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Volumn 583, Issue 7, 2009, Pages 1053-1059

Retraction notice to "Why proteins evolve at different rates: The functional hypothesis versus the mistranslation-induced protein misfolding hypothesis" [FEBS Lett. 583 (2009) 1053-1059] (DOI:10.1016/j.febslet.2009.02.033);Why proteins evolve at different rates: The functional hypothesis versus the mistranslation-induced protein misfolding hypothesis

Author keywords

Expression abundance; Functional hypothesis; Mistranslation induced protein misfolding hypothesis; Protein evolutionary rate; Translational robustness

Indexed keywords

NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SHORT SURVEY;

EID: 62849128373     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.08.024     Document Type: Erratum
Times cited : (3)

References (62)
  • 1
    • 0001753988 scopus 로고
    • Primary structure and evolution of cytochrome C
    • Margoliash E. Primary structure and evolution of cytochrome C. Proc. Natl. Acad. Sci. USA 50 (1963) 672-679
    • (1963) Proc. Natl. Acad. Sci. USA , vol.50 , pp. 672-679
    • Margoliash, E.1
  • 2
    • 0017227120 scopus 로고
    • Evolutionary processes and evolutionary noise at the molecular level. I. Functional density in proteins
    • Zuckerkandl E. Evolutionary processes and evolutionary noise at the molecular level. I. Functional density in proteins. J. Mol. Evol. 7 (1976) 167-183
    • (1976) J. Mol. Evol. , vol.7 , pp. 167-183
    • Zuckerkandl, E.1
  • 3
    • 33748980210 scopus 로고    scopus 로고
    • Evolutionary systems biology: links between gene evolution and function
    • Koonin E.V., and Wolf Y.I. Evolutionary systems biology: links between gene evolution and function. Curr. Opin. Biotechnol. 17 (2006) 481-487
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 481-487
    • Koonin, E.V.1    Wolf, Y.I.2
  • 4
    • 33746192317 scopus 로고    scopus 로고
    • Unifying measures of gene function and evolution
    • Wolf Y.I., Carmel L., and Koonin E.V. Unifying measures of gene function and evolution. Proc. Biol. Sci. 273 (2006) 1507-1515
    • (2006) Proc. Biol. Sci. , vol.273 , pp. 1507-1515
    • Wolf, Y.I.1    Carmel, L.2    Koonin, E.V.3
  • 5
    • 33746885883 scopus 로고    scopus 로고
    • Systemic determinants of gene evolution and function
    • Koonin E.V. Systemic determinants of gene evolution and function. Mol. Syst. Biol. 1 (2005) 0021
    • (2005) Mol. Syst. Biol. , vol.1 , pp. 0021
    • Koonin, E.V.1
  • 6
    • 30744441602 scopus 로고    scopus 로고
    • A single determinant dominates the rate of yeast protein evolution
    • Drummond D.A., Raval A., and Wilke CO. A single determinant dominates the rate of yeast protein evolution. Mol. Biol. Evol. 23 (2006) 327-337
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 327-337
    • Drummond, D.A.1    Raval, A.2    Wilke, CO.3
  • 7
    • 0033565762 scopus 로고    scopus 로고
    • Do essential genes evolve slowly?
    • Hurst LD., and Smith N.G. Do essential genes evolve slowly?. Curr. Biol. 9 (1999) 747-750
    • (1999) Curr. Biol. , vol.9 , pp. 747-750
    • Hurst, LD.1    Smith, N.G.2
  • 8
    • 0035963414 scopus 로고    scopus 로고
    • Protein dispensability and rate of evolution
    • Hirsh A.E., and Fraser H.B. Protein dispensability and rate of evolution. Nature 411 (2001) 1046-1049
    • (2001) Nature , vol.411 , pp. 1046-1049
    • Hirsh, A.E.1    Fraser, H.B.2
  • 9
    • 0036078078 scopus 로고    scopus 로고
    • Essential genes are more evolutionary conserved than are nonessential genes in bacteria
    • Jordan I.K., Rogozin I.B., Wolf Y.I., and Koonin E.V. Essential genes are more evolutionary conserved than are nonessential genes in bacteria. Genome Res. 12 (2002) 962-968
    • (2002) Genome Res. , vol.12 , pp. 962-968
    • Jordan, I.K.1    Rogozin, I.B.2    Wolf, Y.I.3    Koonin, E.V.4
  • 11
    • 10744225908 scopus 로고    scopus 로고
    • Molecular correlates of genes exhibiting RNAi phenotypes in Caenorhabditis elegans
    • Cutter A.D., et al. Molecular correlates of genes exhibiting RNAi phenotypes in Caenorhabditis elegans. Genome Res. 13 (2003) 2651-2657
    • (2003) Genome Res. , vol.13 , pp. 2651-2657
    • Cutter, A.D.1
  • 13
    • 16344381521 scopus 로고    scopus 로고
    • Comparative genomics of centrality and essentiality in three eukaryotic protein-interaction networks
    • Hahn M.W., and Kern A.D. Comparative genomics of centrality and essentiality in three eukaryotic protein-interaction networks. Mol. Biol. Evol. 22 (2005) 803-806
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 803-806
    • Hahn, M.W.1    Kern, A.D.2
  • 14
    • 0242284421 scopus 로고    scopus 로고
    • A simple dependence between protein evolution rate and the number of protein-protein interactions
    • Fraser H.B., Wall DP., and Hirsh A.E. A simple dependence between protein evolution rate and the number of protein-protein interactions. BMC Evol. Biol. 3 (2003) 11
    • (2003) BMC Evol. Biol. , vol.3 , pp. 11
    • Fraser, H.B.1    Wall, DP.2    Hirsh, A.E.3
  • 15
    • 17744376961 scopus 로고    scopus 로고
    • Evolution of proteins and gene expression levels are coupled in Drosophila and are independently associated with mRNA abundance, protein length, and number of protein-protein interactions
    • Lemos B., Bettencourt B.R., Meiklejohn C.D., and Hartl D.L. Evolution of proteins and gene expression levels are coupled in Drosophila and are independently associated with mRNA abundance, protein length, and number of protein-protein interactions. Mol. Biol. Evol. 22 (2005) 1345-1354
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1345-1354
    • Lemos, B.1    Bettencourt, B.R.2    Meiklejohn, C.D.3    Hartl, D.L.4
  • 16
    • 23344451687 scopus 로고    scopus 로고
    • Structure, function, and evolution of transient and obligate protein-protein interactions
    • Mintseris J., and Weng Z. Structure, function, and evolution of transient and obligate protein-protein interactions. Proc. Natl. Acad. Sci. USA 102 (2005) 10930-10935
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10930-10935
    • Mintseris, J.1    Weng, Z.2
  • 17
    • 0034978556 scopus 로고    scopus 로고
    • Highly expressed genes in yeast evolve slowly
    • Pal C., Papp B., and Hurst L.D. Highly expressed genes in yeast evolve slowly. Genetics 158 (2001) 927-931
    • (2001) Genetics , vol.158 , pp. 927-931
    • Pal, C.1    Papp, B.2    Hurst, L.D.3
  • 18
    • 5044252972 scopus 로고    scopus 로고
    • Gene expression intensity shapes evolutionary rates of the proteins encoded by the vertebrate genome
    • Subramanian S., and Kumar S. Gene expression intensity shapes evolutionary rates of the proteins encoded by the vertebrate genome. Genetics 168 (2004) 373-381
    • (2004) Genetics , vol.168 , pp. 373-381
    • Subramanian, S.1    Kumar, S.2
  • 19
    • 16344369543 scopus 로고    scopus 로고
    • Significant impact of protein dispensability on the instantaneous rate of protein evolution
    • Zhang J., and He X. Significant impact of protein dispensability on the instantaneous rate of protein evolution. Mol. Biol. Evol. 22 (2005) 1147-1155
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1147-1155
    • Zhang, J.1    He, X.2
  • 20
    • 33847686233 scopus 로고    scopus 로고
    • Gene expression and protein length influence codon usage and rates of sequence evolution in Populus tremula
    • Ingvarsson P.K. Gene expression and protein length influence codon usage and rates of sequence evolution in Populus tremula. Mol. Biol. Evol. 24 (2007) 836-844
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 836-844
    • Ingvarsson, P.K.1
  • 21
    • 47549097539 scopus 로고    scopus 로고
    • Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution
    • Drummond D.A., and Wilke CO. Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution. Cell 134 (2008) 341-352
    • (2008) Cell , vol.134 , pp. 341-352
    • Drummond, D.A.1    Wilke, CO.2
  • 23
    • 0033977618 scopus 로고    scopus 로고
    • Determinants of substitution rates in mammalian genes: expression pattern affects selection intensity but not mutation rate
    • Duret L., and Mouchiroud D. Determinants of substitution rates in mammalian genes: expression pattern affects selection intensity but not mutation rate. Mol. Biol. Evol. 17 (2000) 68-74
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 68-74
    • Duret, L.1    Mouchiroud, D.2
  • 24
    • 0142124263 scopus 로고    scopus 로고
    • Gene loss, protein sequence divergence, gene dispensability, expression level, and interactivity are correlated in eukaryotic evolution
    • Krylov D.M., Wolf Y.I., Rogozin I.B., and Koonin E.V. Gene loss, protein sequence divergence, gene dispensability, expression level, and interactivity are correlated in eukaryotic evolution. Genome Res. 13 (2003) 2229-2235
    • (2003) Genome Res. , vol.13 , pp. 2229-2235
    • Krylov, D.M.1    Wolf, Y.I.2    Rogozin, I.B.3    Koonin, E.V.4
  • 25
    • 33746631391 scopus 로고    scopus 로고
    • Evolutionary and physiological importance of hub proteins
    • Batada N.N., Hurst L.D., and Tyers M. Evolutionary and physiological importance of hub proteins. PLoS Comput. Biol. 2 (2006) e88
    • (2006) PLoS Comput. Biol. , vol.2
    • Batada, N.N.1    Hurst, L.D.2    Tyers, M.3
  • 28
    • 17444387503 scopus 로고    scopus 로고
    • Comparative analysis of the Saccharomyces cerevisiae and Caenorhabditis elegans protein interaction networks
    • Agrafioti I., Swire J., Abbott J., Huntley D., Butcher S., and Stumpf M.P. Comparative analysis of the Saccharomyces cerevisiae and Caenorhabditis elegans protein interaction networks. BMC Evol. Biol. 5 (2005) 23
    • (2005) BMC Evol. Biol. , vol.5 , pp. 23
    • Agrafioti, I.1    Swire, J.2    Abbott, J.3    Huntley, D.4    Butcher, S.5    Stumpf, M.P.6
  • 29
    • 0037472928 scopus 로고    scopus 로고
    • Genomic function: rate of evolution and gene dispensability
    • [discussion 497-498]
    • Pal C., Papp B., and Hurst L.D. Genomic function: rate of evolution and gene dispensability. Nature 421 (2003) 496-497 [discussion 497-498]
    • (2003) Nature , vol.421 , pp. 496-497
    • Pal, C.1    Papp, B.2    Hurst, L.D.3
  • 30
    • 2942683220 scopus 로고    scopus 로고
    • Evolutionary rate depends on number of protein-protein interactions independently of gene expression level: response
    • Bloom J.D., and Adami C. Evolutionary rate depends on number of protein-protein interactions independently of gene expression level: response. BMC Evol. Biol. 4 (2004) 14
    • (2004) BMC Evol. Biol. , vol.4 , pp. 14
    • Bloom, J.D.1    Adami, C.2
  • 31
    • 34548357121 scopus 로고    scopus 로고
    • Assessing the determinants of evolutionary rates in the presence of noise
    • Plotkin J.B., and Fraser H.B. Assessing the determinants of evolutionary rates in the presence of noise. Mol. Biol. Evol. 24 (2007) 1113-1121
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1113-1121
    • Plotkin, J.B.1    Fraser, H.B.2
  • 32
    • 33748143748 scopus 로고    scopus 로고
    • Structural determinants of the rate of protein evolution in yeast
    • Bloom J.D., Drummond D.A., Arnold F.H., and Wilke C.O. Structural determinants of the rate of protein evolution in yeast. Mol. Biol. Evol. 23 (2006) 1751-1761
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 1751-1761
    • Bloom, J.D.1    Drummond, D.A.2    Arnold, F.H.3    Wilke, C.O.4
  • 33
    • 2942624159 scopus 로고    scopus 로고
    • Apparent dependence of protein evolutionary rate on number of interactions is linked to biases in protein-protein interactions data sets
    • Bloom J.D., and Adami C. Apparent dependence of protein evolutionary rate on number of interactions is linked to biases in protein-protein interactions data sets. BMC Evol. Biol. 3 (2003) 21
    • (2003) BMC Evol. Biol. , vol.3 , pp. 21
    • Bloom, J.D.1    Adami, C.2
  • 34
    • 33646375934 scopus 로고    scopus 로고
    • The causes of protein evolutionary rate variation
    • Mclnerney J.O. The causes of protein evolutionary rate variation. Trends Ecol. Evol. 21 (2006) 230-232
    • (2006) Trends Ecol. Evol. , vol.21 , pp. 230-232
    • Mclnerney, J.O.1
  • 35
    • 33746237576 scopus 로고    scopus 로고
    • The quest for the universals of protein evolution
    • Rocha E.P. The quest for the universals of protein evolution. Trends Genet. 22 (2006) 412-416
    • (2006) Trends Genet. , vol.22 , pp. 412-416
    • Rocha, E.P.1
  • 36
    • 1242284655 scopus 로고    scopus 로고
    • An analysis of determinants of amino acids substitution rates in bacterial proteins
    • Rocha E.P., and Danchin A. An analysis of determinants of amino acids substitution rates in bacterial proteins. Mol. Biol. Evol. 21 (2004) 108-116
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 108-116
    • Rocha, E.P.1    Danchin, A.2
  • 37
    • 33645242016 scopus 로고    scopus 로고
    • Evolutionary rates and expression level in Chlamydomonas
    • Popescu C.E., Borza T., Bielawski J.P., and Lee R.W. Evolutionary rates and expression level in Chlamydomonas. Genetics 172 (2006) 1567-1576
    • (2006) Genetics , vol.172 , pp. 1567-1576
    • Popescu, C.E.1    Borza, T.2    Bielawski, J.P.3    Lee, R.W.4
  • 38
    • 4143122090 scopus 로고    scopus 로고
    • Effects of gene expression on molecular evolution in Arabidopsis thaliana and Arabidopsis lyrata
    • Wright S.I., Yau C.B., Looseley M., and Meyers B.C. Effects of gene expression on molecular evolution in Arabidopsis thaliana and Arabidopsis lyrata. Mol. Biol. Evol. 21 (2004) 1719-1726
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1719-1726
    • Wright, S.I.1    Yau, C.B.2    Looseley, M.3    Meyers, B.C.4
  • 39
    • 0035012056 scopus 로고    scopus 로고
    • Synonymous codon usage, accuracy of translation, and gene length in Caenorhabditis elegans
    • Marais G., and Duret L. Synonymous codon usage, accuracy of translation, and gene length in Caenorhabditis elegans. J. Mol. Evol. 52 (2001) 275-280
    • (2001) J. Mol. Evol. , vol.52 , pp. 275-280
    • Marais, G.1    Duret, L.2
  • 40
    • 0020491327 scopus 로고
    • Codon usage in bacteria: correlation with gene expressivity
    • Gouy M., and Gautier C. Codon usage in bacteria: correlation with gene expressivity. Nucleic Acids Res. 10 (1982) 7055-7074
    • (1982) Nucleic Acids Res. , vol.10 , pp. 7055-7074
    • Gouy, M.1    Gautier, C.2
  • 41
    • 0028220048 scopus 로고
    • Synonymous codon usage in Drosophila melanogaster: natural selection and translational accuracy
    • Akashi H. Synonymous codon usage in Drosophila melanogaster: natural selection and translational accuracy. Genetics 136 (1994) 927-935
    • (1994) Genetics , vol.136 , pp. 927-935
    • Akashi, H.1
  • 42
    • 0041817645 scopus 로고    scopus 로고
    • Translational selection and yeast proteome evolution
    • Akashi H. Translational selection and yeast proteome evolution. Genetics 164 (2003) 1291-1303
    • (2003) Genetics , vol.164 , pp. 1291-1303
    • Akashi, H.1
  • 43
    • 0021712452 scopus 로고
    • Interaction of silent and replacement changes in eukaryotic coding sequences
    • Lipman D.J., and Wilbur W.J. Interaction of silent and replacement changes in eukaryotic coding sequences. J. Mol. Evol. 21 (1984) 161-167
    • (1984) J. Mol. Evol. , vol.21 , pp. 161-167
    • Lipman, D.J.1    Wilbur, W.J.2
  • 45
    • 3042681604 scopus 로고    scopus 로고
    • Protein tolerance to random amino acid change
    • Guo H.H., Choe J., and Loeb L.A. Protein tolerance to random amino acid change. Proc. Natl. Acad. Sci. USA 101 (2004) 9205-9210
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9205-9210
    • Guo, H.H.1    Choe, J.2    Loeb, L.A.3
  • 46
    • 0028076771 scopus 로고
    • Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence
    • Markiewicz P., Kleina L.G., Cruz C., Ehret S., and Miller J.H. Genetic studies of the lac repressor. XIV. Analysis of 4000 altered Escherichia coli lac repressors reveals essential and non-essential residues, as well as "spacers" which do not require a specific sequence. J. Mol. Biol. 240 (1994) 421-433
    • (1994) J. Mol. Biol. , vol.240 , pp. 421-433
    • Markiewicz, P.1    Kleina, L.G.2    Cruz, C.3    Ehret, S.4    Miller, J.H.5
  • 47
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch W.E., Morimoto R.I., Dillin A., and Kelly J.W. Adapting proteostasis for disease intervention. Science 319 (2008) 916-919
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 48
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • Cohen E., Bieschke J., Perciavalle R.M., Kelly J.W., and Dillin A. Opposing activities protect against age-onset proteotoxicity. Science 313 (2006) 1604-1610
    • (2006) Science , vol.313 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 49
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • Gidalevitz T., Ben-Zvi A., Ho K.H., Brignull H.R., and Morimoto R.I. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311 (2006) 1471-1474
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 50
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4 (2003) 49-60
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 51
    • 33748432548 scopus 로고    scopus 로고
    • Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration
    • Lee J.W., et al. Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration. Nature 443 (2006) 50-55
    • (2006) Nature , vol.443 , pp. 50-55
    • Lee, J.W.1
  • 52
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao L., Longo-Guess C., Harris B.S., Lee J.W., and Ackerman S.L. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat. Genet. 37 (2005) 974-979
    • (2005) Nat. Genet. , vol.37 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.W.4    Ackerman, S.L.5
  • 53
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings C.J., Sun Y., Opal P., Antalffy B., Mestril R., Orr H.T., Dillmann W.H., and Zoghbi H.Y. Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. 10 (2001) 1511-1518
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.T.6    Dillmann, W.H.7    Zoghbi, H.Y.8
  • 54
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck P.K., Chan H.Y., Trojanowski J.Q., Lee V.M., and Bonini N.M. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295 (2002) 865-868
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 55
    • 20644465818 scopus 로고    scopus 로고
    • A highly unexpected strong correlation between fixation probability of nonsynonymous mutations and mutation rate
    • Wyckoff G.J., Malcom CM., Vallender E.J., and Lahn B.T. A highly unexpected strong correlation between fixation probability of nonsynonymous mutations and mutation rate. Trends Genet. 21 (2005) 381-385
    • (2005) Trends Genet. , vol.21 , pp. 381-385
    • Wyckoff, G.J.1    Malcom, CM.2    Vallender, E.J.3    Lahn, B.T.4
  • 56
    • 54949151498 scopus 로고    scopus 로고
    • Comparable contributions of structural-functional constraints and expression level to the rate of protein sequence evolution
    • Wolf M.Y., Wolf Y.I., and Koonin E.V. Comparable contributions of structural-functional constraints and expression level to the rate of protein sequence evolution. Biol. Direct. 3 (2008) 40
    • (2008) Biol. Direct. , vol.3 , pp. 40
    • Wolf, M.Y.1    Wolf, Y.I.2    Koonin, E.V.3
  • 57
    • 33646182934 scopus 로고    scopus 로고
    • An integrated view of protein evolution
    • Pal C., Papp B., and Lercher M.J. An integrated view of protein evolution. Nat. Rev. Genet. 7 (2006) 337-348
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 337-348
    • Pal, C.1    Papp, B.2    Lercher, M.J.3
  • 58
    • 0037307413 scopus 로고    scopus 로고
    • Signatures of natural selection in the human genome
    • Bamshad M., and Wooding S.P. Signatures of natural selection in the human genome. Nat. Rev. Genet. 4 (2003) 99-111
    • (2003) Nat. Rev. Genet. , vol.4 , pp. 99-111
    • Bamshad, M.1    Wooding, S.P.2
  • 59
    • 43149112799 scopus 로고    scopus 로고
    • Contact density affects protein evolutionary rate from bacteria to animals
    • Zhou T., Drummond D.A., and Wilke CO. Contact density affects protein evolutionary rate from bacteria to animals. J. Mol. Evol. 66 (2008) 395-404
    • (2008) J. Mol. Evol. , vol.66 , pp. 395-404
    • Zhou, T.1    Drummond, D.A.2    Wilke, CO.3
  • 60
    • 6344241652 scopus 로고    scopus 로고
    • Conservation and coevolution in the scale-free human gene coexpression network
    • Jordan I.K., Marino-Ramirez L., Wolf Y.I., and Koonin E.V. Conservation and coevolution in the scale-free human gene coexpression network. Mol. Biol. Evol. 21 (2004) 2058-2070
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 2058-2070
    • Jordan, I.K.1    Marino-Ramirez, L.2    Wolf, Y.I.3    Koonin, E.V.4
  • 61
    • 0842291785 scopus 로고    scopus 로고
    • No simple dependence between protein evolution rate and the number of protein-protein interactions: only the most prolific interactors tend to evolve slowly
    • Jordan I.K., Wolf Y.I., and Koonin E.V. No simple dependence between protein evolution rate and the number of protein-protein interactions: only the most prolific interactors tend to evolve slowly. BMC Evol. Biol. 3 (2003) 1
    • (2003) BMC Evol. Biol. , vol.3 , pp. 1
    • Jordan, I.K.1    Wolf, Y.I.2    Koonin, E.V.3
  • 62
    • 0038708556 scopus 로고    scopus 로고
    • Rate of protein evolution versus fitness effect of gene deletion
    • Yang J., Gu Z., and Li W.H. Rate of protein evolution versus fitness effect of gene deletion. Mol. Biol. Evol. 20 (2003) 772-774
    • (2003) Mol. Biol. Evol. , vol.20 , pp. 772-774
    • Yang, J.1    Gu, Z.2    Li, W.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.