The frequency of errors in protein biosynthesis

THE FREQUENCY OF ERRORS IN PROTEIN BIOSYNTHESIS

Loftfield, R. B. (1963) · Biochemical Journal · doi:10.1042/bj0890082 · Cited by 160

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

Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases

Živković, I., Ivkovic, K., Cvetešić, N., Maršavelski, A., & Gruic‐Sovulj, I. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac207 · Cited by 10

Fluorophore Labeling to Monitor tRNA Dynamics

Liu, C., Betteridge, T., & Hou, Y. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(09)69004-2 · Cited by 10

Fidelity of protein synthesis affects the readthrough translation of tobacco mosaic virus RNA

Kurkinen, M. T. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80058-0 · Cited by 10

Crucial Role of Conserved Lysine 277 in the Fidelity of tRNA Aminoacylation by Escherichia coli Valyl-tRNA Synthetase

Hountondji, C., Lazennec‐Schurdevin, C., Beauvallet, C., Dessen, P., Pernollet, J., Plateau, P., & Blanquet, S. (2002) · Biochemistry · doi:10.1021/bi0205101 · Cited by 10

Free energy cost and accuracy in branched selection processes of biosynthesis

Blomberg, C. (1983) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005205 · Cited by 10

Microheterogeneous Collagen Model on the Basis of a Chromatographic Study on Hydroxyapatite Columns

川崎, 力. (1982) · Separation Science and Technology · doi:10.1080/01496398208068550 · Cited by 10

Recoding Therapies for Genetic Diseases

Keeling, K. M., & Bedwell, D. M. (2009) · Nucleic acids and molecular biology · doi:10.1007/978-0-387-89382-2_6 · Cited by 9

Rewiring protein synthesis: From natural to synthetic amino acids

Fan, Y., Evans, C. R., & Ling, J. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.01.014 · Cited by 9

Isoleucyl-tRNA Synthetase fromEscherichia coliMRE 600: Discrimination between Isoleucine and Valine with Modulated Accuracy

Freist, W., & Cramer, F. (1987) · Biological Chemistry Hoppe-Seyler · doi:10.1515/bchm3.1987.368.1.229 · Cited by 9

In Vivo Translational Inaccuracy inEscherichia coli: Missense Reporting Using Extremely Low Activity Mutants ofVibrio harveyiLuciferase

Ortego, B. C., Whittenton, J., Li, H., Tu, S., & Willson, R. C. (2007) · Biochemistry · doi:10.1021/bi602660s · Cited by 9

National Cancer Institute Think-Tank Meeting Report on Proteomic Cartography and Biomarkers at the Single-Cell Level: Interrogation of Premalignant Lesions

Kagan, J., Moritz, R. L., Mazurchuk, R. V., Lee, J. H., Kharchenko, P. V., Rozenblatt–Rosen, O., Ruppin, E., Edfors, F., Ginty, F., Goltsev, Y., et al. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00021 · Cited by 8

The fidelity of protein synthesis: can mischarging by aspartyl-tRNAAsp synthetase lead to the formation of isoaspartyl residues in proteins?

Momand, J. A., & Clarke, S. G. (1990) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(90)90070-v · Cited by 8

Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo

Martin, F. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh751 · Cited by 8

Isoleucyl‐tRNA Synthetase: An Enzyme with Several Catalytic Cycles Displaying Variation in Specificity and Energy Consumption

Freist, W. (1988) · Angewandte Chemie International Edition in English · doi:10.1002/anie.198807731 · Cited by 8

The evolution of the protein synthesis system.I. A. Model of a primitive protein synthesis system

Mizutani, H. (1978) · Origins of Life and Evolution of Biospheres · doi:10.1007/bf00929716 · Cited by 8

Errors in Translation

DAVIES, J. E. (1969) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-46200-9_3 · Cited by 8

Isoleucine-to-valine substitutions support cellular physiology during isoleucine deprivation

Kok, G., Schene, I. F., Ilcken, E. F., Alcaraz, P. S., Mendes, M. I. S., Smith, D. E. C., Salomons, G. S., Shehata, S., Jans, J. J. M., Maroofian, R., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1184 · Cited by 7

A molecular dynamics simulation study of amino acid selectivity of LeuRS editing domain from Thermus thermophilus

Rayevsky, A. V., Sharifi, M., & Tukalo, M. A. (2018) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2018.06.015 · Cited by 7

Pseudoverification of Mixed Aminoacyl Transfer Ribonucleic Acids

Yarus, M. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43418-2 · Cited by 7

Isoleucyl‐tRNA‐Synthetase: Ein Enzym mit mehreren Katalysewegen, variabel in Spezifität und Energieverbrauch

Freist, W. (1988) · Angewandte Chemie · doi:10.1002/ange.19881000605 · Cited by 7

STRINGENT CONTROL OF TRANSLATIONAL ACCURACY

Gallant, J., & Foley, D. (1979) · Elsevier eBooks · doi:10.1016/b978-0-12-417580-8.50009-5 · Cited by 7

Ribosomal Proteins Tune Rate and Accuracy in Translation

Ehrenberg, M., Andersson, D. I., Bohman, K., Jelenc, P. C., Ruusala, T., & Kurland, C. G. (1986) · Springer series in molecular biology · doi:10.1007/978-1-4612-4884-2_33 · Cited by 7

Measurement of translational accuracy in vivo: missense reporting using inactive enzyme mutants

Cornut, B., & Willson, R. C. (1991) · Biochimie · doi:10.1016/0300-9084(91)90192-4 · Cited by 6

Identification of sites of cysteine misincorporation during in vivo synthesis of bacteriophage T7 0.3 protein

Rice, J. B., Seyer, J. J., & Reeve, J. N. (1986) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(86)90029-1 · Cited by 6

Mechanistic Insights Into Catalytic RNA–Protein Complexes Involved in Translation of the Genetic Code

Routh, S. B., & Sankaranarayanan, R. (2017) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2017.04.002 · Cited by 6

Inhibition of growth of cells in culture by L‐phenylalanine as a model system for the analysis of phenylketonuria. I. Amino acid antagonism and the inhibition of protein synthesis

Dillehay, L. E., Bass, R., & Englesberg, E. (1980) · Journal of Cellular Physiology · doi:10.1002/jcp.1041020314 · Cited by 6

The Translational Machinery: Components and Mechanism

Hershey, J. W. B. (1980) · Elsevier eBooks · doi:10.1016/b978-0-12-289504-3.50007-3 · Cited by 6

Application of Two-Dimensional Polyacrylamide Gel Electrophoresis to Studies of Mistranslation in Animal and Bacterial Cells

Pollard, J. W. (1984) · Elsevier eBooks · doi:10.1016/b978-0-12-164720-9.50015-5 · Cited by 6

Structure and Function of tRNA and Aminoacyl tRNA Synthetases in Eukaryotes

Ofengand, J. (1982) · Springer eBooks · doi:10.1007/978-1-4684-4124-6_1 · Cited by 6

Therapies of Nonsense-Associated Diseases

Maquat, L. E. (2006) · CRC Press eBooks · doi:10.1201/9781498713399-17 · Cited by 5

A practical synthesis of 2′-aminoacylamino-2′-deoxyadenosines

O’Mahony, G., Sundgren, A., Svensson, S., & Grøtli, M. (2007) · Tetrahedron · doi:10.1016/j.tet.2007.04.038 · Cited by 5

Mistranslation of human phosphoglycerate kinase in yeast in the presence of paromomycin

Grant, C. M., & Tuite, M. F. (1994) · Current Genetics · doi:10.1007/bf00313794 · Cited by 4

Enzymic editing mechanisms and the origin of biological information transfer

Lambert, G. R. (1984) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(84)80098-3 · Cited by 4

Editing by a tRNA Synthetase: DNA Aptamer-Induced Translocation and Hydrolysis of a Misactivated Amino Acid

Farrow, M. A., & SCHIMMEL, P. R. (2001) · Biochemistry · doi:10.1021/bi0024052 · Cited by 4

Starvation for His-tRNAHis in yeast causes translational arrest without a high level of misincorporation of glutamine at histidine codons

Hirst, K. L., & Piper, P. W. (1992) · Current Genetics · doi:10.1007/bf00336838 · Cited by 4

Mammalian Tolerance to Amino Acid Heterochirality

Taniguchi, S., Adachi, K., Tran, X. T., Suzuki, M., & Sasabe, J. (2025) · ChemBioChem · doi:10.1002/cbic.202500273 · Cited by 3

Strategies to Correct Nonsense Mutations

Benhabiles, H., Jia, J., & Lejeune, F. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-804468-1.00003-8 · Cited by 3

An introduction to the problem of accuracy

Galas, D. J., Kirkwood, T. B. L., & Rosenberger, R. F. (1986) · Springer eBooks · doi:10.1007/978-94-009-4097-0_1 · Cited by 3

A model for mRNA transcription suggested by some characteristics of 2-aminopurine mutagenesis in Salmonella.

Margolin, P., & Mukai, F. H. (1966) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.55.2.282 · Cited by 3

Information-theoretic significance of Gibbs energy supply to editing mechanisms

Křemen, A. (1982) · Biophysical Journal · doi:10.1016/s0006-3495(82)84469-x · Cited by 3

Why should transfer RNAs be so elaborate?

Chantrenne, H. (1978) · Molecular and Cellular Biochemistry · doi:10.1007/bf00230190 · Cited by 3

The accuracy of RNA synthesis

Anderson, R. P., & Menninger, J. R. (1986) · Springer eBooks · doi:10.1007/978-94-009-4097-0_7 · Cited by 3

Plant-exclusive domain of trans-editing enzyme ProXp-ala confers dimerization and enhanced tRNA binding

Byun, J., Vu, J. A., He, S.-L., Jang, J.-C., & Musier‐Forsyth, K. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102255 · Cited by 2

Role of tRNAPro in pretransfer editing of alanine by prolyl-tRNA synthetase

Boyarshin, K. S., Priss, A., Kriklivyi, I. A., Kovalenko, O. P., Yaremchuk, A. D., & Tukalo, M. A. (2013) · Biopolymers and Cell · doi:10.7124/bc.00082d · Cited by 2

Potential Effect of Post-Transcriptional Substitutions of Tyrosine for Cysteine Residues on Transformation of Amyloidogenic Proteins

Muronetz, V. I., Pozdyshev, D. V., Medvedeva, M. V., & Sevostyanova, I. A. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922020080 · Cited by 2

Über die Proteinbiosynthese und den Genetischen Code

Schmidt, H., Gosda, W., & Wallwitz, U. (1964) · Genetic Resources and Crop Evolution · doi:10.1007/bf02095793 · Cited by 2

Leucine inhibition of an altered phenylalanyl-transfer ribonucleic acid synthetase

Kondo, M. (1971) · Die Naturwissenschaften · doi:10.1007/bf00598723 · Cited by 2

Aminoacyl‐tRNA synthetases: inter‐site interaction as a possible proofreading mechanism

Degtyarev, S. K. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)80169-0 · Cited by 2

Evidence that non-cognate proteinogenic amino acids generate immunogenic neoepitopes

Rodgers, K. J. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111349 · Cited by 1

Biosensors Involved in Drug Discovery

Sadana, A., & Sadana, N. (2010) · Elsevier eBooks · doi:10.1016/b978-0-444-53262-6.00004-8 · Cited by 1

THE STRUCTURES AND FUNCTIONS OF TRANSFER RNA

GODDARD, J. P. (1978) · Elsevier eBooks · doi:10.1016/b978-0-08-020295-2.50008-8 · Cited by 1

When Paul Berg meets Donald Crothers: an achiral connection through protein biosynthesis

Kumar, P., & Sankaranarayanan, R. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae117 · Cited by 1

Errors During Elongation Can Cause Translational Frameshifting

Farabaugh, P. J. (1997) · Springer eBooks · doi:10.1007/978-1-4615-5999-3_3 · Cited by 1

Identification of minor tightly bound H1 histone subfractions which fail to cleave their initiator methionine

Медведев, Ж. А., & MEDVEDEVA, M. N. (1989) · Molecular Biology Reports · doi:10.1007/bf00444310 · Cited by 1

A high-throughput competitive scintillation proximity aminoacyl–tRNA synthetase charging assay to measure amino acid concentration

Forbes, C. D., Myung, J., & Landro, J. A. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.01.027 · Cited by 1

Logical elements in living cells

Křemen, A. (1984) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(84)80195-2 · Cited by 1

Function of eukaryotic ribosomes

BIELKA, H. (1982) · Springer eBooks · doi:10.1007/978-3-642-68272-8_11 · Cited by 1

Departamento de Ciências Médicas

ALENCAR, F. H., & Shrimpton, R. (1981) · Acta Amazonica · doi:10.1590/1809-43921981111s055 · Cited by 1

Physics and the Riddle of Life

Perutz, M. F. (1990) · Comprehensive biochemistry · doi:10.1016/b978-0-444-81216-2.50009-3 · Cited by 1

Methylation of basic residues in structural proteins

Reporter, M. (1972) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(72)90081-4 · Cited by 1

Varied forms of mutant tRNA mistranslation produce distinct phenotypes across multiple model organismsPreprint

Charles, B., & Moehring, A. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.25.747118 · Cited by 1

CP1 domain of leucyl-tRNA synthetase: dissecting its dual roles in amino acid editing and RNA splicing

Sarkar, J. (2012) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)

The Development of Novel In Vitro Binding Assays to Further Elucidate the Role of tRNAs in Protein Synthesis

Anthony, J., Jr., Ellzey, S., McDougald, D. S., & Serrano, C. (2011) · InTech eBooks · doi:10.5772/21822

Design of Restriction Endonucleases with Novel Specificity

Lanio, T., Jeltsch, A., & Pingoud, A. M. (2008) · Protein Science Encyclopedia · doi:10.1002/9783527610754.ed03

THE BINDING OF AAtRNA TO PROKARYOTIC RIBOSOMES

Miller, D. L. (1978) · Elsevier eBooks · doi:10.1016/b978-0-08-022624-8.50012-0

Structural Implications of Universal Complementarities in Translation—High Accuracy at the Decoding Site

Nagano, K. (2015) · Advances in Biological Chemistry · doi:10.4236/abc.2015.52012

A paradigm for ribosome fidelity modulation in protein synthesis

Schaup, H. W. (1978) · Journal of Theoretical Biology · doi:10.1016/0022-5193(78)90268-0

Single-particle cryo-electron microscopy of macromolecular assemblies

Cheng, K. (2009) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Accuracy of mRNA Translation in Bacterial Protein Synthesis

Zhang, J. (2015) · Uppsala University Publications (Uppsala University)

Probing Editing Domain Conformational Changes Upon E. coli Prolyl-tRNA Synthetase•YbaK Complex Formation

Saçkes, Z. (2010) · OhioLink ETD Center (Ohio Library and Information Network)

Characterization of Leucyl -Trna Synthetase From Homo Sapiens and Escherichia Coli in Aminoacylation, Amino Acid Editing and Interdomain Interactions

Pang, Y. L. J. (2010) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)

CRYSTALLOGRAPHIC STUDIES OF TYROSYL tRNA SYNTHETASE

Blow, D. M., & Rubin, J. R. (1980) · Elsevier eBooks · doi:10.1016/b978-0-08-024417-4.50022-6

Transfer RNA: Its Role in Decoding the Message

Székely, M. (1980) · doi:10.1007/978-1-349-16264-2_8

The role of a highly conserved eubacterial ribosomal protein in translation quality control

Naganathan, A. (2015) · Journal of International Crisis and Risk Communication Research

Substrate Recognition

Brocklehurst, K., Gul, S., & Pickersgill, R. W. (2009) · Wiley eBooks · doi:10.1002/9783527631780.ch11

Genetic Code Expansion in Mammalian Cells

Beranek, V. (2018) · Apollo (University of Cambridge) · doi:10.17863/cam.41725

Is there an infant mortality in bacteria?Preprint

García-Roger, E. M., Richmond, P., & Roehner, B. M. (2021) · arXiv (Cornell University) · doi:10.48550/arxiv.2103.13919

Ribosomal Contributions to messenger RNA Directed Selection of transfer RNA

Nygârd, O., & Westermann, P. (1983) · Humana Press eBooks · doi:10.1007/978-1-4612-5310-5_13

Highlights on Trypanosomatid Aminoacyl-tRNA Synthesis

Polycarpo, C. R. (2013) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-7305-9_12

Elongation Cycle, Step I: Aminoacyl-tRNA Binding

(2005) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-46815-8_10

Faculty Opinions recommendation of tRNA properties help shape codon pair preferences in open reading frames.

Pan, T. (2006) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1006158.372982

Потенциальное влияние посттранскрипционных замен тирозиновых остатков на цистеиновые на трансформацию амилоидогенных белков

Муронец, В. И., Pozdyshev, D. V., Medvedeva, M. V., & Севостьянова, И. А. (2022) · Biochemistry (Moscow) · doi:10.31857/s0320972522020051

Analysis of translational fidelity in cellular proteins

Garofalo, R. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7371

Bibliography

(1983) · Elsevier eBooks · doi:10.1016/b978-0-12-507360-8.50019-7

Translational Editing

SCHIMMEL, P. R. (2002) · Encyclopedia of Molecular Biology · doi:10.1002/047120918x.emb1588

Gly56 in the synthetic site of isoleucyl‐tRNA synthetase confers specificity and maintains communication with the editing site

Dulić, M., Krpan, N., & Gruic‐Sovulj, I. (2023) · FEBS Letters · doi:10.1002/1873-3468.14780

Maximal Genetic Code Symmetry Is a Physicochemical Purine–Pyrimidine Symmetry Language for Transcription and Translation in the Flow of Genetic Information from DNA to Proteins

Rosandić, M., & Paar, V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25179543

Alternative substrate‐assisted hydrolysis pathways of posttransfer editing by prokaryotic leucyl‐ tRNA synthetase

Ilchenko, M. M., Rayevsky, A. V., Kovalenko, O. P., Demianenko, E. M., Skydanovych, O. I., Dubey, I. Y., & Tukalo, M. A. (2025) · FEBS Journal · doi:10.1111/febs.70153

Effect of Elongation Inhibitors on the Accuracy of Poly(U) Translation

Nygârd, O., & Westermann, P. (1983) · Humana Press eBooks · doi:10.1007/978-1-4612-5310-5_15

Elongation Cycle, Step I: Aminoacyl-tRNA Binding

Spirin, A. S. (1999) · Springer eBooks · doi:10.1007/978-1-4615-7817-8_10

Review Translational dynamics

Nygârd, O., & Nilsson, L. (1990) · Springer eBooks · doi:10.1007/978-3-642-76168-3_9

TGF-β/activin signaling balances the activity of two major protein quality control mechanisms during growth of Drosophila larval body wall muscle

Kim, M.-J., & Connor, M. B. O. R. (2026) · iScience · doi:10.1016/j.isci.2026.118008

Engineering aminoacyl-tRNA synthetase activity to enhance branched-chain amino acid biosynthesis

Derunets, A. S., & Yanenko, A. S. (2026) · Biochimie · doi:10.1016/j.biochi.2026.03.014

Halogen Bonding as a Molecular Recognition Strategy for Genetic Code Expansion

Jakka, S. R., Jaiswal, S., Reddy, K. M., Agarwal, R., Kumar, S., & Mugesh, G. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.5508153

Halogen Bonding as a Molecular Recognition Strategy for Genetic Code Expansion

Jakka, S. R., Jaiswal, S., Reddy, K. M., Agarwal, R., Kumar, S., & Mugesh, G. (2026) · Angewandte Chemie · doi:10.1002/ange.5508153

Fidelity during bacterial protein synthesis

Wilson, C., Lyu, Z., & Ling, J. (2026) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00337-25

Amino Acid Pools and the Role of PheRS in the Fidelity of Translation

Caitlin, B. (2009) · The Knowledge Bank (The Ohio State University)

No evidence for accumulation of random errors in proteins

Gershon, D. (1977) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(77)90106-2

[Problem of protein biosynthesis].

SZAFRANSKI, P. (1959) · PubMed

Molecular Mechanisms of Protein Biosynthesis

Cannon, M. (1978) · Biochemical Society Transactions · doi:10.1042/bst0060707 · Cited by 82

Errors in representing protein and nucleic acid structures

Indge, G. E. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90278-j

The biosynthesis of protein. 1

Bresler, S. E. (1953) · Biochemical Journal · doi:10.1042/bj05400i3d · Cited by 1