메뉴 건너뛰기




Volumn 2, Issue 8, 2003, Pages 613-623

Pharmacophylogenomics: Genes, evolution and drug targets

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; ANTIDIABETIC AGENT; DNA TOPOISOMERASE; DNA TOPOISOMERASE (ATP HYDROLYSING); DNA TOPOISOMERASE INHIBITOR; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PROTEIN FARNESYLTRANSFERASE INHIBITOR; RETINOID X RECEPTOR; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR FOXP2; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNCLASSIFIED DRUG;

EID: 0042568725     PISSN: 14741776     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrd1152     Document Type: Review
Times cited : (77)

References (148)
  • 1
    • 0030862610 scopus 로고    scopus 로고
    • Gastrogenomic delights: A moveable feast
    • Eisen, J. A., Kaiser, D. & Myers, R. M. Gastrogenomic delights: a moveable feast. Nature Med. 3, 1076 (1997).
    • (1997) Nature Med. , vol.3 , pp. 1076
    • Eisen, J.A.1    Kaiser, D.2    Myers, R.M.3
  • 2
    • 0031976258 scopus 로고    scopus 로고
    • Phylogenomics: Improving functional predictions for uncharacterized genes by evolutionary analysis
    • Eisen, J. A. Phylogenomics: improving functional predictions for uncharacterized genes by evolutionary analysis. Genome Res. 8, 163-167 (1998).
    • (1998) Genome Res. , vol.8 , pp. 163-167
    • Eisen, J.A.1
  • 3
    • 0029587166 scopus 로고
    • A method to predict functional residues in proteins
    • Casari, G., Sander, C. & Valencia, A. A method to predict functional residues in proteins. Nature Struct. Biol. 2, 171-178 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 171-178
    • Casari, G.1    Sander, C.2    Valencia, A.3
  • 4
    • 0036352010 scopus 로고    scopus 로고
    • Using orthologous and paralogous proteins to identify specificity-determining residues in bacterial transcription factors
    • Mirney, L. A. & Gelfand, M. S. Using orthologous and paralogous proteins to identify specificity-determining residues in bacterial transcription factors. J. Mol. Biol. 321, 7-20 (2002).
    • (2002) J. Mol. Biol. , vol.321 , pp. 7-20
    • Mirney, L.A.1    Gelfand, M.S.2
  • 5
    • 0036595632 scopus 로고    scopus 로고
    • Phylogenetic analysis and gene functional predictions: Phylogenomics in action
    • Eisen, J. A. & Wu, M. Phylogenetic analysis and gene functional predictions: phylogenomics in action. Theor. Popul. Biol. 61, 481-487 (2002).
    • (2002) Theor. Popul. Biol. , vol.61 , pp. 481-487
    • Eisen, J.A.1    Wu, M.2
  • 6
    • 0034465632 scopus 로고    scopus 로고
    • Evolution of human hypoxia tolerance physiology
    • Hochachka, P. W. & Monge, C. Evolution of human hypoxia tolerance physiology. Adv. Exp. Med. Biol. 475, 25-43 (2000).
    • (2000) Adv. Exp. Med. Biol. , vol.475 , pp. 25-43
    • Hochachka, P.W.1    Monge, C.2
  • 7
    • 0033592940 scopus 로고    scopus 로고
    • Ig-like domains: Evolution from simple interaction molecules to sophisticated antigen recognition
    • Barclay, A. N. Ig-like domains: evolution from simple interaction molecules to sophisticated antigen recognition. Proc. Natl. Acad. Sci. USA 96, 14672-14674 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14672-14674
    • Barclay, A.N.1
  • 9
    • 17944377728 scopus 로고    scopus 로고
    • Evolutionary epidemiology and manic depression
    • Wilson, D. R. Evolutionary epidemiology and manic depression. Br. J. Med. Psychol. 71, 375-395 (1998).
    • (1998) Br. J. Med. Psychol. , vol.71 , pp. 375-395
    • Wilson, D.R.1
  • 10
    • 0033648041 scopus 로고    scopus 로고
    • Evolutionary biology and the concept of disease
    • Gammelgaard, A. Evolutionary biology and the concept of disease. Med. Health Care Philos. 3, 109-116 (2000).
    • (2000) Med. Health Care Philos. , vol.3 , pp. 109-116
    • Gammelgaard, A.1
  • 11
    • 0035162592 scopus 로고    scopus 로고
    • The COG database: New developments in phylogenetic classification of proteins from complete genomes
    • Tatusov, R. L. et al. The COG database: new developments in phylogenetic classification of proteins from complete genomes. Nucleic Acids Res. 29, 22-28 (2001).
    • (2001) Nucleic Acids Res. , vol.29 , pp. 22-28
    • Tatusov, R.L.1
  • 12
    • 12244283680 scopus 로고    scopus 로고
    • Modeling the percolation of annotation errors in a database of protein sequences
    • Gilks, W. R. et al. Modeling the percolation of annotation errors in a database of protein sequences. Bioinformatics 18, 1641-1649 (2002).
    • (2002) Bioinformatics , vol.18 , pp. 1641-1649
    • Gilks, W.R.1
  • 14
    • 0036721254 scopus 로고    scopus 로고
    • Protein domain identification and improved sequence similarity searching using PSI-BLAST
    • George, R. A. & Heringa, J. Protein domain identification and improved sequence similarity searching using PSI-BLAST. Proteins 48, 672-681 (2002).
    • (2002) Proteins , vol.48 , pp. 672-681
    • George, R.A.1    Heringa, J.2
  • 15
    • 0032919371 scopus 로고    scopus 로고
    • Protein folds and families: Sequence and structure alignments
    • Holm, L. & Sander, C. Protein folds and families: sequence and structure alignments. Nucleic Acids Res. 27, 244-247 (1999).
    • (1999) Nucleic Acids Res. , vol.27 , pp. 244-247
    • Holm, L.1    Sander, C.2
  • 18
    • 0034350428 scopus 로고    scopus 로고
    • A new method to localize and test the significance of incongruence: Detecting domain shuffling in the nuclear receptor superfamily
    • Thornton, J. W. & DeSalle, R. A new method to localize and test the significance of incongruence: detecting domain shuffling in the nuclear receptor superfamily. Syst. Biol. 49, 183-201 (2000).
    • (2000) Syst. Biol. , vol.49 , pp. 183-201
    • Thornton, J.W.1    DeSalle, R.2
  • 19
    • 0034992826 scopus 로고    scopus 로고
    • The closest BLAST hit is often not the nearest neighbor
    • Koski, L. B. & Golding, G. B. The closest BLAST hit is often not the nearest neighbor J. Mol. Evol. 52, 540-542 (2001).
    • (2001) J. Mol. Evol. , vol.52 , pp. 540-542
    • Koski, L.B.1    Golding, G.B.2
  • 20
    • 0033360956 scopus 로고    scopus 로고
    • Concerted evolution: Molecular mechanism and biological implications
    • Liao, D. Concerted evolution: molecular mechanism and biological implications. Am. J. Hum. Genet. 64, 24-30 (1999).
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 24-30
    • Liao, D.1
  • 21
    • 0033025723 scopus 로고    scopus 로고
    • Evolution of the MHC class I region: The framework hypothesis
    • Amadou, C. Evolution of the MHC class I region: the framework hypothesis. Immunogenetics 49, 362-367 (1999).
    • (1999) Immunogenetics , vol.49 , pp. 362-367
    • Amadou, C.1
  • 22
    • 0003671904 scopus 로고    scopus 로고
    • (eds Hillis, D. M., Moritz, C. & Mable, B. K.) (Sinauer Associates, Sunderland)
    • Swofford, D. L., Olsen, G. J., Waddell, P. J. & Hillis, D. M. in Molecular Systematics (eds Hillis, D. M., Moritz, C. & Mable, B. K.) 407-514 (Sinauer Associates, Sunderland, 1996).
    • (1996) Molecular Systematics , pp. 407-514
    • Swofford, D.L.1    Olsen, G.J.2    Waddell, P.J.3    Hillis, D.M.4
  • 23
    • 0036173130 scopus 로고    scopus 로고
    • Automated ortholog inference from phylogenetic trees and calculation of orthology reliability
    • Storm, C. E. & Sonnhammer, E. L. Automated ortholog inference from phylogenetic trees and calculation of orthology reliability. Bioinformatics 18, 92-99 (2002).
    • (2002) Bioinformatics , vol.18 , pp. 92-99
    • Storm, C.E.1    Sonnhammer, E.L.2
  • 24
    • 0013017592 scopus 로고    scopus 로고
    • Analyzing proteomes by automated phylogenomics using resampled inference of orthologs
    • Zmasek, C. M. & Eddy, S. R. Analyzing proteomes by automated phylogenomics using resampled inference of orthologs. BMC Bioinformatics 3, 14 (2002).
    • (2002) BMC Bioinformatics , vol.3 , pp. 14
    • Zmasek, C.M.1    Eddy, S.R.2
  • 26
    • 0034204479 scopus 로고    scopus 로고
    • What determines the rate of sequence evolution?
    • Brookfield, J. F. What determines the rate of sequence evolution? Curr. Biol. 10, R410-R411 (2000).
    • (2000) Curr. Biol. , vol.10
    • Brookfield, J.F.1
  • 27
    • 0032767738 scopus 로고    scopus 로고
    • Coumarin metabolism, toxicity and carcinogenicity: Relevance for human risk assessment
    • Lake, B. G. Coumarin metabolism, toxicity and carcinogenicity: relevance for human risk assessment. Food Chem. Toxicol. 37, 423-453 (1999).
    • (1999) Food Chem. Toxicol. , vol.37 , pp. 423-453
    • Lake, B.G.1
  • 28
    • 0003421005 scopus 로고    scopus 로고
    • (Sinauer Associates, Sunderland)
    • Li, W.-H. Molecular Evolution (Sinauer Associates, Sunderland, 1997).
    • (1997) Molecular Evolution
    • Li, W.-H.1
  • 29
    • 0031033277 scopus 로고    scopus 로고
    • Episodic adaptive evolution of primate lysozymes
    • Messier, W. & Stewart, C. B. Episodic adaptive evolution of primate lysozymes. Nature 385, 151-154 (1997).
    • (1997) Nature , vol.385 , pp. 151-154
    • Messier, W.1    Stewart, C.B.2
  • 30
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • Yang, Z. PAML: a program package for phylogenetic analysis by maximum likelihood. Comput. Appl. Biosci. 13, 555-556 (1997).
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 555-556
    • Yang, Z.1
  • 31
    • 0034040754 scopus 로고    scopus 로고
    • Functional inferences from reconstructed evolutionary biology involving rectified databases - An evolutionarily grounded approach to functional genomics
    • Benner, S. A. et al. Functional inferences from reconstructed evolutionary biology involving rectified databases - an evolutionarily grounded approach to functional genomics. Res. Microbiol. 151, 97-106 (2000).
    • (2000) Res. Microbiol. , vol.151 , pp. 97-106
    • Benner, S.A.1
  • 32
    • 0036606898 scopus 로고    scopus 로고
    • Predicting functional divergence in protein evolution by site-specific rate shifts
    • Gaucher, E. A. et al. Predicting functional divergence in protein evolution by site-specific rate shifts. Trends Biochem. Sci. 27, 315-321 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 315-321
    • Gaucher, E.A.1
  • 33
    • 0036134757 scopus 로고    scopus 로고
    • Heterotachy, an important process in protein evolution
    • Lopez, P., Casane, D. & Philippe, H. Heterotachy, an important process in protein evolution. Mol. Biol. Evol. 19, 1-7 (2002).
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1-7
    • Lopez, P.1    Casane, D.2    Philippe, H.3
  • 34
    • 0037307413 scopus 로고    scopus 로고
    • Signatures of natural selection in the human genome
    • Bamshad, M. & Wooding, S. P. Signatures of natural selection in the human genome. Nature Rev. Genet. 4, 99-111 (2003).
    • (2003) Nature Rev. Genet. , vol.4 , pp. 99-111
    • Bamshad, M.1    Wooding, S.P.2
  • 35
    • 0016220238 scopus 로고
    • The hitch-hiking effect of a favourable gene
    • Smith, J. M. & Haigh, J. The hitch-hiking effect of a favourable gene. Genet. Res. Camb. 23, 23-35 (1974).
    • (1974) Genet. Res. Camb. , vol.23 , pp. 23-35
    • Smith, J.M.1    Haigh, J.2
  • 36
    • 0036196885 scopus 로고    scopus 로고
    • The signature of positive selection at randomly chosen loci
    • Przeworski, M. The signature of positive selection at randomly chosen loci. Genetics 160, 1179-1189 (2002).
    • (2002) Genetics , vol.160 , pp. 1179-1189
    • Przeworski, M.1
  • 37
    • 0037015016 scopus 로고    scopus 로고
    • Evidence for an ancient selective sweep in the MHC class I gene repertoire of chimpanzees
    • de Groot, N. G. et al. Evidence for an ancient selective sweep in the MHC class I gene repertoire of chimpanzees. Proc. Natl Acad. Sci. USA 99, 11748-11753 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11748-11753
    • de Groot, N.G.1
  • 38
    • 0036911353 scopus 로고    scopus 로고
    • Interrogating a high-density SNP map for signatures of natural selection
    • Akey, J. M. et al. Interrogating a high-density SNP map for signatures of natural selection. Genome Res. 12, 1805-1814(2002).
    • (2002) Genome Res. , vol.12 , pp. 1805-1814
    • Akey, J.M.1
  • 39
    • 0037158715 scopus 로고    scopus 로고
    • Molecular evolution of FOXP2, a gene involved in speech and language
    • Enard, W. et al. Molecular evolution of FOXP2, a gene involved in speech and language. Nature 418, 869-872 (2002).
    • (2002) Nature , vol.418 , pp. 869-872
    • Enard, W.1
  • 40
    • 0035184334 scopus 로고    scopus 로고
    • Speech disorder in schizophrenia: Review of the literature and exploration of its relation to the uniquely human capacity for language
    • DeLisi, L. E. Speech disorder in schizophrenia: review of the literature and exploration of its relation to the uniquely human capacity for language. Schizophr. Bull. 27, 481-496 (2001).
    • (2001) Schizophr. Bull. , vol.27 , pp. 481-496
    • DeLisi, L.E.1
  • 41
    • 0037224073 scopus 로고    scopus 로고
    • Sequencing the chimpanzee genome: Insights into human evolution and disease
    • Olson, M. V. & Varki, A. Sequencing the chimpanzee genome: insights into human evolution and disease. Nature Rev. Genet. 4, 20-28 (2003).
    • (2003) Nature Rev. Genet. , vol.4 , pp. 20-28
    • Olson, M.V.1    Varki, A.2
  • 42
    • 0036855185 scopus 로고    scopus 로고
    • Abundant raw material for cis-regulatory evolution in humans
    • Rockman, M. V. & Wray, G. A. Abundant raw material for cis-regulatory evolution in humans. Mol. Biol. Evol. 19, 1991-2004 (2002).
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1991-2004
    • Rockman, M.V.1    Wray, G.A.2
  • 43
    • 0035546157 scopus 로고    scopus 로고
    • Gene expression and molecular evolution
    • Akashi, H. Gene expression and molecular evolution. Curr. Opin. Genet. Dev. 11, 660-666 (2001).
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 660-666
    • Akashi, H.1
  • 44
    • 0037320652 scopus 로고    scopus 로고
    • 2 (DRD2) affect mRNA stability and synthesis of the receptor
    • 2 (DRD2) affect mRNA stability and synthesis of the receptor. Hum. Mol. Genet. 12, 205-216 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 205-216
    • Duan, J.1
  • 45
    • 0035252561 scopus 로고    scopus 로고
    • Evidence for purifying selection acting on silent sites in BRCA1
    • Hurst, L. D. & Pal, C. Evidence for purifying selection acting on silent sites in BRCA1. Trends Genet. 17, 62-65 (2001).
    • (2001) Trends Genet. , vol.17 , pp. 62-65
    • Hurst, L.D.1    Pal, C.2
  • 46
    • 0037213551 scopus 로고    scopus 로고
    • Vertebrate evolution: Doubling and shuffling with a full deck
    • Durand, D. Vertebrate evolution: doubling and shuffling with a full deck. Trends Genet. 19, 2-5 (2003).
    • (2003) Trends Genet. , vol.19 , pp. 2-5
    • Durand, D.1
  • 47
    • 0036245495 scopus 로고    scopus 로고
    • Segmental duplications and the evolution of the primate genome
    • Samonte, R. V. & Eichler, E. E. Segmental duplications and the evolution of the primate genome. Nature Rev. Genet. 3, 65-72 (2002).
    • (2002) Nature Rev. Genet. , vol.3 , pp. 65-72
    • Samonte, R.V.1    Eichler, E.E.2
  • 48
    • 0037047628 scopus 로고    scopus 로고
    • Recent segmental duplications in the human genome
    • Bailey, J. A. et al. Recent segmental duplications in the human genome. Science 297, 1003-1007 (2002).
    • (2002) Science , vol.297 , pp. 1003-1007
    • Bailey, J.A.1
  • 49
    • 0037227485 scopus 로고    scopus 로고
    • The temporal distribution of gene duplication events in a set of highly conserved human gene families
    • Friedman, R. & Hughes, A. L. The temporal distribution of gene duplication events in a set of highly conserved human gene families. Mol. Biol. Evol. 20, 154-161 (2003).
    • (2003) Mol. Biol. Evol. , vol.20 , pp. 154-161
    • Friedman, R.1    Hughes, A.L.2
  • 50
    • 18444408683 scopus 로고    scopus 로고
    • TRPV3 is a temperature-sensitive vanilloid receptor-like protein
    • Smith G. D. et al. TRPV3 is a temperature-sensitive vanilloid receptor-like protein. Nature 418, 186-190 (2002).
    • (2002) Nature , vol.418 , pp. 186-190
    • Smith, G.D.1
  • 51
    • 0003293442 scopus 로고    scopus 로고
    • Molecular identification of high and low affinity receptors for nicotinic acid
    • Wise, A. et al. Molecular identification of high and low affinity receptors for nicotinic acid. J. Biol. Chem. 278, 9869-9874 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 9869-9874
    • Wise, A.1
  • 52
    • 0037204017 scopus 로고    scopus 로고
    • Novel angular benzophenazines: Dual topoisomerase I and topoisomerase II inhibitors as potential anticancer agents
    • Vicker, N. et al. Novel angular benzophenazines: dual topoisomerase I and topoisomerase II inhibitors as potential anticancer agents. J. Med. Chem. 45, 721-739 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 721-739
    • Vicker, N.1
  • 53
    • 0037068741 scopus 로고    scopus 로고
    • Anti-tumor activity of GW572016: A dual tyrosine kinase inhibitor blocks EGF activation of EGFR/erbB2 and downstream Erk1/2 and AKT pathways
    • Xia, W. et al. Anti-tumor activity of GW572016: a dual tyrosine kinase inhibitor blocks EGF activation of EGFR/erbB2 and downstream Erk1/2 and AKT pathways. Oncogene 21, 6255-6263 (2002).
    • (2002) Oncogene , vol.21 , pp. 6255-6263
    • Xia, W.1
  • 54
    • 0035893740 scopus 로고    scopus 로고
    • Evaluation of farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical models
    • Lobell, R. B. et al. Evaluation of farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical models. Cancer Res. 61, 8758-8768 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 8758-8768
    • Lobell, R.B.1
  • 55
    • 0037241073 scopus 로고    scopus 로고
    • 5α-reductase inhibitors: What's new?
    • Foley, C. L. & Kirby, R. S. 5α-reductase inhibitors: what's new? Curr. Opin. Urol. 13, 31-37 (2003).
    • (2003) Curr. Opin. Urol. , vol.13 , pp. 31-37
    • Foley, C.L.1    Kirby, R.S.2
  • 56
    • 0034804919 scopus 로고    scopus 로고
    • Lipid biosynthesis as a target for antibacterial agents
    • Heath, R. J., White, S. W. & Rock, C. O. Lipid biosynthesis as a target for antibacterial agents. Prog. Lipid Res. 40, 467-497 (2001).
    • (2001) Prog. Lipid Res. , vol.40 , pp. 467-497
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 57
    • 0034531543 scopus 로고    scopus 로고
    • The new generation of antipsychotic drugs: How atypical are they?
    • Goldstein, J. M. The new generation of antipsychotic drugs: how atypical are they? Int. J. Neuropsychopharmacol. 3, 339-349 (2000).
    • (2000) Int. J. Neuropsychopharmacol. , vol.3 , pp. 339-349
    • Goldstein, J.M.1
  • 58
    • 0031800626 scopus 로고    scopus 로고
    • Seven types of pleiotropy
    • Hodgkin, J. Seven types of pleiotropy. Int. J. Dev. Biol. 42, 501-505 (1998).
    • (1998) Int. J. Dev. Biol. , vol.42 , pp. 501-505
    • Hodgkin, J.1
  • 59
  • 60
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • Copley, S. D. Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr. Opin. Chem. Biol. 7, 265-272 (2003).
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 265-272
    • Copley, S.D.1
  • 61
    • 0023225865 scopus 로고
    • Recruitment of enzymes as lens structural proteins
    • Wistow, G. & Piatigorsky, J. Recruitment of enzymes as lens structural proteins. Science 236, 1554-1556 (1987).
    • (1987) Science , vol.236 , pp. 1554-1556
    • Wistow, G.1    Piatigorsky, J.2
  • 62
    • 0027079977 scopus 로고
    • Identity of 4α-carbinolamine dehydratase, a component of the phenylalanine hydroxylation system, and DCoH, a transregulator of homeodomain proteins
    • Citron, B. A. et al. Identity of 4α-carbinolamine dehydratase, a component of the phenylalanine hydroxylation system, and DCoH, a transregulator of homeodomain proteins. Proc. Natl Acad. Sci. USA 89, 11891-11894 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11891-11894
    • Citron, B.A.1
  • 63
    • 0033545874 scopus 로고    scopus 로고
    • The crystal structure of a multifunctional protein: Phosphoglucose isomerase/autocrine motility factor/neuroleukin
    • Sun, Y. J. et al. The crystal structure of a multifunctional protein: phosphoglucose isomerase/autocrine motility factor/neuroleukin. Proc. Natl Acad. Sci. USA 96, 5412-5417 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5412-5417
    • Sun, Y.J.1
  • 64
    • 0038634973 scopus 로고    scopus 로고
    • Do current sequence analysis algorithms disclose multifunctional (moonlighting) proteins?
    • Gomez, A., Domedel, N., Cedano J., Pinol, J. & Querol, E. Do current sequence analysis algorithms disclose multifunctional (moonlighting) proteins? Bioinformatics 19, 895-896 (2003).
    • (2003) Bioinformatics , vol.19 , pp. 895-896
    • Gomez, A.1    Domedel, N.2    Cedano, J.3    Pinol, J.4    Querol, E.5
  • 65
    • 0035831020 scopus 로고    scopus 로고
    • Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: Dissociation from transcriptional activity
    • Kousteni, S. et al. Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: dissociation from transcriptional activity. Cell 104, 719-730 (2002).
    • (2002) Cell , vol.104 , pp. 719-730
    • Kousteni, S.1
  • 66
    • 0036716752 scopus 로고
    • Adaptive evolution after gene duplication
    • Hughes, A. L. Adaptive evolution after gene duplication. Trends Genet. 18, 433-434 (1994).
    • (1994) Trends Genet. , vol.18 , pp. 433-434
    • Hughes, A.L.1
  • 67
    • 0036338127 scopus 로고    scopus 로고
    • Alternative splicing and genome complexity
    • Brett, D. et al. Alternative splicing and genome complexity. Nature Genet. 30, 29-30 (2002).
    • (2002) Nature Genet. , vol.30 , pp. 29-30
    • Brett, D.1
  • 68
    • 0034100201 scopus 로고    scopus 로고
    • The role of population size, pleiotropy and fitness effects of mutations in the evolution of overlapping gene functions
    • Wagner, A. The role of population size, pleiotropy and fitness effects of mutations in the evolution of overlapping gene functions. Genetics 154, 1389-1401 (2000).
    • (2000) Genetics , vol.154 , pp. 1389-1401
    • Wagner, A.1
  • 69
    • 0347033256 scopus 로고    scopus 로고
    • Role of duplicate genes in genetic robustness against null mutations
    • Gu, Z. et al. Role of duplicate genes in genetic robustness against null mutations. Nature 421, 63-66 (2003).
    • (2003) Nature , vol.421 , pp. 63-66
    • Gu, Z.1
  • 70
    • 0037189057 scopus 로고    scopus 로고
    • Serotonin uptake into dopamine neurons via dopamine transporters: A compensatory alternative
    • Zhou, F. C., Lesch, K. P. & Murphy, D. L. Serotonin uptake into dopamine neurons via dopamine transporters: a compensatory alternative. Brain Res. 942, 109-119 (2002).
    • (2002) Brain Res. , vol.942 , pp. 109-119
    • Zhou, F.C.1    Lesch, K.P.2    Murphy, D.L.3
  • 71
    • 0037135623 scopus 로고    scopus 로고
    • Fatty acid homeostasis and induction of lipid regulatory genes in skeletal muscles of peroxisome proliferator-activated receptor (PPAR)-α knock-out mice. Evidence for compensatory regulation by PPAR-δ
    • Muoio D. M. et al. Fatty acid homeostasis and induction of lipid regulatory genes in skeletal muscles of peroxisome proliferator-activated receptor (PPAR)-α knock-out mice. Evidence for compensatory regulation by PPAR-δ. J. Biol. Chem. 277, 26089-26097 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26089-26097
    • Muoio, D.M.1
  • 72
    • 0035879074 scopus 로고    scopus 로고
    • Death in the balance: Alternative participation of the caspase-2 and -9 pathways in neuronal death induced by nerve growth factor deprivation
    • Troy, C. M. et al. Death in the balance: alternative participation of the caspase-2 and -9 pathways in neuronal death induced by nerve growth factor deprivation. J. Neurosci. 21, 5007-5016 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 5007-5016
    • Troy, C.M.1
  • 73
    • 0036131441 scopus 로고    scopus 로고
    • The tissue-specific, compensatory expression of cyclooxygenase-1 and -2 in transgenic mice
    • Zhang, J. et al. The tissue-specific, compensatory expression of cyclooxygenase-1 and -2 in transgenic mice. Prostaglandins Other Lipid Mediat. 67, 121-135 (2002).
    • (2002) Prostaglandins Other Lipid Mediat. , vol.67 , pp. 121-135
    • Zhang, J.1
  • 74
    • 18444377348 scopus 로고    scopus 로고
    • Redundant pathways for negative feedback regulation of bile acid production
    • Wang, L. et al. Redundant pathways for negative feedback regulation of bile acid production. Dev. Cell 2, 721-731 (2002).
    • (2002) Dev. Cell , vol.2 , pp. 721-731
    • Wang, L.1
  • 75
    • 0037012468 scopus 로고    scopus 로고
    • Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine
    • Mesulam, M. M. et al. Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine. Neuroscience 110, 627-639 (2002).
    • (2002) Neuroscience , vol.110 , pp. 627-639
    • Mesulam, M.M.1
  • 76
    • 0036029247 scopus 로고    scopus 로고
    • Cytokines and related receptor-mediated signaling pathways
    • Haddad, J. J. Cytokines and related receptor-mediated signaling pathways. Biochem. Biophys. Res. Commun. 297, 700-713 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 700-713
    • Haddad, J.J.1
  • 77
    • 0034978579 scopus 로고    scopus 로고
    • Crosstalk and specificity in signalling. Are we crosstalking ourselves into general confusion?
    • Dumont, J. E., Pecasse, F. & Maenhaut, C. Crosstalk and specificity in signalling. Are we crosstalking ourselves into general confusion? Cell Signal. 13, 457-463 (2001).
    • (2001) Cell Signal. , vol.13 , pp. 457-463
    • Dumont, J.E.1    Pecasse, F.2    Maenhaut, C.3
  • 78
    • 0036066956 scopus 로고    scopus 로고
    • STAT and SMAD signalling in cancer
    • Iwamoto, T. et al. STAT and SMAD signalling in cancer. Histol. Histopathol. 17, 887-895 (2002).
    • (2002) Histol. Histopathol. , vol.17 , pp. 887-895
    • Iwamoto, T.1
  • 79
    • 0034735773 scopus 로고    scopus 로고
    • T-cell-mediated regulation of osteoclastogenesis by signalling cross-talk between RANKL and IFN-γ
    • Takayanagi, H. et al. T-cell-mediated regulation of osteoclastogenesis by signalling cross-talk between RANKL and IFN-γ. Nature 408, 600-605 (2000).
    • (2000) Nature , vol.408 , pp. 600-605
    • Takayanagi, H.1
  • 80
    • 0036607064 scopus 로고    scopus 로고
    • Crosstalk between cAMP and MAP kinase signaling in the regulation of cell proliferation
    • Stork, P. J. & Schmitt, J. M. Crosstalk between cAMP and MAP kinase signaling in the regulation of cell proliferation. Trends Cell Biol. 12, 258-266 (2002).
    • (2002) Trends Cell Biol. , vol.12 , pp. 258-266
    • Stork, P.J.1    Schmitt, J.M.2
  • 81
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: Integrin signalling spreads
    • Schwartz, M. A. & Ginsberg, M. H. Networks and crosstalk: integrin signalling spreads. Nature Cell Biol. 4, E65-E68 (2002).
    • (2002) Nature Cell Biol. , vol.4
    • Schwartz, M.A.1    Ginsberg, M.H.2
  • 82
    • 0032847046 scopus 로고    scopus 로고
    • B receptors function as heterodimers
    • B receptors function as heterodimers. Biochem. Soc. Trans. 27, 530-535 (1999).
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 530-535
    • Marshall, F.H.1
  • 83
    • 0035815174 scopus 로고    scopus 로고
    • Biochemical and biophysical demonstration of GPCR oligomerization in mammalian cells
    • Angers, S., Salahpour A. & Bouvier, M. Biochemical and biophysical demonstration of GPCR oligomerization in mammalian cells. Life Sci. 68, 2243-2250 (2002).
    • (2002) Life Sci. , vol.68 , pp. 2243-2250
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 84
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North, R. A. Molecular physiology of P2X receptors. Physiol. Rev. 82, 1013-1067 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 85
    • 0037085478 scopus 로고    scopus 로고
    • Formation of functional heterodimers between the TASK-1 and TASK-3 two-pore domain potassium channel subunits
    • Czirjak, G. & Enyedi P. Formation of functional heterodimers between the TASK-1 and TASK-3 two-pore domain potassium channel subunits. J. Biol. Chem. 277, 5426-5432 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 5426-5432
    • Czirjak, G.1    Enyedi, P.2
  • 86
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu, Y. & Eisenberg, D. 3D domain swapping: as domains continue to swap. Protein Sci. 11, 1285-1299 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 87
    • 0032549157 scopus 로고    scopus 로고
    • Pleiotropy and the preservation of perfection
    • Waxman, D. & Peck, J. R. Pleiotropy and the preservation of perfection. Science 279, 1210-1213 (1998).
    • (1998) Science , vol.279 , pp. 1210-1213
    • Waxman, D.1    Peck, J.R.2
  • 88
    • 0036803305 scopus 로고    scopus 로고
    • Conservation of the segmented germband stage: Robustness or pleiotropy?
    • Galis, F., van Dooren, T. J. & Metz, J. A. Conservation of the segmented germband stage: robustness or pleiotropy? Trends Genet. 18, 504-509 (2002).
    • (2002) Trends Genet. , vol.18 , pp. 504-509
    • Galis, F.1    van Dooren, T.J.2    Metz, J.A.3
  • 89
    • 0347568598 scopus 로고    scopus 로고
    • The relationship of protein conservation and sequence length
    • Lipman, D. J. et al. The relationship of protein conservation and sequence length. BMC Evol. Biol. 2, 20 (2002).
    • (2002) BMC Evol. Biol. , vol.2 , pp. 20
    • Lipman, D.J.1
  • 90
    • 0033977618 scopus 로고    scopus 로고
    • Determinants of substitution rates in mammalian genes: Expression pattern affects selection intensity but not mutation rate
    • Duret, L. & Mouchiroud, D. Determinants of substitution rates in mammalian genes: expression pattern affects selection intensity but not mutation rate. Mol. Biol. Evol. 17, 68-74 (2000).
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 68-74
    • Duret, L.1    Mouchiroud, D.2
  • 91
    • 0029888297 scopus 로고    scopus 로고
    • Strong evolutionary conservation of broadly expressed protein isoforms in the troponin I gene family and other vertebrate gene families
    • Hastings, K. E. M. Strong evolutionary conservation of broadly expressed protein isoforms in the troponin I gene family and other vertebrate gene families. J. Mol. Evol. 42, 631-640 (1996).
    • (1996) J. Mol. Evol. , vol.42 , pp. 631-640
    • Hastings, K.E.M.1
  • 92
    • 0036412170 scopus 로고    scopus 로고
    • Is angiotensin I-converting enzyme a "master" disease gene?
    • Moskowitz, D. W. Is angiotensin I-converting enzyme a "master" disease gene? Diabetes Technol. Ther. 4, 683-711 (2002).
    • (2002) Diabetes Technol. Ther. , vol.4 , pp. 683-711
    • Moskowitz, D.W.1
  • 93
    • 0036896978 scopus 로고    scopus 로고
    • Chemoprevention of colorectal cancer: Problems, progress, and prospects
    • Viner, J. L., Umar, A. & Hawk, E. T. Chemoprevention of colorectal cancer: problems, progress, and prospects. Gastroenterol. Clin. North Am. 31, 971-999 (2002).
    • (2002) Gastroenterol. Clin. North Am. , vol.31 , pp. 971-999
    • Viner, J.L.1    Umar, A.2    Hawk, E.T.3
  • 94
    • 0013092230 scopus 로고
    • (eds Bryson, V. & Vogel, H. J.) (Academic Press, New York)
    • Horowitz, N. H. in Evolving Genes and Proteins (eds Bryson, V. & Vogel, H. J.) 15-23 (Academic Press, New York, 1965).
    • (1965) Evolving Genes and Proteins , pp. 15-23
    • Horowitz, N.H.1
  • 95
    • 0001353133 scopus 로고
    • Evolution of biosynthetic pathways: Two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region
    • Belfaiza J. et al. Evolution of biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. Proc. Natl Acad. Sci. USA 83, 867-871 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 867-871
    • Belfaiza, J.1
  • 96
    • 0026014458 scopus 로고
    • Structural conservation in parallel β/α-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis
    • Wilmanns, M. et al. Structural conservation in parallel β/α-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis. Biochemistry 30, 9161-9169 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9161-9169
    • Wilmanns, M.1
  • 97
    • 0028355575 scopus 로고
    • The evolution of the histidine biosynthetic genes in prokaryotes: A common ancestor for the hisA and hisF genes
    • Fani, R., Lio, P., Chiarelli, I. & Bazzicalupo, M. The evolution of the histidine biosynthetic genes in prokaryotes: a common ancestor for the hisA and hisF genes. J. Mol. Evol. 38, 489-495 (1994).
    • (1994) J. Mol. Evol. , vol.38 , pp. 489-495
    • Fani, R.1    Lio, P.2    Chiarelli, I.3    Bazzicalupo, M.4
  • 98
    • 0036303685 scopus 로고    scopus 로고
    • Evolution of enzymes in metabolism: A network perspective
    • Alves, R., Chaleil, R. A. & Sternberg, M. J. Evolution of enzymes in metabolism: a network perspective. J. Mol. Biol. 320, 751-770 (2002).
    • (2002) J. Mol. Biol. , vol.320 , pp. 751-770
    • Alves, R.1    Chaleil, R.A.2    Sternberg, M.J.3
  • 99
    • 0034601917 scopus 로고    scopus 로고
    • 8 barrels: Implications for the evolution of metabolic pathways
    • 8 barrels: implications for the evolution of metabolic pathways. J. Mol. Biol. 303, 627-641 (2000).
    • (2000) J. Mol. Biol. , vol.303 , pp. 627-641
    • Copley, R.R.1    Bork, P.2
  • 100
    • 0034991456 scopus 로고    scopus 로고
    • Phylogenetic analysis of metabolic pathways
    • Forst, C. V. & Schulten, K. Phylogenetic analysis of metabolic pathways. J. Mol. Evol. 52, 471-489 (2001).
    • (2001) J. Mol. Evol. , vol.52 , pp. 471-489
    • Forst, C.V.1    Schulten, K.2
  • 101
    • 0034029892 scopus 로고    scopus 로고
    • Robustness against mutations in genetic networks of yeast
    • Wagner, A. Robustness against mutations in genetic networks of yeast. Nature Genet. 24, 355-361 (2001).
    • (2001) Nature Genet. , vol.24 , pp. 355-361
    • Wagner, A.1
  • 102
    • 0035205239 scopus 로고    scopus 로고
    • Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice
    • Grange, R. W. et al. Functional and molecular adaptations in skeletal muscle of myoglobin-mutant mice. Am. J. Physiol. Cell Physiol. 281, C1487-C1494 (2001).
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Grange, R.W.1
  • 103
    • 0034890250 scopus 로고    scopus 로고
    • Changes in glycolytic network and mitochondrial design in creatine kinase-deficient muscles
    • de Groot, A. J., Oerlemans, F. T., Jost, C. R. & Wieringa, B. Changes in glycolytic network and mitochondrial design in creatine kinase-deficient muscles. Muscle Nerve 24, 1188-1196 (2001).
    • (2001) Muscle Nerve , vol.24 , pp. 1188-1196
    • de Groot, A.J.1    Oerlemans, F.T.2    Jost, C.R.3    Wieringa, B.4
  • 104
    • 0033709907 scopus 로고    scopus 로고
    • Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation
    • Zheng, T. S. et al. Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation. Nature Med. 6, 1241-1247 (2001).
    • (2001) Nature Med. , vol.6 , pp. 1241-1247
    • Zheng, T.S.1
  • 105
    • 0037193473 scopus 로고    scopus 로고
    • Intrinsic and extrinsic pathway signaling during neuronal apoptosis: Lessons from the analysis of mutant mice
    • Putcha, G. V. et al. Intrinsic and extrinsic pathway signaling during neuronal apoptosis: lessons from the analysis of mutant mice. J. Cell Biol. 157, 441-453 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 441-453
    • Putcha, G.V.1
  • 106
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte, E. M. et al. Detecting protein function and protein-protein interactions from genome sequences. Science 285, 751-753 (1999).
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1
  • 107
    • 0033551248 scopus 로고    scopus 로고
    • Assigning protein functions by comparative genome analysis: Protein phylogenetic profiles
    • Pellegrini, M. et al. Assigning protein functions by comparative genome analysis: protein phylogenetic profiles. Proc. Natl Acad. Sci. USA 96, 4285-4288 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4285-4288
    • Pellegrini, M.1
  • 109
    • 0034595516 scopus 로고    scopus 로고
    • Co-evolution of proteins with their interaction partners
    • Goh, C. S. et al. Co-evolution of proteins with their interaction partners. J. Mol. Biol. 299, 283-293 (2000).
    • (2000) J. Mol. Biol. , vol.299 , pp. 283-293
    • Goh, C.S.1
  • 110
    • 0036435908 scopus 로고    scopus 로고
    • Co-evolutionary analysis reveals insights into protein-protein interactions
    • Goh, C. S. & Cohen, F. E. Co-evolutionary analysis reveals insights into protein-protein interactions, J. Mol. Biol. 324, 177-192 (2002).
    • (2002) J. Mol. Biol. , vol.324 , pp. 177-192
    • Goh, C.S.1    Cohen, F.E.2
  • 112
    • 0035177259 scopus 로고    scopus 로고
    • Similarity of phylogenetic trees as indicator of protein-protein interaction
    • Pazos, F. & Valencia, A. Similarity of phylogenetic trees as indicator of protein-protein interaction. Protein Eng. 14, 609-614 (2001).
    • (2001) Protein Eng. , vol.14 , pp. 609-614
    • Pazos, F.1    Valencia, A.2
  • 113
    • 0033635880 scopus 로고    scopus 로고
    • Evolution of two-component signal transduction
    • Koretke, K. K. et al. Evolution of two-component signal transduction. Mol. Biol. Evol. 17, 1956-1970 (2000).
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 1956-1970
    • Koretke, K.K.1
  • 114
    • 0037177560 scopus 로고    scopus 로고
    • Evolutionary rate in the protein interaction network
    • Fraser, H. B. et al. Evolutionary rate in the protein interaction network. Science 296, 750-752 (2002).
    • (2002) Science , vol.296 , pp. 750-752
    • Fraser, H.B.1
  • 115
    • 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. & 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, 1 (2003).
    • (2003) BMC Evol. Biol. , vol.3 , pp. 1
    • Jordan, I.K.1    Wolf, Y.I.2    Koonin, E.V.3
  • 116
    • 0242284421 scopus 로고    scopus 로고
    • A simple dependence between protein evolution rate and the number of protein-protein interactions
    • Fraser, H. B., Wall, D. P. & Hirsh, A. E. A simple dependence between protein evolution rate and the number of protein-protein interactions. BMC Evol. Biol. 3, 11 (2003).
    • (2003) BMC Evol. Biol. , vol.3 , pp. 11
    • Fraser, H.B.1    Wall, D.P.2    Hirsh, A.E.3
  • 117
    • 0037012880 scopus 로고    scopus 로고
    • Specificity and stability in topology of protein networks
    • Maslov, S. & Sneppen, K. Specificity and stability in topology of protein networks. Science 296, 910-913 (2002).
    • (2002) Science , vol.296 , pp. 910-913
    • Maslov, S.1    Sneppen, K.2
  • 118
    • 0036006175 scopus 로고    scopus 로고
    • Wrestling with pleiotropy: Genomic and topological analysis of the yeast expression network
    • Featherstone, D. E. & Broadie, K. Wrestling with pleiotropy: genomic and topological analysis of the yeast expression network. Bioessays 24, 267-274 (2002).
    • (2002) Bioessays , vol.24 , pp. 267-274
    • Featherstone, D.E.1    Broadie, K.2
  • 119
    • 0003515251 scopus 로고
    • Evolution by Gene and Genome Duplication
    • (Springer, Berlin)
    • Ohno, S. Evolution by Gene and Genome Duplication (Springer, Berlin, 1970).
    • (1970)
    • Ohno, S.1
  • 121
    • 0036078078 scopus 로고    scopus 로고
    • Essential genes are more evolutionarily conserved than are nonessential genes in bacteria
    • Jordan, I. K., Rogozin, I. B., Wolf, Y. I. & Koonin, E. V. Essential genes are more evolutionarily conserved than are nonessential genes in bacteria. Genome Res. 12, 962-968 (2002).
    • (2002) Genome Res. , vol.12 , pp. 962-968
    • Jordan, I.K.1    Rogozin, I.B.2    Wolf, Y.I.3    Koonin, E.V.4
  • 122
    • 0035963414 scopus 로고    scopus 로고
    • Protein dispensability and rate of evolution
    • Hirsh, A. E. & Fraser, H. B. Protein dispensability and rate of evolution. Nature 411, 1046-1049 (2001).
    • (2001) Nature , vol.411 , pp. 1046-1049
    • Hirsh, A.E.1    Fraser, H.B.2
  • 123
    • 0037472928 scopus 로고    scopus 로고
    • Genomic function: Rate of evolution and gene dispensability
    • Pal, C., Papp, B. & Hurst, L. D. Genomic function: rate of evolution and gene dispensability. Nature 421, 496-497 (2003).
    • (2003) Nature , vol.421 , pp. 496-497
    • Pal, C.1    Papp, B.2    Hurst, L.D.3
  • 124
    • 0037472928 scopus 로고    scopus 로고
    • Genomic function: Rate of evolution and gene dispensability
    • Hirsh, A. E. & Fraser, H. B. Genomic function: Rate of evolution and gene dispensability. Nature 421, 497-498 (2003).
    • (2003) Nature , vol.421 , pp. 497-498
    • Hirsh, A.E.1    Fraser, H.B.2
  • 125
    • 0033565762 scopus 로고    scopus 로고
    • Do essential genes evolve slowly?
    • Hurst, L. D. & Smith, N. G. C. Do essential genes evolve slowly? Curr. Biol. 9, 747-750 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 747-750
    • Hurst, L.D.1    Smith, N.G.C.2
  • 126
    • 0036682357 scopus 로고    scopus 로고
    • GenomeHistory: A software tool and its application to fully sequenced genomes
    • Conant, G. C. & Wagner, A. GenomeHistory: a software tool and its application to fully sequenced genomes. Nucleic Acids Res. 30, 3378-3386 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3378-3386
    • Conant, G.C.1    Wagner, A.2
  • 127
    • 0026701302 scopus 로고
    • Pancreatic lipases: Evolutionary intermediates in a positional change of catalytic carboxylates?
    • Schrag, J. D., Winkler, F. K. & Cygler, M. Pancreatic lipases: evolutionary intermediates in a positional change of catalytic carboxylates? J. Biol. Chem. 267, 4300-4303 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 4300-4303
    • Schrag, J.D.1    Winkler, F.K.2    Cygler, M.3
  • 128
    • 0034712830 scopus 로고    scopus 로고
    • Evolution of the rodent eosinophil-associated RNase gene family by rapid gene sorting and positive selection
    • Zhang, J., Dyer, K. D. & Rosenberg, H. F. Evolution of the rodent eosinophil-associated RNase gene family by rapid gene sorting and positive selection. Proc. Natl Acad. Sci. USA 97, 4701-4706 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4701-4706
    • Zhang, J.1    Dyer, K.D.2    Rosenberg, H.F.3
  • 129
    • 0036724899 scopus 로고    scopus 로고
    • DNA sequence variation in a 3.7-kb noncoding sequence 5′ of the CYP1A2 gene: Implications for human population history and natural selection
    • Wooding, S. P. et al. DNA sequence variation in a 3.7-kb noncoding sequence 5′ of the CYP1A2 gene: implications for human population history and natural selection. Am. J. Hum. Genet. 71, 528-542 (2002).
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 528-542
    • Wooding, S.P.1
  • 131
    • 0037373563 scopus 로고    scopus 로고
    • The modern molecular clock
    • Bromham, L. & Penn, D. The modern molecular clock. Nature Rev. Genet. 4, 216-224 (2003).
    • (2003) Nature Rev. Genet. , vol.4 , pp. 216-224
    • Bromham, L.1    Penn, D.2
  • 132
    • 84924460094 scopus 로고
    • Abraham Wald's work on aircraft survivability
    • Mangel, M. & Samaniego, F. J. Abraham Wald's work on aircraft survivability. J. Amer. Statistical Assoc. 79, 259-270 (1984).
    • (1984) J. Amer. Statistical Assoc. , vol.79 , pp. 259-270
    • Mangel, M.1    Samaniego, F.J.2
  • 133
    • 0030722935 scopus 로고    scopus 로고
    • Long human-mouse sequence alignments reveal novel regulatory elements: A reason to sequence the mouse genome
    • Hardison, R. C., Oeltjen, J. & Miller, W. Long human-mouse sequence alignments reveal novel regulatory elements: a reason to sequence the mouse genome. Genome Res. 8, 959-966 (1997).
    • (1997) Genome Res. , vol.8 , pp. 959-966
    • Hardison, R.C.1    Oeltjen, J.2    Miller, W.3
  • 135
    • 0242418246 scopus 로고    scopus 로고
    • Phylogenetic shadowing of primate sequences to find functional regions of the human genome
    • Bofelli, D. et al. Phylogenetic shadowing of primate sequences to find functional regions of the human genome. Science 299, 1391-1394 (2003).
    • (2003) Science , vol.299 , pp. 1391-1394
    • Bofelli, D.1
  • 136
    • 0014800108 scopus 로고
    • Distinguishing homologous from analogous proteins
    • Fitch, W. M. Distinguishing homologous from analogous proteins. Syst. Zool. 19, 99-113 (1970).
    • (1970) Syst. Zool. , vol.19 , pp. 99-113
    • Fitch, W.M.1
  • 137
    • 0002027029 scopus 로고
    • A new evolutionary law
    • Van Valen, L. A new evolutionary law. Evol. Theory 1, 1-30 (1973).
    • (1973) Evol. Theory , vol.1 , pp. 1-30
    • Van Valen, L.1
  • 138
    • 0034494349 scopus 로고    scopus 로고
    • Synonymous and non-synonymous mutations in a region of the Plasmodium chabaudi genome and evidence for selection acting on a malaria vaccine candidate
    • Black, C. G. & Coppel, R. L. Synonymous and non-synonymous mutations in a region of the Plasmodium chabaudi genome and evidence for selection acting on a malaria vaccine candidate. Mol. Biochem. Parasitol. 111, 447-451 (2000).
    • (2000) Mol. Biochem. Parasitol. , vol.111 , pp. 447-451
    • Black, C.G.1    Coppel, R.L.2
  • 139
    • 0036899166 scopus 로고    scopus 로고
    • Biological and biomedical implications of the co-evolution of pathogens and their hosts
    • Woolhouse, M. E., Webster, J. P., Domingo, E., Charlesworth, B. & Levin, B. R. Biological and biomedical implications of the co-evolution of pathogens and their hosts. Nature Genet. 32, 569-577 (2002).
    • (2002) Nature Genet. , vol.32 , pp. 569-577
    • Woolhouse, M.E.1    Webster, J.P.2    Domingo, E.3    Charlesworth, B.4    Levin, B.R.5
  • 140
    • 0037066542 scopus 로고    scopus 로고
    • Intra- and interspecific variation in primate gene expression patterns
    • Enard, W. et al. Intra- and interspecific variation in primate gene expression patterns. Science 296, 340-343 (2002).
    • (2002) Science , vol.296 , pp. 340-343
    • Enard, W.1
  • 141
    • 0033028596 scopus 로고    scopus 로고
    • Systematic determination of genetic network architecture
    • Tavazoie, S. et al. Systematic determination of genetic network architecture. Nature Genet. 22, 281-285 (1999).
    • (1999) Nature Genet. , vol.22 , pp. 281-285
    • Tavazoie, S.1
  • 142
    • 0030025046 scopus 로고    scopus 로고
    • Functional redundancy of the muscle-specific transcription factors Myf5 and myogenin
    • Wang, Y., Schnegelsberg, P. N., Dausman, J. & Jaenisch, R. Functional redundancy of the muscle-specific transcription factors Myf5 and myogenin. Nature 379, 823-825 (1996).
    • (1996) Nature , vol.379 , pp. 823-825
    • Wang, Y.1    Schnegelsberg, P.N.2    Dausman, J.3    Jaenisch, R.4
  • 143
    • 0037059461 scopus 로고    scopus 로고
    • A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules
    • Tong, A. H. et al. A combined experimental and computational strategy to define protein interaction networks for peptide recognition modules. Science 295, 321-324 (2002).
    • (2002) Science , vol.295 , pp. 321-324
    • Tong, A.H.1
  • 144
    • 0032572819 scopus 로고    scopus 로고
    • Can we learn to distinguish between "drug-like" and "nondrug-like" molecules?
    • Ajay, A., Walters, W. P. & Murcko, M. A. Can we learn to distinguish between "drug-like" and "nondrug-like" molecules? J. Med. Chem. 41, 3314-3324 (1998).
    • (1998) J. Med. Chem. , vol.41 , pp. 3314-3324
    • Ajay, A.1    Walters, W.P.2    Murcko, M.A.3
  • 145
    • 0035821596 scopus 로고    scopus 로고
    • Simple selection criteria for drug-like chemical matter
    • Muegge, I., Heald, S. L. & Brittelli, D. Simple selection criteria for drug-like chemical matter J. Med. Chem. 44, 1841-1846 (2001).
    • (2001) J. Med. Chem. , vol.44 , pp. 1841-1846
    • Muegge, I.1    Heald, S.L.2    Brittelli, D.3
  • 146
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C. A., Lombardo, F., Dominy, B. W. & Feeney, P. J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 23, 4-25 (1997).
    • (1997) Adv. Drug Deliv. Rev. , vol.23 , pp. 4-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 147
    • 0037030653 scopus 로고    scopus 로고
    • Molecular properties that influence oral bioavailability of drug candidates
    • Veber, D. F. et al. Molecular properties that influence oral bioavailability of drug candidates. J. Med. Chem. 45, 2615-2623 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 2615-2623
    • Veber, D.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.