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Volumn 11, Issue 5, 2012, Pages 2982-2995

Characterization of domain-peptide interaction interface: Prediction of SH3 domain-mediated protein-protein interaction network in yeast by generic structure-based models

Author keywords

binding interface; MM GBSA; molecular dynamics; molecular interaction energy component (MIEC); protein recognition code; support vector machine (SVM)

Indexed keywords

PROTEIN SH3; PROTEOME;

EID: 84860635411     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr3000688     Document Type: Article
Times cited : (199)

References (71)
  • 1
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T.; Nash, P. Assembly of cell regulatory systems through protein interaction domains Science 2003, 300 (5618) 445-452
    • (2003) Science , vol.300 , Issue.5618 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 2
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: Complexity in moderation
    • Mayer, B. J. SH3 domains: complexity in moderation J. Cell Sci. 2001, 114 (7) 1253-1263
    • (2001) J. Cell Sci. , vol.114 , Issue.7 , pp. 1253-1263
    • Mayer, B.J.1
  • 3
    • 0026749753 scopus 로고
    • Sh3 - An abundant protein domain in search of a function
    • Musacchio, A.; Gibson, T.; Lehto, V. P.; Saraste, M. Sh3-an abundant protein domain in search of a function Febs Lett. 1992, 307 (1) 55-61
    • (1992) Febs Lett. , vol.307 , Issue.1 , pp. 55-61
    • Musacchio, A.1    Gibson, T.2    Lehto, V.P.3    Saraste, M.4
  • 4
    • 0027102571 scopus 로고
    • Solution structure of the Sh3 domain of Src and identification of its ligand-binding site
    • Yu, H. T.; Rosen, M. K.; Shin, T. B.; Seideldugan, C.; Brugge, J. S.; Schreiber, S. L. Solution structure of the Sh3 domain of Src and identification of its ligand-binding site Science 1992, 258 (5088) 1665-1668
    • (1992) Science , vol.258 , Issue.5088 , pp. 1665-1668
    • Yu, H.T.1    Rosen, M.K.2    Shin, T.B.3    Seideldugan, C.4    Brugge, J.S.5    Schreiber, S.L.6
  • 5
    • 0028485085 scopus 로고
    • High-resolution crystal-structures of tyrosine kinase Sh3 domains complexed with proline-rich peptides
    • Musacchio, A.; Saraste, M.; Wilmanns, M. High-resolution crystal-structures of tyrosine kinase Sh3 domains complexed with proline-rich peptides Nat. Struct. Biol. 1994, 1 (8) 546-551
    • (1994) Nat. Struct. Biol. , vol.1 , Issue.8 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 6
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in Sh3 domains
    • Lim, W. A.; Richards, F. M.; Fox, R. O. Structural determinants of peptide-binding orientation and of sequence specificity in Sh3 domains Nature 1994, 372 (6504) 375-379
    • (1994) Nature , vol.372 , Issue.6504 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 7
    • 0032541641 scopus 로고    scopus 로고
    • From Src Homology domains to other signaling modules: Proposal of the protein recognition code
    • Sudol, M. From Src Homology domains to other signaling modules: proposal of the protein recognition code Oncogene 1998, 17 (11) 1469-1474
    • (1998) Oncogene , vol.17 , Issue.11 , pp. 1469-1474
    • Sudol, M.1
  • 8
    • 0027962645 scopus 로고
    • 2 Binding orientations for peptides to the Src Sh3 domain - Development of a general-model for Sh3-ligand interactions
    • Feng, S. B.; Chen, J. K.; Yu, H. T.; Simon, J. A.; Schreiber, S. L. 2 Binding orientations for peptides to the Src Sh3 domain-development of a general-model for Sh3-ligand interactions Science 1994, 266 (5188) 1241-1247
    • (1994) Science , vol.266 , Issue.5188 , pp. 1241-1247
    • Feng, S.B.1    Chen, J.K.2    Yu, H.T.3    Simon, J.A.4    Schreiber, S.L.5
  • 9
    • 0029959928 scopus 로고    scopus 로고
    • Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLC gamma, Crk, and Grb2
    • Sparks, A. B.; Rider, J. E.; Hoffman, N. G.; Fowlkes, D. M.; Quilliam, L. A.; Kay, B. K. Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLC gamma, Crk, and Grb2 Proc. Natl. Acad. Sci. U.S.A. 1996, 93 (4) 1540-1544
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , Issue.4 , pp. 1540-1544
    • Sparks, A.B.1    Rider, J.E.2    Hoffman, N.G.3    Fowlkes, D.M.4    Quilliam, L.A.5    Kay, B.K.6
  • 11
  • 12
    • 0027971687 scopus 로고
    • Identification of Src, Fyn, Lyn, Pi3k and Abl Sh3 domain ligands using phage display libraries
    • Rickles, R. J.; Botfield, M. C.; Weng, Z. G.; Taylor, J. A.; Green, O. M.; Brugge, J. S.; Zoller, M. J. Identification of Src, Fyn, Lyn, Pi3k and Abl Sh3 domain ligands using phage display libraries EMBO J. 1994, 13 (23) 5598-5604
    • (1994) EMBO J. , vol.13 , Issue.23 , pp. 5598-5604
    • Rickles, R.J.1    Botfield, M.C.2    Weng, Z.G.3    Taylor, J.A.4    Green, O.M.5    Brugge, J.S.6    Zoller, M.J.7
  • 14
    • 0034724569 scopus 로고    scopus 로고
    • SH3-SPOT: An algorithm to predict preferred ligands to different members of the SH3 gene family
    • Brannetti, B.; Via, A.; Cestra, G.; Cesareni, G.; Citterich, M. H. SH3-SPOT: An algorithm to predict preferred ligands to different members of the SH3 gene family J. Mol. Biol. 2000, 298 (2) 313-328
    • (2000) J. Mol. Biol. , vol.298 , Issue.2 , pp. 313-328
    • Brannetti, B.1    Via, A.2    Cestra, G.3    Cesareni, G.4    Citterich, M.H.5
  • 15
    • 33750030012 scopus 로고    scopus 로고
    • A novel structure-based encoding for machine-learning applied to the inference of SH3 domain specificity
    • Ferraro, E.; Via, A.; Ausiello, G.; Helmer-Citterich, M. A novel structure-based encoding for machine-learning applied to the inference of SH3 domain specificity Bioinformatics 2006, 22 (19) 2333-2339
    • (2006) Bioinformatics , vol.22 , Issue.19 , pp. 2333-2339
    • Ferraro, E.1    Via, A.2    Ausiello, G.3    Helmer-Citterich, M.4
  • 16
    • 33644870557 scopus 로고    scopus 로고
    • A regularized discriminative model for the prediction of protein-peptide interactions
    • Lehrach, W. P.; Husmeier, D.; Williams, C. K. I. A regularized discriminative model for the prediction of protein-peptide interactions Bioinformatics 2006, 22 (5) 532-540
    • (2006) Bioinformatics , vol.22 , Issue.5 , pp. 532-540
    • Lehrach, W.P.1    Husmeier, D.2    Williams, C.K.I.3
  • 17
    • 33644828578 scopus 로고    scopus 로고
    • Prediction of binding sites of peptide recognition domains: An application on Grb2 and SAP SH2 domains
    • McLaughlin, W. A.; Hou, T. J.; Wang, W. Prediction of binding sites of peptide recognition domains: An application on Grb2 and SAP SH2 domains J. Mol. Biol. 2006, 357 (4) 1322-1334
    • (2006) J. Mol. Biol. , vol.357 , Issue.4 , pp. 1322-1334
    • McLaughlin, W.A.1    Hou, T.J.2    Wang, W.3
  • 18
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • Obenauer, J. C.; Cantley, L. C.; Yaffe, M. B. Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs Nucleic Acids Res. 2003, 31 (13) 3635-3641
    • (2003) Nucleic Acids Res. , vol.31 , Issue.13 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 19
    • 39049111013 scopus 로고    scopus 로고
    • Characterization of domain-peptide interaction interface: A case study on the amphiphysin-1 SH3 domain
    • Hou, T. J.; Zhang, W.; Case, D. A.; Wang, W. Characterization of domain-peptide interaction interface: A case study on the amphiphysin-1 SH3 domain J. Mol. Biol. 2008, 376 (4) 1201-1214
    • (2008) J. Mol. Biol. , vol.376 , Issue.4 , pp. 1201-1214
    • Hou, T.J.1    Zhang, W.2    Case, D.A.3    Wang, W.4
  • 20
    • 66149146342 scopus 로고    scopus 로고
    • Characterization of domain-peptide interaction interface: A generic structure-based model to decipher the binding specificity of SH3 domains
    • Hou, T. J.; Xu, Z.; Zhang, W.; McLaughlin, W. A.; Case, D. A.; Xu, Y.; Wang, W. Characterization of domain-peptide interaction interface: a generic structure-based model to decipher the binding specificity of SH3 domains Mol. Cell. Proteomics 2009, 8 (4) 639-649
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.4 , pp. 639-649
    • Hou, T.J.1    Xu, Z.2    Zhang, W.3    McLaughlin, W.A.4    Case, D.A.5    Xu, Y.6    Wang, W.7
  • 21
    • 33645776269 scopus 로고    scopus 로고
    • Computational analysis and prediction of the binding motif and protein interacting partners of the Abl SH3 domain
    • Hou, T. J.; Chen, K.; McLaughlin, W. A.; Lu, B. Z.; Wang, W. Computational analysis and prediction of the binding motif and protein interacting partners of the Abl SH3 domain PLoS Comput. Biol. 2006, 2 (1) 46-55
    • (2006) PLoS Comput. Biol. , vol.2 , Issue.1 , pp. 46-55
    • Hou, T.J.1    Chen, K.2    McLaughlin, W.A.3    Lu, B.Z.4    Wang, W.5
  • 22
    • 33746285302 scopus 로고    scopus 로고
    • An integrated machine learning system to computationally screen protein databases for protein binding peptide ligands
    • Zhang, L.; Shao, C.; Zheng, D. X.; Gao, Y. H. An integrated machine learning system to computationally screen protein databases for protein binding peptide ligands Mol. Cell. Proteomics 2006, 5 (7) 1224-1232
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.7 , pp. 1224-1232
    • Zhang, L.1    Shao, C.2    Zheng, D.X.3    Gao, Y.H.4
  • 23
    • 69049083531 scopus 로고    scopus 로고
    • Using genome-wide measurements for computational prediction of SH2-peptide interactions
    • Wunderlich, Z.; Mirny, L. A. Using genome-wide measurements for computational prediction of SH2-peptide interactions Nucleic Acids Res. 2009, 37 (14) 4629-41
    • (2009) Nucleic Acids Res. , vol.37 , Issue.14 , pp. 4629-4641
    • Wunderlich, Z.1    Mirny, L.A.2
  • 24
    • 84862908730 scopus 로고    scopus 로고
    • Proteome-wide detection of Abl1 SH3 binding peptides by integrating computational prediction and peptide microarray
    • Xu, Z.; Hou, T. J.; Li, N.; Xu, Y.; Wang, W. Proteome-wide detection of Abl1 SH3 binding peptides by integrating computational prediction and peptide microarray Mol. Cell. Proteomics 2012, 11 (1) O111.010389
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.1 , pp. 111010389
    • Xu, Z.1    Hou, T.J.2    Li, N.3    Xu, Y.4    Wang, W.5
  • 27
    • 0033527653 scopus 로고    scopus 로고
    • The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity
    • Cestra, G.; Castagnoli, L.; Dente, L.; Minenkova, O.; Petrelli, A.; Migone, N.; Hoffmuller, U.; Schneider-Mergener, J.; Cesareni, G. The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity J. Biol. Chem. 1999, 274 (45) 32001-32007
    • (1999) J. Biol. Chem. , vol.274 , Issue.45 , pp. 32001-32007
    • Cestra, G.1    Castagnoli, L.2    Dente, L.3    Minenkova, O.4    Petrelli, A.5    Migone, N.6    Hoffmuller, U.7    Schneider-Mergener, J.8    Cesareni, G.9
  • 28
    • 0032555743 scopus 로고    scopus 로고
    • Crystal structure of the Abl-SH3 domain complexed with a designed high-affinity peptide ligand: Implications for SH3-ligand interactions
    • Pisabarro, M. T.; Serrano, L.; Wilmanns, M. Crystal structure of the Abl-SH3 domain complexed with a designed high-affinity peptide ligand: Implications for SH3-ligand interactions J. Mol. Biol. 1998, 281 (3) 513-521
    • (1998) J. Mol. Biol. , vol.281 , Issue.3 , pp. 513-521
    • Pisabarro, M.T.1    Serrano, L.2    Wilmanns, M.3
  • 29
    • 0029589911 scopus 로고
    • Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
    • Feng, S. B.; Kasahara, C.; Rickles, R. J.; Schreiber, S. L. Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands Proc. Natl. Acad. Sci. U.S.A. 1995, 92 (26) 12408-12415
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.26 , pp. 12408-12415
    • Feng, S.B.1    Kasahara, C.2    Rickles, R.J.3    Schreiber, S.L.4
  • 30
    • 33846019560 scopus 로고    scopus 로고
    • Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes
    • Schmidt, H.; Hoffmann, S.; Tran, T.; Stoldt, M.; Stangler, T.; Wiesehan, K.; Willbold, D. Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes J. Mol. Biol. 2007, 365 (5) 1517-1532
    • (2007) J. Mol. Biol. , vol.365 , Issue.5 , pp. 1517-1532
    • Schmidt, H.1    Hoffmann, S.2    Tran, T.3    Stoldt, M.4    Stangler, T.5    Wiesehan, K.6    Willbold, D.7
  • 32
    • 0031564611 scopus 로고    scopus 로고
    • Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: Direct refinement against NOEs, J-couplings and H-1 and C-13 chemical shifts
    • Wittekind, M.; Mapelli, C.; Lee, V.; Goldfarb, V.; Friedrichs, M. S.; Meyers, C. A.; Mueller, L. Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: Direct refinement against NOEs, J-couplings and H-1 and C-13 chemical shifts J. Mol. Biol. 1997, 267 (4) 933-952
    • (1997) J. Mol. Biol. , vol.267 , Issue.4 , pp. 933-952
    • Wittekind, M.1    Mapelli, C.2    Lee, V.3    Goldfarb, V.4    Friedrichs, M.S.5    Meyers, C.A.6    Mueller, L.7
  • 34
    • 0031029781 scopus 로고    scopus 로고
    • Regulatory intramolecular association in a tyrosine kinase of the Tec family
    • Andreotti, A. H.; Bunnell, S. C.; Feng, S.; Berg, L. J.; Schreiber, S. L. Regulatory intramolecular association in a tyrosine kinase of the Tec family Nature 1997, 385 (6611) 93-97
    • (1997) Nature , vol.385 , Issue.6611 , pp. 93-97
    • Andreotti, A.H.1    Bunnell, S.C.2    Feng, S.3    Berg, L.J.4    Schreiber, S.L.5
  • 35
    • 25844525760 scopus 로고    scopus 로고
    • Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity
    • Bauer, F.; Schweimer, K.; Meiselbach, H.; Hoffmann, S.; Rosch, P.; Sticht, H. Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity Protein Sci. 2005, 14 (10) 2487-2498
    • (2005) Protein Sci. , vol.14 , Issue.10 , pp. 2487-2498
    • Bauer, F.1    Schweimer, K.2    Meiselbach, H.3    Hoffmann, S.4    Rosch, P.5    Sticht, H.6
  • 39
    • 0029980671 scopus 로고    scopus 로고
    • Crystal structure of PI3K SH3 domain at 2.0 angstrom resolution
    • Liang, J.; Chen, J. K.; Schreiber, S. L.; Clardy, J. Crystal structure of PI3K SH3 domain at 2.0 angstrom resolution J. Mol. Biol. 1996, 257 (3) 632-643
    • (1996) J. Mol. Biol. , vol.257 , Issue.3 , pp. 632-643
    • Liang, J.1    Chen, J.K.2    Schreiber, S.L.3    Clardy, J.4
  • 40
    • 34548564106 scopus 로고    scopus 로고
    • Structural basis for ubiquitin recognition by SH3 domains
    • He, Y.; Hicke, L.; Radhakrishnan, I. Structural basis for ubiquitin recognition by SH3 domains J. Mol. Biol. 2007, 373 (1) 190-196
    • (2007) J. Mol. Biol. , vol.373 , Issue.1 , pp. 190-196
    • He, Y.1    Hicke, L.2    Radhakrishnan, I.3
  • 41
    • 34247144140 scopus 로고    scopus 로고
    • Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: Loop flexibility and amyloid aggregation
    • Martin-Garcia, J. M.; Luque, I.; Mateo, P. L.; Ruiz-Sanz, J.; Camara-Artigas, A. Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: Loop flexibility and amyloid aggregation Febs Lett. 2007, 581 (9) 1701-1706
    • (2007) Febs Lett. , vol.581 , Issue.9 , pp. 1701-1706
    • Martin-Garcia, J.M.1    Luque, I.2    Mateo, P.L.3    Ruiz-Sanz, J.4    Camara-Artigas, A.5
  • 44
    • 84860626102 scopus 로고    scopus 로고
    • Accelrys Inc. San Diego
    • Discovery Studio 2.5 Guide; Accelrys Inc.: San Diego, 2009; http://www.accelrys.com.
    • (2009) Discovery Studio 2.5 Guide
  • 46
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • Eisenberg, D.; Luthy, R.; Bowie, J. U. VERIFY3D: Assessment of protein models with three-dimensional profiles Macromol. Crystallogr., Part B 1997, 277, 396-404
    • (1997) Macromol. Crystallogr., Part B , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 47
    • 0035838974 scopus 로고    scopus 로고
    • Extending the accuracy limits of prediction for side-chain conformations
    • Xiang, Z. X.; Honig, B. Extending the accuracy limits of prediction for side-chain conformations J. Mol. Biol. 2001, 311 (2) 421-430
    • (2001) J. Mol. Biol. , vol.311 , Issue.2 , pp. 421-430
    • Xiang, Z.X.1    Honig, B.2
  • 50
    • 33846823909 scopus 로고
    • Particle Mesh Ewald - An N.Log(N) method for Ewald sums in large systems
    • Darden, T.; York, D.; Pedersen, L. Particle Mesh Ewald-an N.Log(N) method for Ewald sums in large systems J. Chem. Phys. 1993, 98 (12) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , Issue.12 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 51
    • 33646940952 scopus 로고
    • Numerical-integration of cartesian equations of motion of a system with constraints - Molecular-dynamics of N-alkanes
    • Ryckaert, J. P.; Ciccotti, G.; Berendsen, H. J. C. Numerical-integration of cartesian equations of motion of a system with constraints-molecular-dynamics of N-alkanes J. Comput. Phys. 1977, 23 (3) 327-341
    • (1977) J. Comput. Phys. , vol.23 , Issue.3 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 52
    • 0029643950 scopus 로고
    • Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal Sh3 domain of C-Crk
    • Wu, X. D.; Knudsen, B.; Feller, S. M.; Zheng, J.; Sali, A.; Cowburn, D.; Hanafusa, H.; Kuriyan, J. Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal Sh3 domain of C-Crk Structure 1995, 3 (2) 215-226
    • (1995) Structure , vol.3 , Issue.2 , pp. 215-226
    • Wu, X.D.1    Knudsen, B.2    Feller, S.M.3    Zheng, J.4    Sali, A.5    Cowburn, D.6    Hanafusa, H.7    Kuriyan, J.8
  • 53
    • 23944483930 scopus 로고    scopus 로고
    • Structural basis for recognition of the T cell adaptor protein SLP-76 by the SH3 domain of phospholipase C gamma 1
    • Deng, L.; Velikovsky, C. A.; Swaminathan, C. P.; Cho, S. W.; Mariuzza, R. A. Structural basis for recognition of the T cell adaptor protein SLP-76 by the SH3 domain of phospholipase C gamma 1 J. Mol. Biol. 2005, 352 (1) 1-10
    • (2005) J. Mol. Biol. , vol.352 , Issue.1 , pp. 1-10
    • Deng, L.1    Velikovsky, C.A.2    Swaminathan, C.P.3    Cho, S.W.4    Mariuzza, R.A.5
  • 55
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina, S.; Pavletich, N. P. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2 Science 1996, 274 (5289) 1001-1005
    • (1996) Science , vol.274 , Issue.5289 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 57
    • 30744471940 scopus 로고    scopus 로고
    • Prediction of binding affinities between the human amphiphysin-1 SH3 domain and its peptide ligands using homology modeling, molecular dynamics and molecular field analysis
    • Hou, T. J.; McLaughlin, W.; Lu, B.; Chen, K.; Wang, W. Prediction of binding affinities between the human amphiphysin-1 SH3 domain and its peptide ligands using homology modeling, molecular dynamics and molecular field analysis J. Proteome Res. 2006, 5 (1) 32-43
    • (2006) J. Proteome Res. , vol.5 , Issue.1 , pp. 32-43
    • Hou, T.J.1    McLaughlin, W.2    Lu, B.3    Chen, K.4    Wang, W.5
  • 59
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • Onufriev, A.; Bashford, D.; Case, D. A. Exploring protein native states and large-scale conformational changes with a modified generalized born model Proteins-Struct. Function Bioinform. 2004, 55 (2) 383-394
    • (2004) Proteins-Struct. Function Bioinform. , vol.55 , Issue.2 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3
  • 60
    • 0043245780 scopus 로고    scopus 로고
    • Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RaIGDS complexes
    • Gohlke, H.; Kiel, C.; Case, D. A. Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RaIGDS complexes J. Mol. Biol. 2003, 330 (4) 891-913
    • (2003) J. Mol. Biol. , vol.330 , Issue.4 , pp. 891-913
    • Gohlke, H.1    Kiel, C.2    Case, D.A.3
  • 61
    • 61449101624 scopus 로고    scopus 로고
    • Predicting drug resistance of the HIV-1 protease using molecular interaction energy components
    • Hou, T. J.; Zhang, W.; Wang, J.; Wang, W. Predicting drug resistance of the HIV-1 protease using molecular interaction energy components Proteins-Struct. Function Bioinform. 2009, 74 (4) 837-846
    • (2009) Proteins-Struct. Function Bioinform. , vol.74 , Issue.4 , pp. 837-846
    • Hou, T.J.1    Zhang, W.2    Wang, J.3    Wang, W.4
  • 62
    • 79951996670 scopus 로고    scopus 로고
    • Assessing the performance of the molecular mechanics/Poisson Boltzmann surface area and molecular mechanics/generalized Born surface area methods. II. The accuracy of ranking poses generated from docking
    • Hou, T. J.; Wang, J.; Li, Y. Y.; Wang, W. Assessing the performance of the molecular mechanics/Poisson Boltzmann surface area and molecular mechanics/generalized Born surface area methods. II. The accuracy of ranking poses generated from docking J. Comput. Chem. 2011, 32 (5) 866-877
    • (2011) J. Comput. Chem. , vol.32 , Issue.5 , pp. 866-877
    • Hou, T.J.1    Wang, J.2    Li, Y.Y.3    Wang, W.4
  • 63
    • 79952588669 scopus 로고    scopus 로고
    • Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations
    • Hou, T. J.; Wang, J.; Li, Y. Y.; Wang, W. Assessing the performance of the MM/PBSA and MM/GBSA methods. 1. The accuracy of binding free energy calculations based on molecular dynamics simulations J. Chem. Inf. Model. 2011, 51 (1) 69-82
    • (2011) J. Chem. Inf. Model. , vol.51 , Issue.1 , pp. 69-82
    • Hou, T.J.1    Wang, J.2    Li, Y.Y.3    Wang, W.4
  • 64
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser, J.; Shenkin, P. S.; Still, W. C. Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO) J. Comput. Chem. 1999, 20 (2) 217-230
    • (1999) J. Comput. Chem. , vol.20 , Issue.2 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 66
    • 34848824629 scopus 로고    scopus 로고
    • Applications of support vector machines in chemistry
    • Lipkowitz, K. B. Cundari, T. R. Boyd, D. B. VCH: New York
    • Ivanciuc, O. Applications of support vector machines in chemistry. In Reviews in Computational Chemistry; Lipkowitz, K. B.; Cundari, T. R.; Boyd, D. B., Eds.; VCH: New York, 2007; Vol. 23, pp 291-400.
    • (2007) Reviews in Computational Chemistry , vol.23 , pp. 291-400
    • Ivanciuc, O.1
  • 67
    • 29144499905 scopus 로고    scopus 로고
    • Working set selection using the second order information for training SVM
    • Fan, R. E.; Chen, P. H.; Lin, C. J. Working set selection using the second order information for training SVM J. Machine Learning Res. 2005, 6, 1889-1918
    • (2005) J. Machine Learning Res. , vol.6 , pp. 1889-1918
    • Fan, R.E.1    Chen, P.H.2    Lin, C.J.3
  • 69
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D.; Gibson, T. J.; Plewniak, F.; Jeanmougin, F.; Higgins, D. G. The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 1997, 25 (24) 4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 71
    • 0037264280 scopus 로고    scopus 로고
    • Osprey: A network visualization system
    • Breitkreutz, B. J.; Stark, C.; Tyers, M. Osprey: a network visualization system Genome Biol. 2003, 4 (3) R22
    • (2003) Genome Biol. , vol.4 , Issue.3 , pp. 22
    • Breitkreutz, B.J.1    Stark, C.2    Tyers, M.3


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