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260} 261 262p { 263 margin: 0 0 0px; 264 font-size: 16px; 265} 266/*.bg-primary { 267 background-color: #0874c4; 268}*/ 269 </style> 270 271 272 273 274 <div class="navbar navbar-expand-lg navbar-dark bg-primary" style='border-radius: 0; border: 0;' role="navigation"> 275 276 <div class="container-fluid" style='max-width: 75%;'> 277 <div class="navbar-header"> 278 <button type="button" class="navbar-toggle collapsed" data-toggle="collapse" data-target="#navbar-collapse-1" aria-expanded="false"> 279 <span class="sr-only">Toggle navigation</span> 280 <span class="icon-bar"></span> 281 <span class="icon-bar"></span> 282 <span class="icon-bar"></span> 283 </button> 284 285 <a class="navbar-brand" href="/"> 286 287 <img class="navbar-brand" src="/images/ribocentre-logo.svg" style='height:50px;margin-top:-14px;margin-bottom:0;padding:2px 2px;border-radius: 0;' alt="logo"> 288 <!--b style='font-size: 32px; color: #eeeeee;'>Ribocentre</b--> 289 </a> 290 </div> 291 <div class="collapse navbar-collapse" id="navbar-collapse-1"> 292 <ul class="nav navbar-nav navbar-right"> 293 <li><a class="nav-link-1" href="/" style="font-size: 20px">Home</a></li> 294 <li><a class="nav-link-1" href="/ribozyme" style="font-size: 20px">Ribozymes</a></li> 295 <li><a class="nav-link-1" href="/sequence" style="font-size: 20px">Sequences</a></li> 296 <li><a class="nav-link-1" href="/structure" style="font-size: 20px">Structures</a></li> 297 <li><a class="nav-link-1" href="/catalysis" style="font-size: 20px">Catalysis</a></li> 298 <li><a class="nav-link-1" href="/application" style="font-size: 20px">Applications</a></li> 299 <li><a class="nav-link-1" href="/publications" style="font-size: 20px">Publications</a></li> 300 <li><a class="nav-link-1" href="/Helps" style="font-size: 20px">Help</a></li> 301 </ul> 302 </div> 303 </div> 304 </div> 305 306 307 <div class="container-fluid"> 308 <div class="row"> 309 <div id="homeid" class="col-sm-8"> 310 <p><br /></p> 311 312<div class="well" style="border: 1px solid #C9C9C9; background-color: #fff;"> 313 314 <!--h3><strong> Welcome to Ribocentre</strong></h3--> 315 316 <p><strong style="color:#0874c4;font-weight: bold">Ribocentre</strong> is designed to contain comprehensive information of all natural ribozymes. Ribozymes are good systems for understanding the âsequence - structure - functionâ relationship of RNA molecules, since ribozymes are found in the genomes of species from all kingdoms of life and play a role in important reactions such as peptide-bond formation, RNA splicing, transfer RNA biosynthesis, and viral replication. This is therefore an excellent time to summarise these properties, and our new web-based database will make this generally accessible.<br /></p> 317 318 <p>In addition to a brief introduction to ribozymes, on each <font color="black"><strong>ribozyme</strong></font> page, youâll see a timeline of vital breakthroughs in ribozyme research, representative structures and the chemical mechanism of this ribozyme. Besides, we provide multiple indexing and searching methods, you can index/search about the <font color="black"><strong>
318publications</strong></font>, <font color="black"><strong>structures</strong></font>, <font color="black"><strong>catalyses</strong></font> and <font color="black"><strong>applications</strong></font> of ribozymes that interest you. Users are welcomed to submit new ribozyme cases or related comments through the submission portal to help us improve our database.<br /><br /> 319<strong style="color:#005826;font-weight: bold"><a href="https://riboswitch.ribocentre.org/" target="_blank">Riboswitch</a> </strong>is a regulatory segment of a messenger RNA molecule that binds a small molecule, resulting in a change in the production of the proteins encoded by the mRNA. Welcome to the Ribocentre-switch database!<br /></p> 320</div> 321<div class="well" style="border: 1px solid #C9C9C9; background-color: #fff;"> 322 <p><strong><font size="4">Cite usï¼</font></strong><br /> 323Jie Deng, Yaohuang Shi, Xuemei Peng, Yuanlin He, Xiaoxue Chen, Mengxiao Li, 324Xiaowei Lin, Wenjian Liao, Yuanyin Huang, Taijiao Jiang, David M.J. Lilley, 325Zhichao Miao, and Lin Huang<br /> 326<strong><font size="4">Ribocentre: a database of ribozymes</font></strong><br /> 327<a href="https://academic.oup.com/nar/article/51/D1/D262/6731740" target="_blank">Nucleic Acids Research, gkac840, https://doi.org/10.1093/nar/gkac840<a></a></a></p> 328</div> 329<p><br /></p> 330 331<p>The following content of ribozymes information is adapted from <a href="https://en.wikipedia.org/">Wikipedia</a>.<br />
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The 1982 discovery of ribozymes demonstrated that RNA can be both genetic material (like DNA) and a biological catalyst (like protein enzymes), and contributed to the RNA world hypothesis, which suggests that RNA may have been important in the evolution of prebiotic self-replicating systems<sup>[1]</sup>. The most common activities of natural or in vitro-evolved ribozymes are the cleavage or ligation of RNA and DNA and peptide bond formation<sup>[2]</sup>. For example, the ribozyme that carries out a complex group transfer is the sequence GUGGC-3â², acting to aminoacylate GCCU-3â² (and host a manifold of further reactions) in the presence of substrate PheAMP<sup>[3]</sup>. Within the ribosome, ribozymes function as part of the large subunit ribosomal RNA to link amino acids during protein synthesis. They also participate in a variety of RNA processing reactions, including RNA splicing, viral replication, and transfer RNA biosynthesis. Examples of ribozymes include the hammerhead ribozyme, the VS ribozyme, Leadzyme and the hairpin ribozyme.<br /> 415 Before the discovery of ribozymes, enzymes, which are defined as catalytic proteins<sup>[6]</sup>, were the only known biological catalysts. In 1967, Carl Woese, Francis Crick, and Leslie Orgel were the first to suggest that RNA could act as a catalyst. This idea was based upon the discovery that RNA can form complex secondary structures<sup>[7]</sup>. These ribozymes were found in the intron of an RNA transcript, which removed itself from the transcript, as well as in the RNA component of the RNase P complex, which is involved in the maturation of pre-tRNAs. In 1989, Thomas R. Cech and Sidney Altman shared the Nobel Prize in chemistry for their âdiscovery of catalytic properties of RNA<sup>[8]</sup>.â The term ribozyme was first introduced by Kelly Kruger et al. in 1982 in a paper published in Cell<sup>[1]</sup>.<br /> 416 It had been a firmly established belief in biology that catalysis was reserved for proteins. However, the idea of RNA catalysis is motivated in part by the old question regarding the origin of life: Which comes first, enzymes that do the work of the cell or nucleic acids that carry the information required to produce the enzymes? The concept of âribonucleic acids as catalystsâ circumvents this problem. RNA, in essence, can be both the chicken and the egg<sup>[9]</sup>.<br /> 417 In the 1980s Thomas Cech, at the University of Colorado at Boulder, was studying the excision of introns in a ribosomal RNA gene in Tetrahymena thermophila. While trying to purify the enzyme responsible for the splicing reaction, he found that the intron could be spliced out in the absence of any added cell extract. As much as they tried, Cech and his colleagues could not identify any protein associated with the splicing reaction. After much work, Cech proposed that the intron sequence portion of the RNA could break and reform phosphodiester bonds. At about the same time, Sidney Altman, a professor at Yale University, was studying the way tRNA molecules are processed in the cell when he and his colleagues isolated an enzyme called RNase-P, which is responsible for conversion of a precursor tRNA into the active tRNA. Much to their surprise, they found that RNase-P contained RNA in addition to protein and that RNA was an essential component of the active enzyme. This was such a foreign idea that they had difficulty publishing their findings. The following year, Altman demonstrated that RNA can act as a catalyst by showing that the RNase-P RNA subunit could catalyze the cleavage of precursor tRNA into active tRNA in the absence of any protein component.<br /> 418 Since Cechâs and Altmanâs discovery, other investigators have discovered other examples of self
418-cleaving RNA or catalytic RNA molecules. Many ribozymes have either a hairpin - or hammerhead - shaped active center and a unique secondary structure that allows them to cleave other RNA molecules at specific sequences. It is now possible to make ribozymes that will specifically cleave any RNA molecule. These RNA catalysts may have pharmaceutical applications. For example, a ribozyme has been designed to cleave the RNA of HIV. If such a ribozyme were made by a cell, all incoming virus particles would have their RNA genome cleaved by the ribozyme, which would prevent infection.<br /> 419<br /> 420 You can find more details in <a href="https://www.ribocentre.org/ribozyme/"><strong>Ribozyme</strong></a> pages and click the link into the single ribozyme page such as <a href="https://www.ribocentre.org/docs/twister.html"><strong>Twister</strong></a>. The page gives the information of research timeline,structure,catalysis and relative publications.<br /><br /> 421 422 [1] Kruger K, Grabowski PJ, Zaug AJ, Sands J, Gottschling DE, Cech TR (November 1982). âSelf-splicing RNA: autoexcision and autocyclization of the ribosomal RNA intervening sequence of Tetrahymenaâ. Cell. 31 (1): 147-157. doi:10.1016/0092-8674(82)90414-7. PMID 6297745. S2CID 14787080.<br /> 423 [2] Fedor MJ, Williamson JR (May 2005). âThe catalytic diversity of RNAsâ. Nature Reviews. Molecular Cell Biology. 6(5): 399-412. doi:10.1038/nrm1647. PMID 15956979. S2CID 33304782.<br /> 424 [3] Yarus M (October 2011). âThe meaning of a minuscule ribozymeâ. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 366 (1580): 2902-2909. doi:10.1098/rstb.2011.0139. PMC 3158920. PMID 21930581.<br /> 425 [4] Martin LL, Unrau PJ, Müller UF (January 2015). âRNA synthesis by in vitro selected ribozymes for recreating an RNA worldâ. Life. Basel, Switzerland. 5 (1): 247-68. doi:10.3390/life5010247. PMC 4390851. PMID 25610978.<br /> 426 [5] Hean J, Weinberg MS (2008). âThe Hammerhead Ribozyme Revisited: New Biological Insights for the Development of Therapeutic Agents and for Reverse Genomics Applicationsâ. In Morris KL (ed.). RNA and the Regulation of Gene Expression: A Hidden Layer of Complexity. Norfolk, England: Caister Academic Press. ISBN 978-1-904455-25-7.<br /> 427 [6] Enzyme definition Dictionary.com Accessed 6 April 2007<br /> 428 [7] Woese C (1967). The Genetic Code. New York: Harper and Row. 429 [8] The Nobel Prize in Chemistry 1989 was awarded to Thomas R. Cech and Sidney Altman âfor their discovery of catalytic properties of RNAâ.<br /> 430 [9] Visser CM (1984). âEvolution of biocatalysis 1. Possible pre-genetic-code RNA catalysts which are their own replicaseâ. Origins of Life. 14 (1-4): 291-300. Bibcode:1984OrLiâ¦14..291V. doi:10.1007/BF00933670. PMID 6205343. S2CID 31409366.<br /> 431 </p> 432 </div> 433 434 <div id="News" class="tabcontent" style="width: 100%;height: 800px; overflow-x:hidden;overflow-y: auto;"> 435 <h5><b>Structure and mechanism</b></h5> 436 <div id="ribozymewikisection0"></div> 437 438 <div id="carousel" class="carousel slide" data-ride="carousel" data-interval="4000" data-pause="hover"> 439 <!-- Menu --> 440 <ol class="carousel-indicators" style="weight:300px;"> 441 <li data-target="#carousel" data-slide-to="0" class="active"></li> 442 <li data-target="#carousel" data-slide-to="1"></li> 443 <li data-target="#carousel" data-slide-to="2"></li> 444 <li data-target="#carousel" data-slide-to="3"></li> 445 <li data-target="#carousel" data-slide-to="4"></li> 446 <li data-target="#carousel" data-slide-to="5"></li> 447 </ol> 448 449 <!-- Items --> 450 <div class="carousel-inner"> 451 <div class="item active"> 452 <a href="https://www.ribocentre.org/docs/VS-ribozyme.html" target="_blank"><img src="/images/homepic/VS_Home.png" alt="Slide 1" style="height:350px;display:block;margin:0 auto;" /></a> 453 </div> 454 <div class="item"> 455 <a href="https://www.ribocentre.org/docs/HDV.html" target="_blank"><img src="/images/homepic/HDV_Home.png" alt="Slide 2" style="height:350px;display:block;margin:0 auto;" /></a> 456 </div> 457 <div class="item"> 458 <a href="https://www.ribocentre.org/docs/glms.html" target="_blank"><img src="/images/homepic/GlmS_Home.png" alt="Slide 3" style="height:350px;display:block;margin:0 auto;" /></a> 459 </div> 460 <div class="item"> 461 <a href="https://www.ribocentre.org/docs/Hairpin.html" target="_blank"><img src="/images/homepic/Hairpin_Home.png" alt="Slide 4" style="height:350px;display:block;margin:0 auto;" /></a> 462 </div> 463 <div class="item"> 464 <a href="https://www.ribocentre.org/docs/twister.html" target="_blank"><img src="/images/homepic/Twister_Home.png" alt="Slide 5" style="height:350px;display:block;margin:0 auto;" /></a> 465 </div> 466 <div class="item"> 467 <a href="https://www.ribocentre.org/docs/twister-sister.html" target="_blank"><img src="/images/homepic/Twister-sister_Home.png" alt="Slide 6" style="height:350px;display:block;margin:0 auto;" /></a> 468 </div> 469 470 </div> 471 <a class="left carousel-control" href="#carousel" role="button" data-sli
471de="prev"> 472 <span class="glyphicon glyphicon-chevron-left" aria-hidden="true"></span> 473 <span class="sr-only">Previous</span> 474 </a> 475 <a class="right carousel-control" href="#carousel" role="button" data-slide="next"> 476 <span class="glyphicon glyphicon-chevron-right" aria-hidden="true"></span> 477 <span class="sr-only">Next</span> 478 </a> 479</div> 480 481 <div id="ribozymewikisection1"></div> 482 <div id="ribozymewikisection2"></div> 483 <div id="ribozymewikisection3"></div> 484 <div id="ribozymewikisection4"></div> 485 <div id="ribozymewikisection5"></div> 486 <p><br /></p> 487 488 <p> (Representative figures. More details found at <a href="https://www.ribocentre.org/ribozyme/" target="_blank"><strong>here</strong></a>)<br /><br /> 489 Despite having only four choices for each monomer unit (nucleotides), compared to 20 amino acid side chains found in proteins, ribozymes have diverse structures and mechanisms. In many cases they are able to mimic the mechanism used by their protein counterparts. For example, in self cleaving ribozyme RNAs, an in-line SN2 reaction is carried out using the 2â hydroxyl group as a nucleophile attacking the bridging phosphate and causing 5â oxygen of the N+1 base to act as a leaving group. In comparison, RNase A, a protein that catalyzes the same reaction, uses a coordinating histidine and lysine to act as a base to attack the phosphate backbone<sup>[2]</sup> (clarification needed).<br /> 490 Like many protein enzymes metal binding is also critical to the function of many ribozymes<sup>[10]</sup>. Often these interactions use both the phosphate backbone and the base of the nucleotide, causing drastic conformational changes<sup>[11]</sup>. There are two mechanism classes for the cleavage of phosphodiester backbone in the presence of metal. In the first mechanism, the internal 2â- OH group attacks phosphorus center in a SN2 mechanism. Metal ions promote this reaction by first coordinating the phosphate oxygen and later stabling the oxyanion. The second mechanism also follows a SN2 displacement, but the nucleophile comes from water or exogenous hydroxyl groups rather than RNA itself. The UUU ribozyme can promote the cleavage between G and A of the GAAA tetranucleotide via the first mechanism in the presence of Mn<sup>2+</sup>. The reason why this trinucleotide rather than the complementary tetramer catalyze this reaction may be because the UUU-AAA pairing is the weakest and most flexible trinucleotide among the 64 conformations, which provides the binding site for Mn<sup>2+</sup> <sup>[12]</sup>. <br /> 491 Phosphoryl transfer can also be catalyzed without metal ions. For example, pancreatic ribonuclease A and hepatitis delta virus(HDV) ribozymes can catalyze the cleavage of RNA backbone through acid-base catalysis without metal ions.<sup>[13]</sup><sup>[14]</sup> Hairpin ribozyme can also catalyze the self-cleavage of RNA without metal ions but the mechanism is still unclear<sup>[14]</sup>.<br /> 492 Ribozyme can also catalyze the formation of peptide bond between adjacent amino acid by lowering the activation entropy <sup>[13]</sup>. 493 <br /> 494 You can find more details in <a href="https://www.ribocentre.org/ribozyme/" target="_blank"><strong>Ribozyme</strong></a> and <a href="https://www.ribocentre.org/structure/" target="_blank"><strong>Structure</strong></a> pages!<br /><br /> 495 [10] Pyle AM (August 1993). âRibozymes: a distinct class of metalloenzymesâ. Science. 261 (5122): 709-714. Bibcode:1993Sciâ¦261..709P. doi:10.1126/science.7688142. PMID 7688142.<br /> 496 [11] Freisinger E, Sigel RK (2007). âFrom nucleotides to ribozymesâA comparison of their metal ion binding propertiesâ (PDF). Coord. Chem. Rev. 251 (13-14): 1834-1851. doi:10.1016/j.ccr.2007.03.008.<br /> 497 [12] Pyle AM (August 1993). âRibozymes: a distinct class of metalloenzymesâ. Science. 261 (5122): 709-714. Bibcode:1993Sciâ¦261..709P. doi:10.1126/science.7688142. JSTOR 2882234. PMID 7688142.<br /> 498 [13] Lilley DM (October 2011). âMechanisms of RNA catalysisâ. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 366 (1580): 2910-2917. doi:10.1098/rstb.2011.0132. JSTOR 23035661. PMC 3158914. PMID 21930582.<br /> 499 [14] Doudna JA, Cech TR (July 2002). âThe chemical repertoire of natural ribozymesâ. Nature. 418 (6894): 222-228.Bibcode:2002Natur.418..222D. doi:10.1038/418222a. PMID 12110898. S2CID 4417095.<br /> 500 </p> 501 </div> 502 503 <div id="Contact" class="tabcontent" style="width: 100%;height: 600px; overflow-x:hidden;overflow-y: auto;"> 504 <h5><b>Activities</b></h5> 505 <p>Although ribozymes are quite rare in most cells, their roles are sometimes essential to life. For example, the functional part of the ribosome, the biological machine that translates RNA into proteins, is fundamentally a ribozyme, composed of RNA tertiary structural motifs that are often coordinated to metal ions such as Mg<sup>2+</sup> as cofactors<sup>
505[15]</sup>. In a model system, there is no requirement for divalent cations in a five-nucleotide RNA catalyzing trans-phenylalanation of a four-nucleotide substrate with 3 base pairs complementary with the catalyst, where the catalyst/substrate were devised by truncation of the C3 ribozyme<sup>[16]</sup>.<br /> 506 The best-studied ribozymes are probably those that cut themselves or other RNAs, as in the original discovery by Cech<sup>[17]</sup> and Altman<sup>[18]</sup>. However, ribozymes can be designed to catalyze a range of reactions (see below), many of which may occur in life but have not been discovered in cells<sup>[19]</sup>.<br /> 507 RNA may catalyze folding of the pathological protein conformation of a prion in a manner similar to that of a chaperonin<sup>[20]</sup>.<br /> 508 You can find more catalysis details in <a href="https://www.ribocentre.org/catalysis/" target="_blank"><strong>Catalysis</strong></a> page!<br /><br /> 509 510 [15] Ban N, Nissen P, Hansen J, Moore PB, Steitz TA (August 2000). âThe complete atomic structure of the large ribosomal subunit at 2.4 A resolutionâ. Science. 289 (5481): 905-920. Bibcode:2000Sciâ¦289..905B. CiteSeerX 10.1.1.58.2271. doi:10.1126/science.289.5481.905. PMID 10937989.<br /> 511 [16] Turk RM, Chumachenko NV, Yarus M (March 2010). âMultiple translational products from a five-nucleotide ribozymeâ. Proceedings of the National Academy of Sciences of the United States of America. 107 (10): 4585-4589. Bibcode:2010PNAS..107.4585T. doi:10.1073/pnas.0912895107. PMC 2826339. PMID 20176971.<br /> 512 [17] Cech TR (August 2000). âStructural biology. The ribosome is a ribozymeâ. Science. 289 (5481): 878-879. doi:10.1126/science.289.5481.878. PMID 10960319. S2CID 24172338.<br /> 513 [18] Altman S (August 1990). âNobel lecture. Enzymatic cleavage of RNA by RNAâ. Bioscience Reports. 10 (4): 317-337. doi:10.1007/BF01117232. PMID 1701103. S2CID 12733970.<br /> 514 [19] Walter NG, Engelke DR (October 2002). âRibozymes: catalytic RNAs that cut things, make things, and do odd and useful jobsâ. Biologist. 49 (5): 199-203. PMC 3770912. PMID 12391409.<br /> 515 [20] Supattapone S (June 2004). âPrion protein conversion in vitroâ. Journal of Molecular Medicine. 82 (6): 348-356. doi:10.1007/s00109-004-0534-3. PMID 15014886. S2CID 24908667.<br /></p> 516 </div> 517 518 <div id="About" class="tabcontent" style="width: 100%;height: 600px; overflow-x:hidden;overflow-y: auto;"> 519 <h5><b>And Moreâ¦</b></h5> 520 <p>RNA can also act as a hereditary molecule, which encouraged Walter Gilbert to propose that in the distant past, the cell used RNA as both the genetic material and the structural and catalytic molecule rather than dividing these functions between DNA and protein as they are today; this hypothesis is known as the âRNA world hypothesisâ of the origin of life<sup>[21]</sup>.<br /> 521 RNA-centric research is becoming more and more important in recent years with a wide application in RNA virus inhibitor, mRNA vaccine design during the pandemic. Ribozyme is a perfect system in understanding the âsequence - structure - functionâ relationship of RNA molecules, since ribozymes are found in the genomes of species from all kingdoms of life and play a role in many vital reactions such as peptide-bond formation, RNA splicing, transfer RNA biosynthesis, and viral replication. A ribozyme database may greatly facilitate the inspection of the fundamental folding rules of functional RNA molecules as well as the comparison between ribozymes of different functions.<br /> 522 We believe that the data of ribozymes accumulated over the last 40 years would better serve the scientific community if presented as an online resource.Users are more than welcome to submit new ribozyme cases or related comments through the submission portal to help us improve our database easier to be used.<br /> 523 524 You can find more details,such as how to use this database or summit a new discovery in <a href="https://www.ribocentre.org/Helps/" target="_blank"><strong>Help</strong></a> page! <br /><br /> 525 526 [21] Gilbert W (1986). âOrigin of life: The RNA worldâ. Nature. 319 (6055): 618. Bibcode:1986Natur.319..618G. doi:10.1038/319618a0. S2CID 8026658 527 </p> 528 </div> 529 530
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547 548 549</body> 550 551<p><br /><br /></p> 552 553 554 </div> 555 <div id="newsid" class="col-sm-4" > 556 557 558 <div class="well" style="margin-top:24px;" > 559 <h4>News: </h4> 560 561 562 <p><br> 563</p> 564 565 <p><span class="glyphicon glyphicon-bullhorn"></span> 01. October 2023<br><p>Ribocentre-switch paper online, please see the link Nucleic Acids Research, gkad891, https://doi.org/10.1093/nar/gkad891.</p> 566</p> 567 568 <p><span class="glyphicon glyphicon-bullhorn"></span> 07. March 2023<br><p>Ribocentre updated to v1.5, thanks to the sequence search function from RNAcentral.</p> 569</p> 570 571 <p><span class="glyphicon glyphicon-bullhorn"></span> 30. Sept 2022<br><p>Ribocentre database paper online, please see the link Nucleic Acids Research, gkac840, https://doi.org/10.1093/nar/gkac840.</p> 572</p> 573 574 <p><span class="glyphicon glyphicon-bullhorn"></span> 28. July 2022<br><p>Ribocentre updated to v1.4, add 3D dynamic interactive visualization.</p> 575</p> 576 577 <p><span class="glyphicon glyphicon-bullhorn"></span> 18. July 2022<br><p>Ribocentre updated to v1.3, add 2D dynamic interactive visualization.</p> 578</p> 579 580 <p><span class="glyphicon glyphicon-bullhorn"></span> 25. June 2022<br><p>Ribocentre updated to v1.2, add Catalysis section.</p> 581</p> 582 583 <p><span class="glyphicon glyphicon-bullhorn"></span> 12. June 2022<br><p>Ribocentre updated to v1.1, add Applications section.</p> 584</p> 585 586 <p><span class="glyphicon glyphicon-bullhorn"></span> 1. June 2022<br><p>Ribocentre database v1.0 version online.</p> 587</p> 588 589 590 <h4><a href="/allnews.html">... see all News</a></h4> 591 592 </div> 593 594 <div class="well"> 595 <h4>Visualization: </h4> 596 597 <meta name="viewport" content="width=device-width, initial-scale=1"> 598 <head> 599 </head> 600 <style type="text/css"> 601 </style> 602 603 <p> 604 <a href="https://www.ribocentre.org/docs/twister.html"><img src="https://www.ribocentre.org/images/homepic/4OJI.png" width="" height="100px"></a> 605 <a href="https://www.ribocentre.org/docs/VS-ribozyme.html"><img src="https://www.ribocentre.org/images/homepic/4R4V.png" width="" height="100px"></a><br> 606 <a href="https://www.ribocentre.org/docs/hammer.html"><img src="https://www.ribocentre.org/images/homepic/3ZD5.png" width="" height="100px"></a> 607 <a href="https://www.ribocentre.org/docs/groupII.html"><img src="https://www.ribocentre.org/images/homepic/4FAR.png" width="" height="100px"></a><br> 608 <a href="https://www.ribocentre.org/docs/glms.html"><img src="https://www.ribocentre.org/images/homepic/2HO7.png" width="" height="100px"></a> 609 <a href="https://www.ribocentre.org/docs/HDV.html"><img src="https://www.ribocentre.org/images/homepic/1DRZ.png" width="" height="100px"></a><br> 610 611 </p> (Representative Data. Full list found at <a href="https://www.ribocentre.org/ribozyme/"><strong>here</strong></a>)</div> 612 <div class="well"> 613 <h4>Submit/Feedback : </h4> 614 <a href="https://www.ribocentre.org/Helps" target="_blank"><button>Clink here</button></a><br> 615 616 </div> 617 618 619 <div class="well"> 620 <h4>Related websites:</h4> 621 622 <meta name="viewport" content="width=device-width, initial-scale=1"> 623 <head> 624 </head> 625 <style type="text/css"> 626 </style> 627 628 <p> 629 <a href="https://riboswitch.ribocentre.org/"><img src="/images/riboswitch.svg" width="" height="50px"></a> 630 <a href="https://aptamer.ribocentre.org/"><img src="/images/riboaptamer.svg" width="" height="50px"></a> 631 632 633 </p></div> 634 635 636 637 </div> 638 639 </div> 640 </div> 641 642 <div id="footer" class="panel"> 643 <div class="panel-footer" style='background-color: #333333; color: #eeeeee;'> 644 <div class="container-fluid"> 645 <div class="row"> 646 <div class="col-sm-4"> 647 648 <p>© 2024 GZNL-RDC. </p> 649 <p>We are part of the <a href="https://gzlab.ac.cn">Guangzhou Laboratory</a> and <a href="http://www.rnacentre.org/">RNAcentre</a> and <a href="http://www.gzsys.org.cn/">Sun Yat-sen University</a>.</p> 650 <p>Site made with <a href="https://jekyllrb.com">Jekyll</a>; <a href="/aboutwebsite.html">copy and modify it for your own research group</a>.</p> 651 <p> </p> 652 <p> </p> 653 </div> 654 655 <div class="col-sm-4"> 656 Funding:<br /> 657 - <a href="https://gzlab.ac.cn">R&D Programs of Guangzhou Laboratory</a><br /> 658 - <a href="http://www.most.gov.cn/">MOST IT+BT projects</a> <br /> 659 - <a href="https://www.nsfc.gov.cn/">NSFC</a> <br /> 660 <br> 661
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