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Volumn 9, Issue 2, 2014, Pages

A model of proteostatic energy cost and its use in analysis of proteome trends and sequence evolution

Author keywords

[No Author keywords available]

Indexed keywords

PROTEOME; ESCHERICHIA COLI PROTEIN;

EID: 84896515245     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0090504     Document Type: Article
Times cited : (26)

References (84)
  • 2
    • 0002655873 scopus 로고
    • Life as a manifestation of the second law of thermodynamics
    • Schneider ED, Kay JJ (1994). Life as a manifestation of the second law of thermodynamics. Math Comput Model 19: 25-48.
    • (1994) Math Comput Model , vol.19 , pp. 25-48
    • Schneider, E.D.1    Kay, J.J.2
  • 3
    • 78649676398 scopus 로고    scopus 로고
    • Natural patterns of energy dispersal
    • Makela T, Annila A (2010) Natural patterns of energy dispersal. Phys Life Rev 7: 477-498.
    • (2010) Phys Life Rev , vol.7 , pp. 477-498
    • Makela, T.1    Annila, A.2
  • 4
    • 33646182934 scopus 로고    scopus 로고
    • An integrated view of protein evolution
    • Pal 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
    • Pal, C.1    Papp, B.2    Lercher, M.J.3
  • 5
    • 23944490117 scopus 로고    scopus 로고
    • Missense meanderings in sequence space: A biophysical view of protein evolution
    • DOI 10.1038/nrg1672
    • DePristo MA, Weinreich DM, Hartl DL (2005) Missense meanderings in sequence space: a biophysical view of protein evolution. Nat Rev Genet 6: 678-687. (Pubitemid 41192319)
    • (2005) Nature Reviews Genetics , vol.6 , Issue.9 , pp. 678-687
    • DePristo, M.A.1    Weinreich, D.M.2    Hartl, D.L.3
  • 6
    • 0035823119 scopus 로고    scopus 로고
    • Understanding hierarchical protein evolution from first principles
    • DOI 10.1006/jmbi.2001.4949
    • Dokholyan NV, Shakhnovich EI (2001) Understanding hierarchical protein evolution from first principles. J Mol Biol 312: 289-307. (Pubitemid 32835693)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.1 , pp. 289-307
    • Dokholyan, N.V.1    Shakhnovich, E.I.2
  • 7
    • 0036306115 scopus 로고    scopus 로고
    • Why are proteins so robust to site mutations?
    • DOI 10.1006/jmbi.2001.5226
    • Taverna DM, Goldstein RA (2002) Why are proteins so robust to site mutations? J Mol Biol 315: 479-484. (Pubitemid 34729355)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.3 , pp. 479-484
    • Taverna, D.M.1    Goldstein, R.A.2
  • 8
    • 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
  • 9
    • 0021799353 scopus 로고
    • Insertion mutagenesis to increase secondary structure within the 5' noncoding region of a eukaryotic mRNA reduces translational efficiency
    • Pelletier J, Sonenberg N (1985). Insertion mutagenesis to increase secondary structure within the 59 noncoding region of a eukaryotic mRNA reduces translational efficiency. Cell 40: 515-526. (Pubitemid 15076569)
    • (1985) Cell , vol.40 , Issue.3 , pp. 515-526
    • Pelletier, J.1    Sonenberg, N.2
  • 10
  • 12
    • 41949103740 scopus 로고    scopus 로고
    • The structure of protein evolution and the evolution of protein structure
    • Goldstein RA (2008) The structure of protein evolution and the evolution of protein structure. Curr Opin Struct Biol 18: 170-177.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 170-177
    • Goldstein, R.A.1
  • 13
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • Tokuriki N, Tawfik DS (2009) Stability effects of mutations and protein evolvability. Curr Opin Struct Biol 19: 596-604.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 14
    • 47649121227 scopus 로고    scopus 로고
    • Natural selection against protein aggregation on self-interacting and essential proteins in yeast, fly, and worm
    • DOI 10.1093/molbev/msn122
    • Chen Y, Dokholyan NV (2008) Natural selection against protein aggregation on self-interacting and essential proteins in yeast, fly, and worm. Mol Biol Evol 25: 1530-1533. (Pubitemid 352019857)
    • (2008) Molecular Biology and Evolution , vol.25 , Issue.8 , pp. 1530-1533
    • Chen, Y.1    Dokholyan, N.V.2
  • 16
    • 47549097539 scopus 로고    scopus 로고
    • Mistranslation-Induced Protein Misfolding as a Dominant Constraint on Coding-Sequence Evolution
    • DOI 10.1016/j.cell.2008.05.042, PII S0092867408007058
    • Drummond DA, Wilke CO (2008). Mistranslation-induced protein misfolding as a dominant constraint on coding-sequence evolution. Cell 134: 341-352. (Pubitemid 352010328)
    • (2008) Cell , vol.134 , Issue.2 , pp. 341-352
    • Drummond, D.A.1    Wilke, C.O.2
  • 18
    • 0026002819 scopus 로고
    • Determinants of DNA sequence divergence between Escherichia coli and Salmonella typhimurium: Codon usage, map position and concerted evolution
    • Sharp PM (1991) Determinants of DNA sequence divergence between Escherichia coli and Salmonella typhimurium: codon usage, map position and concerted evolution. J Mol Evol 33: 23-33.
    • (1991) J Mol Evol , vol.33 , pp. 23-33
    • Sharp, P.M.1
  • 19
    • 0034978556 scopus 로고    scopus 로고
    • Highly expressed genes in yeast evolve slowly
    • Pal C, Papp B, Hurst LD (2001) Highly expressed genes in yeast evolve slowly. Genetics 158: 927-931. (Pubitemid 32552328)
    • (2001) Genetics , vol.158 , Issue.2 , pp. 927-931
    • Pal, C.1    Papp, B.2    Hurst, L.D.3
  • 20
    • 1542286776 scopus 로고    scopus 로고
    • Mammalian Housekeeping Genes Evolve More Slowly than Tissue-Specific Genes
    • DOI 10.1093/molbev/msh010
    • Zhang L, Li WH (2004) Mammalian housekeeping genes evolve more slowly than tissue-specific genes. Mol Biol Evol 21: 236-239. (Pubitemid 38314611)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.2 , pp. 236-239
    • Zhang, L.1    Li, W.-H.2
  • 21
    • 6344241652 scopus 로고    scopus 로고
    • Conservation and coevolution in the scale-free human gene coexpression network
    • DOI 10.1093/molbev/msh222
    • Jordan IK, Marino-Ramirez L, Wolf YI, Koonin EV (2004) Conservation and coevolution in the scale-free human gene coexpression network. Mol Biol Evol 21: 2058-2070. (Pubitemid 39391982)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.11 , pp. 2058-2070
    • Jordan, I.K.1    Marino-Ramirez, L.2    Wolf, Y.I.3    Koonin, E.V.4
  • 22
    • 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 rep 2: 249-256.
    • (2012) Cell Rep , vol.2 , pp. 249-256
    • Serohijos, A.W.R.1    Rimas, Z.2    Shakhnovich, E.I.3
  • 24
    • 77649250720 scopus 로고    scopus 로고
    • Universal distribution of protein evolution rates as a consequence of protein folding physics
    • Lobkovsky AE, Wolf YI, Koonin EV (2010) Universal distribution of protein evolution rates as a consequence of protein folding physics. Proc Natl Acad Sci USA 107: 2983-2988.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2983-2988
    • Lobkovsky, A.E.1    Wolf, Y.I.2    Koonin, E.V.3
  • 25
    • 84864258618 scopus 로고    scopus 로고
    • A whole-cell computational model predicts phenotype from genotype
    • Karr JR, Sanghvi JC, Macklin DN, Gutschow MV, Jacobs JM, et al. (2012) A whole-cell computational model predicts phenotype from genotype. Cell: 150, 389-401.
    • (2012) Cell , vol.150 , pp. 389-401
    • Karr, J.R.1    Sanghvi, J.C.2    Macklin, D.N.3    Gutschow, M.V.4    Jacobs, J.M.5
  • 26
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S, Maurizi MR, Gottesman S (1999) Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins. Science 286: 1888-1893. (Pubitemid 129515889)
    • (1999) Science , vol.286 , Issue.5446 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 28
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov PL, Khechinashvili NN (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J Mol Biol 86: 665-684.
    • (1974) J Mol Biol , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 29
    • 34248674895 scopus 로고    scopus 로고
    • The Stability Effects of Protein Mutations Appear to be Universally Distributed
    • DOI 10.1016/j.jmb.2007.03.069, PII S0022283607004342
    • Tokuriki N, Stricher F, Schymkowitz J, Serrano L, Tawfik DS (2007) The stability effects of protein mutations appear to be universally distributed. J Mol Biol 369: 1318-1332. (Pubitemid 46770766)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.5 , pp. 1318-1332
    • Tokuriki, N.1    Stricher, F.2    Schymkowitz, J.3    Serrano, L.4    Tawfik, D.S.5
  • 31
    • 65349188084 scopus 로고    scopus 로고
    • Do amino acid biosynthetic costs constrain protein evolution in Saccharomyces cerevisiae?
    • Raiford DW, Heizer EM Jr, Miller RV, Akashi H, Raymer ML, et al. (2008) Do amino acid biosynthetic costs constrain protein evolution in Saccharomyces cerevisiae? J Mol Evol 67: 621-630.
    • (2008) J Mol Evol , vol.67 , pp. 621-630
    • Raiford, D.W.1    Heizer Jr., E.M.2    Miller, R.V.3    Akashi, H.4    Raymer, M.L.5
  • 32
    • 19544389317 scopus 로고    scopus 로고
    • Energy constraints on the evolution of gene expression
    • DOI 10.1093/molbev/msi126
    • Wagner A (2005) Energy constraints on the evolution of gene expression. Mol Biol Evol 22: 1365-1374. (Pubitemid 40734188)
    • (2005) Molecular Biology and Evolution , vol.22 , Issue.6 , pp. 1365-1374
    • Wagner, A.1
  • 33
    • 34248157233 scopus 로고    scopus 로고
    • Selection on synthesis cost affects interprotein amino acid usage in all three domains of life
    • DOI 10.1007/s00239-006-0206-8
    • Swire J (2007) Selection on synthesis cost affects interprotein amino acid usage in all three domains of life. J Mol Evol 64: 558-571. (Pubitemid 46717932)
    • (2007) Journal of Molecular Evolution , vol.64 , Issue.5 , pp. 558-571
    • Swire, J.1
  • 34
    • 0002430462 scopus 로고
    • Metabolic basis of energy expenditure with particular reference to protein
    • (eds. Garrow JS, Halliday D), John Libbey, London
    • Reeds PJ, Fuller MF, Nicholson BA (1985). Metabolic basis of energy expenditure with particular reference to protein. In Substrate and Energy Metabolism in Man (eds. Garrow JS, Halliday D), pp. 46-57. John Libbey, London.
    • (1985) Substrate and Energy Metabolism in Man , pp. 46-57
    • Reeds, P.J.1    Fuller, M.F.2    Nicholson, B.A.3
  • 35
    • 0029131988 scopus 로고
    • Whole-body protein turnover in humans-past, present, and future
    • Waterlow JC (1995) Whole-body protein turnover in humans-past, present, and future. Annu Rev Nutr 15: 57-92.
    • (1995) Annu Rev Nutr , vol.15 , pp. 57-92
    • Waterlow, J.C.1
  • 36
    • 79957477837 scopus 로고    scopus 로고
    • Post-prandial changes in protein synthesis in red drum (Sciaenops ocellatus) larvae
    • McCarthy ID, Fuiman LA (2011) Post-prandial changes in protein synthesis in red drum (Sciaenops ocellatus) larvae. J Exp Biol 214: 1821-1828.
    • (2011) J Exp Biol , vol.214 , pp. 1821-1828
    • McCarthy, I.D.1    Fuiman, L.A.2
  • 37
    • 0002178806 scopus 로고
    • Protein synthesis and oxygen consumption in fish cells
    • Smith RW, Houlihan DF (1995) Protein synthesis and oxygen consumption in fish cells. J Comp Physiol B 165: 93-101.
    • (1995) J Comp Physiol B , vol.165 , pp. 93-101
    • Smith, R.W.1    Houlihan, D.F.2
  • 38
    • 0034046580 scopus 로고    scopus 로고
    • Respiratory costs and rate of protein turnover in the roots of a fast-growing (Dactylis glomerata L.) and a slow-growing (Festuca ovina L.) grass species
    • Scheurwater I, Dünnebacke M, Eising R, Lambers H (2000) Respiratory costs and rate of protein turnover in the roots of a fast-growing (Dactylis glomerata L.) and a slow-growing (Festuca ovina L.) grass species. J Exp Bot 51: 1089-1097. (Pubitemid 30343428)
    • (2000) Journal of Experimental Botany , vol.51 , Issue.347 , pp. 1089-1097
    • Scheurwater, I.1    Dunnebacke, M.2    Eising, R.3    Lambers, H.4
  • 40
    • 33846829568 scopus 로고    scopus 로고
    • Protein metabolism in marine animals: The underlying mechanism of growth
    • DOI 10.1016/S0065-2881(06)52003-6, PII S0065288106520036
    • Fraser KPP, Rogers AD (2007). Protein metabolism in marine animals: the underlying mechanism of growth. Adv Mar Biol 52: 267-362. (Pubitemid 46217105)
    • (2007) Advances in Marine Biology , vol.52 , pp. 267-362
    • Fraser, K.P.P.1    Rogers, A.D.2
  • 41
    • 84867460758 scopus 로고    scopus 로고
    • Bioinorganic chemistry of Alzheimer's disease
    • Kepp KP (2012) Bioinorganic chemistry of Alzheimer's disease. Chem Rev 112: 5193-5239.
    • (2012) Chem Rev , vol.112 , pp. 5193-5239
    • Kepp, K.P.1
  • 43
    • 84859163965 scopus 로고    scopus 로고
    • Allosteric function and dysfunction of the prion protein
    • Linden R, Cordeiro Y, Lima LM (2012) Allosteric function and dysfunction of the prion protein. Cell Mol Life Sci 69: 1105-1124.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1105-1124
    • Linden, R.1    Cordeiro, Y.2    Lima, L.M.3
  • 44
    • 77957129279 scopus 로고    scopus 로고
    • The rate of the molecular clock and the cost of gratuitous protein synthesis
    • Plata G, Gottesman ME, Vitkup D (2010) The rate of the molecular clock and the cost of gratuitous protein synthesis. Genome Biol 11: R98.
    • (2010) Genome Biol , vol.11
    • Plata, G.1    Gottesman, M.E.2    Vitkup, D.3
  • 45
    • 0024456475 scopus 로고
    • The role of mRNA and protein stability in gene expression
    • Hargrove JL, Schmidt FH (1989) The role of mRNA and protein stability in gene expression. FASEB J 3: 2360-2370. (Pubitemid 19263711)
    • (1989) FASEB Journal , vol.3 , Issue.12 , pp. 2360-2370
    • Hargrove, J.L.1    Schmidt, F.H.2
  • 46
    • 0021760637 scopus 로고
    • Codon usage can affect efficiency of translation of genes in Escherichia coli
    • Robinson M, Lilley R, Little S, Emtage JS, Yarranton G, et al. (1984) Codon usage can affect efficiency of translation of genes in Escherichia coli. Nucleic Acids Res 12: 6663-6671.
    • (1984) Nucleic Acids Res , vol.12 , pp. 6663-6671
    • Robinson, M.1    Lilley, R.2    Little, S.3    Emtage, J.S.4    Yarranton, G.5
  • 47
    • 84888838351 scopus 로고    scopus 로고
    • Primate transcript and protein expression levels evolve under compensatory selection pressures
    • Khan Z, Ford MJ, Cusanovich DA, Mitrano A, Pritchard JK, et al. (2013) Primate transcript and protein expression levels evolve under compensatory selection pressures. Science 342: 1100-1104.
    • (2013) Science , vol.342 , pp. 1100-1104
    • Khan, Z.1    Ford, M.J.2    Cusanovich, D.A.3    Mitrano, A.4    Pritchard, J.K.5
  • 48
    • 84872272432 scopus 로고    scopus 로고
    • Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness
    • Bershtein S, Mu W, Serohijos AWR, Zhou J, Shakhnovich EI (2013). Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness. Mol Cell 49: 133-144.
    • (2013) Mol Cell , vol.49 , pp. 133-144
    • Bershtein, S.1    Mu, W.2    Serohijos, A.W.R.3    Zhou, J.4    Shakhnovich, E.I.5
  • 51
    • 80053254848 scopus 로고    scopus 로고
    • Integrated prediction of protein folding and unfolding rates from only size and structural class
    • De Sancho D, Muñoz V (2011) Integrated prediction of protein folding and unfolding rates from only size and structural class. Phys Chem Chem Phys 13: 17030-17043.
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 17030-17043
    • De Sancho, D.1    Muñoz, V.2
  • 53
    • 84870169302 scopus 로고    scopus 로고
    • Driving the cell cycle through metabolism
    • Cai L, Tu BP (2012) Driving the Cell Cycle Through Metabolism. Annu Rev Cell Dev Biol 28: 59-87.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 59-87
    • Cai, L.1    Tu, B.P.2
  • 54
    • 0035929127 scopus 로고    scopus 로고
    • Effects of size and temperature on metabolic rate
    • DOI 10.1126/science.1061967
    • Gillooly JF, Brown JH, West GB, Savage VM, Charnov EL (2001) Effects of size and temperature on metabolic rate. Science 293: 2248-2251. (Pubitemid 32900233)
    • (2001) Science , vol.293 , Issue.5538 , pp. 2248-2251
    • Gillooly, J.F.1    Brown, J.H.2    West, G.B.3    Savage, V.M.4    Charnov, E.L.5
  • 55
    • 0037327334 scopus 로고    scopus 로고
    • Identification of pseudogenes in the Drosophila melanogaster genome
    • DOI 10.1093/nar/gkg169
    • Harrison PM, Milburn D, Zhang Z, Bertone P, Gerstein M (2003) Identification of pseudogenes in the Drosophila melanogaster genome. Nucleic Acids Res 31:1033-1037. (Pubitemid 36240442)
    • (2003) Nucleic Acids Research , vol.31 , Issue.3 , pp. 1033-1037
    • Harrison, P.M.1    Milburn, D.2    Zhang, Z.3    Bertone, P.4    Gerstein, M.5
  • 56
    • 0037248908 scopus 로고    scopus 로고
    • ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation
    • DOI 10.1016/S1097-2765(02)00775-X
    • Benaroudj N, Zwickl P, Seemuller E, Baumeister W, Goldberg AL (2003). ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol Cell 11: 69-78. (Pubitemid 36126591)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 69-78
    • Benaroudj, N.1    Zwickl, P.2    Seemuller, E.3    Baumeister, W.4    Goldberg, A.L.5
  • 58
    • 0002063111 scopus 로고
    • Energy costs of protein turnover: Theoretical calculation and experimental estimation from regression of respiration on protein concentration of fullgrown leaves
    • Eds: Lambers H, van der Plas LHW. SPB Acad Publ, The Hague
    • De Visser R, Spitters CJT, Bouma TJ (1992) Energy costs of protein turnover: theoretical calculation and experimental estimation from regression of respiration on protein concentration of fullgrown leaves. In: Molecular, biochemical and physiological aspects of plant respiration Eds: Lambers H, van der Plas LHW. SPB Acad Publ, The Hague: 493-508.
    • (1992) Molecular, Biochemical and Physiological Aspects of Plant Respiration , pp. 493-508
    • De Visser, R.1    Spitters, C.J.T.2    Bouma, T.J.3
  • 59
    • 0000822580 scopus 로고
    • Further studies on the nature and causes of gene mutations
    • Muller HJ (1932) Further studies on the nature and causes of gene mutations. Proc 6th Int Congr Genet 1: 213-255.
    • (1932) Proc 6th Int Congr Genet , vol.1 , pp. 213-255
    • Muller, H.J.1
  • 60
    • 78650652614 scopus 로고    scopus 로고
    • Compensatory expression and substrate inducibility of gamma-glutamyl transferase GGT2 isoform in Arabidopsis thaliana
    • Destro T, Prasad D, Martignago D, Bernet IL, Trentin AR, et al. (2011) Compensatory expression and substrate inducibility of gamma-glutamyl transferase GGT2 isoform in Arabidopsis thaliana. J Exp Bot 62(2): 805-814.
    • (2011) J Exp Bot , vol.62 , Issue.2 , pp. 805-814
    • Destro, T.1    Prasad, D.2    Martignago, D.3    Bernet, I.L.4    Trentin, A.R.5
  • 61
    • 22144475073 scopus 로고    scopus 로고
    • OxyR mediated compensatory expression between ahpC and katA and the significance of ahpC in protection from hydrogen peroxide in Xanthomonas campestris
    • DOI 10.1016/j.femsle.2005.06.002, PII S0378109705003642
    • Charoenlap N, Eiamphungporn W, Chauvatcharin N, Utamapongchai S, Vattanaviboon P, et al. (2005) OxyR mediated compensatory expression between ahpC and katA and the significance of ahpC in protection from hydrogen peroxide in Xanthomonas campestris. FEMS Microbiol Lett 249: 73-78. (Pubitemid 40981882)
    • (2005) FEMS Microbiology Letters , vol.249 , Issue.1 , pp. 73-78
    • Charoenlap, N.1    Eiamphungporn, W.2    Chauvatcharin, N.3    Utamapongchai, S.4    Vattanaviboon, P.5    Mongkolsuk, S.6
  • 62
    • 0021343093 scopus 로고
    • Is there a threshold level of fetal hemoglobin that ameliorates morbidity in sickle cell anemia?
    • Powars D, Weiss JN, Chan LS, Schroeder WA (1984) Is there a threshold level of fetal hemoglobin that ameliorates morbidity in sickle cell anemia? Blood 63(4): 921-926. (Pubitemid 14141316)
    • (1984) Blood , vol.63 , Issue.4 , pp. 921-926
    • Powars, D.R.1    Weiss, J.N.2    Chan, L.S.3    Schroeder, W.A.4
  • 63
    • 0024393875 scopus 로고
    • Whole body protein turnover and resting metabolite rate in homozygous sickle cell disease
    • Badaloo A, Jackson AA, Jahoor F (1989) Whole body protein turnover and resting metabolic rate in homozygous sickle cell disease. Clinical Sci 77: 93-97. (Pubitemid 19154030)
    • (1989) Clinical Science , vol.77 , Issue.1 , pp. 93-97
    • Badaloo, A.1    Jackson, A.A.2    Jahoor, F.3
  • 64
    • 0025265724 scopus 로고
    • Increased expression of mutant forms of p53 oncogene in primary lung cancer
    • DOI 10.1016/0140-6736(90)90801-B
    • Iggo R, Gatter K, Bartek J, Lane D, Harris AL (1990) Increased expression of mutant forms of p53 oncogene in primary lung cancer. Lancet 335: 675-679. (Pubitemid 20089305)
    • (1990) Lancet , vol.335 , Issue.8691 , pp. 675-679
    • Iggo, R.1    Gatter, K.2    Bartek, J.3    Lane, D.4    Harris, A.L.5
  • 65
    • 23644454631 scopus 로고    scopus 로고
    • Network motifs are enriched with transcription factors whose transcripts have short half-lives
    • DOI 10.1016/j.tig.2005.06.013, PII S0168952505001903
    • Wang E, Purisima E (2005) Network motifs are enriched with transcription factors whose transcripts have short half-lives. Trends Genet 21: 492-495. (Pubitemid 41132582)
    • (2005) Trends in Genetics , vol.21 , Issue.9 , pp. 492-495
    • Wang, E.1    Purisima, E.2
  • 66
    • 33748143748 scopus 로고    scopus 로고
    • Structural determinants of the rate of protein evolution in yeast
    • DOI 10.1093/molbev/msl040
    • Bloom JD, Drummond DA, Arnold FH, Wilke CO (2006) Structural determinants of the rate of protein evolution in yeast (2006) Mol Biol Evol 23: 1751-1761. (Pubitemid 44309769)
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.9 , pp. 1751-1761
    • Bloom, J.D.1    Drummond, D.A.2    Arnold, F.H.3    Wilke, C.O.4
  • 67
    • 0000800333 scopus 로고
    • On the probability of fixation of mutant genes in a population
    • Kimura M (1962) On the probability of fixation of mutant genes in a population. Genetics 47: 713-719.
    • (1962) Genetics , vol.47 , pp. 713-719
    • Kimura, M.1
  • 68
    • 78650217130 scopus 로고    scopus 로고
    • Cellular proteomes have broad distributions of protein stability
    • Ghosh K, Dill K (2010) Cellular proteomes have broad distributions of protein stability. Biophys J 99: 3996-4002.
    • (2010) Biophys J , vol.99 , pp. 3996-4002
    • Ghosh, K.1    Dill, K.2
  • 70
    • 79551674254 scopus 로고    scopus 로고
    • Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast
    • Geiler-Samerotte KA, Dion MF, Budnik VA, Wang SM, Hartl DL, et al. (2011) Misfolded proteins impose a dosage-dependent fitness cost and trigger a cytosolic unfolded protein response in yeast. Proc Natl Acad Sci USA 108: 680-685.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 680-685
    • Geiler-Samerotte, K.A.1    Dion, M.F.2    Budnik, V.A.3    Wang, S.M.4    Hartl, D.L.5
  • 71
    • 80052449370 scopus 로고    scopus 로고
    • How do thermophilic proteins and proteomes withstand high temperature?
    • Sawle L, Ghosh K (2011) How Do Thermophilic Proteins and Proteomes Withstand High Temperature? Biophys J 101: 217-227.
    • (2011) Biophys J , vol.101 , pp. 217-227
    • Sawle, L.1    Ghosh, K.2
  • 72
    • 77950605529 scopus 로고    scopus 로고
    • Thermal adaptation of viruses and bacteria
    • Chen P, Shakhnovich EI (2010) Thermal adaptation of viruses and bacteria. Biophys J 98: 1109-1118.
    • (2010) Biophys J , vol.98 , pp. 1109-1118
    • Chen, P.1    Shakhnovich, E.I.2
  • 73
    • 84873387339 scopus 로고    scopus 로고
    • Highly Abundant Proteins Favor More Stable 3D Structures in Yeast
    • Serohijos AWR, Lee SY, Shakhnovich EI (2013) Highly Abundant Proteins Favor More Stable 3D Structures in Yeast. Biophys J 104: L1-L3.
    • (2013) Biophys J , vol.104
    • Serohijos, A.W.R.1    Lee, S.Y.2    Shakhnovich, E.I.3
  • 74
    • 0002116249 scopus 로고
    • Respiration rates in heterotrophic, free-living protozoa
    • Fenchel T, Finlay BJ (1983) Respiration Rates in Heterotrophic, Free-living Protozoa. Microb Ecol 9: 99-122.
    • (1983) Microb Ecol , vol.9 , pp. 99-122
    • Fenchel, T.1    Finlay, B.J.2
  • 75
    • 0038814293 scopus 로고    scopus 로고
    • Protein turnover in relation to maintenance metabolism at low photon flux in two marine microalgae
    • DOI 10.1046/j.1365-3040.2003.01004.x
    • Quigg A, Beardall J (2003) Protein turnover in relation to maintenance metabolism at low photon flux in two marine microalgae. Plant Cell Environ 26: 693-703. (Pubitemid 36631986)
    • (2003) Plant, Cell and Environment , vol.26 , Issue.5 , pp. 693-703
    • Quigg, A.1    Beardall, J.2
  • 76
    • 0034731415 scopus 로고    scopus 로고
    • Trends of Amino Acid Usage in the proteins from the Unicellular Parasite Giardia lamblia
    • DOI 10.1006/bbrc.2000.4051
    • Garat B, Musto H (2000) Trends of amino acid usage in the proteins from the unicellular parasite Giardia lamblia. Biochem Biophys Res Commun 279: 996-1000. (Pubitemid 32042891)
    • (2000) Biochemical and Biophysical Research Communications , vol.279 , Issue.3 , pp. 996-1000
    • Garat, B.1    Musto, H.2
  • 78
    • 0037308511 scopus 로고    scopus 로고
    • Cost-minimization of amino acid usage
    • DOI 10.1007/s00239-002-2388-z
    • Seligmann H (2003) Cost-minimization of amino acid usage. J Mol Evol 56: 151-161. (Pubitemid 36169683)
    • (2003) Journal of Molecular Evolution , vol.56 , Issue.2 , pp. 151-161
    • Seligmann, H.1
  • 79
    • 0034666040 scopus 로고    scopus 로고
    • Relationship of codon bias to mRNA concentration and protein length in Saccharomyces cerevisiae
    • Coghlan A, Wolfe KH (2000) Relationship of codon bias to mRNA concentration and protein length in Saccharomyces cerevisiae. Yeast 16: 1131-1145.
    • (2000) Yeast , vol.16 , pp. 1131-1145
    • Coghlan, A.1    Wolfe, K.H.2
  • 80
    • 67649774570 scopus 로고    scopus 로고
    • Computing Protein Stabilities from their Chain lengths
    • Ghosh K, Dill KA (2009) Computing Protein Stabilities from their Chain lengths. Proc Natl Acad Sci USA 106: 10649-10654.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10649-10654
    • Ghosh, K.1    Dill, K.A.2
  • 82
    • 79954542203 scopus 로고    scopus 로고
    • The evolution and evolutionary consequences of marginal thermostability in proteins
    • Goldstein RA (2011) The evolution and evolutionary consequences of marginal thermostability in proteins. Proteins 79(5): 1396-1407.
    • (2011) Proteins , vol.79 , Issue.5 , pp. 1396-1407
    • Goldstein, R.A.1
  • 83
    • 77649219156 scopus 로고    scopus 로고
    • Minimization of biosynthetic costs in adaptive gene expression responses of yeast to environmental changes
    • Vilaprinyo E, Alves R, Sorribas A (2010) Minimization of biosynthetic costs in adaptive gene expression responses of yeast to environmental changes. Plos Comput Biol 6: e1000674.
    • (2010) Plos Comput Biol , vol.6
    • Vilaprinyo, E.1    Alves, R.2    Sorribas, A.3
  • 84
    • 84875986323 scopus 로고    scopus 로고
    • Positively selected sites in cetacean myoglobins contribute to protein stability
    • Dasmeh P, Serohijos A, Kepp KP, Shakhnovich EI (2013) Positively Selected Sites in Cetacean Myoglobins Contribute to Protein Stability. Plos Comput Biol 9(3): e1002929.
    • (2013) Plos Comput Biol , vol.9 , Issue.3
    • Dasmeh, P.1    Serohijos, A.2    Kepp, K.P.3    Shakhnovich, E.I.4


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