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

The DOI matches its Crossref record; 2 of the 3 references it cites were found in a registry or an index.

The frequency of errors in protein biosynthesis

Open access

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

DOI 10.1042/bj1281353PMC PMC1174024

Open this paper in CoChat — free account Open PDF

Abstract

Every protein molecule consists basically of a

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1042/bj1281353

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

THE FREQUENCY OF ERRORS IN PROTEIN BIOSYNTHESIS
Loftfield, R. B. (1963) · Biochemical Journal · doi:10.1042/bj0890082 · Cited by 160
Self-citation
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

Flagged first, then by citations

Show all 3 references

1 of the 3 references couldn’t be matched to a known paper.

Sorted by citations

Evolution of the mutation rate
Lynch, M. (2010) · Trends in Genetics · doi:10.1016/j.tig.2010.05.003 · Cited by 1,175
How many human proteoforms are there?
Aebersold, R., Agar, J. N., Amster, I. J., Baker, M. S., Bertozzi, C. R., Boja, E. S., Costello, C. E., Cravatt, B. F., Fenselau, C., Garcia, B. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/nchembio.2576 · Cited by 907
In and Out of the ER: Protein Folding, Quality Control, Degradation, and Related Human Diseases
Hebert, D. N., & Molinari, M. (2007) · Physiological Reviews · doi:10.1152/physrev.00050.2006 · Cited by 704
Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
Lee, J.-W., Beebe, K. D., Nangle, L. A., Jang, J.-S., Longo-Guess, C. M., Cook, S. A., Davisson, M. T., Sundberg, J. P., SCHIMMEL, P. R., & Ackerman, S. L. (2006) · Nature · doi:10.1038/nature05096 · Cited by 591
STRUCTURAL INSIGHTS INTO TRANSLATIONAL FIDELITY
Ogle, J. M., & Ramakrishnan, V. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.061903.155440 · Cited by 596
The evolutionary consequences of erroneous protein synthesis
Allan Drummond, D., & Wilke, C. O. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2662 · Cited by 515
RNA Virus Populations as Quasispecies
Holland, J. J., de la Torre, J. C., & Steinhauer, D. A. (1992) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-77011-1_1 · Cited by 515
Recent Evidence for Evolution of the Genetic Code
Jukes, T. H., & Osawa, S. (1991) · Springer eBooks · doi:10.1007/978-4-431-68302-5_6 · Cited by 506
Aminoacyl-tRNA synthetases
Rubio, M. Á., & Ibba, M. (2020) · RNA · doi:10.1261/rna.071720.119 · Cited by 478
Errors and alternatives in reading the universal genetic code
Parker, J. (1989) · Microbiological Reviews · doi:10.1128/mr.53.3.273-298.1989 · Cited by 457
The frequency of translational misreading errors in E. coli is largely determined by tRNA competition
Kramer, E. B., & Farabaugh, P. J. (2006) · RNA · doi:10.1261/rna.294907 · Cited by 442
Lack of evidence for proofreading mechanisms associated with an RNA virus polymerase
Steinhauer, D. A., Domingo, E., & Holland, J. J. (1992) · Gene · doi:10.1016/0378-1119(92)90216-c · Cited by 415
Insights into Editing from an Ile-tRNA Synthetase Structure with tRNA Ile and Mupirocin
Silvian, L. F., Wang, J., & Steitz, T. A. (1999) · Science · doi:10.1126/science.285.5430.1074 · Cited by 403
Structure of tyrosyl-tRNA synthetase refined at 2.3 Å resolution
Brick, P., Bhat, T. N., & Blow, D. M. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90090-9 · Cited by 376
Aminoacyl-tRNA Synthesis and Translational Quality Control
Ling, J., Reynolds, N. M., & Ibba, M. (2009) · Annual Review of Microbiology · doi:10.1146/annurev.micro.091208.073210 · Cited by 368
Fidelity of Aminoacyl-tRNA Selection on the Ribosome: Kinetic and Structural Mechanisms
Rodnina, M. V., & Wintermeyer, W. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.415 · Cited by 334
Editing of errors in selection of amino acids for protein synthesis
Jakubowski, H., & Goldman, E. (1992) · Microbiological Reviews · doi:10.1128/mr.56.3.412-429.1992 · Cited by 305
Proteomic and interactomic insights into the molecular basis of cell functional diversity
Bludau, I., & Aebersold, R. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0231-2 · Cited by 297
Nucleoside triphosphate regeneration decreases the frequency of translation errors.
Jelenc, P. C., & Kurland, C. G. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.7.3174 · Cited by 293
Mistranslation in E. coli
Edelmann, P. L., & Gallant, J. (1977) · Cell · doi:10.1016/0092-8674(77)90147-7 · Cited by 285
Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase
Fersht, A. R. (1977) · Biochemistry · doi:10.1021/bi00624a034 · Cited by 231
Quality Control Mechanisms During Translation
Ibba, M., & Söll, A. D. (1999) · Science · doi:10.1126/science.286.5446.1893 · Cited by 223
Structural and Mechanistic Basis of Pre- and Posttransfer Editing by Leucyl-tRNA Synthetase
Lincecum, T. L., Tukalo, M. A., Yaremchuk, A. D., Mursinna, R. S., Williams, A. M., Sproat, B. S., Eynde, W. V. D., Link, A., Calenbergh, S. V., Grøtli, M., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00098-4 · Cited by 218
Translational fidelity and mistranslation in the cellular response to stress
Mohler, K., & Ibba, M. (2017) · Nature Microbiology · doi:10.1038/nmicrobiol.2017.117 · Cited by 204
Base pairing and fidelity in codon–anticodon interaction
Topal, M. D., & Fresco, J. R. (1976) · Nature · doi:10.1038/263289a0 · Cited by 202
The suppression of defective translation by ppGpp and its role in the stringent response
O’Farrell, P. H. (1978) · Cell · doi:10.1016/0092-8674(78)90241-6 · Cited by 198
Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing
Fersht, A. R., & Kaethner, M. M. (1976) · Biochemistry · doi:10.1021/bi00660a026 · Cited by 193
Transfer RNA–Mediated Editing in Threonyl-tRNA Synthetase
Dock‐Brégeon, A., Sankaranarayanan, R., Romby, P., Caillet, J., Springer, M., Rees, B., Francklyn, C. S., Ehresmann, C., & Moras, D. (2000) · Cell · doi:10.1016/s0092-8674(00)00191-4 · Cited by 188
Enlarging the Amino Acid Set of Escherichia coli by Infiltration of the Valine Coding Pathway
Döring, V., Mootz, H. D., Nangle, L. A., Hendrickson, T. L., de Crécy‐Lagard, V., SCHIMMEL, P. R., & Marlière, P. (2001) · Science · doi:10.1126/science.1057718 · Cited by 183
Codon‐specific missense errors in vivo.
Bouadloun, F., Donner, D., & Kurland, C. G. (1983) · The EMBO Journal · doi:10.1002/j.1460-2075.1983.tb01591.x · Cited by 175
Protein synthesis and quality control in aging
Anisimova, A. S., Alexandrov, A. I., Makarova, N. E., Gladyshev, V. N., & Dmitriev, S. E. (2018) · Aging · doi:10.18632/aging.101721 · Cited by 172
In vitro and in vivo modifications of recombinant and human IgG antibodies
Liu, H., Ponniah, G., Zhang, H., Nowak, C., Neill, A., Gonzalez, N., Patel, R., Cheng, G. C., Kita, A., & Andrien, B. A. (2014) · mAbs · doi:10.4161/mabs.29883 · Cited by 174
Leaky termination at premature stop codons antagonizes nonsense-mediated mRNA decay in S. cerevisiae
Keeling, K. M., Lanier, J., Du, M., Salas-Marco, J., Gao, L., Kaenjak, A., & Bedwell, D. M. (2004) · RNA · doi:10.1261/rna.5147804 · Cited by 169
tRNA synthetase: tRNA aminoacylation and beyond
Pang, Y. L. J., Poruri, K., & Martinis, S. A. (2014) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1224 · Cited by 179
Translational dynamics
Nygârd, O., & NILSSON, L. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19087.x · Cited by 162
Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshiftPreprint
Brégeon, D., Colot, V., Radman, M., & Taddéi, F. (2001) · Genes & Development · doi:10.1101/gad.207701 · Cited by 161
Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases
Jakubowski, H., & Fersht, A. R. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.13.3105 · Cited by 156
Protein mistranslation: friend or foe?
de Pouplana, L. R., Santos, M. A. S., Zhu, J., Farabaugh, P. J., & Javid, B. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.06.002 · Cited by 155
Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase
Sankaranarayanan, R., Dock‐Brégeon, A., Rees, B., Bovée, M., Caillet, J., Romby, P., Francklyn, C. S., & Moras, D. (2000) · Nature Structural Biology · doi:10.1038/75856 · Cited by 149
Cellular mechanisms that control mistranslation
Reynolds, N. M., Lazazzera, B. A., & Ibba, M. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2472 · Cited by 147
The tRNA identity landscape for aminoacylation and beyond
Giegé, R., & Eriani, G. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad007 · Cited by 141
Stuttering: high-level mistranslation in animal and bacterial cells.
Parker, J., Pollard, J. W., Friesen, J. D., & Stanners, C. P. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.3.1091 · Cited by 135
Accuracy of in Vivo Aminoacylation Requires Proper Balance of tRNA and Aminoacyl-tRNA Synthetase
Swanson, R., Hoben, P. J., Sumner-Smith, M., Uemura, H., Watson, L. A., & Söll, D. G. (1988) · Science · doi:10.1126/science.3144042 · Cited by 135
Transfer RNAs: diversity in form and function
Berg, M. D., & Brandl, C. J. (2020) · RNA Biology · doi:10.1080/15476286.2020.1809197 · Cited by 151
Quality control in aminoacyl-tRNA synthesis
Yadavalli, S. S., & Ibba, M. (2012) · Advances in protein chemistry and structural biology · doi:10.1016/b978-0-12-386497-0.00001-3 · Cited by 128
Direct experimental evidence for kinetic proofreading in amino acylation of tRNAIle.
Hopfield, J. J., Yamane, T., Yue, V. T., & Coutts, S. M. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.4.1164 · Cited by 126
The evolution of a universal genetic code
Wong, J. T.-F. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.7.2336 · Cited by 120
Global Effects of Mistranslation from an Editing Defect in Mammalian Cells
Nangle, L. A., Motta, C. M., & SCHIMMEL, P. R. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.08.011 · Cited by 121
Rate and accuracy of bacterial protein synthesis revisited
Johansson, M., Lovmar, M., & Ehrenberg, M. (2008) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.02.015 · Cited by 117
Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine
Brick, P., & Blow, D. M. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90376-7 · Cited by 115
Naturally occurring aminoacyl-tRNA synthetases editing-domain mutations that cause mistranslation in Mycoplasma parasites
Li, L., Boniecki, M. T., Jaffe, J. D., Imai, B. S., Yau, P. M., Luthey-Schulten, Z. A., & Martinis, S. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016460108 · Cited by 110
Achieving Error-Free Translation
Dock‐Brégeon, A., Rees, B., Torres‐Larios, A., Bey, G., Caillet, J., & Moras, D. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.002 · Cited by 110
tRNA properties help shape codon pair preferences in open reading frames
Buchan, J. R. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj488 · Cited by 108
Adaptive evolution of genomically recoded Escherichia coli
Wannier, T. M., Kunjapur, A. M., Rice, D. P., McDonald, M. J., Desai, M. M., & Church, G. M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715530115 · Cited by 109
Yeast Ribosomal Protein L24 Affects the Kinetics of Protein Synthesis and Ribosomal Protein L39 Improves Translational Accuracy, While Mutants Lacking Both Remain Viable
Dresios, J., Derkatch, I. L., Liebman, S. W., & Synetos, D. (2000) · Biochemistry · doi:10.1021/bi9925266 · Cited by 107
Thermodynamic constraints on kinetic proofreading in biosynthetic pathways
Ehrenberg, M., & Blomberg, C. (1980) · Biophysical Journal · doi:10.1016/s0006-3495(80)85063-6 · Cited by 106
Aminoacyl‐tRNA Synthetases: Some Recent Results and Achievements
Kisselev, L. L., & Favorova, O. O. (1974) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122853.ch5 · Cited by 106
Deletion of a Conserved, Central Ribosomal Intersubunit RNA Bridge
Ali, I. K., Lancaster, L., Feinberg, J. S., Joseph, S., & Noller, H. F. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.011 · Cited by 106
Misincorporation of amino acid analogues into proteins by biosynthesis
Rodgers, K. J., & Shiozawa, N. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.01.009 · Cited by 105
The accuracy of protein biosynthesis is limited by its speed: high fidelity selection by ribosomes of aminoacyl-tRNA ternary complexes containing GTP[gamma S]
Thompson, R. C., & Karim, A. M. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.16.4922 · Cited by 102
An estimate of the global error frequency in translation
Ellis, N. A., & Gallant, J. (1982) · Molecular and General Genetics MGG · doi:10.1007/bf00332670 · Cited by 101
Missense misreading of asparagine codons as a function of codon identity and context.
Precup, J. W., & Parker, J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60966-4 · Cited by 99
Attenuation of the Editing Activity of theEscherichia coliLeucyl-tRNA Synthetase Allows Incorporation of Novel Amino Acids into Proteins in Vivo
Tang, Y., & Tirrell, D. A. (2002) · Biochemistry · doi:10.1021/bi026130x · Cited by 99
Amino Acid Discrimination by a Class I Aminoacyl-tRNA Synthetase Specified by Negative Determinants
Bullock, T. L., Uter, N. T., Nissan, T. A., & Perona, J. J. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00305-x · Cited by 98
Influence of modification next to the anticodon in tRNA on codon context sensitivity of translational suppression and accuracy
Bouadloun, F., Srichaiyo, T., Isaksson, L. A., & Björk, G. R. (1986) · Journal of Bacteriology · doi:10.1128/jb.166.3.1022-1027.1986 · Cited by 94
Missense translation errors in Saccharomyces cerevisiae
Stansfield, I., Jones, K. M., Herbert, P., Lewendon, A., Shaw, W. V., & Tuite, M. F. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1976 · Cited by 91
A critical review of the postulated role of the non-essential amino acid, β-N-methylamino-L-alanine, in neurodegenerative disease in humans
Chernoff, N., Hill, D., Diggs, D. L., Faison, B. D., Francis, B. M., Lang, J. R., Larue, M. M., Le, T. T., Loftin, K. A., Lugo, J. N., et al. (2017) · Journal of Toxicology and Environmental Health Part B · doi:10.1080/10937404.2017.1297592 · Cited by 95
Discrete Determinants in Transfer RNA for Editing and Aminoacylation
Hale, S. P., Auld, D. S., Schmidt, E., & SCHIMMEL, P. R. (1997) · Science · doi:10.1126/science.276.5316.1250 · Cited by 91
Evolution of a Transfer RNA Gene Through a Point Mutation in the Anticodon
Saks, M. E., Sampson, J. R., & Abelson, J. N. (1998) · Science · doi:10.1126/science.279.5357.1665 · Cited by 91
Structure, Assembly, and Function of Ribosomes
Nierhaus, K. H. (1982) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-68318-3_3 · Cited by 91
tRNA-dependent Aminoacyl-adenylate Hydrolysis by a Nonediting Class I Aminoacyl-tRNA Synthetase
Gruic‐Sovulj, I., Uter, N. T., Bullock, T. L., & Perona, J. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414260200 · Cited by 90
Probing the limits of protein-amino acid side chain recognition with the aminoacyl-tRNA synthetases. Discrimination against phenylalanine by tyrosyl-tRNA synthetases
Fersht, A. R., Shindler, J. S., & Tsui, W.-C. (1980) · Biochemistry · doi:10.1021/bi00565a009 · Cited by 90
Allosteric mechanism for codon-dependent tRNA selection on ribosomes.
Kurland, C. G., Rigler, R. W., Ehrenberg, M., & Blomberg, C. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.11.4248 · Cited by 90
Deficiencies in tRNA synthetase editing activity cause cardioproteinopathy
Liu, Y., Satz, J. S., Vo, M., Nangle, L. A., SCHIMMEL, P. R., & Ackerman, S. L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420196111 · Cited by 88
Protein synthetic errors do not increase during aging of cultured human fibroblasts.
Harley, C. B., Pollard, J. W., Chamberlain, J. W., Stanners, C. P., & Goldstein, S. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.4.1885 · Cited by 88
Resampling and Editing of Mischarged tRNA Prior to Translation Elongation
Ling, J., So, B. R., Yadavalli, S. S., Roy, H., Shoji, S., Fredrick, K. L., Musier‐Forsyth, K., & Ibba, M. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.031 · Cited by 87
“Two out of three” codon reading leading to mistranslation in vivo
Parker, J., & Friesen, J. D. (1980) · Molecular and General Genetics MGG · doi:10.1007/bf00271482 · Cited by 87
Sequences that direct significant levels of frameshifting are frequent in coding regions of Escherichia coli
Gurvich, O. L., Baranov, P. V., Zhou, J., Hammer, A. W., Gesteland, R. F., & Atkins, J. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg561 · Cited by 87
Discovery of a potent benzoxaborole-based anti-pneumococcal agent targeting leucyl-tRNA synthetase
Hu, Q., Liu, R., Fang, Z., Zhang, J., Ding, Y., Tan, M., Wang, M., Pan, W. X., Zhou, H., & Wang, E. (2013) · Scientific Reports · doi:10.1038/srep02475 · Cited by 86
The Evolution of Multimeric Protein Assemblages
Lynch, M. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msr300 · Cited by 86
Artificially ambiguous genetic code confers growth yield advantage
Pezo, V., Metzgar, D., Hendrickson, T. L., Waas, W. F., Hazebrouck, S., Döring, V., Marlière, P., SCHIMMEL, P. R., & de Crécy‐Lagard, V. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402893101 · Cited by 83
The proofreading of hydroxy analogues of leucine and isoleucine by leucyl-tRNA synthetases fromE. coliand yeast
Englisch, S., ENGLISCH, U., von der Haar, F., & Cramer, F. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.19.7529 · Cited by 82
Aminoglycoside suppression at UAG, UAA and UGA codons inEscherichia coli and human tissue culture cells
Martin, R., Mogg, A. E., Heywood, L. A., Nitschke, L., & Burke, J. F. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf02464911 · Cited by 82
The Evolving Trna Molecul
Cedergren, R., Sankoff, D., Larue, B., Grosjean, H., & Söil, D. (1981) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238109108699 · Cited by 82
The structures and functions of transfer RNA
Goddard, J. P. (1978) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(78)90021-4 · Cited by 82
Oxidation of cellular amino acid pools leads to cytotoxic mistranslation of the genetic code
Bullwinkle, T. J., Reynolds, N. M., Raina, M., Moghal, A., Matsa, E., Rajkovic, A., Kayadibi, H., Fazlollahi, F., Ryan, C., Howitz, N., et al. (2014) · eLife · doi:10.7554/elife.02501 · Cited by 80
Aminoacyl-tRNA synthetases: A new image for a classical family
Martinis, S. A., Plateau, P., Cavarelli, J., & Florentz, C. (1999) · Biochimie · doi:10.1016/s0300-9084(99)80126-6 · Cited by 80
The balance between pre‐ and post‐transfer editing in tRNA synthetases
Martinis, S. A., & Boniecki, M. T. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.11.071 · Cited by 78
Identification of Codon-Specific Serine to Asparagine Mistranslation in Recombinant Monoclonal Antibodies by High-Resolution Mass Spectrometry
Yu, X. C., Borisov, O. V., Alvarez, M., Michels, D. A., Wang, Y. J., & Ling, V. (2009) · Analytical Chemistry · doi:10.1021/ac901541h · Cited by 77
Cysteinyl-tRNA synthetase from Escherichia coli does not need an editing mechanism to reject serine and alanine. High binding energy of small groups in specific molecular interactions
Fersht, A. R., & Dingwall, C. (1979) · Biochemistry · doi:10.1021/bi00574a020 · Cited by 76
Physics and the riddle of life
Perutz, M. F. (1987) · Nature · doi:10.1038/326555a0 · Cited by 76
Cell-specific differences in the requirements for translation quality control
Reynolds, N. M., Ling, J., Roy, H., Banerjee, R., Repasky, S. E., Hamel, P. P., & Ibba, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909640107 · Cited by 75
Transfer RNA–Dependent Translocation of Misactivated Amino Acids to Prevent Errors in Protein Synthesis
Nomanbhoy, T. K., Hendrickson, T. L., & SCHIMMEL, P. R. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80203-8 · Cited by 74
Residues in a Class I tRNA Synthetase Which Determine Selectivity of Amino Acid Recognition in the Context of tRNA
Schmidt, E., & SCHIMMEL, P. R. (1995) · Biochemistry · doi:10.1021/bi00035a028 · Cited by 73
An Aminoacyl-tRNA Synthetase with a Defunct Editing Site
Lue, S. W., & Kelley, S. O. (2005) · Biochemistry · doi:10.1021/bi047901v · Cited by 72
Protein synthesis by single ribosomes
Vanzi, F., Vladimirov, S. N., Knudsen, C. R., Goldman, Y. E., & Cooperman, B. S. (2003) · RNA · doi:10.1261/rna.5800303 · Cited by 72
Codon usage and mistranslation. In vivo basal level misreading of the MS2 coat protein message.
Parker, J., Johnston, T. C., Borgia, P. T., Holtz, G., Remaut, E., & Fiers, W. C. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44598-4 · Cited by 72
A GTPase reaction accompanying the rejection of Leu-tRNA2 by UUU-programmed ribosomes. Proofreading of the codon-anticodon interaction by ribosomes.
Thompson, R. C., Dix, D. B., Gerson, R. B., & Karim, A. M. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70100-8 · Cited by 72
THE SEQUENTIAL SYNTHESIS OF THE POLYPEPTIDE CHAIN OF SERUM ALBUMIN BY THE MICROSOME FRACTION OF RAT LIVER
Sargent, J., & Campbell, P. N. (1965) · Biochemical Journal · doi:10.1042/bj0960134 · Cited by 71
Genetic Code Ambiguity
Nangle, L. A., de Crécy‐Lagard, V., Döring, V., & SCHIMMEL, P. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208093200 · Cited by 70

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

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

The frequency of errors in protein biosynthesis

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks