메뉴 건너뛰기




Volumn 80, Issue 1, 2012, Pages 126-141

A novel method for protein-protein interaction site prediction using phylogenetic substitution models

Author keywords

Mutation pattern; Phylogenetic substitution model; Protein interaction site prediction; Protein protein interaction; Sequence analysis

Indexed keywords

DNA; RNA;

EID: 83555177311     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23169     Document Type: Article
Times cited : (26)

References (62)
  • 4
    • 18044397545 scopus 로고    scopus 로고
    • Progress of structural genomics initiatives: an analysis of solved target structures
    • Todd AE, Marsden RL, Thornton JM, Orengo CA. Progress of structural genomics initiatives: an analysis of solved target structures. J Mol Biol 2005; 348: 1235-1260.
    • (2005) J Mol Biol , vol.348 , pp. 1235-1260
    • Todd, A.E.1    Marsden, R.L.2    Thornton, J.M.3    Orengo, C.A.4
  • 5
    • 31144467558 scopus 로고    scopus 로고
    • The impact of structural genomics: expectations and outcomes
    • Chandonia JM, Brenner SE. The impact of structural genomics: expectations and outcomes. Science 2006; 311: 347-351.
    • (2006) Science , vol.311 , pp. 347-351
    • Chandonia, J.M.1    Brenner, S.E.2
  • 6
    • 1842526090 scopus 로고    scopus 로고
    • ProMate: a structure based prediction program to identify the location of protein-protein binding sites
    • Neuvirth H, Raz R, Schreiber G. ProMate: a structure based prediction program to identify the location of protein-protein binding sites. J Mol Biol 2004; 338: 181-199.
    • (2004) J Mol Biol , vol.338 , pp. 181-199
    • Neuvirth, H.1    Raz, R.2    Schreiber, G.3
  • 7
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • Jones S, Thornton JM. Analysis of protein-protein interaction sites using surface patches. J Mol Biol 1997; 272: 121-132.
    • (1997) J Mol Biol , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 8
    • 34547597799 scopus 로고    scopus 로고
    • PI2PE: protein interface/interior prediction engine
    • Tjong H, Qin S, Zhou HX. PI2PE: protein interface/interior prediction engine. Nucleic Acids Res 2007; 35: W357-W362.
    • (2007) Nucleic Acids Res , vol.35
    • Tjong, H.1    Qin, S.2    Zhou, H.X.3
  • 9
    • 33846200437 scopus 로고    scopus 로고
    • Prediction-based fingerprints of protein-protein interactions
    • Porollo A, Meller J. Prediction-based fingerprints of protein-protein interactions. Proteins 2007; 66: 630-645.
    • (2007) Proteins , vol.66 , pp. 630-645
    • Porollo, A.1    Meller, J.2
  • 10
    • 17444372787 scopus 로고    scopus 로고
    • Improved prediction of protein-protein binding sites using a support vector machines approach
    • Bradford JR, Westhead DR. Improved prediction of protein-protein binding sites using a support vector machines approach. Bioinformatics 2005; 21: 1487-1494.
    • (2005) Bioinformatics , vol.21 , pp. 1487-1494
    • Bradford, J.R.1    Westhead, D.R.2
  • 11
    • 0031565725 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using patch analysis
    • Jones S, Thornton JM. Prediction of protein-protein interaction sites using patch analysis. J Mol Biol 1997; 272: 133-143.
    • (1997) J Mol Biol , vol.272 , pp. 133-143
    • Jones, S.1    Thornton, J.M.2
  • 12
    • 10844235653 scopus 로고    scopus 로고
    • Optimal docking area: a new method for predicting protein-protein interaction sites
    • Fernandez-Recio J, Totrov M, Skorodumov C, Abagyan R. Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins 2005; 58: 134-143.
    • (2005) Proteins , vol.58 , pp. 134-143
    • Fernandez-Recio, J.1    Totrov, M.2    Skorodumov, C.3    Abagyan, R.4
  • 13
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D, Tsai CJ, Nussinov R. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng 1997; 10: 999-1012.
    • (1997) Protein Eng , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 14
    • 0036122073 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites in heterocomplexes with neural networks
    • Fariselli P, Pazos F, Valencia A, Casadio R. Prediction of protein-protein interaction sites in heterocomplexes with neural networks. Eur J Biochem 2002; 269: 1356-1361.
    • (2002) Eur J Biochem , vol.269 , pp. 1356-1361
    • Fariselli, P.1    Pazos, F.2    Valencia, A.3    Casadio, R.4
  • 15
    • 24344484686 scopus 로고    scopus 로고
    • Prediction of interface residues in protein-protein complexes by a consensus neural network method: test against NMR data
    • Chen H, Zhou HX. Prediction of interface residues in protein-protein complexes by a consensus neural network method: test against NMR data. Proteins 2005; 61: 21-35.
    • (2005) Proteins , vol.61 , pp. 21-35
    • Chen, H.1    Zhou, H.X.2
  • 17
    • 84901534791 scopus 로고    scopus 로고
    • Predicting binding interfaces of protein-protein interactions
    • Li XL,Ng SK, editors. Philadelphia: IGI-GLobal;
    • La D, Kihara D. Predicting binding interfaces of protein-protein interactions. In: Li XL, Ng SK, editors. Biological data mining in protein interaction networks. Philadelphia: IGI-GLobal; 2010. pp 64-79.
    • (2010) Biological data mining in protein interaction networks , pp. 64-79
    • La, D.1    Kihara, D.2
  • 18
    • 33750075732 scopus 로고    scopus 로고
    • Specificity of molecular interactions in transient protein-protein interaction interfaces
    • Cho KI, Lee K, Lee KH, Kim D, Lee D. Specificity of molecular interactions in transient protein-protein interaction interfaces. Proteins 2006; 65: 593-606.
    • (2006) Proteins , vol.65 , pp. 593-606
    • Cho, K.I.1    Lee, K.2    Lee, K.H.3    Kim, D.4    Lee, D.5
  • 19
    • 0034213559 scopus 로고    scopus 로고
    • Conservation of polar residues as hot spots at protein interfaces
    • Hu Z, Ma B, Wolfson H, Nussinov R. Conservation of polar residues as hot spots at protein interfaces. Proteins 2000; 39: 331-342.
    • (2000) Proteins , vol.39 , pp. 331-342
    • Hu, Z.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 20
    • 34548133728 scopus 로고    scopus 로고
    • Predicting functionally important residues from sequence conservation
    • Capra JA, Singh M. Predicting functionally important residues from sequence conservation. Bioinformatics 2007; 23: 1875-1882.
    • (2007) Bioinformatics , vol.23 , pp. 1875-1882
    • Capra, J.A.1    Singh, M.2
  • 21
    • 0346733329 scopus 로고    scopus 로고
    • Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey DR, Somaroo S, Hughes JD, Mintseris J, Huang ES. Are protein-protein interfaces more conserved in sequence than the rest of the protein surface? Protein Sci 2004; 13: 190-202.
    • (2004) Protein Sci , vol.13 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 22
    • 1042264059 scopus 로고    scopus 로고
    • Searching for functional sites in protein structures
    • Jones S, Thornton JM. Searching for functional sites in protein structures. Curr Opin Chem Biol 2004; 8: 3-7.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 3-7
    • Jones, S.1    Thornton, J.M.2
  • 23
    • 23044487169 scopus 로고    scopus 로고
    • Statistical analysis and prediction of protein-protein interfaces
    • Bordner AJ, Abagyan R. Statistical analysis and prediction of protein-protein interfaces. Proteins 2005; 60: 353-366.
    • (2005) Proteins , vol.60 , pp. 353-366
    • Bordner, A.J.1    Abagyan, R.2
  • 24
    • 0029664921 scopus 로고    scopus 로고
    • Evolutionarily conserved Galphabetagamma binding surfaces support a model of the G protein-receptor complex
    • Lichtarge O, Bourne HR, Cohen FE. Evolutionarily conserved Galphabetagamma binding surfaces support a model of the G protein-receptor complex. Proc Natl Acad Sci U S A 1996; 93: 7507-7511.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7507-7511
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 25
    • 33646766064 scopus 로고    scopus 로고
    • Correlated mutations: advances and limitations. A study on fusion proteins and on the Cohesin-Dockerin families
    • Halperin I, Wolfson H, Nussinov R. Correlated mutations: advances and limitations. A study on fusion proteins and on the Cohesin-Dockerin families. Proteins 2006; 63: 832-845.
    • (2006) Proteins , vol.63 , pp. 832-845
    • Halperin, I.1    Wolfson, H.2    Nussinov, R.3
  • 26
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O, Bourne HR, Cohen FE. An evolutionary trace method defines binding surfaces common to protein families. J Mol Biol 1996; 257: 342-358.
    • (1996) J Mol Biol , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 27
    • 25444468321 scopus 로고    scopus 로고
    • Predicting functional sites with an automated algorithm suitable for heterogeneous datasets
    • La D, Livesay DR. Predicting functional sites with an automated algorithm suitable for heterogeneous datasets. BMC Bioinformatics 2005; 6: 116.
    • (2005) BMC Bioinformatics , vol.6 , pp. 116
    • La, D.1    Livesay, D.R.2
  • 28
    • 17744397525 scopus 로고    scopus 로고
    • The evolutionary origins and catalytic importance of conserved electrostatic networks within TIM-barrel proteins
    • Livesay DR, La D. The evolutionary origins and catalytic importance of conserved electrostatic networks within TIM-barrel proteins. Protein Sci 2005; 14: 1158-1170.
    • (2005) Protein Sci , vol.14 , pp. 1158-1170
    • Livesay, D.R.1    La, D.2
  • 29
    • 0036468670 scopus 로고    scopus 로고
    • Evolutionary predictions of binding surfaces and interactions
    • Lichtarge O, Sowa ME. Evolutionary predictions of binding surfaces and interactions. Curr Opin Struct Biol 2002; 12: 21-27.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 21-27
    • Lichtarge, O.1    Sowa, M.E.2
  • 30
    • 54949145058 scopus 로고    scopus 로고
    • INTREPID-INformation-theoretic TREe traversal for protein functional site IDentification
    • Sankararaman S, Sjolander K. INTREPID-INformation-theoretic TREe traversal for protein functional site IDentification. Bioinformatics 2008; 24: 2445-2452.
    • (2008) Bioinformatics , vol.24 , pp. 2445-2452
    • Sankararaman, S.1    Sjolander, K.2
  • 31
    • 76649113438 scopus 로고    scopus 로고
    • Protein interactions and ligand binding: from protein subfamilies to functional specificity
    • Rausell A, Juan D, Pazos F, Valencia A. Protein interactions and ligand binding: from protein subfamilies to functional specificity. Proc Natl Acad Sci U S A 2010; 107: 1995-2000.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1995-2000
    • Rausell, A.1    Juan, D.2    Pazos, F.3    Valencia, A.4
  • 32
    • 13844264506 scopus 로고    scopus 로고
    • iPfam: visualization of protein-protein interactions in PDB at domain and amino acid resolutions
    • Finn RD, Marshall M, Bateman A. iPfam: visualization of protein-protein interactions in PDB at domain and amino acid resolutions. Bioinformatics 2005; 21: 410-412.
    • (2005) Bioinformatics , vol.21 , pp. 410-412
    • Finn, R.D.1    Marshall, M.2    Bateman, A.3
  • 33
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • Uniprot Consortium. The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res 2010; 38: D142-D148.
    • (2010) Nucleic Acids Res , vol.38
    • Uniprot, C.1
  • 34
    • 0032169688 scopus 로고    scopus 로고
    • PQS: a protein quaternary structure file server
    • Henrick K, Thornton JM. PQS: a protein quaternary structure file server. Trends Biochem Sci 1998; 23: 358-361.
    • (1998) Trends Biochem Sci , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 35
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 2004; 32: 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 36
    • 77957944014 scopus 로고    scopus 로고
    • Protein-protein docking benchmark version 4.0
    • Hwang H, Vreven T, Janin J, Weng Z. Protein-protein docking benchmark version 4.0. Proteins 2010; 78: 3111-3114.
    • (2010) Proteins , vol.78 , pp. 3111-3114
    • Hwang, H.1    Vreven, T.2    Janin, J.3    Weng, Z.4
  • 37
  • 38
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM. The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 1992; 8: 275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 39
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S, Henikoff JG. Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci U S A 1992; 89: 10915-10919.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 40
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon S, Gascuel O. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol 2003; 52: 696-704.
    • (2003) Syst Biol , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 41
    • 0030807655 scopus 로고    scopus 로고
    • BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data
    • Gascuel O. BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data. Mol Biol Evol 1997; 14: 685-695.
    • (1997) Mol Biol Evol , vol.14 , pp. 685-695
    • Gascuel, O.1
  • 42
    • 26444452202 scopus 로고    scopus 로고
    • Assessment of protein distance measures and tree-building methods for phylogenetic tree reconstruction
    • Hollich V, Milchert L, Arvestad L, Sonnhammer EL. Assessment of protein distance measures and tree-building methods for phylogenetic tree reconstruction. Mol Biol Evol 2005; 22: 2257-2264.
    • (2005) Mol Biol Evol , vol.22 , pp. 2257-2264
    • Hollich, V.1    Milchert, L.2    Arvestad, L.3    Sonnhammer, E.L.4
  • 43
    • 0001969211 scopus 로고    scopus 로고
    • Use of receiver operating characteristic (ROC) analysis to evaluate sequence matching
    • Gribskov M, Robinson NL. Use of receiver operating characteristic (ROC) analysis to evaluate sequence matching. Comput Chem 1996; 20: 25-33.
    • (1996) Comput Chem , vol.20 , pp. 25-33
    • Gribskov, M.1    Robinson, N.L.2
  • 44
    • 30744465573 scopus 로고    scopus 로고
    • Estimation of amino acid residue substitution rates at local spatial regions and application in protein function inference: a Bayesian Monte Carlo approach
    • Tseng YY, Liang J. Estimation of amino acid residue substitution rates at local spatial regions and application in protein function inference: a Bayesian Monte Carlo approach. Mol Biol Evol 2006; 23: 421-436.
    • (2006) Mol Biol Evol , vol.23 , pp. 421-436
    • Tseng, Y.Y.1    Liang, J.2
  • 45
    • 13944250570 scopus 로고    scopus 로고
    • A new method for estimating the importance of hydrophobic groups in the binding site of a protein
    • Kelly MD, Mancera RL. A new method for estimating the importance of hydrophobic groups in the binding site of a protein. J Med Chem 2005; 48: 1069-1078.
    • (2005) J Med Chem , vol.48 , pp. 1069-1078
    • Kelly, M.D.1    Mancera, R.L.2
  • 48
    • 0035853280 scopus 로고    scopus 로고
    • Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins
    • Landgraf R, Xenarios I, Eisenberg D. Three-dimensional cluster analysis identifies interfaces and functional residue clusters in proteins. J Mol Biol 2001; 307: 1487-1502.
    • (2001) J Mol Biol , vol.307 , pp. 1487-1502
    • Landgraf, R.1    Xenarios, I.2    Eisenberg, D.3
  • 50
    • 21644469377 scopus 로고    scopus 로고
    • Assessment of CAPRI predictions in rounds 3-5 shows progress in docking procedures
    • Mendez R, Leplae R, Lensink MF, Wodak SJ. Assessment of CAPRI predictions in rounds 3-5 shows progress in docking procedures. Proteins 2005; 60: 150-169.
    • (2005) Proteins , vol.60 , pp. 150-169
    • Mendez, R.1    Leplae, R.2    Lensink, M.F.3    Wodak, S.J.4
  • 52
    • 0020083498 scopus 로고
    • The meaning and use of the area under a receiver operating characteristic (ROC) curve
    • Hanley JA, McNeil BJ. The meaning and use of the area under a receiver operating characteristic (ROC) curve. Radiology 1982; 143: 29-36.
    • (1982) Radiology , vol.143 , pp. 29-36
    • Hanley, J.A.1    McNeil, B.J.2
  • 53
    • 33645972948 scopus 로고    scopus 로고
    • Servers for protein structure prediction
    • Fischer D. Servers for protein structure prediction. Curr Opin Struct Biol 2006; 16: 178-182.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 178-182
    • Fischer, D.1
  • 55
    • 33847107996 scopus 로고    scopus 로고
    • EMD: an ensemble algorithm for discovering regulatory motifs in DNA sequences
    • Hu J, Yang YD, Kihara D. EMD: an ensemble algorithm for discovering regulatory motifs in DNA sequences. BMC Bioinformatics 2006; 7: 342.
    • (2006) BMC Bioinformatics , vol.7 , pp. 342
    • Hu, J.1    Yang, Y.D.2    Kihara, D.3
  • 58
    • 0034843597 scopus 로고    scopus 로고
    • AL2CO: calculation of positional conservation ina protein sequence alignment
    • Pei J, Grishin NV. AL2CO: calculation of positional conservation ina protein sequence alignment. Bioinformatics 2001; 17: 700-712.
    • (2001) Bioinformatics , vol.17 , pp. 700-712
    • Pei, J.1    Grishin, N.V.2
  • 60
    • 19544384204 scopus 로고    scopus 로고
    • Using evolutionary expectation maximization to estimate indel rates
    • Holmes I. Using evolutionary expectation maximization to estimate indel rates. Bioinformatics 2005; 21: 2294-2300.
    • (2005) Bioinformatics , vol.21 , pp. 2294-2300
    • Holmes, I.1
  • 62
    • 33744907021 scopus 로고    scopus 로고
    • Efficient methods for estimating amino acid replacement rates
    • Arvestad L. Efficient methods for estimating amino acid replacement rates. J Mol Evol 2006; 62: 663-673.
    • (2006) J Mol Evol , vol.62 , pp. 663-673
    • Arvestad, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.