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Volumn 21, Issue 2, 2011, Pages 180-188

Protein function prediction: Towards integration of similarity metrics

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; BIOLOGICAL ACTIVITY; CLASSIFICATION ALGORITHM; COMPUTER PREDICTION; COMPUTER PROGRAM; MATHEMATICAL COMPUTING; MOLECULAR EVOLUTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DATABASE; PROTEIN FUNCTION; REVIEW; SENSITIVITY ANALYSIS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION; THREE DIMENSIONAL IMAGING;

EID: 79953077647     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2011.02.001     Document Type: Review
Times cited : (34)

References (83)
  • 3
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res 2010, 38:D142-D148.
    • (2010) Nucleic Acids Res , vol.38
  • 5
    • 0036308741 scopus 로고    scopus 로고
    • Enzyme function less conserved than anticipated
    • Rost B. Enzyme function less conserved than anticipated. J Mol Biol 2002, 318:595-608.
    • (2002) J Mol Biol , vol.318 , pp. 595-608
    • Rost, B.1
  • 6
    • 0142106373 scopus 로고    scopus 로고
    • How well is enzyme function conserved as a function of pairwise sequence identity?
    • Tian W., Skolnick J. How well is enzyme function conserved as a function of pairwise sequence identity?. J Mol Biol 2003, 333:863-882.
    • (2003) J Mol Biol , vol.333 , pp. 863-882
    • Tian, W.1    Skolnick, J.2
  • 7
    • 34250790725 scopus 로고    scopus 로고
    • Estimating the annotation error rate of curated GO database sequence annotations
    • Jones C.E., Brown A.L., Baumann U. Estimating the annotation error rate of curated GO database sequence annotations. BMC Bioinformatics 2007, 8:170.
    • (2007) BMC Bioinformatics , vol.8 , pp. 170
    • Jones, C.E.1    Brown, A.L.2    Baumann, U.3
  • 8
    • 74549221383 scopus 로고    scopus 로고
    • Annotation error in public databases: misannotation of molecular function in enzyme superfamilies
    • Schnoes A.M., Brown S.D., Dodevski I., Babbitt P.C. Annotation error in public databases: misannotation of molecular function in enzyme superfamilies. PLoS Comput Biol 2009, 5:e1000605.
    • (2009) PLoS Comput Biol , vol.5
    • Schnoes, A.M.1    Brown, S.D.2    Dodevski, I.3    Babbitt, P.C.4
  • 10
    • 0031970686 scopus 로고    scopus 로고
    • Multifunctional lens crystallins and corneal enzymes. More than meets the eye
    • Piatigorsky J. Multifunctional lens crystallins and corneal enzymes. More than meets the eye. Ann N Y Acad Sci 1998, 842:7-15.
    • (1998) Ann N Y Acad Sci , vol.842 , pp. 7-15
    • Piatigorsky, J.1
  • 11
    • 77951557120 scopus 로고    scopus 로고
    • Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution
    • Omelchenko M.V., Galperin M.Y., Wolf Y.I., Koonin E.V. Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution. Biol Direct 2010, 5:31.
    • (2010) Biol Direct , vol.5 , pp. 31
    • Omelchenko, M.V.1    Galperin, M.Y.2    Wolf, Y.I.3    Koonin, E.V.4
  • 12
    • 77951245620 scopus 로고    scopus 로고
    • On the diversity of physicochemical environments experienced by identical ligands in binding pockets of unrelated proteins
    • Kahraman A., Morris R.J., Laskowski R.A., Favia A.D., Thornton J.M. On the diversity of physicochemical environments experienced by identical ligands in binding pockets of unrelated proteins. Proteins 2010, 78:1120-1136.
    • (2010) Proteins , vol.78 , pp. 1120-1136
    • Kahraman, A.1    Morris, R.J.2    Laskowski, R.A.3    Favia, A.D.4    Thornton, J.M.5
  • 13
    • 0035783063 scopus 로고    scopus 로고
    • Fold change in evolution of protein structures
    • Grishin N.V. Fold change in evolution of protein structures. J Struct Biol 2001, 134:167-185.
    • (2001) J Struct Biol , vol.134 , pp. 167-185
    • Grishin, N.V.1
  • 14
    • 77952356281 scopus 로고    scopus 로고
    • Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors
    • Rodriguez G.J., Yao R., Lichtarge O., Wensel T.G. Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors. Proc Natl Acad Sci U S A 2010, 107:7787-7792.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7787-7792
    • Rodriguez, G.J.1    Yao, R.2    Lichtarge, O.3    Wensel, T.G.4
  • 17
    • 77950855514 scopus 로고    scopus 로고
    • Quantitative comparison of catalytic mechanisms and overall reactions in convergently evolved enzymes: implications for classification of enzyme function
    • Almonacid D.E., Yera E.R., Mitchell J.B., Babbitt P.C. Quantitative comparison of catalytic mechanisms and overall reactions in convergently evolved enzymes: implications for classification of enzyme function. PLoS Comput Biol 2010, 6:e1000700.
    • (2010) PLoS Comput Biol , vol.6
    • Almonacid, D.E.1    Yera, E.R.2    Mitchell, J.B.3    Babbitt, P.C.4
  • 20
    • 0037805576 scopus 로고    scopus 로고
    • The KEGG database
    • discussion 101-103, 119-128, 144-152
    • Kanehisa M. The KEGG database. Novartis Found Symp 2002, 247:91-101. discussion 101-103, 119-128, 144-152.
    • (2002) Novartis Found Symp , vol.247 , pp. 91-101
    • Kanehisa, M.1
  • 24
    • 33744471931 scopus 로고    scopus 로고
    • Enhanced automated function prediction using distantly related sequences and contextual association by PFP
    • Hawkins T., Luban S., Kihara D. Enhanced automated function prediction using distantly related sequences and contextual association by PFP. Protein Sci 2006, 15:1550-1556.
    • (2006) Protein Sci , vol.15 , pp. 1550-1556
    • Hawkins, T.1    Luban, S.2    Kihara, D.3
  • 25
    • 67649868148 scopus 로고    scopus 로고
    • ESG: extended similarity group method for automated protein function prediction
    • Chitale M., Hawkins T., Park C., Kihara D. ESG: extended similarity group method for automated protein function prediction. Bioinformatics 2009, 25:1739-1745.
    • (2009) Bioinformatics , vol.25 , pp. 1739-1745
    • Chitale, M.1    Hawkins, T.2    Park, C.3    Kihara, D.4
  • 26
    • 78650509490 scopus 로고    scopus 로고
    • Novel genes exhibit distinct patterns of function acquisition and network integration
    • Capra J.A., Pollard K.S., Singh M. Novel genes exhibit distinct patterns of function acquisition and network integration. Genome Biol 2010, 11:R127.
    • (2010) Genome Biol , vol.11
    • Capra, J.A.1    Pollard, K.S.2    Singh, M.3
  • 28
    • 0035091008 scopus 로고    scopus 로고
    • Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different
    • Seffernick J.L., de Souza M.L., Sadowsky M.J., Wackett L.P. Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different. J Bacteriol 2001, 183:2405-2410.
    • (2001) J Bacteriol , vol.183 , pp. 2405-2410
    • Seffernick, J.L.1    de Souza, M.L.2    Sadowsky, M.J.3    Wackett, L.P.4
  • 30
    • 13444280436 scopus 로고    scopus 로고
    • EFICAz: a comprehensive approach for accurate genome-scale enzyme function inference
    • Tian W., Arakaki A.K., Skolnick J. EFICAz: a comprehensive approach for accurate genome-scale enzyme function inference. Nucleic Acids Res 2004, 32:6226-6239.
    • (2004) Nucleic Acids Res , vol.32 , pp. 6226-6239
    • Tian, W.1    Arakaki, A.K.2    Skolnick, J.3
  • 31
    • 40749111548 scopus 로고    scopus 로고
    • ConFunc - functional annotation in the twilight zone
    • Wass M.N., Sternberg M.J. ConFunc - functional annotation in the twilight zone. Bioinformatics 2008, 24:798-806.
    • (2008) Bioinformatics , vol.24 , pp. 798-806
    • Wass, M.N.1    Sternberg, M.J.2
  • 32
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L., Rosenstrom P. Dali server: conservation mapping in 3D. Nucleic Acids Res 2010, 38(Suppl.):W545-W549.
    • (2010) Nucleic Acids Res , vol.38 , Issue.SUPPL.
    • Holm, L.1    Rosenstrom, P.2
  • 36
    • 0035815113 scopus 로고    scopus 로고
    • Evolution of function in protein superfamilies, from a structural perspective
    • Todd A.E., Orengo C.A., Thornton J.M. Evolution of function in protein superfamilies, from a structural perspective. J Mol Biol 2001, 307:1113-1143.
    • (2001) J Mol Biol , vol.307 , pp. 1113-1143
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 37
    • 34047273007 scopus 로고    scopus 로고
    • Functional differentiation of proteins: implications for structural genomics
    • Friedberg I., Godzik A. Functional differentiation of proteins: implications for structural genomics. Structure 2007, 15:405-415.
    • (2007) Structure , vol.15 , pp. 405-415
    • Friedberg, I.1    Godzik, A.2
  • 38
    • 52749091256 scopus 로고    scopus 로고
    • TOPS++FATCAT: fast flexible structural alignment using constraints derived from TOPS+ Strings Model
    • Veeramalai M., Ye Y., Godzik A. TOPS++FATCAT: fast flexible structural alignment using constraints derived from TOPS+ Strings Model. BMC Bioinformatics 2008, 9:358.
    • (2008) BMC Bioinformatics , vol.9 , pp. 358
    • Veeramalai, M.1    Ye, Y.2    Godzik, A.3
  • 39
    • 33845885769 scopus 로고    scopus 로고
    • Rapid detection of similarity in protein structure and function through contact metric distances
    • Lisewski A.M., Lichtarge O. Rapid detection of similarity in protein structure and function through contact metric distances. Nucleic Acids Res 2006, 34:e152.
    • (2006) Nucleic Acids Res , vol.34
    • Lisewski, A.M.1    Lichtarge, O.2
  • 40
    • 77949420656 scopus 로고    scopus 로고
    • Comparison of structure-based and threading-based approaches to protein functional annotation
    • Brylinski M., Skolnick J. Comparison of structure-based and threading-based approaches to protein functional annotation. Proteins 2010, 78:118-134.
    • (2010) Proteins , vol.78 , pp. 118-134
    • Brylinski, M.1    Skolnick, J.2
  • 41
    • 61649106689 scopus 로고    scopus 로고
    • Predicting protein function and binding profile via matching of local evolutionary and geometric surface patterns
    • Tseng Y.Y., Dundas J., Liang J. Predicting protein function and binding profile via matching of local evolutionary and geometric surface patterns. J Mol Biol 2009, 387:451-464.
    • (2009) J Mol Biol , vol.387 , pp. 451-464
    • Tseng, Y.Y.1    Dundas, J.2    Liang, J.3
  • 42
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas J., Ouyang Z., Tseng J., Binkowski A., Turpaz Y., Liang J. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res 2006, 34:W116-W118.
    • (2006) Nucleic Acids Res , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 43
    • 0028881975 scopus 로고
    • SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions
    • 307-328
    • Laskowski R.A. SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions. J Mol Graph 1995, 13:323-330. 307-328.
    • (1995) J Mol Graph , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 44
    • 12944257228 scopus 로고    scopus 로고
    • The ConSurf-HSSP database: the mapping of evolutionary conservation among homologs onto PDB structures
    • Glaser F., Rosenberg Y., Kessel A., Pupko T., Ben-Tal N. The ConSurf-HSSP database: the mapping of evolutionary conservation among homologs onto PDB structures. Proteins 2005, 58:610-617.
    • (2005) Proteins , vol.58 , pp. 610-617
    • Glaser, F.1    Rosenberg, Y.2    Kessel, A.3    Pupko, T.4    Ben-Tal, N.5
  • 45
    • 0036288284 scopus 로고    scopus 로고
    • Identification of protein functions from a molecular surface database, eF-site
    • Kinoshita K., Furui J., Nakamura H. Identification of protein functions from a molecular surface database, eF-site. J Struct Funct Genomics 2002, 2:9-22.
    • (2002) J Struct Funct Genomics , vol.2 , pp. 9-22
    • Kinoshita, K.1    Furui, J.2    Nakamura, H.3
  • 46
    • 48449092564 scopus 로고    scopus 로고
    • MultiBind and MAPPIS: webservers for multiple alignment of protein 3D-binding sites and their interactions
    • Shulman-Peleg A., Shatsky M., Nussinov R., Wolfson H.J. MultiBind and MAPPIS: webservers for multiple alignment of protein 3D-binding sites and their interactions. Nucleic Acids Res 2008, 36:W260-W264.
    • (2008) Nucleic Acids Res , vol.36
    • Shulman-Peleg, A.1    Shatsky, M.2    Nussinov, R.3    Wolfson, H.J.4
  • 47
    • 38349100452 scopus 로고    scopus 로고
    • A threading-based method (FINDSITE) for ligand-binding site prediction and functional annotation
    • Brylinski M., Skolnick J. A threading-based method (FINDSITE) for ligand-binding site prediction and functional annotation. Proc Natl Acad Sci U S A 2008, 105:129-134.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 129-134
    • Brylinski, M.1    Skolnick, J.2
  • 48
    • 0029973830 scopus 로고    scopus 로고
    • Derivation of 3D coordinate templates for searching structural databases: application to Ser-His-Asp catalytic triads in the serine proteinases and lipases
    • Wallace A.C., Laskowski R.A., Thornton J.M. Derivation of 3D coordinate templates for searching structural databases: application to Ser-His-Asp catalytic triads in the serine proteinases and lipases. Protein Sci 1996, 5:1001-1013.
    • (1996) Protein Sci , vol.5 , pp. 1001-1013
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 50
    • 0345864027 scopus 로고    scopus 로고
    • The Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural data
    • Porter C.T., Bartlett G.J., Thornton J.M. The Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural data. Nucleic Acids Res 2004, 32:D129-D133.
    • (2004) Nucleic Acids Res , vol.32
    • Porter, C.T.1    Bartlett, G.J.2    Thornton, J.M.3
  • 51
    • 22544486576 scopus 로고    scopus 로고
    • Protein function prediction using local 3D templates
    • Laskowski R.A., Watson J.D., Thornton J.M. Protein function prediction using local 3D templates. J Mol Biol 2005, 351:614-626.
    • (2005) J Mol Biol , vol.351 , pp. 614-626
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 52
    • 33645098516 scopus 로고    scopus 로고
    • Automated discovery of 3D motifs for protein function annotation
    • Polacco B.J., Babbitt P.C. Automated discovery of 3D motifs for protein function annotation. Bioinformatics 2006, 22:723-730.
    • (2006) Bioinformatics , vol.22 , pp. 723-730
    • Polacco, B.J.1    Babbitt, P.C.2
  • 54
    • 65649110443 scopus 로고    scopus 로고
    • Evolutionary Trace Annotation Server: automated enzyme function prediction in protein structures using 3D templates
    • Ward R.M., Venner E., Daines B., Murray S., Erdin S., Kristensen D.M., Lichtarge O. Evolutionary Trace Annotation Server: automated enzyme function prediction in protein structures using 3D templates. Bioinformatics 2009, 25:1426-1427.
    • (2009) Bioinformatics , vol.25 , pp. 1426-1427
    • Ward, R.M.1    Venner, E.2    Daines, B.3    Murray, S.4    Erdin, S.5    Kristensen, D.M.6    Lichtarge, O.7
  • 55
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O., Bourne H.R., Cohen F.E. 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
  • 56
    • 1242339659 scopus 로고    scopus 로고
    • A family of evolution-entropy hybrid methods for ranking protein residues by importance
    • Mihalek I., Res I., Lichtarge O. A family of evolution-entropy hybrid methods for ranking protein residues by importance. J Mol Biol 2004, 336:1265-1282.
    • (2004) J Mol Biol , vol.336 , pp. 1265-1282
    • Mihalek, I.1    Res, I.2    Lichtarge, O.3
  • 58
    • 77955570809 scopus 로고    scopus 로고
    • Evolution: a guide to perturb protein function and networks
    • Lichtarge O., Wilkins A. Evolution: a guide to perturb protein function and networks. Curr Opin Struct Biol 2010, 20:351-359.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 351-359
    • Lichtarge, O.1    Wilkins, A.2
  • 61
    • 47849086673 scopus 로고    scopus 로고
    • De-orphaning the structural proteome through reciprocal comparison of evolutionarily important structural features
    • Ward R.M., Erdin S., Tran T.A., Kristensen D.M., Lisewski A.M., Lichtarge O. De-orphaning the structural proteome through reciprocal comparison of evolutionarily important structural features. PLoS ONE 2008, 3:e2136.
    • (2008) PLoS ONE , vol.3
    • Ward, R.M.1    Erdin, S.2    Tran, T.A.3    Kristensen, D.M.4    Lisewski, A.M.5    Lichtarge, O.6
  • 62
    • 77953963521 scopus 로고    scopus 로고
    • Sequence and structure continuity of evolutionary importance improves protein functional site discovery and annotation
    • Wilkins A.D., Lua R., Erdin S., Ward R.M., Lichtarge O. Sequence and structure continuity of evolutionary importance improves protein functional site discovery and annotation. Protein Sci 2010, 19:1296-1311.
    • (2010) Protein Sci , vol.19 , pp. 1296-1311
    • Wilkins, A.D.1    Lua, R.2    Erdin, S.3    Ward, R.M.4    Lichtarge, O.5
  • 63
    • 77649271360 scopus 로고    scopus 로고
    • Evolutionary trace annotation of protein function in the structural proteome
    • Erdin S., Ward R.M., Venner E., Lichtarge O. Evolutionary trace annotation of protein function in the structural proteome. J Mol Biol 2010, 396:1451-1473.
    • (2010) J Mol Biol , vol.396 , pp. 1451-1473
    • Erdin, S.1    Ward, R.M.2    Venner, E.3    Lichtarge, O.4
  • 64
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: a server for predicting protein function from 3D structure
    • Laskowski R.A., Watson J.D., Thornton J.M. ProFunc: a server for predicting protein function from 3D structure. Nucleic Acids Res 2005, 33:W89-W93.
    • (2005) Nucleic Acids Res , vol.33
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 65
    • 11844292002 scopus 로고    scopus 로고
    • Inference of protein function from protein structure
    • Pal D., Eisenberg D. Inference of protein function from protein structure. Structure (Camb) 2005, 13:121-130.
    • (2005) Structure (Camb) , vol.13 , pp. 121-130
    • Pal, D.1    Eisenberg, D.2
  • 67
    • 33947252154 scopus 로고    scopus 로고
    • Network-based prediction of protein function
    • Sharan R., Ulitsky I., Shamir R. Network-based prediction of protein function. Mol Syst Biol 2007, 3:88.
    • (2007) Mol Syst Biol , vol.3 , pp. 88
    • Sharan, R.1    Ulitsky, I.2    Shamir, R.3
  • 68
    • 75949120438 scopus 로고    scopus 로고
    • How and when should interactome-derived clusters be used to predict functional modules and protein function?
    • Song J., Singh M. How and when should interactome-derived clusters be used to predict functional modules and protein function?. Bioinformatics 2009, 25:3143-3150.
    • (2009) Bioinformatics , vol.25 , pp. 3143-3150
    • Song, J.1    Singh, M.2
  • 69
    • 38649138295 scopus 로고    scopus 로고
    • A single gene network accurately predicts phenotypic effects of gene perturbation in Caenorhabditis elegans
    • Lee I., Lehner B., Crombie C., Wong W., Fraser A.G., Marcotte E.M. A single gene network accurately predicts phenotypic effects of gene perturbation in Caenorhabditis elegans. Nat Genet 2008, 40:181-188.
    • (2008) Nat Genet , vol.40 , pp. 181-188
    • Lee, I.1    Lehner, B.2    Crombie, C.3    Wong, W.4    Fraser, A.G.5    Marcotte, E.M.6
  • 70
    • 33745619564 scopus 로고    scopus 로고
    • Exploiting indirect neighbours and topological weight to predict protein function from protein-protein interactions
    • Chua H.N., Sung W.K., Wong L. Exploiting indirect neighbours and topological weight to predict protein function from protein-protein interactions. Bioinformatics 2006, 22:1623-1630.
    • (2006) Bioinformatics , vol.22 , pp. 1623-1630
    • Chua, H.N.1    Sung, W.K.2    Wong, L.3
  • 71
    • 70350235043 scopus 로고    scopus 로고
    • Interaction networks: lessons from large-scale studies in yeast
    • Cagney G. Interaction networks: lessons from large-scale studies in yeast. Proteomics 2009, 9:4799-4811.
    • (2009) Proteomics , vol.9 , pp. 4799-4811
    • Cagney, G.1
  • 73
    • 76749084811 scopus 로고    scopus 로고
    • Protein interaction networks - more than mere modules
    • Pinkert S., Schultz J., Reichardt J. Protein interaction networks - more than mere modules. PLoS Comput Biol 2010, 6:e1000659.
    • (2010) PLoS Comput Biol , vol.6
    • Pinkert, S.1    Schultz, J.2    Reichardt, J.3
  • 75
    • 3142622851 scopus 로고    scopus 로고
    • An integrated probabilistic model for functional prediction of proteins
    • Deng M., Chen T., Sun F. An integrated probabilistic model for functional prediction of proteins. J Comput Biol 2004, 11:463-475.
    • (2004) J Comput Biol , vol.11 , pp. 463-475
    • Deng, M.1    Chen, T.2    Sun, F.3
  • 77
    • 75149153011 scopus 로고    scopus 로고
    • Predicting protein functions by relaxation labelling protein interaction network
    • Hu P., Jiang H., Emili A. Predicting protein functions by relaxation labelling protein interaction network. BMC Bioinformatics 2010, 11(Suppl. 1):S64.
    • (2010) BMC Bioinformatics , vol.11 , Issue.SUPPL. 1
    • Hu, P.1    Jiang, H.2    Emili, A.3
  • 78
    • 27544435126 scopus 로고    scopus 로고
    • Fast protein classification with multiple networks
    • Tsuda K., Shin H., Scholkopf B. Fast protein classification with multiple networks. Bioinformatics 2005, 21(Suppl. 2):ii59-ii65.
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 2
    • Tsuda, K.1    Shin, H.2    Scholkopf, B.3
  • 79
    • 36549013593 scopus 로고    scopus 로고
    • Graph sharpening plus graph integration: a synergy that improves protein functional classification
    • Shin H., Lisewski A.M., Lichtarge O. Graph sharpening plus graph integration: a synergy that improves protein functional classification. Bioinformatics 2007, 23:3217-3224.
    • (2007) Bioinformatics , vol.23 , pp. 3217-3224
    • Shin, H.1    Lisewski, A.M.2    Lichtarge, O.3
  • 80
    • 78650798477 scopus 로고    scopus 로고
    • Accurate protein structure annotation through competitive diffusion of enzymatic functions over a network of local evolutionary similarities
    • Venner E., Lisewski A.M., Erdin S., Ward R.M., Amin S.R., Lichtarge O. Accurate protein structure annotation through competitive diffusion of enzymatic functions over a network of local evolutionary similarities. PLoS One 2010, 5:e14286.
    • (2010) PLoS One , vol.5
    • Venner, E.1    Lisewski, A.M.2    Erdin, S.3    Ward, R.M.4    Amin, S.R.5    Lichtarge, O.6


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