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Volumn 9, Issue 9, 2014, Pages

Combining structural modeling with ensemble machine learning to accurately predict protein fold stability and binding affinity effects upon mutation

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; DISEASE ASSOCIATION; ENSEMBLE LEARNING APPROACH FOR STABILITY PREDICTION OF INTERFACE AND CORE MUTATION; EXPERIMENTAL MODEL; GENE MUTATION; MACHINE LEARNING; MEASUREMENT ACCURACY; MUTATIONAL ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SINGLE NUCLEOTIDE POLYMORPHISM; STOCHASTIC GRADIENT BOOSTING OF DECISION TREES ALGORITHM; STRUCTURE ANALYSIS; WILD TYPE; ARTIFICIAL INTELLIGENCE; CHEMICAL STRUCTURE; COMPUTER PROGRAM; HUMAN; METABOLISM; MUTATION; PROTEIN CONFORMATION; PROTEIN DATABASE; SEQUENCE ANALYSIS;

EID: 84907279766     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0107353     Document Type: Article
Times cited : (72)

References (76)
  • 1
    • 80052964856 scopus 로고    scopus 로고
    • Understanding the contribution of synonymous mutations to human disease
    • Sauna ZE, Kimchi-Sarfaty C (2011) Understanding the contribution of synonymous mutations to human disease. Nat Rev Genet 12: 683-691. doi:10.1038/nrg3051.
    • (2011) Nat Rev Genet , vol.12 , pp. 683-691
    • Sauna, Z.E.1    Kimchi-Sarfaty, C.2
  • 2
    • 0033516391 scopus 로고    scopus 로고
    • A good SNP may be hard to find
    • Hagmann M (1999) A Good SNP May Be Hard to Find. Science 285: 21-22. doi:10.1126/science.285.5424.21a.
    • (1999) Science , vol.285 , pp. 21-22
    • Hagmann, M.1
  • 3
    • 0034660559 scopus 로고    scopus 로고
    • Searching for genetic determinants in the new millennium
    • Risch NJ (2000) Searching for genetic determinants in the new millennium. Nature 405: 847-856. doi:10.1038/35015718.
    • (2000) Nature , vol.405 , pp. 847-856
    • Risch, N.J.1
  • 4
    • 84863556835 scopus 로고    scopus 로고
    • Evolution and functional impact of rare coding variation from deep sequencing of human exomes
    • Tennessen JA, Bigham AW, O'Connor TD, Fu W, Kenny EE, et al. (2012) Evolution and functional impact of rare coding variation from deep sequencing of human exomes. Science 337: 64-69. doi:10.1126/science.1219240.
    • (2012) Science , vol.337 , pp. 64-69
    • Tennessen, J.A.1    Bigham, A.W.2    O'connor, T.D.3    Fu, W.4    Kenny, E.E.5
  • 5
    • 74949138753 scopus 로고    scopus 로고
    • Human genome sequencing using unchained base reads on self-assembling DNA nanoarrays
    • Drmanac R, Sparks AB, Callow MJ, Halpern AL, Burns NL, et al. (2010) Human genome sequencing using unchained base reads on self-assembling DNA nanoarrays. Science 327: 78-81. doi:10.1126/science.1181498.
    • (2010) Science , vol.327 , pp. 78-81
    • Drmanac, R.1    Sparks, A.B.2    Callow, M.J.3    Halpern, A.L.4    Burns, N.L.5
  • 6
    • 84975804424 scopus 로고    scopus 로고
    • Mapping copy number variation by population-scale genome sequencing
    • Mills RE, Walter K, Stewart C, Handsaker RE, Chen K, et al. (2011) Mapping copy number variation by population-scale genome sequencing. Nature 470: 59-65. doi:10.1038/nature09708.
    • (2011) Nature , vol.470 , pp. 59-65
    • Mills, R.E.1    Walter, K.2    Stewart, C.3    Handsaker, R.E.4    Chen, K.5
  • 7
    • 84975742565 scopus 로고    scopus 로고
    • A map of human genome variation from population-scale sequencing
    • Genomes Project Consortium, Abecasis GR, Altshuler D, Auton A, Brooks LD, et al. (2010) A map of human genome variation from population-scale sequencing. Nature 467: 1061-1073. doi:10.1038/nature09534.
    • (2010) Nature , vol.467 , pp. 1061-1073
    • Abecasis, G.R.1    Altshuler, D.2    Auton, A.3    Brooks, L.D.4
  • 8
    • 84975795680 scopus 로고    scopus 로고
    • An integrated map of genetic variation from 1,092 human genomes
    • Consortium T 1000 GP
    • Consortium T 1000 GP (2012) An integrated map of genetic variation from 1,092 human genomes. Nature 491: 56-65. doi:10.1038/nature11632.
    • (2012) Nature , vol.491 , pp. 56-65
  • 9
    • 74449093973 scopus 로고    scopus 로고
    • A comprehensive catalogue of somatic mutations from a human cancer genome
    • Pleasance ED, Cheetham RK, Stephens PJ, McBride DJ, Humphray SJ, et al. (2010) A comprehensive catalogue of somatic mutations from a human cancer genome. Nature 463: 191-196. doi:10.1038/nature08658.
    • (2010) Nature , vol.463 , pp. 191-196
    • Pleasance, E.D.1    Cheetham, R.K.2    Stephens, P.J.3    McBride, D.J.4    Humphray, S.J.5
  • 10
    • 77953006634 scopus 로고    scopus 로고
    • The mutation spectrum revealed by paired genome sequences from a lung cancer patient
    • Lee W, Jiang Z, Liu J, Haverty PM, Guan Y, et al. (2010) The mutation spectrum revealed by paired genome sequences from a lung cancer patient. Nature 465: 473-477. doi:10.1038/nature09004.
    • (2010) Nature , vol.465 , pp. 473-477
    • Lee, W.1    Jiang, Z.2    Liu, J.3    Haverty, P.M.4    Guan, Y.5
  • 11
    • 0035399728 scopus 로고    scopus 로고
    • SNP association studies in Alzheimer's disease highlight problems for complex disease analysis
    • Emahazion T, Feuk L, Jobs M, Sawyer SL, Fredman D, et al. (2001) SNP association studies in Alzheimer's disease highlight problems for complex disease analysis. Trends Genet TIG 17: 407-413.
    • (2001) Trends Genet TIG , vol.17 , pp. 407-413
    • Emahazion, T.1    Feuk, L.2    Jobs, M.3    Sawyer, S.L.4    Fredman, D.5
  • 12
    • 0347755642 scopus 로고    scopus 로고
    • ProTherm, version 4.0: Thermodynamic database for proteins and mutants
    • Bava KA, Gromiha MM, Uedaira H, Kitajima K, Sarai A (2004) ProTherm, version 4.0: thermodynamic database for proteins and mutants. Nucleic Acids Res 32: D120-D121. doi:10.1093/nar/gkh082.
    • (2004) Nucleic Acids Res , vol.32 , pp. D120-D121
    • Bava, K.A.1    Gromiha, M.M.2    Uedaira, H.3    Kitajima, K.4    Sarai, A.5
  • 13
    • 84870409536 scopus 로고    scopus 로고
    • SKEMPI: A Structural Kinetic and Energetic database of Mutant Protein Interactions and its use in empirical models
    • Moal IH, Fernández-Recio J (2012) SKEMPI: a Structural Kinetic and Energetic database of Mutant Protein Interactions and its use in empirical models. Bioinforma Oxf Engl 28: 2600-2607. doi:10.1093/bioinformatics/ bts489.
    • (2012) Bioinforma Oxf Engl , vol.28 , pp. 2600-2607
    • Moal, I.H.1    Fernández-Recio, J.2
  • 14
    • 33750353461 scopus 로고    scopus 로고
    • Predicting the effects of amino acid substitutions on protein function
    • Ng PC, Henikoff S (2006) Predicting the effects of amino acid substitutions on protein function. Annu Rev Genomics Hum Genet 7: 61-80. doi:10.1146/ annurev.genom.7.080505.115630.
    • (2006) Annu Rev Genomics Hum Genet , vol.7 , pp. 61-80
    • Ng, P.C.1    Henikoff, S.2
  • 16
    • 68149165614 scopus 로고    scopus 로고
    • Predicting the effects of coding nonsynonymous variants on protein function using the SIFT algorithm
    • Kumar P, Henikoff S, Ng PC (2009) Predicting the effects of coding nonsynonymous variants on protein function using the SIFT algorithm. Nat Protoc 4: 1073-1081. doi:10.1038/nprot.2009.86.
    • (2009) Nat Protoc , vol.4 , pp. 1073-1081
    • Kumar, P.1    Henikoff, S.2    Ng, P.C.3
  • 17
  • 18
    • 84861052952 scopus 로고    scopus 로고
    • Analyzing effects of naturally occurring missense mutations
    • Zhang Z, Miteva MA, Wang L, Alexov E (2012) Analyzing effects of naturally occurring missense mutations. Comput Math Methods Med 2012: 805827. doi:10.1155/2012/805827.
    • (2012) Comput Math Methods Med , vol.2012 , pp. 805827
    • Zhang, Z.1    Miteva, M.A.2    Wang, L.3    Alexov, E.4
  • 19
    • 74549207309 scopus 로고    scopus 로고
    • Assessing computational methods for predicting protein stability upon mutation: Good on average but not in the details
    • Potapov V, Cohen M, Schreiber G (2009) Assessing computational methods for predicting protein stability upon mutation: good on average but not in the details. Protein Eng Des Sel PEDS 22: 553-560. doi:10.1093/protein/gzp030.
    • (2009) Protein Eng des Sel PEDS , vol.22 , pp. 553-560
    • Potapov, V.1    Cohen, M.2    Schreiber, G.3
  • 20
    • 0034521981 scopus 로고    scopus 로고
    • Calculating structures and free energies of complex molecules: Combining molecular mechanics and continuum models
    • Kollman PA, Massova I, Reyes C, Kuhn B, Huo S, et al. (2000) Calculating Structures and Free Energies of Complex Molecules: Combining Molecular Mechanics and Continuum Models. Acc Chem Res 33: 889-897. doi:10.1021/ ar000033j.
    • (2000) Acc Chem Res , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.5
  • 21
    • 0027191902 scopus 로고
    • Can the stability of protein mutants be predicted by free energy calculations?
    • Yun-yu S, Mark AE, Cun-xin W, Fuhua H, Berendsen HJC, et al. (1993) Can the stability of protein mutants be predicted by free energy calculations? Protein Eng 6: 289-295. doi:10.1093/protein/6.3.289.
    • (1993) Protein Eng , vol.6 , pp. 289-295
    • Yun-Yu, S.1    Mark, A.E.2    Cun-Xin, W.3    Fuhua, H.4    Hjc, B.5
  • 22
    • 0142184268 scopus 로고    scopus 로고
    • How can free energy component analysis explain the difference in protein stability caused by amino acid substitutions? Effect of three hydrophobic mutations at the 56th residue on the stability of human lysozyme
    • Funahashi J, Sugita Y, Kitao A, Yutani K (2003) How can free energy component analysis explain the difference in protein stability caused by amino acid substitutions? Effect of three hydrophobic mutations at the 56th residue on the stability of human lysozyme. Protein Eng 16: 665-671. doi:10.1093/protein/ gzg083.
    • (2003) Protein Eng , vol.16 , pp. 665-671
    • Funahashi, J.1    Sugita, Y.2    Kitao, A.3    Yutani, K.4
  • 23
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • Guerois R, Nielsen JE, Serrano L (2002) Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J Mol Biol 320: 369-387. doi:10.1016/S0022-2836(02)00442-4.
    • (2002) J Mol Biol , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 24
    • 70349847872 scopus 로고    scopus 로고
    • Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0
    • Dehouck Y, Grosfils A, Folch B, Gilis D, Bogaerts P, et al. (2009) Fast and accurate predictions of protein stability changes upon mutations using statistical potentials and neural networks: PoPMuSiC-2.0. Bioinformatics 25: 2537-2543. doi:10.1093/bioinformatics/btp445.
    • (2009) Bioinformatics , vol.25 , pp. 2537-2543
    • Dehouck, Y.1    Grosfils, A.2    Folch, B.3    Gilis, D.4    Bogaerts, P.5
  • 25
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for binding energy hot spots in protein-protein complexes
    • Kortemme T, Baker D (2002) A simple physical model for binding energy hot spots in protein-protein complexes. Proc Natl Acad Sci 99: 14116-14121. doi:10.1073/pnas.202485799.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 14116-14121
    • Kortemme, T.1    Baker, D.2
  • 26
    • 36749018607 scopus 로고    scopus 로고
    • Modeling backbone flexibility improves protein stability estimation
    • Yin S, Ding F, Dokholyan NV (2007) Modeling backbone flexibility improves protein stability estimation. Struct Lond Engl 1993 15: 1567-1576. doi:10.1016/ j.str.2007.09.024.
    • (2007) Struct Lond Engl 1993 , vol.15 , pp. 1567-1576
    • Yin, S.1    Ding, F.2    Dokholyan, N.V.3
  • 27
    • 51749110028 scopus 로고    scopus 로고
    • Accurate prediction of stability changes in protein mutants by combining machine learning with structure based computational mutagenesis
    • Masso M, Vaisman II (2008) Accurate prediction of stability changes in protein mutants by combining machine learning with structure based computational mutagenesis. Bioinformatics 24: 2002-2009. doi:10.1093/bioinformatics/ btn353.
    • (2008) Bioinformatics , vol.24 , pp. 2002-2009
    • Masso, M.1    Vaisman, I.I.2
  • 28
    • 11844281294 scopus 로고    scopus 로고
    • A neural-network-based method for predicting protein stability changes upon single point mutations
    • Capriotti E, Fariselli P, Casadio R (2004) A neural-network-based method for predicting protein stability changes upon single point mutations. Bioinformatics 20: i63-i68. doi:10.1093/bioinformatics/bth928.
    • (2004) Bioinformatics , vol.20 , pp. i63-i68
    • Capriotti, E.1    Fariselli, P.2    Casadio, R.3
  • 29
    • 33644847172 scopus 로고    scopus 로고
    • Prediction of protein stability changes for single-site mutations using support vector machines
    • Cheng J, Randall A, Baldi P (2006) Prediction of protein stability changes for single-site mutations using support vector machines. Proteins 62: 1125-1132. doi:10.1002/prot.20810.
    • (2006) Proteins , vol.62 , pp. 1125-1132
    • Cheng, J.1    Randall, A.2    Baldi, P.3
  • 30
    • 27544469800 scopus 로고    scopus 로고
    • Predicting protein stability changes from sequences using support vector machines
    • Capriotti E, Fariselli P, Calabrese R, Casadio R (2005) Predicting protein stability changes from sequences using support vector machines. Bioinformatics 21: ii54-ii58. doi:10.1093/bioinformatics/bti1109.
    • (2005) Bioinformatics , vol.21 , pp. ii54-ii58
    • Capriotti, E.1    Fariselli, P.2    Calabrese, R.3    Casadio, R.4
  • 31
    • 82255181420 scopus 로고    scopus 로고
    • Protein stability: A single recorded mutation aids in predicting the effects of other mutations in the same amino acid site
    • Wainreb G, Wolf L, Ashkenazy H, Dehouck Y, Ben-Tal N (2011) Protein stability: a single recorded mutation aids in predicting the effects of other mutations in the same amino acid site. Bioinforma Oxf Engl 27: 3286-3292. doi:10.1093/bioinformatics/btr576.
    • (2011) Bioinforma Oxf Engl , vol.27 , pp. 3286-3292
    • Wainreb, G.1    Wolf, L.2    Ashkenazy, H.3    Dehouck, Y.4    Ben-Tal, N.5
  • 32
    • 84857790275 scopus 로고    scopus 로고
    • Protein-protein interaction sites are hot spots for disease-associated nonsynonymous SNPs
    • David A, Razali R, Wass MN, Sternberg MJE (2012) Protein-protein interaction sites are hot spots for disease-associated nonsynonymous SNPs. Hum Mutat 33: 359-363. doi:10.1002/humu.21656.
    • (2012) Hum Mutat , vol.33 , pp. 359-363
    • David, A.1    Razali, R.2    Wass, M.N.3    Mje, S.4
  • 33
    • 84863010950 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of protein networks provides insight into human genetic disease
    • Wang X, Wei X, Thijssen B, Das J, Lipkin SM, et al. (2012) Three-dimensional reconstruction of protein networks provides insight into human genetic disease. Nat Biotechnol 30: 159-164. doi:10.1038/nbt.2106.
    • (2012) Nat Biotechnol , vol.30 , pp. 159-164
    • Wang, X.1    Wei, X.2    Thijssen, B.3    Das, J.4    Lipkin, S.M.5
  • 34
    • 84861090227 scopus 로고    scopus 로고
    • SNPeffect 4.0: On-line prediction of molecular and structural effects of proteincoding variants
    • De Baets G, Van Durme J, Reumers J, Maurer-Stroh S, Vanhee P, et al. (2012) SNPeffect 4.0: on-line prediction of molecular and structural effects of proteincoding variants. Nucleic Acids Res 40: D935-939. doi:10.1093/nar/gkr996.
    • (2012) Nucleic Acids Res , vol.40 , pp. D935-939
    • De Baets, G.1    Van Durme, J.2    Reumers, J.3    Maurer-Stroh, S.4    Vanhee, P.5
  • 36
    • 84883574360 scopus 로고    scopus 로고
    • BeAtMuSiC: Prediction of changes in protein-protein binding affinity on mutations
    • Dehouck Y, Kwasigroch JM, Rooman M, Gilis D (2013) BeAtMuSiC: prediction of changes in protein-protein binding affinity on mutations. Nucleic Acids Res. doi:10.1093/nar/gkt450.
    • (2013) Nucleic Acids Res
    • Dehouck, Y.1    Kwasigroch, J.M.2    Rooman, M.3    Gilis, D.4
  • 37
    • 84884695874 scopus 로고    scopus 로고
    • Characterizing Changes in the Rate of Protein-Protein Dissociation upon Interface Mutation Using Hotspot Energy and Organization
    • Agius R, Torchala M, Moal IH, Fernández-Recio J, Bates PA (2013) Characterizing Changes in the Rate of Protein-Protein Dissociation upon Interface Mutation Using Hotspot Energy and Organization. PLoS Comput Biol 9: e1003216. doi:10.1371/journal.pcbi.1003216.
    • (2013) PLoS Comput Biol , vol.9 , pp. e1003216
    • Agius, R.1    Torchala, M.2    Moal, I.H.3    Fernández-Recio, J.4    Bates, P.A.5
  • 38
    • 66149102833 scopus 로고    scopus 로고
    • Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
    • Teng S, Madej T, Panchenko A, Alexov E (2009) Modeling effects of human single nucleotide polymorphisms on protein-protein interactions. Biophys J 96: 2178-2188. doi:10.1016/j.bpj.2008.12.3904.
    • (2009) Biophys J , vol.96 , pp. 2178-2188
    • Teng, S.1    Madej, T.2    Panchenko, A.3    Alexov, E.4
  • 39
    • 84871967106 scopus 로고    scopus 로고
    • Interactome3D: Adding structural details to protein networks
    • Mosca R, Céol A, Aloy P (2013) Interactome3D: adding structural details to protein networks. Nat Methods 10: 47-53. doi:10.1038/nmeth.2289.
    • (2013) Nat Methods , vol.10 , pp. 47-53
    • Mosca, R.1    Céol, A.2    Aloy, P.3
  • 40
    • 84864555615 scopus 로고    scopus 로고
    • Structure-based mutant stability predictions on proteins of unknown structure
    • Gonnelli G, Rooman M, Dehouck Y (2012) Structure-based mutant stability predictions on proteins of unknown structure. J Biotechnol 161: 287-293. doi:10.1016/j.jbiotec.2012.06.020.
    • (2012) J Biotechnol , vol.161 , pp. 287-293
    • Gonnelli, G.1    Rooman, M.2    Dehouck, Y.3
  • 41
    • 84879157943 scopus 로고    scopus 로고
    • Cancer missense mutations alter binding properties of proteins and their interaction networks
    • Nishi H, Tyagi M, Teng S, Shoemaker BA, Hashimoto K, et al. (2013) Cancer Missense Mutations Alter Binding Properties of Proteins and Their Interaction Networks. PLoS ONE 8: e66273. doi:10.1371/journal.pone.0066273.
    • (2013) PLoS ONE , vol.8 , pp. e66273
    • Nishi, H.1    Tyagi, M.2    Teng, S.3    Shoemaker, B.A.4    Hashimoto, K.5
  • 43
    • 0036387236 scopus 로고    scopus 로고
    • Evaluation of structural and evolutionary contributions to deleterious mutation prediction
    • Saunders CT, Baker D (2002) Evaluation of structural and evolutionary contributions to deleterious mutation prediction. J Mol Biol 322: 891-901.
    • (2002) J Mol Biol , vol.322 , pp. 891-901
    • Saunders, C.T.1    Baker, D.2
  • 44
    • 77954062293 scopus 로고    scopus 로고
    • Predicting changes in protein thermostability brought about by single- or multi-site mutations
    • Tian J, Wu N, Chu X, Fan Y (2010) Predicting changes in protein thermostability brought about by single- or multi-site mutations. BMC Bioinformatics 11: 370. doi:10.1186/1471-2105-11-370.
    • (2010) BMC Bioinformatics , vol.11 , pp. 370
    • Tian, J.1    Wu, N.2    Chu, X.3    Fan, Y.4
  • 45
    • 0346733329 scopus 로고    scopus 로고
    • Are proteinprotein interfaces more conserved in sequence than the rest of the protein surface?
    • Caffrey DR, Somaroo S, Hughes JD, Mintseris J, Huang ES (2004) Are proteinprotein interfaces more conserved in sequence than the rest of the protein surface? Protein Sci Publ Protein Soc 13: 190-202. doi:10.1110/ps.03323604.
    • (2004) Protein Sci Publ Protein Soc , vol.13 , pp. 190-202
    • Caffrey, D.R.1    Somaroo, S.2    Hughes, J.D.3    Mintseris, J.4    Huang, E.S.5
  • 46
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren IMA, Thornton JM (2003) Diversity of protein-protein interactions. EMBO J 22: 3486-3492. doi:10.1093/emboj/cdg359.
    • (2003) EMBO J , vol.22 , pp. 3486-3492
    • Ima, N.1    Thornton, J.M.2
  • 47
    • 34248545940 scopus 로고    scopus 로고
    • Characterization of interfacial solvent in protein complexes and contribution of wet spots to the interface description
    • Teyra J, Pisabarro MT (2007) Characterization of interfacial solvent in protein complexes and contribution of wet spots to the interface description. Proteins 67: 1087-1095. doi:10.1002/prot.21394.
    • (2007) Proteins , vol.67 , pp. 1087-1095
    • Teyra, J.1    Pisabarro, M.T.2
  • 48
    • 84866108547 scopus 로고    scopus 로고
    • Versatility and invariance in the evolution of homologous heteromeric interfaces
    • Andreani J, Faure G, Guerois R (2012) Versatility and Invariance in the Evolution of Homologous Heteromeric Interfaces. PLoS Comput Biol 8: e1002677. doi:10.1371/journal.pcbi.1002677.
    • (2012) PLoS Comput Biol , vol.8 , pp. e1002677
    • Andreani, J.1    Faure, G.2    Guerois, R.3
  • 49
    • 0035065485 scopus 로고    scopus 로고
    • SNPs, protein structure, and disease
    • Wang Z, Moult J (2001) SNPs, protein structure, and disease. Hum Mutat 17: 263-270. doi:10.1002/humu.22.
    • (2001) Hum Mutat , vol.17 , pp. 263-270
    • Wang, Z.1    Moult, J.2
  • 50
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA (1995) A hot spot of binding energy in a hormone-receptor interface. Science 267: 383-386. doi:10.1126/science.7529940.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 51
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan AA, Thorn KS (1998) Anatomy of hot spots in protein interfaces. J Mol Biol 280: 1-9. doi:10.1006/jmbi.1998.1843.
    • (1998) J Mol Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 52
    • 72849142731 scopus 로고    scopus 로고
    • Edgetic perturbation models of human inherited disorders
    • Zhong Q, Simonis N, Li Q-R, Charloteaux B, Heuze F, et al. (2009) Edgetic perturbation models of human inherited disorders. Mol Syst Biol 5: 321. doi:10.1038/msb.2009.80.
    • (2009) Mol Syst Biol , vol.5 , pp. 321
    • Zhong, Q.1    Simonis, N.2    Li, Q.-R.3    Charloteaux, B.4    Heuze, F.5
  • 53
    • 0032991552 scopus 로고    scopus 로고
    • Characterization of single-nucleotide polymorphisms in coding regions of human genes
    • Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, et al. (1999) Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet 22: 231-238. doi:10.1038/10290.
    • (1999) Nat Genet , vol.22 , pp. 231-238
    • Cargill, M.1    Altshuler, D.2    Ireland, J.3    Sklar, P.4    Ardlie, K.5
  • 54
    • 0032990407 scopus 로고    scopus 로고
    • Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis
    • Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, et al. (1999) Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet 22: 239-247. doi:10.1038/10297.
    • (1999) Nat Genet , vol.22 , pp. 239-247
    • Halushka, M.K.1    Fan, J.B.2    Bentley, K.3    Hsie, L.4    Shen, N.5
  • 55
    • 78650373804 scopus 로고    scopus 로고
    • Network medicine: A networkbased approach to human disease
    • Barabási A-L, Gulbahce N, Loscalzo J (2011) Network medicine: a networkbased approach to human disease. Nat Rev Genet 12: 56-68. doi:10.1038/ nrg2918.
    • (2011) Nat Rev Genet , vol.12 , pp. 56-68
    • Barabási, A.-L.1    Gulbahce, N.2    Loscalzo, J.3
  • 56
    • 77955151784 scopus 로고    scopus 로고
    • MutationTaster evaluates disease-causing potential of sequence alterations
    • Schwarz JM, Rödelsperger C, Schuelke M, Seelow D (2010) MutationTaster evaluates disease-causing potential of sequence alterations. Nat Methods 7: 575-576. doi:10.1038/nmeth0810-575.
    • (2010) Nat Methods , vol.7 , pp. 575-576
    • Schwarz, J.M.1    Rödelsperger, C.2    Schuelke, M.3    Seelow, D.4
  • 57
    • 53749105617 scopus 로고    scopus 로고
    • SNAP predicts effect of mutations on protein function
    • Bromberg Y, Yachdav G, Rost B (2008) SNAP predicts effect of mutations on protein function. Bioinformatics 24: 2397-2398. doi:10.1093/bioinformatics/ btn435.
    • (2008) Bioinformatics , vol.24 , pp. 2397-2398
    • Bromberg, Y.1    Yachdav, G.2    Rost, B.3
  • 58
    • 77949601825 scopus 로고    scopus 로고
    • CD-HIT Suite: A web server for clustering and comparing biological sequences
    • Huang Y, Niu B, Gao Y, Fu L, Li W (2010) CD-HIT Suite: a web server for clustering and comparing biological sequences. Bioinformatics 26: 680-682. doi:10.1093/bioinformatics/btq003.
    • (2010) Bioinformatics , vol.26 , pp. 680-682
    • Huang, Y.1    Niu, B.2    Gao, Y.3    Fu, L.4    Li, W.5
  • 59
    • 13444266370 scopus 로고    scopus 로고
    • Online Mendelian Inheritance in Man (OMIM), a knowledgebase of human genes and genetic disorders
    • Hamosh A, Scott AF, Amberger JS, Bocchini CA, McKusick VA (2005) Online Mendelian Inheritance in Man (OMIM), a knowledgebase of human genes and genetic disorders. Nucleic Acids Res 33: D514-D517. doi:10.1093/nar/gki033.
    • (2005) Nucleic Acids Res , vol.33 , pp. D514-D517
    • Hamosh, A.1    Scott, A.F.2    Amberger, J.S.3    Bocchini, C.A.4    McKusick, V.A.5
  • 60
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P, Hunter T (2001) Oncogenic kinase signalling. Nature 411: 355-365. doi:10.1038/35077225.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 62
    • 78651330430 scopus 로고    scopus 로고
    • COSMIC: Mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer
    • Forbes SA, Bindal N, Bamford S, Cole C, Kok CY, et al. (2011) COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer. Nucleic Acids Res 39: D945-D950. doi:10.1093/nar/gkq929.
    • (2011) Nucleic Acids Res , vol.39 , pp. D945-D950
    • Forbes, S.A.1    Bindal, N.2    Bamford, S.3    Cole, C.4    Kok, C.Y.5
  • 63
    • 67349262466 scopus 로고    scopus 로고
    • Cancer driver mutations in protein kinase genes
    • Torkamani A, Verkhivker G, Schork NJ (2009) Cancer driver mutations in protein kinase genes. Cancer Lett 281: 117-127. doi:10.1016/j.canlet. 2008.11.008.
    • (2009) Cancer Lett , vol.281 , pp. 117-127
    • Torkamani, A.1    Verkhivker, G.2    Schork, N.J.3
  • 64
    • 84876911760 scopus 로고    scopus 로고
    • Distinct types of disorder in the human proteome: Functional implications for alternative splicing
    • Colak R, Kim T, Michaut M, Sun M, Irimia M, et al. (2013) Distinct Types of Disorder in the Human Proteome: Functional Implications for Alternative Splicing. PLoS Comput Biol 9: e1003030. doi:10.1371/journal.pcbi.1003030.
    • (2013) PLoS Comput Biol , vol.9 , pp. e1003030
    • Colak, R.1    Kim, T.2    Michaut, M.3    Sun, M.4    Irimia, M.5
  • 65
    • 0042121261 scopus 로고    scopus 로고
    • POPS: A fast algorithm for solvent accessible surface areas at atomic and residue level
    • Cavallo L, Kleinjung J, Fraternali F (2003) POPS: a fast algorithm for solvent accessible surface areas at atomic and residue level. Nucleic Acids Res 31: 3364-3366.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3364-3366
    • Cavallo, L.1    Kleinjung, J.2    Fraternali, F.3
  • 66
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: Interactive sequence similarity searching
    • Finn RD, Clements J, Eddy SR (2011) HMMER web server: interactive sequence similarity searching. Nucleic Acids Res 39: W29-W37. doi:10.1093/ nar/gkr367.
    • (2011) Nucleic Acids Res , vol.39 , pp. W29-W37
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 68
    • 84874724662 scopus 로고    scopus 로고
    • Update on activities at the Universal Protein Resource (UniProt) in 2013
    • The UniProt Consortium
    • The UniProt Consortium (2012) Update on activities at the Universal Protein Resource (UniProt) in 2013. Nucleic Acids Res 41: D43-D47. doi:10.1093/nar/ gks1068.
    • (2012) Nucleic Acids Res , vol.41 , pp. D43-D47
  • 69
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Accessed 10 July 2013
    • Sievers F, Wilm A, Dineen D, Gibson TJ, Karplus K, et al. (2011) Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol Syst Biol 7. Available: http://www.nature.com/msb/journal/v7/ n1/full/msb201175.html. Accessed 10 July 2013.
    • (2011) Mol Syst Biol , vol.7
    • Sievers, F.1    Wilm, A.2    Dineen, D.3    Gibson, T.J.4    Karplus, K.5
  • 71
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein structure and how it might fold
    • Taylor WR (2000) A deeply knotted protein structure and how it might fold. Nature 406: 916-919. doi:10.1038/35022623.
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 73
    • 80053915391 scopus 로고    scopus 로고
    • SCOWLP update: 3D classification of protein-protein, -peptide, -saccharide and -nucleic acid interactions, and structure-based binding inferences across folds
    • Teyra J, Samsonov SA, Schreiber S, Pisabarro MT (2011) SCOWLP update: 3D classification of protein-protein, -peptide, -saccharide and -nucleic acid interactions, and structure-based binding inferences across folds. BMC Bioinformatics 12: 398. doi:10.1186/1471-2105-12-398.
    • (2011) BMC Bioinformatics , vol.12 , pp. 398
    • Teyra, J.1    Samsonov, S.A.2    Schreiber, S.3    Pisabarro, M.T.4
  • 74
    • 0037186544 scopus 로고    scopus 로고
    • Stochastic gradient boosting
    • Friedman JH (2002) Stochastic gradient boosting. Comput Stat Data Anal 38: 367-378. doi:10.1016/S0167-9473(01)00065-2.
    • (2002) Comput Stat Data Anal , vol.38 , pp. 367-378
    • Friedman, J.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.