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Determinants of translation efficiency and accuracy
Open accessAbstract
Proper functioning of biological cells requires that the process of protein expression be carried out with high efficiency and fidelity. Given an amino-acid sequence of a protein, multiple degrees of freedom still remain that may allow evolution to tune efficiency and fidelity for each gene under various conditions and cell types. Particularly, the redundancy of the genetic code allows the choice between alternative codons for the same amino acid, which, although 'synonymous,' may exert dramatic effects on the process of translation. Here we review modern developments in genomics and systems biology that have revolutionized our understanding of the multiple means by which translation is regulated. We suggest new means to model the process of translation in a richer framework that will incorporate information about gene sequences, the tRNA pool of the organism and the thermodynamic stability of the mRNA transcripts. A practical demonstration of a better understanding of the process would be a more accurate prediction of the proteome, given the transcriptome at a diversity of biological conditions.
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Cites
WebLogo: A Sequence Logo Generator: Figure 1
Crooks, G. E., Hon, G., Chandonia, J.-M., & Brenner, S. E. (2004) · Genome Research · doi:10.1101/gr.849004 · Cited by 12,386
Kozak, M. (1986) · Cell · doi:10.1016/0092-8674(86)90762-2 · Cited by 4,741
Sharp, P. M., & Li, W.-H. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.3.1281 · Cited by 3,992
Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853
Shine, J., & Dalgarno, L. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.4.1342 · Cited by 3,621
The mechanism of eukaryotic translation initiation and principles of its regulation
Jackson, R. J., Hellen, C. U. T., & Pestova, T. V. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2838 · Cited by 2,759
The Transcriptional Landscape of the Yeast Genome Defined by RNA Sequencing
Nagalakshmi, U., Wang, Z., Waern, K., Shou, C., Raha, D., Gerstein, M., & Snyder, M. (2008) · Science · doi:10.1126/science.1158441 · Cited by 2,479
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
A "Silent" Polymorphism in the MDR 1 Gene Changes Substrate Specificity
Kimchi-Sarfaty, C., Oh, J. M., Kim, I.-W., Sauna, Z. E., Calcagno, A. M., Ambudkar, S. V., & Gottesman, M. M. (2007) · Science · doi:10.1126/science.1135308 · Cited by 2,416
The ‘effective number of codons’ used in a gene
Wright, F. (1990) · Gene · doi:10.1016/0378-1119(90)90491-9 · Cited by 2,309
Why are ?natively unfolded? proteins unstructured under physiologic conditions?
Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins: Structure, Function, and Genetics · doi:10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7 · Cited by 2,078
Codon—anticodon pairing: The wobble hypothesis
Crick, F. H. C. (1966) · Journal of Molecular Biology · doi:10.1016/s0022-2836(66)80022-0 · Cited by 2,029
Codon usage and tRNA content in unicellular and multicellular organisms.
(1985) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a040335 · Cited by 1,703
Stefani, M., & Dobson, C. M. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0464-5 · Cited by 1,651
Bennetzen, J. L., & Hall, B. D. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81068-2 · Cited by 1,580
Ibba, M., & Söll, D. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.617 · Cited by 1,459
Coding-Sequence Determinants of Gene Expression in Escherichia coli
Kudla, G., Murray, A. W., Tollervey, D., & Plotkin, J. B. (2009) · Science · doi:10.1126/science.1170160 · Cited by 1,458
Ikemura, T. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90003-6 · Cited by 1,417
Codon usage in bacteria: correlation with gene expressivity
Gouy, M., & Gautier, C. (1982) · Nucleic Acids Research · doi:10.1093/nar/10.22.7055 · Cited by 1,250
Global signatures of protein and mRNA expression levels
de Sousa Abreu, R., Penalva, L. O., Marcotte, E. M., & Vogel, C. (2009) · Molecular BioSystems · doi:10.1039/b908315d · Cited by 1,248
Mistranslation-Induced Protein Misfolding as a Dominant Constraint on Coding-Sequence Evolution
Drummond, D. A., & Wilke, C. O. (2008) · Cell · doi:10.1016/j.cell.2008.05.042 · Cited by 1,053
The selection-mutation-drift theory of synonymous codon usage.
Bulmer, M. (1991) · Genetics · doi:10.1093/genetics/129.3.897 · Cited by 1,017
Codon catalog usage is a genome strategy modulated for gene expressivity
Grantham, R., Gautier, C., Gouy, M., Jacobzone, M., & Mercier, R. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.1.213-b · Cited by 939
Pushing the limits of the scanning mechanism for initiation of translation
Kozak, M. (2002) · Gene · doi:10.1016/s0378-1119(02)01056-9 · Cited by 919
An evolutionarily conserved mechanism for controlling the efficiency of protein translation
Tuller, T., Carmi, A., Vestsigian, K., Navon, S., Dorfan, Y., Zaborske, J., Pan, T., Dahan, O., Furman, I., & Pilpel, Y. (2010) · Cell · doi:10.1016/j.cell.2010.03.031 · Cited by 874
Self-citationThe cap and poly(A) tail function synergistically to regulate mRNA translational efficiency.
Gallie, D. R. (1991) · Genes & Development · doi:10.1101/gad.5.11.2108 · Cited by 868
Hearing silence: non-neutral evolution at synonymous sites in mammals
Chamary, J. V., Parmley, J. L., & Hurst, L. D. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1770 · Cited by 831
Duret, L., & Mouchiroud, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.8.4482 · Cited by 813
Co-variation of tRNA Abundance and Codon Usage inEscherichia coliat Different Growth Rates
Dong, H., Nilsson, L., & Kurland, C. G. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0428 · Cited by 790
Optimality and evolutionary tuning of the expression level of a protein
Dekel, E., & Alon, U. (2005) · Nature · doi:10.1038/nature03842 · Cited by 766
Solving the riddle of codon usage preferences: a test for translational selection
Reis, M. D. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh834 · Cited by 755
Attenuation in the control of expression of bacterial operons
Yanofsky, C. (1981) · Nature · doi:10.1038/289751a0 · Cited by 751
Regulation of translation via mRNA structure in prokaryotes and eukaryotes
Kozak, M. (2005) · Gene · doi:10.1016/j.gene.2005.06.037 · Cited by 747
Synonymous codon usage in Drosophila melanogaster: Natural selection and translational accuracy
Akashi, H. (1994) · Genetics · doi:10.1093/genetics/136.3.927 · Cited by 742
Translational Regulation of Gene Expression during Conditions of Cell Stress
Spriggs, K. A., Bushell, M., & Willis, A. E. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.028 · Cited by 723
Steitz, J. A., & Jakes, K. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.12.4734 · Cited by 691
Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G.
Tarun, S. Z., & Sachs, A. B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01108.x · Cited by 688
Regulation of p53 Translation and Induction after DNA Damage by Ribosomal Protein L26 and Nucleolin
Takagi, M., Absalon, M. J., McLure, K. G., & Kastan, M. B. (2005) · Cell · doi:10.1016/j.cell.2005.07.034 · Cited by 663
Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae
Arava, Y., Wang, Y., Storey, J. D., Liu, C. L., Brown, P. O., & Herschlag, D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0635171100 · Cited by 663
Vogel, C., de Sousa Abreu, R., Ko, D., Le, S., Shapiro, B. A., Burns, S. C., Sandhu, D., Boutz, D. R., Marcotte, E. M., & Penalva, L. O. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.59 · Cited by 608
Tissue-Specific Differences in Human Transfer RNA Expression
Dittmar, K. A., Goodenbour, J. M., & Pan, T. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020221 · Cited by 601
Codon usage in regulatory genes in Escherichia coli does not reflect selection for ‘rare’ codons
Sharp, P. M., & Li, W.-H. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.19.7737 · Cited by 585
Translation efficiency is determined by both codon bias and folding energy
Tuller, T., Waldman, Y. Y., Kupiec, M., & Ruppin, E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909910107 · Cited by 584 · cited 9×
“A related study inspected E. coli and S. cerevisiae and found similar trends of relatively loose secondary structure stability near 50 ends of genes (Tuller et al, 2010b).”
BackgroundMethodResultInfluentialCodon usage determines translation rate in Escherichia coli
Sørensen, M. A., Kurland, C. G., & Pedersen, S. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90260-x · Cited by 576
Transient ribosomal attenuation coordinates protein synthesis and co-translational folding
Zhang, G., Hubalewska, M., & Ignatova, Z. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1554 · Cited by 547
"Silent" sites in Drosophila genes are not neutral: evidence of selection among synonymous codons.
(1988) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a040525 · Cited by 533
Codon preferences in free-living microorganisms.
Andersson, S. G., & Kurland, C. G. (1990) · Microbiological Reviews · doi:10.1128/mmbr.54.2.198-210.1990 · Cited by 495
Following translation by single ribosomes one codon at a time
Wen, J.-D., Lancaster, L., Hodges, C., Zeri, A.-C., Yoshimura, S. H., Noller, H. F., Bustamante, C., & Tinoco, I. (2008) · Nature · doi:10.1038/nature06716 · Cited by 492
Kahvejian, A., Svitkin, Y. V., Sukarieh, R., M'Boutchou, M.-N., & Sonenberg, N. (2005) · Genes & Development · doi:10.1101/gad.1262905 · Cited by 491
Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation
Gsponer, J., Futschik, M. E., Teichmann, S. A., & Babu, M. M. (2008) · Science · doi:10.1126/science.1163581 · Cited by 466
Concordant Regulation of Translation and mRNA Abundance for Hundreds of Targets of a Human microRNA
Hendrickson, D. G., Hogan, D. J., McCullough, H. L., Myers, J. W., Herschlag, D., Ferrell, J. E., & Brown, P. O. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000238 · Cited by 418
Kanaya, S., Yamada, Y., Kudo, Y., & Ikemura, T. (1999) · Gene · doi:10.1016/s0378-1119(99)00225-5 · Cited by 417
The Stability Effects of Protein Mutations Appear to be Universally Distributed
Tokuriki, N., Stricher, F., Schymkowitz, J., Serrano, L., & Tawfik, D. S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.03.069 · Cited by 414
Duret, L. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(00)02041-2 · Cited by 398
Causes for the intriguing presence of tRNAs in phages
Bailly-Bechet, M., Vergassola, M., & Rocha, E. (2007) · Genome Research · doi:10.1101/gr.6649807 · Cited by 387
Komar, A. A., Lesnik, T., & Reiss, C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01566-5 · Cited by 385
Translation is a non-uniform process
Varenne, S., Buc, J., Lloubes, R., & Lazdunski, C. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90027-5 · Cited by 384
A Role for Codon Order in Translation Dynamics
Cannarozzi, G., Schraudolph, N. N., Faty, M., von Rohr, P., Friberg, M. T., Roth, A. C., Gonnet, P., Gonnet, G., & Barral, Y. (2010) · Cell · doi:10.1016/j.cell.2010.02.036 · Cited by 354
Design Parameters to Control Synthetic Gene Expression in Escherichia coli
Welch, M., Govindarajan, S., Ness, J. E., Villalobos, A., Gurney, A., Minshull, J., & Gustafsson, C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007002 · Cited by 352
Innate immune and chemically triggered oxidative stress modifies translational fidelity
Netzer, N., Goodenbour, J. M., David, A., Dittmar, K. A., Jones, R. B., Schneider, J. R., Boone, D., Eves, E. M., Rosner, M. R., Gibbs, J. S., et al. (2009) · Nature · doi:10.1038/nature08576 · Cited by 348
Synonymous Codon Usage in Escherichia coli: Selection for Translational Accuracy
Stoletzki, N., & Eyre-Walker, A. (2006) · Molecular Biology and Evolution · doi:10.1093/molbev/msl166 · Cited by 339
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 336
Hamilton, R., Watanabe, C. K., & de Boer, H. A. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.8.3581 · Cited by 333
Codon Usage Bias and tRNA Abundance in Drosophila
Moriyama, E. N., & Powell, J. R. (1997) · Journal of Molecular Evolution · doi:10.1007/pl00006256 · Cited by 318
Gu, W., Zhou, T., & Wilke, C. O. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000664 · Cited by 313
Transfer RNA gene redundancy and translational selection in Saccharomyces cerevisiae
Percudani, R., Pavesi, A., & Ottonello, S. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.0942 · Cited by 303
Codon usage in Caenorhabditis elegans: delineation of translational selection and mutational biases
Stenico, M., Lloyd, A. T., & Sharp, P. M. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.13.2437 · Cited by 291
Kanaya, S., Yamada, Y., Kinouchi, M., Kudo, Y., & Ikemura, T. (2001) · Journal of Molecular Evolution · doi:10.1007/s002390010219 · Cited by 278
Acylation of Proteins with Myristic Acid Occurs Cotranslationally
Wilcox, C., Hu, J.-S., & Olson, E. N. (1987) · Science · doi:10.1126/science.3685978 · Cited by 273
Escherichia coli ribosomes translate in vivo with variable rate.
Pedersen, S. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02227.x · Cited by 270
Viral adaptation to host: a proteome‐based analysis of codon usage and amino acid preferences
Bahir, I., Fromer, M., Prat, Y., & Linial, M. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.71 · Cited by 268
Selective Charging of tRNA Isoacceptors Explains Patterns of Codon Usage
Elf, J., Nilsson, D., Tenson, T., & Ehrenberg, M. (2003) · Science · doi:10.1126/science.1083811 · Cited by 260
Synonymous Mutations and Ribosome Stalling Can Lead to Altered Folding Pathways and Distinct Minima
Tsai, C.-J., Sauna, Z. E., Kimchi-Sarfaty, C., Ambudkar, S. V., Gottesman, M. M., & Nussinov, R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.012 · Cited by 252
Nie, L., Wu, G., & Zhang, W. (2006) · Genetics · doi:10.1534/genetics.106.065862 · Cited by 245
Ribosome‐mediated translational pause and protein domain organization
Thanaraj, T. A., & Argos, P. (1996) · Protein Science · doi:10.1002/pro.5560050814 · Cited by 237
Comparative Functional Analysis of the Caenorhabditis elegans and Drosophila melanogaster Proteomes
Schrimpf, S. P., Weiss, M., Reiter, L., Ahrens, C. H., Jovanovic, M., Malmström, J., Brunner, E., Mohanty, S., Lercher, M. J., Hunziker, P. E., et al. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000048 · Cited by 229
Stoebel, D. M., Dean, A. M., & Dykhuizen, D. E. (2008) · Genetics · doi:10.1534/genetics.107.085399 · Cited by 226
Protein translation components are colocalized in granules in oligodendrocytes
Barbarese, E., Koppel, D. E., Deutscher, M. P., Smith, C. L., Ainger, K., Morgan, F., & Carson, J. H. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.8.2781 · Cited by 217
Translationally Optimal Codons Associate with Structurally Sensitive Sites in Proteins
Zhou, T., Weems, M., & Wilke, C. O. (2009) · Molecular Biology and Evolution · doi:10.1093/molbev/msp070 · Cited by 210
Differential Arginylation of Actin Isoforms Is Regulated by Coding Sequence–Dependent Degradation
Zhang, F., Saha, S., Shabalina, S. A., & Kashina, A. (2010) · Science · doi:10.1126/science.1191701 · Cited by 206
Codon bias as a factor in regulating expression via translation rate in the human genome
Lavner, Y., & Kotlar, D. (2005) · Gene · doi:10.1016/j.gene.2004.11.035 · Cited by 206
A Network of Multiple Regulatory Layers Shapes Gene Expression in Fission Yeast
Lackner, D. H., Beilharz, T. H., Marguerat, S., Mata, J., Watt, S., Schubert, F., Preiss, T., & Bähler, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.002 · Cited by 204
Selective and Mutational Patterns Associated With Gene Expression in Humans
Comeron, J. M. (2004) · Genetics · doi:10.1534/genetics.104.026351 · Cited by 200
Jacob, W. F., Santer, M., & Dahlberg, A. E. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.14.4757 · Cited by 195
Low-usage codons in Escherichia coli, yeast, fruit fly and primates
Zhang, S., Zubay, G., & Goldman, E. (1991) · Gene · doi:10.1016/0378-1119(91)90514-c · Cited by 188
Silent mutations affect in vivo protein folding in Escherichia coli
Cortazzo, P., Cerveñansky, C., Marı́n, M., Reiss, C., Ehrlich, R., & Deana, A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00226-7 · Cited by 179
Protein secondary structural types are differentially coded on messenger RNA
Thanaraj, T. A., & Argos, P. (1996) · Protein Science · doi:10.1002/pro.5560051003 · Cited by 163
Protein abundances are more conserved than mRNA abundances across diverse taxa
Laurent, J. M., Vogel, C., Kwon, T., Craig, S. A., Boutz, D. R., Huse, H. K., Nozue, K., Walia, H., Whiteley, M., Ronald, P. C., et al. (2010) · PROTEOMICS · doi:10.1002/pmic.201000327 · Cited by 156
Genome-wide Analysis of tRNA Charging and Activation of the eIF2 Kinase Gcn2p
Zaborske, J. M., Narasimhan, J., Jiang, L., Wek, S. A., Dittmar, K. A., Freimoser, F. M., Pan, T., & Wek, R. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000877 · Cited by 152
Translational initiation on structured messengers
de Smit, M. H., & DUIN, J. V. (1994) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80024-5 · Cited by 149
Hierarchy of Sequence-Dependent Features Associated With Prokaryotic TranslationPreprint
Lithwick, G. (2003) · Genome Research · doi:10.1101/gr.1485203 · Cited by 147
Man, O., & Pilpel, Y. (2007) · Nature Genetics · doi:10.1038/ng1967 · Cited by 134
Self-citationLü, X., de la Peña, L., Barker, C. S., Camphausen, K. A., & Tofilon, P. J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3459 · Cited by 130
A unification of mosaic structures in the human genome
Lercher, M. J., Urrutia, A. O., Pavlíček, A., & Hurst, L. D. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg251 · Cited by 125
Estimating Translational Selection in Eukaryotic Genomes
dos Reis, M., & Wernisch, L. (2008) · Molecular Biology and Evolution · doi:10.1093/molbev/msn272 · Cited by 111
Tsvetkov, P., Asher, G., Paz, A., Reuven, N. B., Sussman, J. L., Silman, I., & Shaul, Y. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21614 · Cited by 107
Towards a theory of evolutionary adaptation
Hartl, D. L., & Taubes, C. H. (1998) · Contemporary issues in genetics and evolution · doi:10.1007/978-94-011-5210-5_39 · Cited by 100
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
Genome Landscapes and Bacteriophage Codon Usage
Lucks, J. B., Nelson, D. R., Kudla, G., & Plotkin, J. B. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000001 · Cited by 97
Exploring the Regulation of tRNA Distribution on the Genomic Scale
Dittmar, K. A., Mobley, E. M., Radek, A. J., & Pan, T. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.024 · Cited by 96
Impact of translational error‐induced and error‐free misfolding on the rate of protein evolution
Yang, J., Zhuang, S., & Zhang, J. (2010) · Molecular Systems Biology · doi:10.1038/msb.2010.78 · Cited by 96
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
Visualizing high error levels during gene expression in living bacterial cells
Meyerovich, M., Mamou, G., & Ben‐Yehuda, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912989107 · Cited by 86
Codon Bias is a Major Factor Explaining Phage Evolution in Translationally Biased Hosts
Carbone, A. (2008) · Journal of Molecular Evolution · doi:10.1007/s00239-008-9068-6 · Cited by 85
Protein misfolding disorders: Pathogenesis and intervention
Gregersen, N. V. (2006) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-006-0301-4 · Cited by 83
Sørensen, M. A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4525 · Cited by 82
Dynamic Organization of Aminoacyl-tRNA Synthetase Complexes in the Cytoplasm of Human Cells
Kaminska, M., Havrylenko, S., Decottignies, P., Maréchal, P. L., Negrutskii, B. S., & Mirande, M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900480200 · Cited by 80
Wu, G., Nie, L., & Zhang, W. (2008) · Current Microbiology · doi:10.1007/s00284-008-9145-5 · Cited by 77
The Influence of Anticodon-Codon Interactions and Modified Bases on Codon Usage Bias in Bacteria
Ran, W., & Higgs, P. G. (2010) · Molecular Biology and Evolution · doi:10.1093/molbev/msq102 · Cited by 73
Towards a theory of evolutionary adaptation
Hartl, D. L., & Taubes, C. H. (1998) · Genetica · doi:10.1023/a:1017071901530 · Cited by 73
Wang, L., & Wessler, S. R. (2001) · PLANT PHYSIOLOGY · doi:10.1104/pp.125.3.1380 · Cited by 72
Schauder, B., & McCarthy, J. E. G. (1989) · Gene · doi:10.1016/0378-1119(89)90314-4 · Cited by 70
Selection pressures on codon usage in the complete genome of bacteriophage T7
Sharp, P. M., Rogers, M. S., & McConnell, D. J. (1985) · Journal of Molecular Evolution · doi:10.1007/bf02100089 · Cited by 70
Protein folding within the cell is influenced by controlled rates of polypeptide elongation
Crombie, T., Swaffield, J. C., & Brown, A. J. P. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90486-4 · Cited by 57
GroEL dependency affects codon usage—support for a critical role of misfolding in gene evolution
Warnecke, T., & Hurst, L. D. (2010) · Molecular Systems Biology · doi:10.1038/msb.2009.94 · Cited by 54
Huang, Y., Koonin, E. V., Lipman, D. J., & Przytycka, T. M. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp712 · Cited by 43
The role of codon selection in regulation of translation efficiency deduced from synthetic libraries
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Metadata
- Authors
- Gingold, H., & Pilpel, Y.
- Venue
- Molecular Systems Biology
- Published
- 2011-01
- Volume
- 7
- Issue
- 1
- Pages
- 481-481
- ISSN
- 1744-4292 (ISSN-L)
- OpenAlex
- W2166752189
- Cited by
- 489
- References
- 126
- FWCI
- 13.99
- Type
- journal article
- Language
- en
- Open access
- gold
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 ›
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.