메뉴 건너뛰기




Volumn 10, Issue 6, 2014, Pages

Interplay between Chaperones and Protein Disorder Promotes the Evolution of Protein Networks

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; YEAST;

EID: 84903388916     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003674     Document Type: Article
Times cited : (29)

References (87)
  • 1
    • 64849101493 scopus 로고    scopus 로고
    • Protein dynamism and evolvability
    • Tokuriki N, Tawfik DS, (2009) Protein dynamism and evolvability. Science 324: 203-207.
    • (2009) Science , vol.324 , pp. 203-207
    • Tokuriki, N.1    Tawfik, D.S.2
  • 2
    • 23944490117 scopus 로고    scopus 로고
    • Missense meanderings in sequence space: a biophysical view of protein evolution
    • DePristo MA, Weinreich DM, Hartl DL, (2005) Missense meanderings in sequence space: a biophysical view of protein evolution. Nat Rev Genet 6: 678-687.
    • (2005) Nat Rev Genet , vol.6 , pp. 678-687
    • DePristo, M.A.1    Weinreich, D.M.2    Hartl, D.L.3
  • 3
    • 0242609180 scopus 로고    scopus 로고
    • Sequence divergence, functional constraint, and selection in protein evolution
    • Fay JC, Wu C-I, (2003) Sequence divergence, functional constraint, and selection in protein evolution. Annu Rev Genom Human Genet 4: 213-235.
    • (2003) Annu Rev Genom Human Genet , vol.4 , pp. 213-235
    • Fay, J.C.1    Wu, C.-I.2
  • 4
    • 43949093427 scopus 로고    scopus 로고
    • Understanding protein evolution: from protein physics to Darwinian selection
    • Zeldovich KB, Shakhnovich EI, (2008) Understanding protein evolution: from protein physics to Darwinian selection. Annu Rev Phys Chem 59: 105-127.
    • (2008) Annu Rev Phys Chem , vol.59 , pp. 105-127
    • Zeldovich, K.B.1    Shakhnovich, E.I.2
  • 6
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki N, Tawfik DS, (2009) Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 459: 668-673.
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 7
    • 78149452881 scopus 로고    scopus 로고
    • Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms
    • Jarosz DF, Taipale M, Lindquist S, (2010) Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annu Rev Genet 44: 189-216.
    • (2010) Annu Rev Genet , vol.44 , pp. 189-216
    • Jarosz, D.F.1    Taipale, M.2    Lindquist, S.3
  • 8
    • 84876406925 scopus 로고    scopus 로고
    • The role of mutational robustness in RNA virus evolution
    • Lauring AS, Frydman J, Andino R, (2013) The role of mutational robustness in RNA virus evolution. Nat Rev Microbiol 11: 327-336.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 327-336
    • Lauring, A.S.1    Frydman, J.2    Andino, R.3
  • 9
    • 0033979433 scopus 로고    scopus 로고
    • Estimating synonymous and nonsynonymous substitution rates under realistic evolutionary models
    • Yang Z, Nielsen R, (2000) Estimating synonymous and nonsynonymous substitution rates under realistic evolutionary models. Mol Biol Evol 17: 32-43.
    • (2000) Mol Biol Evol , vol.17 , pp. 32-43
    • Yang, Z.1    Nielsen, R.2
  • 10
    • 33646182934 scopus 로고    scopus 로고
    • An integrated view of protein evolution
    • Pál C, Papp B, Lercher MJ, (2006) An integrated view of protein evolution. Nat Rev Genet 7: 337-348.
    • (2006) Nat Rev Genet , vol.7 , pp. 337-348
    • Pál, C.1    Papp, B.2    Lercher, M.J.3
  • 11
    • 67650904949 scopus 로고    scopus 로고
    • Integrated assessment of genomic correlates of protein evolutionary rate
    • Xia Y, Franzosa EA, Gerstein MB, (2009) Integrated assessment of genomic correlates of protein evolutionary rate. PLoS Comput Biol 5: e1000413.
    • (2009) PLoS Comput Biol , vol.5
    • Xia, Y.1    Franzosa, E.A.2    Gerstein, M.B.3
  • 12
    • 33748143748 scopus 로고    scopus 로고
    • Structural determinants of the rate of protein evolution in yeast
    • Bloom JD, Drummond DA, Arnold FH, Wilke CO, (2006) Structural determinants of the rate of protein evolution in yeast. Mol Biol Evol 23: 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
  • 14
    • 47549097539 scopus 로고    scopus 로고
    • Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution
    • Drummond DA, Wilke CO, (2008) Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution. Cell 134: 341-352.
    • (2008) Cell , vol.134 , pp. 341-352
    • Drummond, D.A.1    Wilke, C.O.2
  • 15
    • 77958577844 scopus 로고    scopus 로고
    • Impact of translational error-induced and error-free misfolding on the rate of protein evolution
    • Yang J-R, Zhuang S-M, Zhang J, (2010) Impact of translational error-induced and error-free misfolding on the rate of protein evolution. Mol Syst Biol 6: 421.
    • (2010) Mol Syst Biol , vol.6 , pp. 421
    • Yang, J.-R.1    Zhuang, S.-M.2    Zhang, J.3
  • 16
    • 78149462227 scopus 로고    scopus 로고
    • Derivation of a solubility condition for proteins from an analysis of the competition between folding and aggregation
    • Pechmann S, Vendruscolo M, (2010) Derivation of a solubility condition for proteins from an analysis of the competition between folding and aggregation. Mol BioSyst 6: 2490-2497.
    • (2010) Mol BioSyst , vol.6 , pp. 2490-2497
    • Pechmann, S.1    Vendruscolo, M.2
  • 17
    • 0031805465 scopus 로고    scopus 로고
    • Assessing the impact of secondary structure and solvent accessibility on protein evolution
    • Goldman N, Thorne JL, Jones DT, (1998) Assessing the impact of secondary structure and solvent accessibility on protein evolution. Genetics 149: 445-458.
    • (1998) Genetics , vol.149 , pp. 445-458
    • Goldman, N.1    Thorne, J.L.2    Jones, D.T.3
  • 18
    • 34047204789 scopus 로고    scopus 로고
    • Proportion of solvent-exposed amino acids in a protein and rate of protein evolution
    • Lin Y-S, Hsu W-L, Hwang J-K, Li W-H, (2007) Proportion of solvent-exposed amino acids in a protein and rate of protein evolution. Mol Biol Evol 24: 1005-1011.
    • (2007) Mol Biol Evol , vol.24 , pp. 1005-1011
    • Lin, Y.-S.1    Hsu, W.-L.2    Hwang, J.-K.3    Li, W.-H.4
  • 19
    • 0036856289 scopus 로고    scopus 로고
    • The pattern of amino acid replacements in alpha/beta-barrels
    • Dean AM, Neuhauser C, Grenier E, Golding GB, (2002) The pattern of amino acid replacements in alpha/beta-barrels. Mol Biol Evol 19: 1846-1864.
    • (2002) Mol Biol Evol , vol.19 , pp. 1846-1864
    • Dean, A.M.1    Neuhauser, C.2    Grenier, E.3    Golding, G.B.4
  • 20
    • 84871840207 scopus 로고    scopus 로고
    • Integrating sequence variation and protein structure to identify sites under selection
    • Meyer AG, Wilke CO, (2013) Integrating sequence variation and protein structure to identify sites under selection. Mol Biol Evol 30: 36-44.
    • (2013) Mol Biol Evol , vol.30 , pp. 36-44
    • Meyer, A.G.1    Wilke, C.O.2
  • 21
    • 70349470948 scopus 로고    scopus 로고
    • Structural and functional constraints in the evolution of protein families
    • Worth CL, Gong S, Blundell TL, (2009) Structural and functional constraints in the evolution of protein families. Nat Rev Mol Cell Biol 10: 709-720.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 709-720
    • Worth, C.L.1    Gong, S.2    Blundell, T.L.3
  • 22
    • 34247882072 scopus 로고    scopus 로고
    • Life on the edge: a link between gene expression levels and aggregation rates of human proteins
    • Tartaglia GG, Pechmann S, Dobson CM, Vendruscolo M, (2007) Life on the edge: a link between gene expression levels and aggregation rates of human proteins. Trends Biochem Sci 32: 204-206.
    • (2007) Trends Biochem Sci , vol.32 , pp. 204-206
    • Tartaglia, G.G.1    Pechmann, S.2    Dobson, C.M.3    Vendruscolo, M.4
  • 24
    • 36049027813 scopus 로고    scopus 로고
    • Protein stability imposes limits on organism complexity and speed of molecular evolution
    • Zeldovich KB, Chen P, Shakhnovich EI, (2007) Protein stability imposes limits on organism complexity and speed of molecular evolution. Proc Natl Acad Sci USA 104: 16152-16157.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16152-16157
    • Zeldovich, K.B.1    Chen, P.2    Shakhnovich, E.I.3
  • 25
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM, (1999) Protein misfolding, evolution and disease. Trends Biochem Sci 24: 329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 26
    • 77954743785 scopus 로고    scopus 로고
    • Mutational effects and the evolution of new protein functions
    • Soskine M, Tawfik DS, (2010) Mutational effects and the evolution of new protein functions. Nat Rev Genet 11: 572-582.
    • (2010) Nat Rev Genet , vol.11 , pp. 572-582
    • Soskine, M.1    Tawfik, D.S.2
  • 28
    • 33645649132 scopus 로고    scopus 로고
    • Identification of physicochemical selective pressure on protein encoding nucleotide sequences
    • Wong WSW, Sainudiin R, Nielsen R, (2006) Identification of physicochemical selective pressure on protein encoding nucleotide sequences. BMC Bioinformatics 7: 148.
    • (2006) BMC Bioinformatics , vol.7 , pp. 148
    • Wong, W.S.W.1    Sainudiin, R.2    Nielsen, R.3
  • 29
    • 0033921902 scopus 로고    scopus 로고
    • Rates of conservative and radical nonsynonymous nucleotide substitutions in mammalian nuclear genes
    • Zhang J, (2000) Rates of conservative and radical nonsynonymous nucleotide substitutions in mammalian nuclear genes. J Mol Evol 50: 56-68.
    • (2000) J Mol Evol , vol.50 , pp. 56-68
    • Zhang, J.1
  • 30
    • 43349096923 scopus 로고    scopus 로고
    • A three-state prediction of single point mutations on protein stability changes
    • Capriotti E, Fariselli P, Rossi I, Casadio R, (2008) A three-state prediction of single point mutations on protein stability changes. BMC Bioinformatics 9 (Suppl 2):: S6.
    • (2008) BMC Bioinformatics , vol.9 , Issue.SUPPL. 2
    • Capriotti, E.1    Fariselli, P.2    Rossi, I.3    Casadio, R.4
  • 32
    • 33645764714 scopus 로고    scopus 로고
    • SNPs3D: candidate gene and SNP selection for association studies
    • Yue P, Melamud E, Moult J, (2006) SNPs3D: candidate gene and SNP selection for association studies. BMC Bioinformatics 7: 166.
    • (2006) BMC Bioinformatics , vol.7 , pp. 166
    • Yue, P.1    Melamud, E.2    Moult, J.3
  • 33
    • 84889677831 scopus 로고    scopus 로고
    • Mutational and fitness landscapes of an RNA virus revealed through population sequencing
    • Acevedo A, Brodsky L, Andino R, (2014) Mutational and fitness landscapes of an RNA virus revealed through population sequencing. Nature 505: 686-690.
    • (2014) Nature , vol.505 , pp. 686-690
    • Acevedo, A.1    Brodsky, L.2    Andino, R.3
  • 34
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL, (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41: 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 35
    • 57149116929 scopus 로고    scopus 로고
    • Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation
    • Gsponer J, Futschik ME, Teichmann SA, Babu MM, (2008) Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation. Science 322: 1365-1368.
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 37
    • 70449769325 scopus 로고    scopus 로고
    • Protein-protein interaction networks: how can a hub protein bind so many different partners?
    • Tsai C-J, Ma B, Nussinov R, (2009) Protein-protein interaction networks: how can a hub protein bind so many different partners? Trends Biochem Sci 34: 594-600.
    • (2009) Trends Biochem Sci , vol.34 , pp. 594-600
    • Tsai, C.-J.1    Ma, B.2    Nussinov, R.3
  • 38
    • 0036017388 scopus 로고    scopus 로고
    • Evolutionary rate heterogeneity in proteins with long disordered regions
    • Brown CJ, Takayama S, Campen AM, Vise P, Marshall TW, et al. (2002) Evolutionary rate heterogeneity in proteins with long disordered regions. J Mol Evol 55: 104-110.
    • (2002) J Mol Evol , vol.55 , pp. 104-110
    • Brown, C.J.1    Takayama, S.2    Campen, A.M.3    Vise, P.4    Marshall, T.W.5
  • 40
    • 77249102545 scopus 로고    scopus 로고
    • Comparing models of evolution for ordered and disordered proteins
    • Brown CJ, Johnson AK, Daughdrill GW, (2010) Comparing models of evolution for ordered and disordered proteins. Mol Biol Evol 27: 609-621.
    • (2010) Mol Biol Evol , vol.27 , pp. 609-621
    • Brown, C.J.1    Johnson, A.K.2    Daughdrill, G.W.3
  • 41
    • 0002218484 scopus 로고    scopus 로고
    • Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues
    • Pupko T, Bell RE, Mayrose I, Glaser F, Ben-Tal N, (2002) Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologues. Bioinformatics 18 (Suppl 1):: S71-77.
    • (2002) Bioinformatics , vol.18 , Issue.SUPPL. 1
    • Pupko, T.1    Bell, R.E.2    Mayrose, I.3    Glaser, F.4    Ben-Tal, N.5
  • 42
    • 77953718211 scopus 로고    scopus 로고
    • Sequence space and the ongoing expansion of the protein universe
    • Povolotskaya IS, Kondrashov FA, (2010) Sequence space and the ongoing expansion of the protein universe. Nature 465: 922-926.
    • (2010) Nature , vol.465 , pp. 922-926
    • Povolotskaya, I.S.1    Kondrashov, F.A.2
  • 43
    • 84870427355 scopus 로고    scopus 로고
    • Cellular strategies for regulating functional and nonfunctional protein aggregation
    • Gsponer J, Babu MM, (2012) Cellular strategies for regulating functional and nonfunctional protein aggregation. Cell Rep 2: 1425-1437.
    • (2012) Cell Rep , vol.2 , pp. 1425-1437
    • Gsponer, J.1    Babu, M.M.2
  • 44
    • 67649635978 scopus 로고    scopus 로고
    • Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity
    • Vavouri T, Semple JI, Garcia-Verdugo R, Lehner B, (2009) Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 138: 198-208.
    • (2009) Cell , vol.138 , pp. 198-208
    • Vavouri, T.1    Semple, J.I.2    Garcia-Verdugo, R.3    Lehner, B.4
  • 45
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies, from a structural perspective
    • Todd AE, Orengo CA, Thornton JM, (2001) Evolution of function in protein superfamilies, from a structural perspective. J Mol Biol 307: 1113-1143.
    • (2001) J Mol Biol , vol.307 , pp. 1113-1143
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 46
    • 33847249901 scopus 로고    scopus 로고
    • Specificity and evolvability in eukaryotic protein interaction networks
    • Beltrao P, Serrano L, (2007) Specificity and evolvability in eukaryotic protein interaction networks. PLoS Comput Biol 3: e25.
    • (2007) PLoS Comput Biol , vol.3
    • Beltrao, P.1    Serrano, L.2
  • 49
    • 77957921373 scopus 로고    scopus 로고
    • A simple definition of structural regions in proteins and its use in analyzing interface evolution
    • Levy ED, (2010) A simple definition of structural regions in proteins and its use in analyzing interface evolution. J Mol Biol 403: 660-670.
    • (2010) J Mol Biol , vol.403 , pp. 660-670
    • Levy, E.D.1
  • 52
    • 84870901239 scopus 로고    scopus 로고
    • Cellular crowding imposes global constraints on the chemistry and evolution of proteomes
    • Levy ED, De S, Teichmann SA, (2012) Cellular crowding imposes global constraints on the chemistry and evolution of proteomes. Proc Natl Acad Sci USA 109: 20461-20466.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 20461-20466
    • Levy, E.D.1    De, S.2    Teichmann, S.A.3
  • 53
    • 84873419140 scopus 로고    scopus 로고
    • The Ribosome as a Hub for Protein Quality Control
    • Pechmann S, Willmund F, Frydman J, (2013) The Ribosome as a Hub for Protein Quality Control. Molecular Cell 49: 411-421.
    • (2013) Molecular Cell , vol.49 , pp. 411-421
    • Pechmann, S.1    Willmund, F.2    Frydman, J.3
  • 54
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor of phenotypic variation
    • Queitsch C, Sangster TA, Lindquist S, (2002) Hsp90 as a capacitor of phenotypic variation. Nature 417: 618-624.
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1    Sangster, T.A.2    Lindquist, S.3
  • 55
    • 78650644709 scopus 로고    scopus 로고
    • Hsp90 and environmental stress transform the adaptive value of natural genetic variation
    • Jarosz DF, Lindquist S, (2010) Hsp90 and environmental stress transform the adaptive value of natural genetic variation. Science 330: 1820-1824.
    • (2010) Science , vol.330 , pp. 1820-1824
    • Jarosz, D.F.1    Lindquist, S.2
  • 56
    • 0037379626 scopus 로고    scopus 로고
    • Between genotype and phenotype: protein chaperones and evolvability
    • Rutherford SL, (2003) Between genotype and phenotype: protein chaperones and evolvability. Nat Rev Genet 4: 263-274.
    • (2003) Nat Rev Genet , vol.4 , pp. 263-274
    • Rutherford, S.L.1
  • 57
    • 77954502545 scopus 로고    scopus 로고
    • A more precise characterization of chaperonin substrates
    • Raineri E, Ribeca P, Serrano L, Maier T, (2010) A more precise characterization of chaperonin substrates. Bioinformatics 26: 1685-1689.
    • (2010) Bioinformatics , vol.26 , pp. 1685-1689
    • Raineri, E.1    Ribeca, P.2    Serrano, L.3    Maier, T.4
  • 58
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • Taipale M, Jarosz DF, Lindquist S, (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 11: 515-528.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 59
    • 77958515735 scopus 로고    scopus 로고
    • The effect of chaperonin buffering on protein evolution
    • Williams TA, Fares MA, (2010) The effect of chaperonin buffering on protein evolution. Genome Biol Evol 2: 609-619.
    • (2010) Genome Biol Evol , vol.2 , pp. 609-619
    • Williams, T.A.1    Fares, M.A.2
  • 60
    • 22744447508 scopus 로고    scopus 로고
    • Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
    • Kerner M, Naylor D, Ishihama Y, Maier T, Chang H-C, et al. (2005) Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122: 209-220.
    • (2005) Cell , vol.122 , pp. 209-220
    • Kerner, M.1    Naylor, D.2    Ishihama, Y.3    Maier, T.4    Chang, H.-C.5
  • 62
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT, (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 63
    • 34848926209 scopus 로고    scopus 로고
    • Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches
    • McClellan AJ, Xia Y, Deutschbauer AM, Davis RW, Gerstein M, et al. (2007) Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches. Cell 131: 121-135.
    • (2007) Cell , vol.131 , pp. 121-135
    • McClellan, A.J.1    Xia, Y.2    Deutschbauer, A.M.3    Davis, R.W.4    Gerstein, M.5
  • 64
    • 84865695733 scopus 로고    scopus 로고
    • Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition
    • Taipale M, Krykbaeva I, Koeva M, Kayatekin C, Westover KD, et al. (2012) Quantitative analysis of hsp90-client interactions reveals principles of substrate recognition. Cell 150: 987-1001.
    • (2012) Cell , vol.150 , pp. 987-1001
    • Taipale, M.1    Krykbaeva, I.2    Koeva, M.3    Kayatekin, C.4    Westover, K.D.5
  • 65
    • 84872577837 scopus 로고    scopus 로고
    • The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis
    • Willmund F, Del Alamo M, Pechmann S, Chen T, Albanèse V, et al. (2013) The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis. Cell 152: 196-209.
    • (2013) Cell , vol.152 , pp. 196-209
    • Willmund, F.1    Del Alamo, M.2    Pechmann, S.3    Chen, T.4    Albanèse, V.5
  • 66
    • 79960923840 scopus 로고    scopus 로고
    • Defining the Specificity of Cotranslationally Acting Chaperones by Systematic Analysis of mRNAs Associated with Ribosome-Nascent Chain Complexes
    • del Alamo M, Hogan DJ, Pechmann S, Albanese V, Brown PO, et al. (2011) Defining the Specificity of Cotranslationally Acting Chaperones by Systematic Analysis of mRNAs Associated with Ribosome-Nascent Chain Complexes. PLoS Biol 9: e1001100.
    • (2011) PLoS Biol , vol.9
    • del Alamo, M.1    Hogan, D.J.2    Pechmann, S.3    Albanese, V.4    Brown, P.O.5
  • 68
    • 34247622363 scopus 로고    scopus 로고
    • The importance of bottlenecks in protein networks: correlation with gene essentiality and expression dynamics
    • Yu H, Kim PM, Sprecher E, Trifonov V, Gerstein M, (2007) The importance of bottlenecks in protein networks: correlation with gene essentiality and expression dynamics. PLoS Comput Biol 3: e59.
    • (2007) PLoS Comput Biol , vol.3
    • Yu, H.1    Kim, P.M.2    Sprecher, E.3    Trifonov, V.4    Gerstein, M.5
  • 69
    • 33748074139 scopus 로고    scopus 로고
    • Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes
    • Haynes C, Oldfield CJ, Ji F, Klitgord N, Cusick ME, et al. (2006) Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput Biol 2: e100.
    • (2006) PLoS Comput Biol , vol.2
    • Haynes, C.1    Oldfield, C.J.2    Ji, F.3    Klitgord, N.4    Cusick, M.E.5
  • 70
    • 84865730325 scopus 로고    scopus 로고
    • Protein biophysics explains why highly abundant proteins evolve slowly
    • Serohijos AWR, Rimas Z, Shakhnovich EI, (2012) Protein biophysics explains why highly abundant proteins evolve slowly. Cell Reports 2: 249-256.
    • (2012) Cell Reports , vol.2 , pp. 249-256
    • Serohijos, A.W.R.1    Rimas, Z.2    Shakhnovich, E.I.3
  • 71
    • 79851508882 scopus 로고    scopus 로고
    • Bringing order to protein disorder through comparative genomics and genetic interactions
    • Bellay J, Han S, Michaut M, Kim T, Costanzo M, et al. (2011) Bringing order to protein disorder through comparative genomics and genetic interactions. Genome Biol 12: R14.
    • (2011) Genome Biol , vol.12
    • Bellay, J.1    Han, S.2    Michaut, M.3    Kim, T.4    Costanzo, M.5
  • 72
    • 84876357365 scopus 로고    scopus 로고
    • The Protein Chaperone HSP90 Can Facilitate the Divergence of Gene Duplicates
    • Lachowiec J, Lemus T, Thomas JH, Murphy PJM, Nemhauser JL, et al. (2013) The Protein Chaperone HSP90 Can Facilitate the Divergence of Gene Duplicates. Genetics 193: 1269-1277.
    • (2013) Genetics , vol.193 , pp. 1269-1277
    • Lachowiec, J.1    Lemus, T.2    Thomas, J.H.3    Murphy, P.J.M.4    Nemhauser, J.L.5
  • 73
    • 84866267075 scopus 로고    scopus 로고
    • Escape from Adaptive Conflict follows from weak functional trade-offs and mutational robustness
    • Sikosek T, Chan HS, Bornberg-Bauer E, (2012) Escape from Adaptive Conflict follows from weak functional trade-offs and mutational robustness. Proc Natl Acad Sci USA 109: 14888-14893.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 14888-14893
    • Sikosek, T.1    Chan, H.S.2    Bornberg-Bauer, E.3
  • 74
    • 84876896201 scopus 로고    scopus 로고
    • Evolutionary capacitance and control of protein stability in protein-protein interaction networks
    • Dixit PD, Maslov S, (2013) Evolutionary capacitance and control of protein stability in protein-protein interaction networks. PLoS Comput Biol 9: e1003023.
    • (2013) PLoS Comput Biol , vol.9
    • Dixit, P.D.1    Maslov, S.2
  • 75
    • 79959543603 scopus 로고    scopus 로고
    • Non-adaptive origins of interactome complexity
    • Fernández A, Lynch M, (2011) Non-adaptive origins of interactome complexity. Nature 474: 502-505.
    • (2011) Nature , vol.474 , pp. 502-505
    • Fernández, A.1    Lynch, M.2
  • 76
    • 56849091295 scopus 로고    scopus 로고
    • Network hubs buffer environmental variation in Saccharomyces cerevisiae
    • Levy SF, Siegal ML, (2008) Network hubs buffer environmental variation in Saccharomyces cerevisiae. PLoS Biol 6: e264.
    • (2008) PLoS Biol , vol.6
    • Levy, S.F.1    Siegal, M.L.2
  • 77
    • 84867644046 scopus 로고    scopus 로고
    • A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function
    • Araya CL, Fowler DM, Chen W, Muniez I, Kelly JW, et al. (2012) A fundamental protein property, thermodynamic stability, revealed solely from large-scale measurements of protein function. Proc Natl Acad Sci USA 109: 16858-16863.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 16858-16863
    • Araya, C.L.1    Fowler, D.M.2    Chen, W.3    Muniez, I.4    Kelly, J.W.5
  • 78
    • 84875461582 scopus 로고    scopus 로고
    • Diversity in the origins of proteostasis networks - a driver for protein function in evolution
    • Powers ET, Balch WE, (2013) Diversity in the origins of proteostasis networks- a driver for protein function in evolution. Nat Rev Mol Cell Biol 14: 237-248.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 237-248
    • Powers, E.T.1    Balch, W.E.2
  • 80
    • 0022507362 scopus 로고
    • Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions
    • Nei M, Gojobori T, (1986) Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions. Mol Biol Evol 3: 418-426.
    • (1986) Mol Biol Evol , vol.3 , pp. 418-426
    • Nei, M.1    Gojobori, T.2
  • 84
    • 33846165487 scopus 로고    scopus 로고
    • Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation
    • Lu P, Vogel C, Wang R, Yao X, Marcotte EM, (2007) Absolute protein expression profiling estimates the relative contributions of transcriptional and translational regulation. Nat Biotechnol 25: 117-124.
    • (2007) Nat Biotechnol , vol.25 , pp. 117-124
    • Lu, P.1    Vogel, C.2    Wang, R.3    Yao, X.4    Marcotte, E.M.5
  • 86
    • 80053976720 scopus 로고    scopus 로고
    • An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine
    • Echeverría PC, Bernthaler A, Dupuis P, Mayer B, Picard D, (2011) An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine. PLoS ONE 6: e26044.
    • (2011) PLoS ONE , vol.6
    • Echeverría, P.C.1    Bernthaler, A.2    Dupuis, P.3    Mayer, B.4    Picard, D.5
  • 87
    • 33845401010 scopus 로고    scopus 로고
    • Testing the significance of categorical predictor variables in nonparametric regression models
    • Racine JS, Hart J, Li Q, (2006) Testing the significance of categorical predictor variables in nonparametric regression models. Econometric Reviews 25: 523-544.
    • (2006) Econometric Reviews , vol.25 , pp. 523-544
    • Racine, J.S.1    Hart, J.2    Li, Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.