosome is a ribozyme </td>
2514    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10937990" target="_blank"><b> Science 289 (5481): 920-30.</b></a></td>
2515  </tr>
2516  <tr>
2517    <td>2000</td>
2518    <td>Cech, T. R. </td>
2519    <td>Structural biology. The ribosome is a ribozyme.</td>
2520    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2521    <td>The ribosome is a ribozyme </td>
2522    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10960319" target="_blank"><b> Science 289(5481): 878-9.</b></a></td>
2523  </tr>
2524  <tr>
2525    <td>2000</td>
2526    <td>Muth, G. W., L. Ortoleva-Donnelly and S. A. Strobel </td>
2527    <td>A single adenosine with a neutral pKa in the ribosomal peptidyl transferase center.</td>
2528    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2529    <td>Results are consistent with a mechanism wherein the nucleotide base of A2451 serves as a general acid base during peptide bond formation</td>
2530    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/10937997" target="_blank"><b> Science 289 (5481): 947-50.</b></a></td>
2531  </tr>
2532  <tr>
2533    <td>2000</td>
2534    <td>Schluenzen, F., A. Tocilj, R. Zarivach, J. Harms, M. Gluehmann, D. Janell, A. Bashan, H. Bartels, I. Agmon, F. Franceschi and A. Yonath </td>
2535    <td>Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution.</td>
2536    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2537    <td>Structure of the functionally activated small ribosomal subunit of Thermus thermophilus (3.3Å)</td>
2538    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11007480" target="_blank"><b> Cell 102 (5): 615-23.</b></a></td>
2539  </tr>
2540  <tr>
2541    <td>2000</td>
2542    <td>Wimberly, B. T., D. E. Brodersen, W. M. Clemons, Jr., R. J. Morgan-Warren, A. P. Carter, C. Vonrhein, T. Hartsch and V. Ramakrishnan </td>
2543    <td>Structure of the 30S ribosomal subunit.</td>
2544    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2545    <td>Crystal structure of the 30S subunit of Thermus thermophilus (3 Å)</td>
2546    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11014182" target="_blank"><b> Nature 407(6802): 327-339.</b></a></td>
2547  </tr>
2548  <tr>
2549    <td>2001</td>
2550    <td>Yusupov, M. M., G. Z. Yusupova, A. Baucom, K. Lieberman, T. N. Earnest, J. H. Cate and H. F. Noller </td>
2551    <td>Crystal structure of the ribosome at 5.5 A resolution.</td>
2552    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2553    <td>Crystal structure of the complete 70S ribosome of Thermus thermophilus (5.5 Å)</td>
2554    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/11283358" target="_blank"><b> Science 292 (5518): 883-96.</b></a></td>
2555  </tr>
2556  <tr>
2557    <td>2003</td>
2558    <td>Bashan, A., I. Agmon, R. Zarivach, F. Schluenzen, J. Harms, R. Berisio, H. Bartels, F. Franceschi, T. Auerbach, H. A. Hansen, E. Kossoy, M. Kessler and A. Yonath </td>
2559    <td>Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression.</td>
2560    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2561    <td>A2602, U2585 are important</td>
2562    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/12535524" target="_blank"><b> Mol Cell 11 (1): 91-102.</b></a></td>
2563  </tr>
2564  <tr>
2565    <td>2005</td>
2566    <td>
2566Schuwirth, B. S., M. A. Borovinskaya, C. W. Hau, W. Zhang, A. Vila-Sanjurjo, J. M. Holton and J. H. Cate </td>
2567    <td>Structures of the bacterial ribosome at 3.5 A resolution.</td>
2568    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2569    <td>Structure of the 70s ribosome of E. coli (3.5Å)</td>
2570    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/16272117" target="_blank"><b> Science 310 (5749): 827-34.</b></a></td>
2571  </tr>
2572  <tr>
2573    <td>2011</td>
2574    <td>Rabl, J., M. Leibundgut, S. F. Ataide, A. Haag and N. Ban </td>
2575    <td>Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1.</td>
2576    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2577    <td>Crystal structure of the 40S ribosomal subunit of <em>Tetrahymena</em> thermophila in complex with eIF1 (3.9 Å)</td>
2578    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/21205638" target="_blank"><b> Science 331 (6018): 730-6.</b></a></td>
2579  </tr>
2580  <tr>
2581    <td>2011</td>
2582    <td>Klinge, S., F. Voigts-Hoffmann, M. Leibundgut, S. Arpagaus and N. Ban </td>
2583    <td>Crystal structure of the eukaryotic 60S ribosomal subunit in complex with initiation factor 6.</td>
2584    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2585    <td>Crystal structure of the 60S ribosomal subunit of <em>Tetrahymena</em> thermophila in complex with eIF6 (3.5 Å)</td>
2586    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/22052974" target="_blank"><b> Science 334 (6058): 941-8.</b></a></td>
2587  </tr>
2588  <tr>
2589    <td>2011</td>
2590    <td>Ben-Shem, A., D. L. N. Garreau, S. Melnikov, L. Jenner, G. Yusupova and M. Yusupov </td>
2591    <td>The structure of the eukaryotic ribosome at 3.0 A resolution.</td>
2592    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2593    <td>Crystal structure of the yeast 80S ribosome (3.0 Å)</td>
2594    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/22096102" target="_blank"><b> Science 334 (6062): 1524-9.</b></a></td>
2595  </tr>
2596  <tr>
2597    <td>2013</td>
2598    <td>Hashem, Y., A. des Georges, J. Fu, S. N. Buss, F. Jossinet, A. Jobe, Q. Zhang, H. Y. Liao, R. A. Grassucci, C. Bajaj, E. Westhof, S. Madison-Antenucci and J. Frank </td>
2599    <td>High-resolution cryo-electron microscopy structure of the Trypanosoma brucei ribosome.</td>
2600    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2601    <td>High-resolution Cryo EM structure of the Trypanosoma brucei ribosome</td>
2602    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/23395961" target="_blank"><b> Nature 494 (7437): 385-9.</b></a></td>
2603  </tr>
2604  <tr>
2605    <td>2014</td>
2606    <td>Wong, W., X. C. Bai, A. Brown, I. S. Fernandez, E. Hanssen, M. Condron, Y. H. Tan, J. Baum and S. H. Scheres </td>
2607    <td>Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine.</td>
2608    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2609    <td>Cryo-EM structure of the 80S ribosome of Plasmodium falciparum (3.2 Å)</td>
2610    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/24913268" target="_blank"><b> Elife 3.</b></a></td>
2611  </tr>
2612  <tr>
2613    <td>2014</td>
2614    <td>Amunts, A., A. Brown, X. C. Bai, J. L. Llacer, T. Hussain, P. Emsley, F. Long, G. Murshudov, S. Scheres and V. Ramakrishnan </td>
2615    <td>Structure of the yeast mitochondrial large ribosomal subunit.</td>
2616    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2617    <td>Structure of the yeast mitochondrial large ribosomal subunit (3.2 Å)</td>
2618    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/24675956" target="_blank"><b> Science 343 (6178): 1485-1489.</b></a></td>
2619  </tr>
2620  <tr>
2621    <td>2015</td>
2622    <td>Khatter, H., A. G. Myasnikov, S. K. Natchiar and B. P. Klaholz </td>
2623    <td>Structure of the human 80S ribosome.</td>
2624    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2625    <td>Structure of the human 80S ribosome  (3.6 Å)</td>
2626    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25901680" target="_blank"><b> Nature 520 (7549): 640-5.</b></a></td>
2627  </tr>
2628  <tr>
2629    <td>2015</td>
2630    <td>Behrmann, E., J. Loerke, T. V. Budkevich, K. Yamamoto, A. Schmidt, P. A. Penczek, M. R. Vos, J. Burger, T. Mielke, P. Scheerer and C. M. Spahn </td>
2631    <td>Structural snapshots of actively translating human ribosomes.</td>
2632    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2633    <td>Structural snapshots of actively translating human ribosomes</td>
2634    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/25957688" target="_blank"><b> Cell 161 (4): 845-57.</b></a></td>
2635  </tr>
2636  <tr>
2637    <td>2016</td>
2638    <td>Shalev-Benami, M., Y. Zhang, D. Matzov, Y. Halfon, A. Zackay, H. Rozenberg, E. Zimmerman, A. Bashan, 
2638C. L. Jaffe, A. Yonath and G. Skiniotis </td>
2639    <td>2.8-A Cryo-EM Structure of the Large Ribosomal Subunit from the Eukaryotic Parasite Leishmania.</td>
2640    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2641    <td>Cryo-EM structure of the 60s ribosomal subunit of Leishmania (2.8Å)</td>
2642    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27373148" target="_blank"><b> Cell Rep 16 (2): 288-294.</b></a></td>
2643  </tr>
2644  <tr>
2645    <td>2016</td>
2646    <td>Zhang, X., M. Lai, W. Chang, I. Yu, K. Ding, J. Mrazek, H. L. Ng, O. O. Yang, D. A. Maslov and Z. H. Zhou </td>
2647    <td>Structures and stabilization of kinetoplastid-specific split rRNAs revealed by comparing leishmanial and human ribosomes.</td>
2648    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2649    <td>Structure of the 80s ribosome of Leishmania (2.9Å)</td>
2650    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27752045" target="_blank"><b> Nat Commun 7: 13223.</b></a></td>
2651  </tr>
2652  <tr>
2653    <td>2017</td>
2654    <td>Liu, Z., C. Gutierrez-Vargas, J. Wei, R. A. Grassucci, M. Sun, N. Espina, S. Madison-Antenucci, L. Tong and J. Frank </td>
2655    <td>Determination of the ribosome structure to a resolution of 2.5 A by single-particle cryo-EM.</td>
2656    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2657    <td>Cryo-EM structure of the 60S ribosomal subunit of Plasmodium cruzi (2.5 Å)</td>
2658    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/27750394" target="_blank"><b> Protein Sci 26 (1): 82-92.</b></a></td>
2659  </tr>
2660  <tr>
2661    <td>2017</td>
2662    <td>Wong, W., X. C. Bai, B. E. Sleebs, T. Triglia, A. Brown, J. K. Thompson, K. E. Jackson, E. Hanssen, D. S. Marapana, I. S. Fernandez, S. A. Ralph, A. F. Cowman, S. Scheres and J. Baum </td>
2663    <td>Mefloquine targets the Plasmodium falciparum 80S ribosome to inhibit protein synthesis.</td>
2664    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2665    <td>Cryo-EM structure of the 80S ribosome of Plasmodium falciparum (3.2 Å)</td>
2666    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/28288098" target="_blank"><b> Nat Microbiol 2: 17031.</b></a></td>
2667  </tr>
2668  <tr>
2669    <td>2018</td>
2670    <td>Kummer, E., M. Leibundgut, O. Rackham, R. G. Lee, D. Boehringer, A. Filipovska and N. Ban </td>
2671    <td>Unique features of mammalian mitochondrial translation initiation revealed by cryo-EM.</td>
2672    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2673    <td>Cryo-EM structure of the complete translation initiation complex from mammalian mitochondria (3.2 Å)</td>
2674    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/30089917" target="_blank"><b> Nature 560 (7717): 263-267.</b></a></td>
2675  </tr>
2676  <tr>
2677    <td>2019</td>
2678    <td>Kaledhonkar, S., Z. Fu, K. Caban, W. Li, B. Chen, M. Sun, R. J. Gonzalez and J. Frank </td>
2679    <td>Late steps in bacterial translation initiation visualized using time-resolved cryo-EM.</td>
2680    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2681    <td>Late steps in bacterial translation initiation visualized using time-resolved cryo-EM</td>
2682    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/31108498" target="_blank"><b> Nature 570 (7761): 400-404.</b></a></td>
2683  </tr>
2684  <tr>
2685    <td>2020</td>
2686    <td>Waltz, F., H. Soufari, A. Bochler, P. Giege and Y. Hashem </td>
2687    <td>Cryo-EM structure of the RNA-rich plant mitochondrial ribosome.</td>
2688    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2689    <td>Cryo-EM structure of the RNA-rich plant mitochondrial ribosome</td>
2690    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32251374" target="_blank"><b> Nat Plants 6 (4): 377-383.</b></a></td>
2691  </tr>
2692  <tr>
2693    <td>2020</td>
2694    <td>Loveland, A. B., G. Demo and A. A. Korostelev </td>
2695    <td>Cryo-EM of elongating ribosome with EF-Tu•GTP elucidates tRNA proofreading.</td>
2696    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2697    <td>Cryo-EM of elongating ribosome with EF-Tu•GTP elucidates tRNA proofreading</td>
2698    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32612237" target="_blank"><b> Nature 584 (7822): 640-645.</b></a></td>
2699  </tr>
2700  <tr>
2701    <td>2020</td>
2702    <td>Aibara, S., V. Singh, A. Modelska and A. Amunts </td>
2703    <td>Structural basis of mitochondrial translation.</td>
2704    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2705    <td>Structural basis of mitochondrial translation (3.0 Å)</td>
2706    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32812867" target="_blank"><b> Elife 9.</b></a></td>
2707  </tr>
2708  <tr>
2709    <td>2020</td>
2710    <td>Watson, Z. L., F. R. Ward, R. Meheust, O. Ad, A. Schepartz, J. F. Banfield and J. H. Cate </td>
2711    <td>Structure of the bacterial ribosome at 2 A resolution.</td>
2712    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2713    <td>Structure of the bacterial ribosome at 2 Å resolution</td>
2714    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/32924932" target="_blank"><b> Elife 9.</b></a></td>
2715  </tr>
2716  <tr>
2717    <td>2021</td>
2718    <td>Kummer, E., K. N. Schubert, T. Schoenhut, A. Scaiola and N. Ban </td>
2719    <td>Structural basis of translation termination, rescue, and recycling in mammalian mitochondria.</td>
2720    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2721    <td>Structural basis of translation termination, rescue, and recycling in mammalian mitochondria</td>
2722    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/33878294" target="_blank"><b> Mol Cell 81 (12): 2566-2582.e6.</b></a></td>
2723  </tr>
2724  <tr>
2725    <td>2022</td>
2726    <td>Itoh, Y., A. Khawaja, I. Laptev, M. Cipullo, I. Atanassov, P. Sergiev, J. Rorbach and A. Amunts </td>
2727    <td>Mechanism of mitoribosomal small subunit biogenesis and preinitiation.</td>
2728    <td><a href="https://www.ribocentre.org/docs/Ribosome.html" target="_blank"><b>Ribosome</b></a></td>
2729    <td>Mechanism of mitoribosomal small subunit biogenesis and preinitiation</td>
2730    <td><a href="https://www.ncbi.nlm.nih.gov/pubmed/35676484" target="_blank"><b> Nature 606 (7914): 603-608.</b></a></td>
2731  </tr>
2732  </table><br /><br />
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