The DOI matches its Crossref record; 99 of the 99 references it cites were found in a registry or an index.
The chemical repertoire of natural ribozymes
Abstract
Although RNA is generally thought to be a passive genetic blueprint, some RNA molecules, called ribozymes, have intrinsic enzyme-like activity--they can catalyse chemical reactions in the complete absence of protein cofactors. In addition to the well-known small ribozymes that cleave phosphodiester bonds, we now know that RNA catalysts probably effect a number of key cellular reactions. This versatility has lent credence to the idea that RNA molecules may have been central to the early stages of life on Earth.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Today, RNA serves as the sole genetic molecule in many viruses, and the number of reactions catalyzed by RNA enzymes (“ribozymes”) is ever increasing (Doudna and Cech, 2002; Chen et al., 2007).”
From The Astrobiology Primer v2.0 (2016) · cites this paper as Doudna and Cech, 2002
In the citing paper
“Today, RNA serves as the sole genetic molecule in many viruses, and the number of reactions catalyzed by RNA enzymes (“ribozymes”) is ever increasing (Doudna and Cech, 2002; Chen et al., 2007).”
From The Astrobiology Primer v2.0 (2016) · cites this paper as Doudna and Cech, 2002
Citations
Cites
The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327
The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., & Altman, S. (1983) · Cell · doi:10.1016/0092-8674(83)90117-4 · Cited by 2,684
Kruger, K., Grabowski, P. J., Zaug, A. J., Sands, J., Gottschling, D. E., & Cech, T. R. (1982) · Cell · doi:10.1016/0092-8674(82)90414-7 · Cited by 2,331
Self-citationThe Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269
Crystal Structure of a Group I Ribozyme Domain: Principles of RNA Packing
Cate, J. H. D., Gooding, A. R., Podell, E. R., Zhou, K., Golden, B. L., Kundrot, C. E., Cech, T. R., & Doudna, J. A. (1996) · Science · doi:10.1126/science.273.5282.1678 · Cited by 1,249
Self-citationMichel, F., & Westhof, É. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90386-z · Cited by 1,239
In Vitro Selection of Functional Nucleic Acids
Wilson, D. S., & Szostak, J. W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.611 · Cited by 1,217
Three-dimensional structure of a hammerhead ribozyme
Pley, H. W., Flaherty, K. M., & McKay, D. (1994) · Nature · doi:10.1038/372068a0 · Cited by 946
Reversible Unfolding of Single RNA Molecules by Mechanical Force
Liphardt, J., Onoa, B., Smith, S. B., Tinoco, I., & Bustamante, C. (2001) · Science · doi:10.1126/science.1058498 · Cited by 931
Crystal structure of a hepatitis delta virus ribozyme
Ferré-D’Amaré, A. R., Zhou, K., & Doudna, J. A. (1998) · Nature · doi:10.1038/26912 · Cited by 790
Self-citation
Cited by
Sorted by citations
Functional Nucleic Acid Sensors
Liu, J., Cao, Z. C., & Lu, Y. (2009) · Chemical Reviews · doi:10.1021/cr030183i · Cited by 2,188
RNAstructure: software for RNA secondary structure prediction and analysis
Reuter, J. S., & Mathews, D. H. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-129 · Cited by 2,018
Synthetic biology: applications come of age
Khalil, A. S., & Collins, J. J. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2775 · Cited by 1,413
Rauch, F., & Glorieux, F. H. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16051-0 · Cited by 1,202
Biologically Active Molecules with a “Light Switch”
Mayer, G., & Heckel, A. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200600387 · Cited by 1,113
Kurreck, J. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03555.x · Cited by 1,020
Analysis of aptamer discovery and technology
Dunn, M. R., Jimenez, R. M., & Chaput, J. C. (2017) · Nature Reviews Chemistry · doi:10.1038/s41570-017-0076 · Cited by 938
siRNAs: applications in functional genomics and potential as therapeutics
Dorsett, Y., & Tuschl, T. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1345 · Cited by 917
Nucleases: diversity of structure, function and mechanism
Yang, W. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000181 · Cited by 692
The Structural and Functional Diversity of Metabolite-Binding Riboswitches
Roth, A., & Breaker, R. R. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.070507.135656 · Cited by 557
Engineered riboregulators enable post-transcriptional control of gene expression
Isaacs, F. J., Dwyer, D. J., Ding, C., Pervouchine, D. D., Cantor, C. R., & Collins, J. J. (2004) · Nature Biotechnology · doi:10.1038/nbt986 · Cited by 547
Functional nucleic acid-based hydrogels for bioanalytical and biomedical applications
Li, J., Mo, L., Lü, C., Fu, T., Yang, H., & Tan, W. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00586h · Cited by 529
Transformation of Biomass into Commodity Chemicals Using Enzymes or Cells
Straathof, A. J. J. (2013) · Chemical Reviews · doi:10.1021/cr400309c · Cited by 474
RNAstructure: web servers for RNA secondary structure prediction and analysis
Bellaousov, S., Reuter, J. S., Seetin, M. G., & Mathews, D. H. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt290 · Cited by 434
DNA‐Based Asymmetric Catalysis
Roelfes, G., & Feringa, B. L. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200500298 · Cited by 411
Prediction of RNA secondary structure by free energy minimization
Mathews, D. H., & Turner, D. H. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.05.010 · Cited by 409
Isaacs, F. J., Dwyer, D. J., & Collins, J. J. (2006) · Nature Biotechnology · doi:10.1038/nbt1208 · Cited by 384
Mathews, D. H. (2004) · RNA · doi:10.1261/rna.7650904 · Cited by 373
Pseudoknots: RNA Structures with Diverse Functions
Staple, D. W., & Butcher, S. E. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030213 · Cited by 371
A comprehensive comparison of comparative RNA structure prediction approaches
Gardner, P. P., & Giegerich, R. (2004) · BMC Bioinformatics · doi:10.1186/1471-2105-5-140 · Cited by 353
Unified Prebiotically Plausible Synthesis of Pyrimidine and Purine RNA Ribonucleotides
Becker, S., Feldmann, J., Wiedemann, S., Okamura, H., Schneider, C., Iwan, K., Crisp, A., Rossa, M., Amatov, T., & Carell, T. (2019) · Science · doi:10.1126/science.aax2747 · Cited by 306
Zhang, X., Rice, K., Wang, Y., Chen, W., Zhong, Y., Nakayama, Y., Zhou, Y., & Klibanski, A. (2010) · Endocrinology · doi:10.1210/en.2009-0657 · Cited by 325
In vitro selection, characterization, and application of deoxyribozymes that cleave RNA
Silverman, S. K. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki930 · Cited by 306
Alternative Roles for Metal Ions in Enzyme Catalysis and the Implications for Ribozyme Chemistry
Sigel, R. K. O., & Pyle, A. M. (2006) · Chemical Reviews · doi:10.1021/cr0502605 · Cited by 302
The Biology of Viroid-Host Interactions
Ding, B. (2009) · Annual Review of Phytopathology · doi:10.1146/annurev-phyto-080508-081927 · Cited by 290
mRNA-Initiated, Three-Dimensional DNA Amplifier Able to Function inside Living Cells
He, L., Lu, D., Liang, H., Xie, S., Zhang, X., Liu, Q., Yuan, Q., & Tan, W. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b09789 · Cited by 285
More than the sum of their parts: On the evolution of proteins from peptides
Söding, J., & Lupas, A. N. (2003) · BioEssays · doi:10.1002/bies.10321 · Cited by 252
Biologically Inspired Synthetic Enzymes Made from DNA
Schlosser, K., & Li, Y. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.01.008 · Cited by 284
RNA and Protein Folding: Common Themes and Variations
Thirumalai, D., & Hyeon, C. (2005) · Biochemistry · doi:10.1021/bi047314+ · Cited by 267
Weninger, A., Hatzl, A.-M., Schmid, C., Vogl, T. J., & Glieder, A. (2016) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2016.03.027 · Cited by 271
Fundamental studies of functional nucleic acids: aptamers, riboswitches, ribozymes and DNAzymes
Micura, R., & Höbartner, C. (2020) · Chemical Society Reviews · doi:10.1039/d0cs00617c · Cited by 265
Non-coding RNA: a new frontier in regulatory biology
Fu, X. (2014) · National Science Review · doi:10.1093/nsr/nwu008 · Cited by 265
An autonomous DNA nanomachine maps spatiotemporal pH changes in a multicellular living organism
Surana, S., Bhat, J. M., Koushika, S. P., & Krishnan, Y. (2011) · Nature Communications · doi:10.1038/ncomms1340 · Cited by 254
Drug delivery of siRNA therapeutics: potentials and limits of nanosystems
Reischl, D., & Zimmer, A. (2008) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2008.06.001 · Cited by 256
Wolf, Y. I., & Koonin, E. V. (2007) · Biology Direct · doi:10.1186/1745-6150-2-14 · Cited by 235
“It is often noted that the RNA World is not just a concept supported by the catalytic prowess of ribozymes: while overshadowed by the multitude of proteins with catalytic and structural functions, the RNA World still lurks within modern life forms [57,58].”
BackgroundRNA FOLDING DURING TRANSCRIPTION
Pan, T., & Sosnick, T. R. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102053 · Cited by 244
Mechanism of mRNA destabilization by the glmS ribozymePreprint
Collins, J. A., Irnov, I., Baker, S. C., & Winkler, W. C. (2007) · Genes & Development · doi:10.1101/gad.1605307 · Cited by 247
Biologisch aktive Moleküle mit “Lichtschalter”
Mayer, G., & Heckel, A. (2006) · Angewandte Chemie · doi:10.1002/ange.200600387 · Cited by 223
Of proteins and RNA: the RNase P/MRP family.
Esakova, O., & Krasilnikov, A. S. (2010) · RNA: A publication of the RNA Society · doi:10.1261/rna.2214510 · Cited by 228
Structure of the Tetrahymena Ribozyme
Guo, F., Gooding, A. R., & Cech, T. R. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.003 · Cited by 220
Self-citationMolecular crowding stabilizes folded RNA structure by the excluded volume effect
Kilburn, D., Roh, J. H., Guo, L., Briber, R. M., & Woodson, S. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja101500g · Cited by 211
ProbKnot: Fast prediction of RNA secondary structure including pseudoknots
Bellaousov, S., & Mathews, D. H. (2010) · RNA · doi:10.1261/rna.2125310 · Cited by 219
Targeting RNA with Small Molecules
Tor, Y. (2003) · ChemBioChem · doi:10.1002/cbic.200300680 · Cited by 214
Uzilov, A. V., Keegan, J. M., & Mathews, D. H. (2006) · BMC Bioinformatics · doi:10.1186/1471-2105-7-173 · Cited by 211
Primary open-angle glaucoma genes
Fingert, J. H. (2011) · Eye · doi:10.1038/eye.2011.97 · Cited by 207
Single-molecule transition-state analysis of RNA folding
Bokinsky, G., Rueda, D., Misra, V. K., Rhodes, M. M., Gordus, A. G., Babcock, H. P., Walter, N. G., & Zhuang, X. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1133280100 · Cited by 207
The Ribosomal Peptidyl Transferase Center: Structure, Function, Evolution, Inhibition
Polacek, N., & Mankin, A. S. (2005) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230500326334 · Cited by 218
Structural basis for Diels-Alder ribozyme-catalyzed carbon-carbon bond formation
Serganov, A., Keiper, S., Malinina, L. V., Tereshko, V. A., Skripkin, E. A., Höbartner, C., Polonskaia, A., Phan, A. T., Wombacher, R., Micura, R., et al. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb906 · Cited by 199
A four-way junction accelerates hairpin ribozyme folding via a discrete intermediate
Tan, E., Wilson, T. J., Nahas, M. K., Clegg, R. M., Lilley, D. M. J., & Ha, T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1233536100 · Cited by 196
Chen, X., Gao, C., Guo, L., Hu, G., Luo, Q., Liu, J., Nielsen, J., Chen, J., & Liu, L. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00804 · Cited by 191
Eukaryotic RNase P RNA mediates cleavage in the absence of protein
Kikovska, E., Svärd, S. G., & Kirsebom, L. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607326104 · Cited by 198
Catalytic DNA (deoxyribozymes) for synthetic applications—current abilities and future prospects
Silverman, S. K. (2008) · Chemical Communications · doi:10.1039/b807292m · Cited by 186
Vfold: A Web Server for RNA Structure and Folding Thermodynamics Prediction
Xu, X., Zhao, P., & Chen, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107504 · Cited by 179
Magnesium Is a Key Player in Neuronal Maturation and Neuropathology
Yamanaka, R., Shindo, Y., & Oka, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143439 · Cited by 184
Improvement through novel chemical modifications
Kurreck, J. (2003) · Cited by 179
Deoxyribozymes: useful DNA catalysts in vitro and in vivo
Baum, D. A., & Silverman, S. K. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8029-y · Cited by 174
Exploring the repertoire of RNA secondary motifs using graph theory; implications for RNA design
Gan, H. H. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg365 · Cited by 175
Glorieux, F. H. (2008) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2007.12.012 · Cited by 171
Small Molecule Interactions Were Central to the Origin of Life
Shapiro, R. (2006) · The Quarterly Review of Biology · doi:10.1086/506024 · Cited by 180
Group II Introns: Structure and Catalytic Versatility of Large Natural Ribozymes
Lehmann, K., & Schmidt, U. (2003) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/713609236 · Cited by 170
Catalytic Nucleic Acids: Biochemistry, Chemical Biology, Biosensors, and Nanotechnology
Ma, L., & Liu, J. (2020) · iScience · doi:10.1016/j.isci.2019.100815 · Cited by 164
Atomic level architecture of group I introns revealed
Vicens, Q., & Cech, T. R. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.11.008 · Cited by 162
Self-citationTan, Z., Fu, Y., Gaurav Sharma, A., & Mathews, D. H. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx815 · Cited by 160
Monnard, P.-A., Kanavarioti, A., & Deamer, D. W. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036465h · Cited by 159
Sen, D., & Poon, L. C.-H. (2011) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2011.618220 · Cited by 155
Crystal structure of a DNA catalyst
Ponce-Salvatierra, A., Wawrzyniak-Turek, K., Steuerwald, U., Höbartner, C., & Peña, V. (2016) · Nature · doi:10.1038/nature16471 · Cited by 153
Calculation of pKas in RNA: On the Structural Origins and Functional Roles of Protonated Nucleotides
Tang, C. L., Alexov, E. G., Pyle, A. M., & Honig, B. H. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.001 · Cited by 151
Coarse-Grained Model for Predicting RNA Folding Thermodynamics
Denesyuk, N. A., & Thirumalai, D. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp401087x · Cited by 150
Vicens, Q., & Westhof, É. (2003) · Biopolymers · doi:10.1002/bip.10414 · Cited by 151
Catalytic roles for proton transfer and protonation in ribozymes
Bevilacqua, P. C., Brown, T. S., Nakano, S., & Yajima, R. (2003) · Biopolymers · doi:10.1002/bip.10519 · Cited by 148
Metal ion binding to catalytic RNA molecules
DeRose, V. J. (2003) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(03)00077-0 · Cited by 147
Ligand Requirements for glmS Ribozyme Self-Cleavage
McCarthy, T. J., Plog, M. A., Floy, S. A., Jansen, J. A., Strauss-Soukup, J. K., & Soukup, G. A. (2005) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.09.006 · Cited by 146
RNA Helical Packing in Solution: NMR Structure of a 30 kDa GAAA Tetraloop–Receptor Complex
Davis, J., Tonelli, M., Scott, L. G., Jaeger, L., Williamson, J. R., & Butcher, S. E. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.05.069 · Cited by 144
A Ribozyme for the Aldol Reaction
Fusz, S., Eisenführ, A., Srivatsan, S. G., Heckel, A., & Famulok, M. (2005) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.06.008 · Cited by 143
Recent Progress in Nucleic Acid Aptamer-Based Biosensors and Bioassays
Mok, W. W. K., & Li, Y. (2008) · Sensors · doi:10.3390/s8117050 · Cited by 142
Surfactant Assemblies and their Various Possible Roles for the Origin(S) of Life
Walde, P. (2006) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-005-9004-3 · Cited by 138
Guanine-Rich RNAs and DNAs That Bind Heme Robustly Catalyze Oxygen Transfer Reactions
Poon, L. C.-H., Methot, S. P., Morabi-Pazooki, W., Pio, F., Bennet, A. J., & Sen, D. (2011) · Journal of the American Chemical Society · doi:10.1021/ja108571a · Cited by 137
Lü, Z., Turner, D. H., & Mathews, D. H. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl472 · Cited by 131
Carbohydrate Polymers at the Center of Life’s Origins: The Importance of Molecular Processivity
Stern, R., & Jedrzejas, M. J. (2008) · Chemical Reviews · doi:10.1021/cr078240l · Cited by 136
Bridging the gap betweenin vitroandin vivoRNA folding
Leamy, K. A., Assmann, S. M., Mathews, D. H., & Bevilacqua, P. C. (2016) · Quarterly Reviews of Biophysics · doi:10.1017/s003358351600007x · Cited by 134
Synthetic antibodies for specific recognition and crystallization of structured RNA
Ye, J., Tereshko, V. A., Frederiksen, J. K., Koide, A., Fellouse, F. A., Sidhu, S. S., Koide, S., Kossiakoff, A. A., & Piccirilli, J. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709082105 · Cited by 134
Domagal-Goldman, S. D., Wright, K. E., Domagal-Goldman, S. D., Wright, K. E., Adamala, K., Arina de la Rubia, L., Bond, J., Dartnell, L. R., Goldman, A. D., Lynch, K., et al. (2016) · Astrobiology · doi:10.1089/ast.2015.1460 · Cited by 136
“Today, RNA serves as the sole genetic molecule in many viruses, and the number of reactions catalyzed by RNA enzymes (‘‘ribozymes’’) is ever increasing (Doudna and Cech, 2002; Chen et al., 2007).”
HiRE-RNA: A High Resolution Coarse-Grained Energy Model for RNA
Pasquali, S., & Derreumaux, P. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp102497y · Cited by 133
Lusic, H., Young, D. D., Lively, M. O., & Deiters, A. (2007) · Organic Letters · doi:10.1021/ol070455u · Cited by 133
Deoxyribozymes: DNA catalysts for bioorganic chemistry
Silverman, S. K. (2004) · Organic & Biomolecular Chemistry · doi:10.1039/b411910j · Cited by 132
Das, R., Kwok, L. W., Millett, I. S., Bai, Y., Mills, T. T., Jacob, J., Maskel, G. S., Seifert, S., Mochrie, S. G. J., Thiyagarajan, P., et al. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00854-4 · Cited by 131
DNA‐Based Hybrid Catalysts for Asymmetric Organic Synthesis
Park, S., & Sugiyama, H. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200905382 · Cited by 130
Non-coding RNAs: An Introduction
Yang, J. X., Rastetter, R. H., & Wilhelm, D. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-94-017-7417-8_2 · Cited by 134
DNA‐Based Asymmetric Catalysis
Roelfes, G., & Feringa, B. L. (2005) · Angewandte Chemie · doi:10.1002/ange.200500298 · Cited by 127
A chemical screen for biological small molecule–RNA conjugates reveals CoA-linked RNA
Kowtoniuk, W. E., Shen, Y., Heemstra, J. M., Agarwal, I., & Liu, D. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900528106 · Cited by 129
Structures, Kinetics, Thermodynamics, and Biological Functions of RNA Hairpins
Bevilacqua, P. C., & Blose, J. M. (2007) · Annual Review of Physical Chemistry · doi:10.1146/annurev.physchem.59.032607.093743 · Cited by 124
Coarse-grained model for predicting RNA folding thermodynamicsPreprint
Denesyuk, N. A., & Thirumalai, D. (2016) · Cited by 127
Boussebayle, A., Torka, D., Ollivaud, S., Braun, J., Bofill-Bosch, C., Dombrowski, M., Groher, F., Hamacher, K., & Suess, B. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz216 · Cited by 123
Predicting a set of minimal free energy RNA secondary structures common to two sequences
Mathews, D. H. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti349 · Cited by 120
Frameworks for Programming Biological Function through RNA Parts and Devices
Win, M. N., Liang, J. C., & Smolke, C. D. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.02.011 · Cited by 119
How do metal ions direct ribozyme folding?
Denesyuk, N. A., & Thirumalai, D. (2015) · Nature Chemistry · doi:10.1038/nchem.2330 · Cited by 117
DNA and RNA Can Be Equally Efficient Catalysts for Carbon−Carbon Bond Formation
Chandra, M., & Silverman, S. K. (2008) · Journal of the American Chemical Society · doi:10.1021/ja7111965 · Cited by 115
pknotsRG: RNA pseudoknot folding including near-optimal structures and sliding windows
Reeder, J., Steffen, P., & Giegerich, R. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm258 · Cited by 114
Cryo-EM Structure of the Human Ribonuclease P Holoenzyme
Wu, J., Niu, S., Tan, M., Huang, C., Li, M., Song, Y., Wang, Q., Chen, J., Shi, S., Lan, P., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.003 · Cited by 111
Site-specific RNA methylation by a methyltransferase ribozyme
Scheitl, C. P. M., Maghami, M. G., Lenz, A., & Höbartner, C. (2020) · Nature · doi:10.1038/s41586-020-2854-z · Cited by 115
Metadata
- Authors
- Doudna, J. A., & Cech, T. R.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Nature
- Published
- 2002-07
- Volume
- 418
- Issue
- 6894
- Pages
- 222-228
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1980410097
- Cited by
- 745
- References
- 99
- Citations by year
- 2026: 28 · 2025: 21 · 2024: 25 · 2023: 14 · 2022: 23 · 2021: 24 · 2020: 24 · 2019: 29 · 2018: 15 · 2017: 29 · 2016: 17 · 2015: 22 · 2014: 18 · 2013: 26 · 2012: 26
- FWCI
- 3.90
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- ribozymes, RNA catalysis, RNA chemistry, origin of life, RNA evolution, phosphodiester bond cleavage
- MeSH terms
- Animals, Catalysis, Endoribonucleases, Humans, Introns, Models, Molecular, Nucleic Acid Conformation, Ribonucleoproteins, RNA Splicing, Substrate Specificity, RNA, Catalytic, Ribonuclease P
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
