The DOI matches its Crossref record; 35 of the 36 references it cites were found in a registry or an index.
RNA, the first macromolecular catalyst: the ribosome is a ribozyme
Abstract
Recently, the atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with substrates have been determined. These have provided exciting new insights into the principles of RNA structure, the mechanism of the peptidyl-transferase reaction and early events in the evolution of this RNA-protein complex assembly that is essential in all cells. The structures of the large subunit bound to a variety of antibiotics explain the effects of antibiotic resistance mutations and provide promise for the development of new antibiotics.
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
“The central role of RNA in modern cellular biochemistry, and especially the role of the large ribosomal RNA as the catalyst of protein synthesis (Steitz and Moore 2003), provides a powerful argument in support of RNA as the dominant genetic and functional biopolymer at an early stage in the evolution of life.”
From Protocells and RNA Self-Replication (2018) · cites this paper as Steitz and Moore 2003
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
Self-citationThe 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
The 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
Self-citationRecognition of Cognate Transfer RNA by the 30 S Ribosomal Subunit
Ogle, J. M., Brodersen, D. E., Clemons, W. M., Tarry, M. J., Carter, A. P., & Ramakrishnan, V. (2001) · Science · doi:10.1126/science.1060612 · Cited by 1,162
Schlünzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., Yonath, A., & Franceschi, F. J. (2001) · Nature · doi:10.1038/35101544 · Cited by 1,057
A SMALL PARTICULATE COMPONENT OF THE CYTOPLASM
Palade, G. E. (1955) · The Journal of Cell Biology · doi:10.1083/jcb.1.1.59 · Cited by 1,014
High Resolution Structure of the Large Ribosomal Subunit from a Mesophilic Eubacterium
Harms, J. M., Schluenzen, F., Zarivach, R., Bashan, A., Gat, S., Agmon, I., Bartels, H., Franceschi, F. J., & Yonath, A. (2001) · Cell · doi:10.1016/s0092-8674(01)00546-3 · Cited by 899
Cech, T. R., Zaug, A. J., & Grabowski, P. J. (1981) · Cell · doi:10.1016/0092-8674(81)90390-1 · Cited by 879
The kink‐turn: a new RNA secondary structure motif
Klein, D. J., Schmeing, T. M., Moore, P. B., & Steitz, T. A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4214 · Cited by 740
Self-citationRNA tertiary interactions in the large ribosomal subunit: The A-minor motif
Nissen, P., Ippolito, J. A., Ban, N., Moore, P. B., & Steitz, T. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081082398 · Cited by 659
Self-citation
Research works printed but not linked: 1
- Yonath, 1980, Crystallization of the large ribosomal subunits from Bacillus stearothermophilus, Biochem. Internat., 1, 428
Cited by
Sorted by citations
Mattick, J. S., & Makunin, I. V. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl046 · Cited by 2,546
Morris, K. V., & Mattick, J. S. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3722 · Cited by 1,447
Prebiotic chemistry and the origin of the RNA world.
Leslie E., O. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490460765 · Cited by 1,124
Dobson, C. M. (2004) · Nature · doi:10.1038/nature03192 · Cited by 1,033
Benner, S. A., & Sismour, A. M. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1637 · Cited by 834
The world of subinhibitory antibiotic concentrations
DAVIES, J. E., Spiegelman, G. B., & Yim, G. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.08.006 · Cited by 740
Initiation of Protein Synthesis in Bacteria
Laursen, B. S., Sørensen, H. P., Mortensen, K. K., & Petersen, H. U. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.1.101-123.2005 · Cited by 621
Robertson, M. P., & Joyce, G. F. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003608 · Cited by 556
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
Assembly of Bacterial Ribosomes
Shajani, Z., Sykes, M. T., & Williamson, J. R. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062608-160432 · Cited by 505
Klein, D. J., Moore, P. B., & Steitz, T. A. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.03.076 · Cited by 423
Self-citationIsaacs, F. J., Dwyer, D. J., & Collins, J. J. (2006) · Nature Biotechnology · doi:10.1038/nbt1208 · Cited by 384
The catalytic diversity of RNAs
Fedor, M. J., & Williamson, J. R. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1647 · Cited by 358
Natural and engineered nucleic acids as tools to explore biology
Breaker, R. R. (2004) · Nature · doi:10.1038/nature03195 · Cited by 363
Prebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354
Protocells and RNA Self-Replication
Joyce, G. F., & Szostak, J. W. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034801 · Cited by 308
The role of human ribosomal proteins in the maturation of rRNA and ribosome production
Robledo, S. M., Idol, R. A., Crimmins, D. L., Ladenson, J. H., Mason, P. J., & Bessler, M. (2008) · RNA · doi:10.1261/rna.1132008 · Cited by 254
Wolf, Y. I., & Koonin, E. V. (2007) · Biology Direct · doi:10.1186/1745-6150-2-14 · Cited by 235
“The foremost case of a today's natural ribozyme is the ribosome itself, where the crucial peptidyltransferase reaction is catalyzed by large-subunit rRNA without direct participation of proteins [59-61].”
BackgroundThe 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
How a neutral evolutionary ratchet can build cellular complexity
Lukeš, J., Archibald, J. M., Keeling, P. J., Doolittle, W. F., & Gray, M. W. (2011) · IUBMB Life · doi:10.1002/iub.489 · Cited by 203
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
Ribozyme Catalysis of Metabolism in the RNA World
Chen, X., Li, N., & Ellington, A. D. (2007) · Chemistry & Biodiversity · doi:10.1002/cbdv.200790055 · Cited by 196
Eschenmoser, A. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201103672 · Cited by 193
Ribosomal Proteins in the Spotlight
Wilson, D. N., & Nierhaus, K. H. (2005) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230500256523 · Cited by 193
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
Expanding roles for diverse physical phenomena during the origin of life
Budin, I., & Szostak, J. W. (2010) · Annual Review of Biophysics · doi:10.1146/annurev.biophys.050708.133753 · Cited by 171
Chandonia, J., Fox, N. K., & Brenner, S. E. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1134 · Cited by 167
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
Prebiotic Systems Chemistry: Complexity Overcoming Clutter
Islam, S., & Powner, M. W. (2017) · Chem · doi:10.1016/j.chempr.2017.03.001 · Cited by 154
Regulation of ribosome biogenesis in skeletal muscle hypertrophy
Figueiredo, V. C., & McCarthy, J. J. (2019) · Physiology · doi:10.1152/physiol.00034.2018 · Cited by 140
Scott, W. G. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.05.003 · Cited by 124
Mechanisms of elongation on the ribosome: dynamics of a macromolecular machine
Wintermeyer, W., Peske, F., Beringer, M., Gromadski, K. B., Savelsbergh, A., & Rodnina, M. V. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320733 · Cited by 123
Waku, T., Nakajima, Y., Yokoyama, W., Nomura, N., Kako, K., Kobayashi, A., Shimizu, T., & Fukamizu, A. (2016) · Journal of Cell Science · doi:10.1242/jcs.183723 · Cited by 115
Lapeyre, B., & Purushothaman, S. K. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.022 · Cited by 112
Evolutionary dynamics of RNA-like replicator systems: A bioinformatic approach to the origin of life
Takeuchi, N., & Hogeweg, P. (2012) · Physics of Life Reviews · doi:10.1016/j.plrev.2012.06.001 · Cited by 114
Coenzymes and their role in the evolution of life
Kirschning, A. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.201914786 · Cited by 107
The Conservation and Function of RNA Secondary Structure in Plants
Vandivier, L. E., Anderson, S. J., Foley, S. W., & Gregory, B. D. (2016) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-043015-111754 · Cited by 103
Koonin, E. V. (2007) · Biology Direct · doi:10.1186/1745-6150-2-15 · Cited by 97
“Perhaps, most importantly, the large subunit rRNA itself is a ribozyme that catalyzes the peptidyl transferase reaction [50,51].”
BackgroundBokinsky, G., & Zhuang, X. (2005) · Accounts of Chemical Research · doi:10.1021/ar040142o · Cited by 94
Structural Basis of Single-Stranded RNA Recognition
Messias, A. C., & Sattler, M. (2004) · Accounts of Chemical Research · doi:10.1021/ar030034m · Cited by 93
Biondi, E., Branciamore, S., Maurel, M., & Gallori, E. (2007) · BMC Evolutionary Biology · doi:10.1186/1471-2148-7-s2-s2 · Cited by 94
Mg2+-dependent folding of a Diels-Alderase ribozyme probed by single-molecule FRET analysis
Kobitski, A., Nierth, A., Helm, M., Jäschke, A., & Nienhaus, G. U. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm072 · Cited by 81
Müller, U. F. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6047-1 · Cited by 79
An Interpretive Review of the Origin of Life Research
Penny, D. (2005) · Biology & Philosophy · doi:10.1007/s10539-004-7342-6 · Cited by 77
An mRNA-Derived Noncoding RNA Targets and Regulates the Ribosome
Pircher, A., Bąkowska‐Żywicka, K., Schneider, L., Żywicki, M., & Polacek, N. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.024 · Cited by 76
Molecular Contacts Between Antibiotics and the 30S Ribosomal Particle
Wirmer, J., & Westhof, É. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)15012-0 · Cited by 75
Evolutionary patterns of non-coding RNAs
Bompfünewerer, A. F. (2005) · Theory in Biosciences · doi:10.1016/j.thbio.2005.01.002 · Cited by 75
The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services
Fromm, S. A., O’Connor, K. M., Purdy, M. D., Bhatt, P. R., Loughran, G., Atkins, J. F., Jomaa, A., & Mattei, S. (2023) · Nature Communications · doi:10.1038/s41467-023-36742-3 · Cited by 79
Gene and genon concept: coding versus regulation
Scherrer, K., & Jost, J. (2007) · Theory in Biosciences · doi:10.1007/s12064-007-0012-x · Cited by 75
Riboswitches: From ancient gene-control systems to modern drug targets
Breaker, R. R. (2009) · Future Microbiology · doi:10.2217/fmb.09.46 · Cited by 72
Adaptation of the base-paired double-helix molecular architecture to extreme pressure
Girard, É., Prangé, T., Dhaussy, A., Migianu‐Griffoni, E., Lecouvey, M., Chervin, J. C., Mézouar, M., Kahn, R., & Fourme, R. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm511 · Cited by 70
Goel, A., Eckhardt, T. H., Puri, P., de Jong, A., dos Santos, F. B., Giera, M. A., Fusetti, F., de Vos, W. M., Kok, J., Poolman, B., et al. (2015) · Molecular Microbiology · doi:10.1111/mmi.13012 · Cited by 67
New ligase-derived RNA polymerase ribozymes
LAWRENCE, M. S., & BARTEL, D. P. (2005) · RNA · doi:10.1261/rna.2110905 · Cited by 68
Origins of Life: The Primal Self-Organization
Egel, R., Mulkidjanian, A. Y., & Lankenau, D. (2011) · Springer eBooks · doi:10.1007/978-3-642-21625-1 · Cited by 66
The Origin of Life: Chemical Evolution of a Metabolic System in a Mineral Honeycomb?
Branciamore, S., Gallori, E., Szathmáry, E., & Czárán, T. (2009) · Journal of Molecular Evolution · doi:10.1007/s00239-009-9278-6 · Cited by 63
Prevalence of syn nucleobases in the active sites of functional RNAs
Sokoloski, J. E., Godfrey, S. A., Dombrowski, S. E., & Bevilacqua, P. C. (2011) · RNA · doi:10.1261/rna.2759911 · Cited by 61
Petersson, B., Nielsen, B. B., Rasmussen, H. B., Larsen, I. K., Gajhede, M., Nielsen, P. E., & Kastrup, J. S. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0458726 · Cited by 61
Dynamics‐Based Amplification of RNA Function and Its Characterization by Using NMR Spectroscopy
Al‐Hashimi, H. M. (2005) · ChemBioChem · doi:10.1002/cbic.200500002 · Cited by 59
The Story of RNA Folding, as Told in EpochsPreprint
Herschlag, D., Bonilla, S. L., & Bisaria, N. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032433 · Cited by 57
Crystal structure of Pistol, a class of self-cleaving ribozyme
Nguyen, L. A., Wang, J., & Steitz, T. A. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611191114 · Cited by 56
Self-citationSaccharomyces cerevisiae Ribosomal Protein L26 Is Not Essential for Ribosome Assembly and Function
Babiano, R., Gamalinda, M., Woolford, J. L., & de la Cruz, J. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00539-12 · Cited by 56
Codon Size Reduction as the Origin of the Triplet Genetic Code
Baranov, P. V., Venin, M., & Provan, G. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005708 · Cited by 55
Roles of ribosomal proteins in the functioning of translational machinery of eukaryotes
Graifer, D. M., & Karpova, G. G. (2014) · Biochimie · doi:10.1016/j.biochi.2014.11.016 · Cited by 52
The origin of modern terrestrial life
Forterre, P., & Gribaldo, S. (2007) · HFSP journal · doi:10.2976/1.2759103 · Cited by 73
Efficient Ligation of the Schistosoma Hammerhead Ribozyme
Canny, M. D., Jucker, F. M., & Pardi, A. (2007) · Biochemistry · doi:10.1021/bi062077r · Cited by 53
Meléndez-Hevia, E., Montero-Gómez, N., & Montero, F. (2008) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2007.11.012 · Cited by 52
SMMRNA: a database of small molecule modulators of RNA
Mehta, A., Sonam, S., Gouri, I., Loharch, S., Sharma, D. K., & Parkesh, R. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt976 · Cited by 51
Eschenmoser, A. (2011) · Angewandte Chemie · doi:10.1002/ange.201103672 · Cited by 50
The gene and the genon concept: a functional and information‐theoretic analysis
Scherrer, K., & Jost, J. (2007) · Molecular Systems Biology · doi:10.1038/msb4100123 · Cited by 48
The Peptidyl Transferase Center: a Window to the Past
Tirumalai, M. R., Rivas, M., Tran, Q., & Fox, G. E. (2021) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00104-21 · Cited by 53
Polynucleotides in cellular mimics: Coacervates and lipid vesicles
Vieregg, J., & Tang, T. ‐. D. (2016) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2016.09.004 · Cited by 49
5S rRNA: Structure and Function from Head to Toe.
Dontsova, O. A., & Dinman, J. D. (2005) · Europe PMC (PubMed Central) · Cited by 46
Native Purification and Labeling of RNA for Single Molecule Fluorescence Studies
Rinaldi, A. J., Suddala, K. C., & Walter, N. G. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1896-6_6 · Cited by 45
Structural and functional analysis of 5S rRNA in Saccharomyces cerevisiae
Kiparisov, S. V., Petrov, A. N., Meškauskas, A., Владимирович, С. П., Dontsova, O. А., & Dinman, J. D. (2005) · Molecular Genetics and Genomics · doi:10.1007/s00438-005-0020-9 · Cited by 45
Sharma, P., Chawla, M., Sharma, S., & Mitra, A. (2010) · RNA · doi:10.1261/rna.1919010 · Cited by 42
Using softer X-ray absorption spectroscopy to probe biological systems
Akabayov, B., Doonan, C. J., Pickering, I. J., George, G. N., & Sagi, I. (2005) · Journal of Synchrotron Radiation · doi:10.1107/s0909049505010150 · Cited by 41
The Emergence of Cells During the Origin of Life
Chen, I. A. (2006) · Science · doi:10.1126/science.1137541 · Cited by 42
Structure and function of regulatory RNA elements: Ribozymes that regulate gene expression
Scott, W. G., Martick, M. M., & Chi, Y. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.09.006 · Cited by 37
Takeuchi, N., & Hogeweg, P. (2007) · Journal of Molecular Evolution · doi:10.1007/s00239-007-9044-6 · Cited by 36
Biondi, E., Branciamore, S., Fusi, L., Gago‐Zachert, S., & Gallori, E. (2006) · Gene · doi:10.1016/j.gene.2006.09.002 · Cited by 38
Ribosomal Protein L3: Influence on Ribosome Structure and Function
Petrov, A. N., Meškauskas, A., & Dinman, J. D. (2004) · RNA Biology · doi:10.4161/rna.1.1.957 · Cited by 37
Inhibition of Ricin A-Chain with Pyrrolidine Mimics of the Oxacarbenium Ion Transition State
Roday, S., Amukele, T. K., Evans, G. B., Tyler, P. C., Furneaux, R. H., & Schramm, V. L. (2004) · Biochemistry · doi:10.1021/bi0498499 · Cited by 37
Okuda, K., Seila, A. C., & Strobel, S. A. (2005) · Biochemistry · doi:10.1021/bi047419c · Cited by 37
Monnard, P., & Ziock, H. J. (2008) · Chemistry & Biodiversity · doi:10.1002/cbdv.200890141 · Cited by 37
Steitz, T. A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.11.053 · Cited by 36
Self-citationPiece by piece: Building a ribozyme
Gray, M. W., & Gopalan, V. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.009929 · Cited by 33
Quantum-Mechanical Study on the Mechanism of Peptide Bond Formation in the Ribosome
Acosta‐Silva, C., Bertrán, J., Branchadell, V., & Oliva, A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja209558d · Cited by 34
Hofmeyr, J. S. (2017) · Springer eBooks · doi:10.1007/978-3-319-31737-3_51-1 · Cited by 32
Structure–function relationships in RNA and RNP enzymes: Recent advances
Hoogstraten, C. G., & Sumita, M. (2007) · Biopolymers · doi:10.1002/bip.20836 · Cited by 32
Xiang-rui, L., Zhang, F., Coates, B. S., Zhang, Y., Zhou, X. J., & Cheng, D. (2016) · Scientific Reports · doi:10.1038/srep35668 · Cited by 33
What contemporary viruses tell us about evolution: a personal view
Moelling, K. (2013) · Archives of Virology · doi:10.1007/s00705-013-1679-6 · Cited by 31
Role of epigenetic alterations in aflatoxin‐induced hepatocellular carcinoma
Mungamuri, S. K., & Mavuduru, V. A. (2020) · Liver Cancer International · doi:10.1002/lci2.20 · Cited by 30
GCNCMI: A Graph Convolutional Neural Network Approach for Predicting circRNA-miRNA Interactions
He, J., Xiao, P., Chen, C., Zhu, Z., Zhang, J., & Deng, L. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.959701 · Cited by 30
The human large subunit ribosomal protein L36A-like contacts the CCA end of P-site bound tRNA
Baouz, S., Woisard, A., Sinapah, S., Caër, J. L., Argentini, M., Bulygin, K. N., Aguié, G., & Hountondji, C. (2009) · Biochimie · doi:10.1016/j.biochi.2009.07.013 · Cited by 30
Bayfield, M. A. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh888 · Cited by 32
Cleavage of RNA oligonucleotides by aminoglycosides
Belousoff, M. J., Graham, B., Spiccia, L., & Tor, Y. (2008) · Organic & Biomolecular Chemistry · doi:10.1039/b813252f · Cited by 29
Charafeddine, A., Dayoub, W., Chapuis, H., & Strazewski, P. (2007) · Chemistry - A European Journal · doi:10.1002/chem.200700058 · Cited by 29
Root-Bernstein, R. S., & Root‐Bernstein, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20010140 · Cited by 30
Protein content of minimal and ancestral ribosome
Mushegian, A. R. (2005) · RNA · doi:10.1261/rna.2180205 · Cited by 26
K-Turn Motifs in Spatial RNA Coding
Tiedge, H. (2006) · RNA Biology · doi:10.4161/rna.3.4.3415 · Cited by 27
Metadata
- Authors
- Steitz, T. A., & Moore, P. B.
- Affiliations
- Howard Hughes Medical Institute (US)
- Yale University (US)
- Corresponding author
- Steitz, Thomas A
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2003-08
- Volume
- 28
- Issue
- 8
- Pages
- 411-418
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2162522101
- Cited by
- 319
- References
- 36
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 7 · 2023: 10 · 2022: 7 · 2021: 8 · 2020: 10 · 2019: 7 · 2018: 11 · 2017: 10 · 2016: 13 · 2015: 10 · 2014: 20 · 2013: 10 · 2012: 15
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Agouron Institute
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- ribosome, ribozymes, peptidyl transferase, RNA catalysis, large ribosomal subunit, Haloarcula marismortui, antibiotic resistance, antibiotic binding sites, RNA structure
- MeSH terms
- Drug Resistance, Microbial, Microscopy, Electron, Models, Chemical, Models, Molecular, Nucleic Acid Conformation, Peptide Elongation Factor Tu, Peptidyl Transferases, Protein Binding, Ribosomes, RNA, RNA, Messenger, RNA, Ribosomal, 23S, RNA, Transfer, RNA, Catalytic, Haloarcula marismortui
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