Cited by 399RNA and protein synthesis mechanismsEvolution and Genetic DynamicsProtein Structure and Dynamics

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The frequency of errors in protein biosynthesis

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Loftfield, R B, Vanderjagt, D·1972·Biochemical Journal

DOI 10.1042/bj1281353PMC PMC1174024

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Every protein molecule consists basically of a

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THE FREQUENCY OF ERRORS IN PROTEIN BIOSYNTHESIS
Loftfield, R. B. (1963) · Biochemical Journal · doi:10.1042/bj0890082 · Cited by 160
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Hemoglobin Synthesis in Avian Erythrocytes
Hammel, C. L., & Bessman, S. P. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82224-8 · Cited by 44

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Yamane, T., & Hopfield, J. J. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.6.2246 · Cited by 66
An estimate of the frequency of in vivo transcriptional errors at a nonsense codon in Escherichia coli
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Kirkwood, T. B. L., & Holliday, R. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80038-6 · Cited by 64
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Gruic‐Sovulj, I., Rokov‐Plavec, J., & Weygand-Đurašević, I. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.09.058 · Cited by 61
Structure and Function of Suppressor tRNAs in Higher Eukaryote
Hatfield, D. L., Smith, D. W., Lee, B. J., Worland, P. J., & Oroszlan, S. I. (1990) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239009090606 · Cited by 61
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Igloi, G. L., von der Haar, F., & Cramer, F. (1978) · Biochemistry · doi:10.1021/bi00610a006 · Cited by 60
The role of guanine nucleotides in protein biosynthesis
Kurland, C. G. (1978) · Biophysical Journal · doi:10.1016/s0006-3495(78)85494-0 · Cited by 60
Binding of tyrosine, adenosine triphosphate and analogues to crystalline tyrosyl transfer RNA synthetase
Monteilhet, C., & Blow, D. M. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90418-7 · Cited by 59
Accuracy of initial codon selection by aminoacyl-tRNAs on the mRNA-programmed bacterial ribosome
Zhang, J., Ieong, K.-W., Johansson, M., & Ehrenberg, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1506823112 · Cited by 58
Two proofreading steps amplify the accuracy of genetic code translation
Ieong, K.-W., Uzun, Ü., Selmer, M., & Ehrenberg, M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610917113 · Cited by 57
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Synetos, D., Frantziou, C. P., & Alksne, L. E. (1996) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(96)00128-5 · Cited by 56
Dual Mode Recognition of Two Isoacceptor tRNAs by Mammalian Mitochondrial Seryl-tRNA Synthetase
Shimada, N., Suzuki, T., & Watanabe, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105150200 · Cited by 56
Senescence and the accumulation of abnormal proteins
Rosenberger, R. F. (1991) · Mutation Research/DNAging · doi:10.1016/0921-8734(91)90016-5 · Cited by 56
Ribosome editing and the error catastrophe hypothesis of cellular aging
Menninger, J. R. (1977) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(77)90014-8 · Cited by 56
Electrophoretic Deformation of Individual Transfer RNA Molecules Reveals Their Identity
Henley, R. Y., Ashcroft, B. A., Farrell, I., Cooperman, B. S., Lindsay, S. M., & Wanunu, M. (2015) · Nano Letters · doi:10.1021/acs.nanolett.5b03331 · Cited by 55
The accuracy of aminoacylation — ensuring the fidelity of the genetic code
Söll, D. G. (1990) · Cellular and Molecular Life Sciences · doi:10.1007/bf01936918 · Cited by 55
Multi-stage proofreading in DNA replication
Beckman, R. A., & Loeb, L. A. (1993) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500002869 · Cited by 55
Zinc-mediated Amino Acid Discrimination in Cysteinyl-tRNA Synthetase
Zhang, C., Christian, T., Newberry, K. J., Perona, J. J., & Hou, Y. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00241-9 · Cited by 54
Tests of the ribosomal editing hypothesis: Amino acid starvation differentially enhances the dissociation of peptidyl-tRNA from the ribosome
Caplan, A., & Menninger, J. R. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90370-x · Cited by 54
Fidelity of protein synthesis does not decline during aging of cultured human fibroblasts
Wojtyk, R. I., & Goldstein, S. (1980) · Journal of Cellular Physiology · doi:10.1002/jcp.1041030215 · Cited by 54
tRNA-dependent Pre-transfer Editing by Prokaryotic Leucyl-tRNA Synthetase
Tan, M., Zhu, B., Zhou, X.-L., He, R., Chen, X., Eriani, G., & Wang, E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.060616 · Cited by 53
Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase
Chen, X., Ma, J., Tan, M., Yao, P., Hu, Q., Eriani, G., & Wang, E. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq763 · Cited by 53
tRNA-independent Pretransfer Editing by Class I Leucyl-tRNA Synthetase
Zhu, B., Yao, P., Tan, M., Eriani, G., & Wang, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806717200 · Cited by 53
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Tawfik, D. S., & Gruic‐Sovulj, I. (2019) · FEBS Journal · doi:10.1111/febs.15199 · Cited by 53
Domain-domain communication in aminoacyl-tRNA synthetases
Alexander, R. W., & SCHIMMEL, P. R. (2001) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(01)69050-0 · Cited by 52
Transfer RNA mischarging mediated by a mutant Escherichia coli glutaminyl-tRNA synthetase.
Inokuchi, H., Hoben, P. J., Yamao, F., Ozeki, H., & Söll, D. G. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.16.5076 · Cited by 52
Emergence and Evolution
Bullwinkle, T. J., & Ibba, M. (2013) · Topics in current chemistry · doi:10.1007/128_2013_423 · Cited by 55
Beyond the Triplet Code: Context Cues Transform Translation
Brar, G. A. (2016) · Cell · doi:10.1016/j.cell.2016.09.022 · Cited by 54
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Ou, X., Cao, J., Cheng, A., Peppelenbosch, M. P., & Pan, Q. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008017 · Cited by 54
Mistranslation in cells infected with the bacteriophage MS2: Direct evidence of Lys for Asn substitution
Parker, J., Johnston, T. C., & Borgia, P. T. (1980) · Molecular and General Genetics MGG · doi:10.1007/bf00425839 · Cited by 51
Fidelity Mechanisms of the Aminoacyl-tRNA Synthetases
Mascarenhas, A. P., An, S., Rosen, A. E., Martinis, S. A., & Musier‐Forsyth, K. (2009) · Nucleic acids and molecular biology · doi:10.1007/978-3-540-70941-1_6 · Cited by 50
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Transfer RNA selection at the ribosomal A and P sites
Peters, M., & Yarus, M. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90364-4 · Cited by 50
Error propagation in viable cells
Gallant, J., & Palmer, L. (1979) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(79)90068-x · Cited by 50
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Lin, S., Baltzinger, M., & Rémy, P. (1983) · Biochemistry · doi:10.1021/bi00272a024 · Cited by 49
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Vargas‐Rodriguez, O., & Musier‐Forsyth, K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.467795 · Cited by 49
Codon specificity of starvation induced misreading
Johnston, T. C., Borgia, P. T., & Parker, J. (1984) · Molecular and General Genetics MGG · doi:10.1007/bf00341447 · Cited by 47
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Bouz, G., & Zítko, J. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104806 · Cited by 47
Sieves in Sequence
Fersht, A. R. (1998) · Science · doi:10.1126/science.280.5363.541 · Cited by 46
Mistranslation of the genetic code
Moghal, A., Mohler, K., & Ibba, M. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.08.035 · Cited by 47
Amino acid misincorporation during high-level expression of mouse epidermal growth factor inEscherichia coli
Scorer, C. A., CARRIER, M. J., & Rosenberger, R. F. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.13.3511 · Cited by 45
Isoleucyl-tRNA synthetase from bakers' yeast: multistep proofreading in discrimination between isoleucine and valine with modulated accuracy, a scheme for molecular recognition by energy dissipation
Freist, W., Pardowitz, I., & Cramer, F. (1985) · Biochemistry · doi:10.1021/bi00345a040 · Cited by 45
Twenty-year review of medical findings in a Marshallese population accidentally exposed to radioactive fallout
Brookhaven National Lab., U., & CONARD, R. A. (1975) · doi:10.2172/4148793 · Cited by 45
Selection of tRNA charging quality control mechanisms that increase mistranslation of the genetic code
Yadavalli, S. S., & Ibba, M. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1240 · Cited by 44
Low level genome mistranslations deregulate the transcriptome and translatome and generate proteotoxic stress in yeast
Paredes, J. A., Carreto, L. C., Simões, J., Bezerra, A. R., Gomes, A. C., Santamaría, R., Kapushesky, M., Moura, G., & Santos, M. A. S. (2012) · BMC Biology · doi:10.1186/1741-7007-10-55 · Cited by 44
A stereospecific mechanism for the aminoacyl‐tRNA selection at the ribosome
Potapov, A. P. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80693-5 · Cited by 44
Formation of Two Classes of tRNA Synthetases in Relation to Editing Functions and Genetic CodePreprint
SCHIMMEL, P. R., & de Pouplana, L. R. (2001) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2001.66.161 · Cited by 44
Codon misreading tRNAs promote tumor growth in mice
Santos, M., Pereira, P. M., Varanda, A. S., Carvalho, J., Azevedo, M. C., Mateus, D. D., Mendes, N. M., Oliveira, P., Trindade, F., Pinto, M. T., et al. (2018) · RNA Biology · doi:10.1080/15476286.2018.1454244 · Cited by 45
Leucyl‐tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution
Zhao, M., Zhu, B., Hao, R., Xu, M.-G., Eriani, G., & Wang, E. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600618 · Cited by 42
Genetic selection for mistranslation rescues a defective co-chaperone in yeast
Hoffman, K. S., Berg, M. D., Shilton, B. H., Brandl, C. J., & O’Donoghue, P. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1021 · Cited by 42
Conservation of ribosomal fidelity during ageing
Mori, N., Mizuno, D., & Goto, S. (1979) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(79)90020-4 · Cited by 42
Exposure to BMAA mirrors molecular processes linked to neurodegenerative disease
Beri, J., Nash, T. E., Martin, R. M., & Bereman, M. S. (2017) · PROTEOMICS · doi:10.1002/pmic.201700161 · Cited by 41
The fidelity of the translation of the genetic code.
Sankaranarayanan, R., & Moras, D. (2001) · Acta Biochimica Polonica · doi:10.18388/abp.2001_3918 · Cited by 41
Energy cost of proofreading to increase fidelity of transfer ribonucleic acid aminoacylation
Savageau, M. A., & Freter, R. R. (1979) · Biochemistry · doi:10.1021/bi00583a008 · Cited by 41
Errors from Selective Disruption of the Editing Center in a tRNA Synthetase
Hendrickson, T. L., Nomanbhoy, T. K., & SCHIMMEL, P. R. (2000) · Biochemistry · doi:10.1021/bi0004798 · Cited by 41
Editing activity for eliminating mischarged tRNAs is essential in mammalian mitochondria
Hilander, T., Zhou, X.-L., Konovalova, S. A., Zhang, F., Euro, L., Chilov, D., POUTANEN, M. H., Chihade, J. W., Wang, E., & Tyynismaa, H. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1231 · Cited by 42
Induced Fit and Kinetic Mechanism of Adenylation Catalyzed by Escherichia coli Threonyl-tRNA Synthetase
Bovée, M., Pierce, M. A., & Francklyn, C. S. (2003) · Biochemistry · doi:10.1021/bi0355701 · Cited by 40
Elongation factor Tu can reduce translation errors in poly(U)-directed cell-free systems
Gavrilova, L. P., Perminova, I. N., & Spirin, A. S. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90260-6 · Cited by 40
Progressive decrease in protein synthesis accuracy induced by streptomycin in Escherichia coli
Branscomb, E., & Galas, D. J. (1975) · Nature · doi:10.1038/254161a0 · Cited by 40
Modification of the amino acid specificity of tyrosyl‐tRNA synthetase by protein engineering
Gay, G. D. P., Duckworth, H. W., & Fersht, A. R. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80014-l · Cited by 39
Model for messenger RNA translation during amino acid starvation applied to the calculation of protein synthetic error rates.
Harley, C. B., Pollard, J. W., Stanners, C. P., & Goldstein, S. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68511-x · Cited by 38
Isoleucyl-tRNA synthetase from baker's yeast and from Escherichia coli MRE 600. Discrimination of 20 amino acids in aminoacylation of tRNAIle-C-C-A(3'NH2)
Freist, W., Sternbach, H., & Cramer, F. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13577.x · Cited by 38
The role of RNA polymerase in transcriptional fidelity
Libby, R. T., & Gallant, J. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb01872.x · Cited by 37
Growth and death of diploid and transformed human fibroblasts
Holliday, R. (1975) · Springer eBooks · doi:10.1007/978-1-4684-2631-1_11 · Cited by 37
Codon recognition fidelity of ribosomes at the first and second positions does not decrease during aging
Mori, N., Hiruta, K., Funatsu, Y., & Goto, S. (1983) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(83)90002-7 · Cited by 36
Genetic Code Ambiguity Confers a Selective Advantage on Acinetobacter baylyi
Bacher, J. M., Waas, W. F., Metzgar, D., de Crécy‐Lagard, V., & SCHIMMEL, P. R. (2007) · Journal of Bacteriology · doi:10.1128/jb.00622-07 · Cited by 37
Characterization and biosynthesis of cytochrome b5 in rat liver microsomes
SARGENT, J. R., & Vadlamudi, B. (1968) · Biochemical Journal · doi:10.1042/bj1070839 · Cited by 36
A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia
Kuncha, S. K., Mazeed, M., Singh, R. P., Kattula, B., Routh, S. B., & Sankaranarayanan, R. (2018) · Nature Communications · doi:10.1038/s41467-017-02204-w · Cited by 35
On the Role of Ribosylthymine in Prokaryotic tRNA Function
Kersten, H., Albani, M., MÄNNLEIN, E., PRAISLER, R., Wurmbach, P., & Nierhaus, K. H. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb05166.x · Cited by 35
Mutational Analysis Suggests the Same Design for Editing Activities of Two tRNA Synthetases
Lin, L., & SCHIMMEL, P. R. (1996) · Biochemistry · doi:10.1021/bi960011y · Cited by 35
On the evolution of accuracy and cost of proofreading tRNA aminoacylation.
Savageau, M. A., & Freter, R. R. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4507 · Cited by 34
Yeast tRNAAsp Charging Accuracy Is Threatened by the N-terminal Extension of Aspartyl-tRNA Synthetase
Ryckelynck, M., Giegé, R., & Frugier, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211035200 · Cited by 34
Divergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischarging
Rogers, K. C., & S�ll, D. (1995) · Journal of Molecular Evolution · doi:10.1007/bf00166615 · Cited by 34
Proteome-wide measurement of non-canonical bacterial mistranslation by quantitative mass spectrometry of protein modifications
Cvetešić, N., Šemanjski, M., Soufi, B., Krug, K., Gruic‐Sovulj, I., & Maček, B. (2016) · Scientific Reports · doi:10.1038/srep28631 · Cited by 34
Amino acid misincorporation in recombinant proteins
Wong, H. E., Huang, C., & Zhang, Z. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.10.006 · Cited by 34
Evolutionary aspects of accuracy of phenylalanyl-tRNA synthetase. A comparative study with enzymes from Escherichia coli, Saccharomyces cerevisiae, Neurospora crassa, and turkey liver using phenylalanine analogs
Gabius, H., von der Haar, F., & Cramer, F. (1983) · Biochemistry · doi:10.1021/bi00279a005 · Cited by 33
Kinetic Quality Control of Anticodon Recognition by a Eukaryotic Aminoacyl-tRNA Synthetase
Liu, C., Gamper, H., Shtivelband, S., Hauenstein, S. I., Perona, J. J., & Hou, Y. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.01.050 · Cited by 32
Mistranslation during phenylalanine starvation
Parker, J., & Precup, J. W. (1986) · Molecular and General Genetics MGG · doi:10.1007/bf00330189 · Cited by 32
Ex-translational function of tRNAs and their fragments in cancer.
Mleczko, A. M., Celichowski, P., & Bąkowska‐Żywicka, K. (2014) · Acta Biochimica Polonica · doi:10.18388/abp.2014_1888 · Cited by 31
In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity
Splan, K. E., Musier‐Forsyth, K., Boniecki, M. T., & Martinis, S. A. (2008) · Methods · doi:10.1016/j.ymeth.2007.10.009 · Cited by 31
A threonyl-tRNA synthetase-like protein has tRNA aminoacylation and editing activities
Chen, Y., Ruan, Z.-R., Wang, Y., Huang, Q., Xue, M.-Q., Zhou, X.-L., & Wang, E. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky211 · Cited by 31
The Mechanism of Action of Methionyl‐tRNA Synthetase
Blanquet, S., Pétrissant, G., & Waller, J. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb02904.x · Cited by 31
Isoleucyl‐tRNA synthetase from baker's yeast and from Escherichia coli MRE 600
Freist, W., Sternbach, H., & Cramer, F. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb13962.x · Cited by 31
The G3-U70-independent tRNA recognition by human mitochondrial alanyl-tRNA synthetase
Zeng, Q., Peng, G.-X., Li, G., Zhou, J.-B., Zheng, W.-Q., Xue, M.-Q., Wang, E., & Zhou, X.-L. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz078 · Cited by 30
Making connections: RNA-dependent amino acid recognition
SCHIMMEL, P. R., & Schmidt, E. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)88937-9 · Cited by 30
The tRNA A76 Hydroxyl Groups Control Partitioning of the tRNA-dependent Pre- and Post-transfer Editing Pathways in Class I tRNA Synthetase
Cvetešić, N., Biluš, M., & Gruic‐Sovulj, I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.648568 · Cited by 29
Determinants for tRNA-Dependent Pretransfer Editing in the Synthetic Site of Isoleucyl-tRNA Synthetase
Dulić, M., Perona, J. J., & Gruic‐Sovulj, I. (2014) · Biochemistry · doi:10.1021/bi5007699 · Cited by 29
Amino Acid Discrimination by a Highly Differentiated Metal Center of an Aminoacyl-tRNA Synthetase
Zhang, C., Perona, J. J., & Hou, Y. (2003) · Biochemistry · doi:10.1021/bi034812u · Cited by 29
Couplings between the sites for methionine and adenosine 5'-triphosphate in the amino acid activation reaction catalyzed by trypsin-modified methionyl-transfer RNA synthetase from Escherichia coli
Fayat, G., Fromant, M., & Blanquet, S. (1977) · Biochemistry · doi:10.1021/bi00630a039 · Cited by 29
Unique Residues Crucial for Optimal Editing in Yeast Cytoplasmic Leucyl-tRNA Synthetase Are Revealed by Using a Novel Knockout Yeast Strain
Yao, P., Zhou, X.-L., He, R., Xue, M.-Q., Zheng, Y.-G., Wang, Y.-F., & Wang, E. D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801181200 · Cited by 28

Authors: Loftfield, R. B., & Vanderjagt, D.
Affiliations: University of New Mexico (US)
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1972-08-01
Volume: 128
Issue: 5
Pages: 1353-1356
ISSN: 0306-3283 (ISSN-L)
DOI: 10.1042/bj1281353
PMC: PMC1174024
OpenAlex: W1923250545
Cited by: 399
References: 3
Citations by year: 2026: 7 · 2025: 3 · 2024: 6 · 2023: 5 · 2022: 8 · 2021: 5 · 2020: 5 · 2019: 8 · 2018: 9 · 2017: 11 · 2016: 12 · 2015: 7 · 2014: 15 · 2013: 8 · 2012: 7
FWCI: 2.35
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: protein synthesis, error rate, translation errors, protein synthesis fidelity, aminoacyl-tRNA
MeSH terms: Amino Acid Sequence, Animals, DNA, Genetic Code, Hemoglobins, Hemoglobins, Abnormal, Humans, Rabbits, Reticulocytes, RNA, Transcription, Genetic, Protein Biosynthesis, In Vitro Techniques

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The frequency of errors in protein biosynthesis

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