메뉴 건너뛰기




Volumn 3, Issue 11, 2007, Pages 2122-2134

Detecting coevolution in and among protein domains

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CONTINUOUS TIME SYSTEMS; ECONOMIC AND SOCIAL EFFECTS; MARKOV PROCESSES; NUCLEIC ACIDS; SUPEROXIDE DISMUTASE;

EID: 36949019322     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.0030211     Document Type: Article
Times cited : (142)

References (60)
  • 1
    • 0019830772 scopus 로고
    • Secondary structure of 16S ribosomal RNA
    • Noller HF, Woese CR (1981) Secondary structure of 16S ribosomal RNA. Science 212: 403-411.
    • (1981) Science , vol.212 , pp. 403-411
    • Noller, H.F.1    Woese, C.R.2
  • 2
    • 0022719007 scopus 로고
    • Higher order structure in ribosomal RNA
    • Gutell RR, Noller HF, Woese CR (1986) Higher order structure in ribosomal RNA. EMBO J 5: 1111-1113.
    • (1986) EMBO J , vol.5 , pp. 1111-1113
    • Gutell, R.R.1    Noller, H.F.2    Woese, C.R.3
  • 3
    • 0029091043 scopus 로고
    • Estimating substitution rates in ribosomal RNA genes
    • Rzhetsky A (1995) Estimating substitution rates in ribosomal RNA genes. Genetics 141: 771-783.
    • (1995) Genetics , vol.141 , pp. 771-783
    • Rzhetsky, A.1
  • 4
    • 0032796501 scopus 로고    scopus 로고
    • RNA secondary structure prediction using stochastic context-free grammars and evolutionary history
    • Knudsen B, Hein J (1999) RNA secondary structure prediction using stochastic context-free grammars and evolutionary history. Bioinformatics 15: 446-454.
    • (1999) Bioinformatics , vol.15 , pp. 446-454
    • Knudsen, B.1    Hein, J.2
  • 5
    • 0035656688 scopus 로고    scopus 로고
    • Non-coding RNA genes and the modern RNA world
    • Eddy SR (2001) Non-coding RNA genes and the modern RNA world. Nat Rev Genet 2: 919-929.
    • (2001) Nat Rev Genet , vol.2 , pp. 919-929
    • Eddy, S.R.1
  • 8
    • 33744457709 scopus 로고    scopus 로고
    • A novel method for detecting intramolecular coevolution: Adding a further dimension to select constraints analyses
    • Fares M, Travers SAA (2006) A novel method for detecting intramolecular coevolution: adding a further dimension to select constraints analyses. Genetics 173: 9-13.
    • (2006) Genetics , vol.173 , pp. 9-13
    • Fares, M.1    Travers, S.A.A.2
  • 9
    • 0027297096 scopus 로고
    • Covariation of mutations in the V3 loop of human immunodeficiency virus type 1 envelop protein: An information theoretic analysis
    • Korber BTM, Farber RM, Wolpert DH, Lapedes AS (1993) Covariation of mutations in the V3 loop of human immunodeficiency virus type 1 envelop protein: an information theoretic analysis. Proc Natl Acad Sci U S A 90: 7176-7180.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7176-7180
    • Korber, B.T.M.1    Farber, R.M.2    Wolpert, D.H.3    Lapedes, A.S.4
  • 10
    • 0033977832 scopus 로고    scopus 로고
    • Correlations among amino acid sites in bHLH protein domains: An information theoretic analysis
    • Atchley WR, Wollenberg KR, Fitch WM, Terhalle W, Dress AW (2000) Correlations among amino acid sites in bHLH protein domains: an information theoretic analysis. Mol Biol Evol 17: 164-178.
    • (2000) Mol Biol Evol , vol.17 , pp. 164-178
    • Atchley, W.R.1    Wollenberg, K.R.2    Fitch, W.M.3    Terhalle, W.4    Dress, A.W.5
  • 11
    • 0037433701 scopus 로고    scopus 로고
    • Using multiple interdependency to separate functional from phylogenetic correlations in protein alignments
    • Tillier ERM, Lui TWH (2003) Using multiple interdependency to separate functional from phylogenetic correlations in protein alignments. Bioinformatics 19: 750-755.
    • (2003) Bioinformatics , vol.19 , pp. 750-755
    • Tillier, E.R.M.1    Lui, T.W.H.2
  • 12
    • 0037436412 scopus 로고    scopus 로고
    • Exploiting the co-evolution of interacting proteins to discover interaction specificity
    • Ramani AK, Marcotte EM (2003) Exploiting the co-evolution of interacting proteins to discover interaction specificity. J Mol Biol 327: 273-284.
    • (2003) J Mol Biol , vol.327 , pp. 273-284
    • Ramani, A.K.1    Marcotte, E.M.2
  • 13
    • 18544362952 scopus 로고    scopus 로고
    • Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions
    • Gloor GB, Martin LC, Wahl LM, Dunn SD (2005) Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions. Biochemistry 44: 7156-7165.
    • (2005) Biochemistry , vol.44 , pp. 7156-7165
    • Gloor, G.B.1    Martin, L.C.2    Wahl, L.M.3    Dunn, S.D.4
  • 14
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionary conserved pathways of energetic connectivity in protein families
    • Lockless SW, Ranganathan R (1999) Evolutionary conserved pathways of energetic connectivity in protein families. Science 286: 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.W.1    Ranganathan, R.2
  • 15
    • 0030743758 scopus 로고    scopus 로고
    • Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution
    • Pollock DD, Taylor WR (1997) Effectiveness of correlation analysis in identifying protein residues undergoing correlated evolution. Protein Eng 10: 647-657.
    • (1997) Protein Eng , vol.10 , pp. 647-657
    • Pollock, D.D.1    Taylor, W.R.2
  • 16
    • 85135546643 scopus 로고    scopus 로고
    • Barker D, Pagel M (2005) Predicting functional gene links from phylogenetic-statistical analyses of whole genomes. PLoS Comp Biol 1: e3. doi:10.1371/journal.pcbi.0010003
    • Barker D, Pagel M (2005) Predicting functional gene links from phylogenetic-statistical analyses of whole genomes. PLoS Comp Biol 1: e3. doi:10.1371/journal.pcbi.0010003
  • 17
    • 0028813337 scopus 로고
    • A space-time process model for the evolution of DNA sequences
    • Yang Z (1995) A space-time process model for the evolution of DNA sequences. Genetics 139: 993-1005.
    • (1995) Genetics , vol.139 , pp. 993-1005
    • Yang, Z.1
  • 19
    • 0033582946 scopus 로고    scopus 로고
    • Coevolving protein residues: Maximum likelihood identification and relationship to structure
    • Pollock DD, Taylor WR, Goldman N (1999) Coevolving protein residues: maximum likelihood identification and relationship to structure. J Mol Biol 287: 187-198.
    • (1999) J Mol Biol , vol.287 , pp. 187-198
    • Pollock, D.D.1    Taylor, W.R.2    Goldman, N.3
  • 20
    • 0011542799 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Available:, Accessed 5 October 2007
    • Bateman A, Birney E, Cerruti L, Durbin R, Etwiller L, et al. (2002) The Pfam protein families database. Nucleic Acids Res 30: 276-280. Available: http://www.sanger.ac.uk/Software/Pfam/. Accessed 5 October 2007.
    • (2002) Nucleic Acids Res , vol.30 , pp. 276-280
    • Bateman, A.1    Birney, E.2    Cerruti, L.3    Durbin, R.4    Etwiller, L.5
  • 21
    • 34548457666 scopus 로고    scopus 로고
    • Detecting the coevolution of biosequences: An example of RNA interaction prediction
    • Yeang CH, Darot JFJ, Noller HF, Haussler D (2007) Detecting the coevolution of biosequences: an example of RNA interaction prediction. Mol Biol Evol 24: 2119-2131.
    • (2007) Mol Biol Evol , vol.24 , pp. 2119-2131
    • Yeang, C.H.1    Darot, J.F.J.2    Noller, H.F.3    Haussler, D.4
  • 22
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Available:, Accessed 5 October 2007
    • Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, et al. (2000) The Protein Data Bank. Nucleic Acids Res 28: 235-242. Available: http://www.rcsb.org/pdb/home/home.do. Accessed 5 October 2007.
    • (2000) Nucleic Acids Res , vol.28 , pp. 235-242
    • Berman, H.M.1    Westbrook, J.2    Feng, Z.3    Gilliland, G.4    Bhat, T.N.5
  • 23
    • 0035984426 scopus 로고    scopus 로고
    • The 2.0 Å resolution structure of the catalytic portion of a cyanobacteria membrane-bound manganese superoxide dismutase
    • Atzenhofer W, Regelsberger G, Jacob U, Peschek G, Furtmuller P, et al. (2002) The 2.0 Å resolution structure of the catalytic portion of a cyanobacteria membrane-bound manganese superoxide dismutase. J Mol Biol 321: 479-489.
    • (2002) J Mol Biol , vol.321 , pp. 479-489
    • Atzenhofer, W.1    Regelsberger, G.2    Jacob, U.3    Peschek, G.4    Furtmuller, P.5
  • 24
    • 0032492710 scopus 로고    scopus 로고
    • Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34
    • Guan Y, Hickey MJ, Borgstahl GE, Hallewell RA, Lepock JR, et al. (1998) Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34. Biochemistry 37: 4722-4730.
    • (1998) Biochemistry , vol.37 , pp. 4722-4730
    • Guan, Y.1    Hickey, M.J.2    Borgstahl, G.E.3    Hallewell, R.A.4    Lepock, J.R.5
  • 25
    • 19944406094 scopus 로고    scopus 로고
    • Context dependence and coevolution among amino acid residues in proteins
    • Wang ZO, Pollock DD (2005) Context dependence and coevolution among amino acid residues in proteins. Methods Enzymol 395: 779-790.
    • (2005) Methods Enzymol , vol.395 , pp. 779-790
    • Wang, Z.O.1    Pollock, D.D.2
  • 26
    • 0034699519 scopus 로고    scopus 로고
    • Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics
    • Carter AP, Clemons WM Jr, Brodersen DE, Morgan-Warren RJ, Wimberly BT, et al. (2000) Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics. Nature 407: 340-348.
    • (2000) Nature , vol.407 , pp. 340-348
    • Carter, A.P.1    Clemons Jr, W.M.2    Brodersen, D.E.3    Morgan-Warren, R.J.4    Wimberly, B.T.5
  • 27
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer P, Bushnell DA, Kornberg RD (2001) Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292: 1863-1876.
    • (2001) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 28
    • 0036174748 scopus 로고    scopus 로고
    • Crystal structure of PMM/PGM: An enzyme in the biosynthetic pathway of P. aeruginosa virulence factors
    • Regni C, Topton PA, Beamer LJ (2002) Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors. Structure 10: 269-279.
    • (2002) Structure , vol.10 , pp. 269-279
    • Regni, C.1    Topton, P.A.2    Beamer, L.J.3
  • 29
    • 0034212938 scopus 로고    scopus 로고
    • Crystal structure of human ornithine transcarbamylase complexed with carbamoyl phosphate and L norvaline at 1.9 A resolution
    • Shi D, Morizono H, Aoyagi M, Tuchman M, Allewell NM (2000) Crystal structure of human ornithine transcarbamylase complexed with carbamoyl phosphate and L norvaline at 1.9 A resolution. Proteins 39: 271-277.
    • (2000) Proteins , vol.39 , pp. 271-277
    • Shi, D.1    Morizono, H.2    Aoyagi, M.3    Tuchman, M.4    Allewell, N.M.5
  • 30
    • 0033596743 scopus 로고    scopus 로고
    • Carbamoyl phosphate synthetase: Closure of the B-domain as a result of nucleotide binding
    • Thoden JB, Wesenberg G, Raushel FM, Holden HM (1999) Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding. Biochemistry 38: 2347-2357.
    • (1999) Biochemistry , vol.38 , pp. 2347-2357
    • Thoden, J.B.1    Wesenberg, G.2    Raushel, F.M.3    Holden, H.M.4
  • 31
    • 0029911754 scopus 로고    scopus 로고
    • Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites
    • Herzberg O, Chen CC, Kapadia G, McGuire M, Carroll LJ, et al. (1996) Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites. Proc Natl Acad Sci U S A 93: 2652-2657.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 2652-2657
    • Herzberg, O.1    Chen, C.C.2    Kapadia, G.3    McGuire, M.4    Carroll, L.J.5
  • 32
    • 0036304611 scopus 로고    scopus 로고
    • The structure of apo human glutamate dehydrogenase details subunit communication and allostery
    • Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA (2002) The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol 318: 765-777.
    • (2002) J Mol Biol , vol.318 , pp. 765-777
    • Smith, T.J.1    Schmidt, T.2    Fang, J.3    Wu, J.4    Siuzdak, G.5    Stanley, C.A.6
  • 33
    • 0242516080 scopus 로고    scopus 로고
    • Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase
    • Jørgensen R, Ortiz PA, Carr-Schmid A, Nissen P, Kinzy TG, et al. (2003) Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase. Nat Struct Mol Biol 10: 379-385.
    • (2003) Nat Struct Mol Biol , vol.10 , pp. 379-385
    • Jørgensen, R.1    Ortiz, P.A.2    Carr-Schmid, A.3    Nissen, P.4    Kinzy, T.G.5
  • 34
    • 0037423708 scopus 로고    scopus 로고
    • Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: Thermostability and 1.8 Å resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate
    • Van Boxstael S, Cunin R, Khan S, Maes D (2003) Aspartate transcarbamylase from the hyperthermophilic archaeon Pyrococcus abyssi: thermostability and 1.8 Å resolution crystal structure of the catalytic subunit complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate. J Mol Biol 326: 203-216.
    • (2003) J Mol Biol , vol.326 , pp. 203-216
    • Van Boxstael, S.1    Cunin, R.2    Khan, S.3    Maes, D.4
  • 35
    • 0034049525 scopus 로고    scopus 로고
    • Structure of a closed form of human malic enzyme and implications for catalytic mechanism
    • Yang Z, Floyd DL, Loeber G, Tong L (2000) Structure of a closed form of human malic enzyme and implications for catalytic mechanism. Nat Struct Biol 7: 251-257.
    • (2000) Nat Struct Biol , vol.7 , pp. 251-257
    • Yang, Z.1    Floyd, D.L.2    Loeber, G.3    Tong, L.4
  • 36
    • 0031947190 scopus 로고    scopus 로고
    • Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength
    • Turner MA, Yuan CS, Borchardt RT, Hershfield MS, Smith GD, et al. (1998) Structure determination of selenomethionyl S-adenosylhomocysteine hydrolase using data at a single wavelength. Nat Struct Biol 5: 369-376.
    • (1998) Nat Struct Biol , vol.5 , pp. 369-376
    • Turner, M.A.1    Yuan, C.S.2    Borchardt, R.T.3    Hershfield, M.S.4    Smith, G.D.5
  • 37
    • 0037472127 scopus 로고    scopus 로고
    • Crystal structure of GDP-mannose dehydrogenase: A key enzyme of alginate biosynthesis in P. aeruginosa
    • Snook CF, Tipon PA, Beamer LJ (2003) Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate biosynthesis in P. aeruginosa. Biochemistry 42: 4658-4668.
    • (2003) Biochemistry , vol.42 , pp. 4658-4668
    • Snook, C.F.1    Tipon, P.A.2    Beamer, L.J.3
  • 38
    • 0037044776 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism
    • Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK (2002) Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase binary and ternary complexes. Specificity and catalytic mechanism. J Biol Chem 277: 43433-43442.
    • (2002) J Biol Chem , vol.277 , pp. 43433-43442
    • Kavanagh, K.L.1    Klimacek, M.2    Nidetzky, B.3    Wilson, D.K.4
  • 41
    • 0031047974 scopus 로고    scopus 로고
    • The refined crystal structure of the 3C gene product from hepatitis A virus: Specific proteinase activity and RNA recognition
    • Bergmann EM, Mosimann SC, Chernaia MM, Malcolm BA, James MNG (1997) The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognition. J Virology 71: 2436-2448.
    • (1997) J Virology , vol.71 , pp. 2436-2448
    • Bergmann, E.M.1    Mosimann, S.C.2    Chernaia, M.M.3    Malcolm, B.A.4    James, M.N.G.5
  • 42
    • 0036143826 scopus 로고    scopus 로고
    • Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling
    • Polekhina G, House CM, Traficante N, Mackay JP, Relaix F, et al. (2002) Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling. Nat Struct Biol 9: 68-75.
    • (2002) Nat Struct Biol , vol.9 , pp. 68-75
    • Polekhina, G.1    House, C.M.2    Traficante, N.3    Mackay, J.P.4    Relaix, F.5
  • 43
    • 0032851377 scopus 로고    scopus 로고
    • Structure and mechanism of the glycyl radical enzyme pyruvate formatelyase
    • Becker A, Fritz-Wolf K, Kabsch W, Knappe J, Schiltz S, et al. (1999) Structure and mechanism of the glycyl radical enzyme pyruvate formatelyase. Nat Struct Biol 6: 969-975.
    • (1999) Nat Struct Biol , vol.6 , pp. 969-975
    • Becker, A.1    Fritz-Wolf, K.2    Kabsch, W.3    Knappe, J.4    Schiltz, S.5
  • 45
    • 0035949513 scopus 로고    scopus 로고
    • Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site
    • Hilgers MT, Ludwig ML (2001) Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site. Proc Natl Acad Sci U S A 98: 11169-11174.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11169-11174
    • Hilgers, M.T.1    Ludwig, M.L.2
  • 46
    • 17944368066 scopus 로고    scopus 로고
    • Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: Role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture
    • Peneff C, Ferrari P, Harrier CV, Taburet Y, Monnier C, et al. (2001) Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J 20: 6191-6202.
    • (2001) EMBO J , vol.20 , pp. 6191-6202
    • Peneff, C.1    Ferrari, P.2    Harrier, C.V.3    Taburet, Y.4    Monnier, C.5
  • 47
    • 4444315617 scopus 로고    scopus 로고
    • Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis
    • Rajan SS, Yang X, Collart F, Yip VLY, Withers SG, et al. (2004) Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis. Structure 12: 1619-1629.
    • (2004) Structure , vol.12 , pp. 1619-1629
    • Rajan, S.S.1    Yang, X.2    Collart, F.3    Yip, V.L.Y.4    Withers, S.G.5
  • 48
    • 0035914337 scopus 로고    scopus 로고
    • Three-dimensional structure of a hyperthermophilic 5′-deoxy-5′- methylthioadenosine phosphorylase from Sulfolobus solfataricus
    • Appleby TC, Mathews II, Porcelli M, Cacciapuoti G (2001) Three-dimensional structure of a hyperthermophilic 5′-deoxy-5′- methylthioadenosine phosphorylase from Sulfolobus solfataricus. J Biol Chem 276: 39232-39242.
    • (2001) J Biol Chem , vol.276 , pp. 39232-39242
    • Appleby, T.C.1    Mathews, I.I.2    Porcelli, M.3    Cacciapuoti, G.4
  • 49
    • 0033597205 scopus 로고    scopus 로고
    • Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum
    • Kim SY, Hwang KY, Kim SH, Sung HC, Han YS, et al. (1999) Structural basis for cold adaptation. Sequence, biochemical properties, and crystal structure of malate dehydrogenase from a psychrophile Aquaspirillium arcticum. J Biol Chem 274: 11761-11767.
    • (1999) J Biol Chem , vol.274 , pp. 11761-11767
    • Kim, S.Y.1    Hwang, K.Y.2    Kim, S.H.3    Sung, H.C.4    Han, Y.S.5
  • 50
    • 0037816299 scopus 로고    scopus 로고
    • A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase
    • Siebold C, Fernando GA, Erni B, Baumann U (2003) A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase. Proc Natl Acad Sci U S A 100: 8188-8192.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8188-8192
    • Siebold, C.1    Fernando, G.A.2    Erni, B.3    Baumann, U.4
  • 51
    • 34249945479 scopus 로고    scopus 로고
    • Specificity in protein interactions and relationship with sequence diversity and coevolution
    • Hakes L, Lovell SC, Oliver SG, Robertson DL (2007) Specificity in protein interactions and relationship with sequence diversity and coevolution. Proc Natl Acad Sci U S A 104: 7999-8004.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7999-8004
    • Hakes, L.1    Lovell, S.C.2    Oliver, S.G.3    Robertson, D.L.4
  • 52
    • 0000228203 scopus 로고
    • A model of evolutionary change in proteins
    • Washington D.C, National Biomedical Research Foundation. pp
    • Dayhoff MO, Schwartz RM, Orcutt BC (1978) A model of evolutionary change in proteins. In: Atlas of protein sequence and structure 5 (Supplement 3). Washington (D.C.): National Biomedical Research Foundation. pp. 345-352.
    • (1978) Atlas of protein sequence and structure , vol.5 , Issue.SUPPL.EMENT 3 , pp. 345-352
    • Dayhoff, M.O.1    Schwartz, R.M.2    Orcutt, B.C.3
  • 53
    • 0013237073 scopus 로고    scopus 로고
    • Introduction to inference for Bayesian networks
    • Jordan M, editor, MIT Press. pp
    • Cowell R (1999) Introduction to inference for Bayesian networks. In: Jordan M, editor. Learning in graphical models. MIT Press. pp. 9-26.
    • (1999) Learning in graphical models , pp. 9-26
    • Cowell, R.1
  • 55
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: A maximum likelihood approach
    • Felsenstein J (1981) Evolutionary trees from DNA sequences: a maximum likelihood approach. J Mol Evol 17: 368-376.
    • (1981) J Mol Evol , vol.17 , pp. 368-376
    • Felsenstein, J.1
  • 56
    • 0032010619 scopus 로고    scopus 로고
    • EXPOKIT: A software package for computing matrix exponentials
    • Available:, Accessed 5 October 2007
    • Sidjie RB (1998) EXPOKIT: A software package for computing matrix exponentials. ACM Trans Math Softw 24: 130-156. Available: http://www.maths.uq. edu.au/expokit/. Accessed 5 October 2007.
    • (1998) ACM Trans Math Softw , vol.24 , pp. 130-156
    • Sidjie, R.B.1
  • 57
    • 84872264616 scopus 로고    scopus 로고
    • Available:, Accessed 5 October 2007
    • NCBI taxonomy database. Available: http://www.ncbi.nlm.nih.gov/. Accessed 5 October 2007
    • NCBI taxonomy database
  • 58
    • 0034791426 scopus 로고    scopus 로고
    • A simple algorithm to infer gene duplication and speciation events on a gene tree
    • Zmasek CM, Eddy SR (2001) A simple algorithm to infer gene duplication and speciation events on a gene tree. Bioinformatics 17: 821-828.
    • (2001) Bioinformatics , vol.17 , pp. 821-828
    • Zmasek, C.M.1    Eddy, S.R.2
  • 59
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini Y, Hochberg Y (1995) Controlling the false discovery rate: a practical and powerful approach to multiple testing. J Royal Stat Soc B 57: 289-300.
    • (1995) J Royal Stat Soc B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.