메뉴 건너뛰기




Volumn 10, Issue 1, 2013, Pages 47-53

Interactome3D: Adding structural details to protein networks

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARTICLE; AUTOMATION; CAENORHABDITIS ELEGANS; DROSOPHILA MELANOGASTER; ESCHERICHIA COLI; GENE MUTATION; HELICOBACTER PYLORI; HUMAN; MOLECULAR DOCKING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REFERENCE DATABASE; SACCHAROMYCES CEREVISIAE;

EID: 84871967106     PISSN: 15487091     EISSN: 15487105     Source Type: Journal    
DOI: 10.1038/nmeth.2289     Document Type: Article
Times cited : (376)

References (66)
  • 1
    • 84860851412 scopus 로고    scopus 로고
    • Sequential application of anticancer drugs enhances cell death by rewiring apoptotic signaling networks
    • Lee, M.J. et al. Sequential application of anticancer drugs enhances cell death by rewiring apoptotic signaling networks. Cell 149, 780-794 (2012).
    • (2012) Cell , vol.149 , pp. 780-794
    • Lee, M.J.1
  • 2
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection
    • Shapira, S.D. et al. A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection. Cell 139, 1255-1267 (2009).
    • (2009) Cell , vol.139 , pp. 1255-1267
    • Shapira, S.D.1
  • 3
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome-scale map of the human protein-protein interaction network
    • Rual, J.F. et al. Towards a proteome-scale map of the human protein-protein interaction network. Nature 437, 1173-1178 (2005).
    • (2005) Nature , vol.437 , pp. 1173-1178
    • Rual, J.F.1
  • 4
    • 25144498379 scopus 로고    scopus 로고
    • A human protein-protein interaction network: A resource for annotating the proteome
    • Stelzl, U. et al. A human protein-protein interaction network: A resource for annotating the proteome. Cell 122, 957-968 (2005).
    • (2005) Cell , vol.122 , pp. 957-968
    • Stelzl, U.1
  • 5
    • 33947219266 scopus 로고    scopus 로고
    • Large-scale mapping of human protein-protein interactions by mass spectrometry
    • Ewing, R.M. et al. Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol. Syst. Biol. 3, 89 (2007).
    • (2007) Mol. Syst. Biol. , vol.3 , pp. 89
    • Ewing, R.M.1
  • 6
    • 84863010950 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of protein networks provides insight into human genetic disease
    • Wang, X. et al. Three-dimensional reconstruction of protein networks provides insight into human genetic disease. Nat. Biotechnol. 30, 159-164 (2012).
    • (2012) Nat. Biotechnol. , vol.30 , pp. 159-164
    • Wang, X.1
  • 7
    • 84857790275 scopus 로고    scopus 로고
    • Protein-protein interaction sites are hot spots for disease-associated nonsynonymous SNPs
    • David, A., Razali, R., Wass, M.N. & Sternberg, M.J. Protein-protein interaction sites are hot spots for disease-associated nonsynonymous SNPs. Hum. Mutat. 33, 359-363 (2012).
    • (2012) Hum. Mutat. , vol.33 , pp. 359-363
    • David, A.1    Razali, R.2    Wass, M.N.3    Sternberg, M.J.4
  • 8
    • 70350721508 scopus 로고    scopus 로고
    • Edgetic' perturbation of a C elegans BCL2 ortholog
    • Dreze, M. et al. 'Edgetic' perturbation of a C. elegans BCL2 ortholog. Nat. Methods 6, 843-849 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 843-849
    • Dreze, M.1
  • 9
    • 33845875196 scopus 로고    scopus 로고
    • Relating three-dimensional structures to protein networks provides evolutionary insights
    • Kim, P.M., Lu, L.J., Xia, Y. & Gerstein, M.B. Relating three-dimensional structures to protein networks provides evolutionary insights. Science 314, 1938-1941 (2006).
    • (2006) Science , vol.314 , pp. 1938-1941
    • Kim, P.M.1    Lu, L.J.2    Xia, Y.3    Gerstein, M.B.4
  • 10
    • 0033954256 scopus 로고    scopus 로고
    • The protein data bank
    • Berman, H.M. et al. The Protein Data Bank. Nucleic Acids Res. 28, 235-242 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 11
    • 78651290702 scopus 로고    scopus 로고
    • ModBase, a database of annotated comparative protein structure models, and associated resources
    • Pieper, U. et al. ModBase, a database of annotated comparative protein structure models, and associated resources. Nucleic Acids Res. 39, D465-D474 (2011).
    • (2011) Nucleic Acids Res. , vol.39
    • Pieper, U.1
  • 12
    • 70349345898 scopus 로고    scopus 로고
    • Three-dimensional structural view of the central metabolic network of Thermotoga maritima
    • Zhang, Y. et al. Three-dimensional structural view of the central metabolic network of Thermotoga maritima. Science 325, 1544-1549 (2009).
    • (2009) Science , vol.325 , pp. 1544-1549
    • Zhang, Y.1
  • 13
    • 44649187518 scopus 로고    scopus 로고
    • Incorporating high-throughput proteomics experiments into structural biology pipelines: Identification of the low-hanging fruits
    • Pache, R.A. & Aloy, P. Incorporating high-throughput proteomics experiments into structural biology pipelines: Identification of the low-hanging fruits. Proteomics 8, 1959-1964 (2008).
    • (2008) Proteomics , vol.8 , pp. 1959-1964
    • Pache, R.A.1    Aloy, P.2
  • 14
    • 79953071469 scopus 로고    scopus 로고
    • Three-dimensional modeling of protein interactions and complexes is going 'omics
    • Stein, A., Mosca, R. & Aloy, P. Three-dimensional modeling of protein interactions and complexes is going 'omics. Curr. Opin. Struct. Biol. 21, 200-208 (2011).
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 200-208
    • Stein, A.1    Mosca, R.2    Aloy, P.3
  • 15
    • 0034614678 scopus 로고    scopus 로고
    • Protein interaction mapping in C. elegans using proteins involved in vulval development
    • Walhout, A.J. et al. Protein interaction mapping in C. elegans using proteins involved in vulval development. Science 287, 116-122 (2000).
    • (2000) Science , vol.287 , pp. 116-122
    • Walhout, A.J.1
  • 16
    • 0042386609 scopus 로고    scopus 로고
    • The relationship between sequence and interaction divergence in proteins
    • Aloy, P., Ceulemans, H., Stark, A. & Russell, R.B. The relationship between sequence and interaction divergence in proteins. J. Mol. Biol. 332, 989-998 (2003).
    • (2003) J. Mol. Biol. , vol.332 , pp. 989-998
    • Aloy, P.1    Ceulemans, H.2    Stark, A.3    Russell, R.B.4
  • 17
    • 12144290243 scopus 로고    scopus 로고
    • Structure-based assembly of protein complexes in yeast
    • Aloy, P. et al. Structure-based assembly of protein complexes in yeast. Science 303, 2026-2029 (2004).
    • (2004) Science , vol.303 , pp. 2026-2029
    • Aloy, P.1
  • 18
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: Modelling protein interactions
    • Aloy, P. & Russell, R.B. Structural systems biology: Modelling protein interactions. Nat. Rev. Mol. Cell Biol. 7, 188-197 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 19
    • 84862625522 scopus 로고    scopus 로고
    • Constructing structural networks of signaling pathways on the proteome scale
    • Kuzu, G., Keskin, O., Gursoy, A. & Nussinov, R. Constructing structural networks of signaling pathways on the proteome scale. Curr. Opin. Struct. Biol. 22, 367-377 (2012).
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 367-377
    • Kuzu, G.1    Keskin, O.2    Gursoy, A.3    Nussinov, R.4
  • 20
    • 84859204939 scopus 로고    scopus 로고
    • The IntAct molecular interaction database in 2012
    • Kerrien, S. et al. The IntAct molecular interaction database in 2012. Nucleic Acids Res. 40, D841-D846 (2012).
    • (2012) Nucleic Acids Res. , vol.40
    • Kerrien, S.1
  • 21
    • 84860918589 scopus 로고    scopus 로고
    • MINT, the molecular interaction database: 2012 update
    • Licata, L. et al. MINT, the molecular interaction database: 2012 update. Nucleic Acids Res. 40, D857-D861 (2012).
    • (2012) Nucleic Acids Res. , vol.40
    • Licata, L.1
  • 23
    • 78651344377 scopus 로고    scopus 로고
    • 3did: Identification and classification of domain-based interactions of known three-dimensional structure
    • Stein, A., Ceol, A. & Aloy, P. 3did: Identification and classification of domain-based interactions of known three-dimensional structure. Nucleic Acids Res. 39, D718-D723 (2011).
    • (2011) Nucleic Acids Res. , vol.39
    • Stein, A.1    Ceol, A.2    Aloy, P.3
  • 24
    • 18744382508 scopus 로고    scopus 로고
    • PIBASE: A comprehensive database of structurally defined protein interfaces
    • Davis, F.P. & Sali, A. PIBASE: A comprehensive database of structurally defined protein interfaces. Bioinformatics 21, 1901-1907 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 1901-1907
    • Davis, F.P.1    Sali, A.2
  • 25
    • 21144432882 scopus 로고    scopus 로고
    • PSIbase: A database of Protein Structural Interactome map (PSIMAP)
    • Gong, S. et al. PSIbase: A database of Protein Structural Interactome map (PSIMAP). Bioinformatics 21, 2541-2543 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 2541-2543
    • Gong, S.1
  • 26
    • 13844264506 scopus 로고    scopus 로고
    • IPfam: Visualization of protein-protein interactions in pdb at domain and amino acid resolutions
    • Finn, R.D., Marshall, M. & Bateman, A. iPfam: visualization of protein-protein interactions in PDB at domain and amino acid resolutions. Bioinformatics 21, 410-412 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 410-412
    • Finn, R.D.1    Marshall, M.2    Bateman, A.3
  • 27
    • 77957801217 scopus 로고    scopus 로고
    • Preferential use of protein domain pairs as interaction mediators: Order and transitivity
    • Itzhaki, Z., Akiva, E. & Margalit, H. Preferential use of protein domain pairs as interaction mediators: Order and transitivity. Bioinformatics 26, 2564-2570 (2010).
    • (2010) Bioinformatics , vol.26 , pp. 2564-2570
    • Itzhaki, Z.1    Akiva, E.2    Margalit, H.3
  • 28
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. & Blundell, T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 29
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein structure and how it might fold
    • Taylor, W.R. A deeply knotted protein structure and how it might fold. Nature 406, 916-919 (2000).
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 30
    • 58149305794 scopus 로고    scopus 로고
    • An empirical framework for binary interactome mapping
    • Venkatesan, K. et al. An empirical framework for binary interactome mapping. Nat. Methods 6, 83-90 (2009).
    • (2009) Nat. Methods , vol.6 , pp. 83-90
    • Venkatesan, K.1
  • 31
    • 70049112107 scopus 로고    scopus 로고
    • Pushing structural information into the yeast interactome by high-throughput protein docking experiments
    • Mosca, R., Pons, C., Fernandez-Recio, J. & Aloy, P. Pushing structural information into the yeast interactome by high-throughput protein docking experiments. PLoS Comput. Biol. 5, e1000490 (2009).
    • (2009) PLoS Comput. Biol. , vol.5
    • Mosca, R.1    Pons, C.2    Fernandez-Recio, J.3    Aloy, P.4
  • 32
    • 0038021436 scopus 로고    scopus 로고
    • Assessment of blind predictions of protein-protein interactions: Current status of docking methods
    • Méndez, R., Leplae, R., De Maria, L. & Wodak, S.J. Assessment of blind predictions of protein-protein interactions: Current status of docking methods. Proteins 52, 51-67 (2003).
    • (2003) Proteins , vol.52 , pp. 51-67
    • Méndez, R.1    Leplae, R.2    De Maria, L.3    Wodak, S.J.4
  • 33
    • 84858983547 scopus 로고    scopus 로고
    • KEGG for integration and interpretation of large-scale molecular data sets
    • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M. & Tanabe, M. KEGG for integration and interpretation of large-scale molecular data sets. Nucleic Acids Res. 40, D109-D114 (2012).
    • (2012) Nucleic Acids Res. , vol.40
    • Kanehisa, M.1    Goto, S.2    Sato, Y.3    Furumichi, M.4    Tanabe, M.5
  • 34
    • 58149177166 scopus 로고    scopus 로고
    • Reactome knowledgebase of human biological pathways and processes
    • Matthews, L. et al. Reactome knowledgebase of human biological pathways and processes. Nucleic Acids Res. 37, D619-D622 (2009).
    • (2009) Nucleic Acids Res. , vol.37
    • Matthews, L.1
  • 35
    • 33744931365 scopus 로고    scopus 로고
    • Target selection for complex structural genomics
    • Bravo, J. & Aloy, P. Target selection for complex structural genomics. Curr. Opin. Struct. Biol. 16, 385-392 (2006).
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 385-392
    • Bravo, J.1    Aloy, P.2
  • 36
    • 55949123477 scopus 로고    scopus 로고
    • Stability and structural recovery of the tetramerization domain of p53-R337H mutant induced by a designed templating ligand
    • Gordo, S. et al. Stability and structural recovery of the tetramerization domain of p53-R337H mutant induced by a designed templating ligand. Proc. Natl. Acad. Sci. USA 105, 16426-16431 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16426-16431
    • Gordo, S.1
  • 37
    • 72849142731 scopus 로고    scopus 로고
    • Edgetic perturbation models of human inherited disorders
    • Zhong, Q. et al. Edgetic perturbation models of human inherited disorders. Mol. Syst. Biol. 5, 321 (2009).
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 321
    • Zhong, Q.1
  • 38
    • 82155179340 scopus 로고    scopus 로고
    • Structural and functional protein network analyses predict novel signaling functions for rhodopsin
    • Kiel, C. et al. Structural and functional protein network analyses predict novel signaling functions for rhodopsin. Mol. Syst. Biol. 7, 551 (2011).
    • (2011) Mol. Syst. Biol. , vol.7 , Issue.551
    • Kiel, C.1
  • 39
    • 54249117223 scopus 로고    scopus 로고
    • Targeting and tinkering with interaction networks
    • Russell, R.B. & Aloy, P. Targeting and tinkering with interaction networks. Nat. Chem. Biol. 4, 666-673 (2008).
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 666-673
    • Russell, R.B.1    Aloy, P.2
  • 40
    • 77956548953 scopus 로고    scopus 로고
    • Cytoscape Web: An interactive web-based network browser
    • Lopes, C.T. et al. Cytoscape Web: An interactive web-based network browser. Bioinformatics 26, 2347-2348 (2010).
    • (2010) Bioinformatics , vol.26 , pp. 2347-2348
    • Lopes, C.T.1
  • 41
    • 84856497340 scopus 로고    scopus 로고
    • Putting the pieces together: Integrative modeling platform software for structure determination of macromolecular assemblies
    • Russel, D. et al. Putting the pieces together: Integrative modeling platform software for structure determination of macromolecular assemblies. PLoS Biol. 10, e1001244 (2012).
    • (2012) PLoS Biol. , vol.10
    • Russel, D.1
  • 42
    • 33749444763 scopus 로고    scopus 로고
    • VSIG4, a B7 family-related protein, is a negative regulator of T cell activation
    • Vogt, L. et al. VSIG4, a B7 family-related protein, is a negative regulator of T cell activation. J. Clin. Invest. 116, 2817-2826 (2006).
    • (2006) J. Clin. Invest. , vol.116 , pp. 2817-2826
    • Vogt, L.1
  • 43
    • 33750873601 scopus 로고    scopus 로고
    • Structure of C3b in complex with CRIg gives insights into regulation of complement activation
    • Wiesmann, C. et al. Structure of C3b in complex with CRIg gives insights into regulation of complement activation. Nature 444, 217-220 (2006).
    • (2006) Nature , vol.444 , pp. 217-220
    • Wiesmann, C.1
  • 44
    • 0347755535 scopus 로고    scopus 로고
    • The Database of Interacting Proteins: 2004 update
    • Salwinski, L. et al. The Database of Interacting Proteins: 2004 update. Nucleic Acids Res. 32, D449-D451 (2004).
    • (2004) Nucleic Acids Res. , vol.32
    • Salwinski, L.1
  • 45
    • 48249112175 scopus 로고    scopus 로고
    • MPIDB: The microbial protein interaction database
    • Goll, J. et al. MPIDB: The microbial protein interaction database. Bioinformatics 24, 1743-1744 (2008).
    • (2008) Bioinformatics , vol.24 , pp. 1743-1744
    • Goll, J.1
  • 47
    • 51049113607 scopus 로고    scopus 로고
    • InnateDB: Facilitating systems-level analyses of the mammalian innate immune response
    • Lynn, D.J. et al. InnateDB: Facilitating systems-level analyses of the mammalian innate immune response. Mol. Syst. Biol. 4, 218 (2008).
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 218
    • Lynn, D.J.1
  • 48
    • 78651328883 scopus 로고    scopus 로고
    • The biogrid interaction database: 2011 update
    • Stark, C. et al. The BioGRID Interaction Database: 2011 update. Nucleic Acids Res. 39, D698-D704 (2011).
    • (2011) Nucleic Acids Res. , vol.39
    • Stark, C.1
  • 49
    • 79955667824 scopus 로고    scopus 로고
    • The biomolecular interaction network database in psi-mi 2.5
    • (Oxford) 2011, baq037
    • Isserlin, R., El-Badrawi, R.A. & Bader, G.D. The Biomolecular Interaction Network Database in PSI-MI 2.5. Database (Oxford) 2011, baq037 (2011).
    • (2011) Database
    • Isserlin, R.1    El-Badrawi, R.A.2    Bader, G.D.3
  • 50
    • 58149193222 scopus 로고    scopus 로고
    • Human protein reference databasey2009 update
    • Keshava Prasad, T.S. et al. Human Protein Reference DatabaseY2009 update. Nucleic Acids Res. 37, D767-D772 (2009).
    • (2009) Nucleic Acids Res. , vol.37
    • Keshava Prasad, T.S.1
  • 51
    • 38449100072 scopus 로고    scopus 로고
    • The Protein Identifier Cross-Referencing (PICR) service: Reconciling protein identifiers across multiple source databases
    • Côté, R.G. et al. The Protein Identifier Cross-Referencing (PICR) service: Reconciling protein identifiers across multiple source databases. BMC Bioinformatics 8, 401 (2007).
    • (2007) BMC Bioinformatics , vol.8 , pp. 401
    • Côté, R.G.1
  • 52
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • UniProt Consortium.
    • UniProt Consortium. Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res. 40, D71-D75 (2012).
    • (2012) Nucleic Acids Res. , vol.40
  • 53
    • 84859208501 scopus 로고    scopus 로고
    • Protein interaction data curation: The international molecular exchange (imex) consortium
    • Orchard, S. et al. Protein interaction data curation: The International Molecular Exchange (IMEx) consortium. Nat. Methods 9, 345-350 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 345-350
    • Orchard, S.1
  • 54
    • 34249107988 scopus 로고    scopus 로고
    • The minimum information required for reporting a molecular interaction experiment MIMIx)
    • Orchard, S. et al. The minimum information required for reporting a molecular interaction experiment (MIMIx). Nat. Biotechnol. 25, 894-898 (2007).
    • (2007) Nat. Biotechnol. , vol.25 , pp. 894-898
    • Orchard, S.1
  • 55
    • 75549083295 scopus 로고    scopus 로고
    • MINT the molecular interaction database: 2009 update
    • Ceol, A. et al. MINT, the molecular interaction database: 2009 update. Nucleic Acids Res. 38, D532-D539 (2010).
    • (2010) Nucleic Acids Res. , vol.38
    • Ceol, A.1
  • 56
    • 66049143558 scopus 로고    scopus 로고
    • Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins
    • Hu, P. et al. Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7, e96 (2009).
    • (2009) PLoS Biol. , vol.7
    • Hu, P.1
  • 57
    • 13444288174 scopus 로고    scopus 로고
    • E-MSD: An integrated data resource for bioinformatics
    • Velankar, S. et al. E-MSD: An integrated data resource for bioinformatics. Nucleic Acids Res. 33, D262-D265 (2005).
    • (2005) Nucleic Acids Res. , vol.33
    • Velankar, S.1
  • 58
    • 0043123167 scopus 로고    scopus 로고
    • Tools for comparative protein structure modeling and analysis
    • Eswar, N. et al. Tools for comparative protein structure modeling and analysis. Nucleic Acids Res. 31, 3375-3380 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3375-3380
    • Eswar, N.1
  • 59
    • 0037250158 scopus 로고    scopus 로고
    • InterPreTS: Protein interaction prediction through tertiary structure
    • Aloy, P. & Russell, R.B. InterPreTS: Protein interaction prediction through tertiary structure. Bioinformatics 19, 161-162 (2003).
    • (2003) Bioinformatics , vol.19 , pp. 161-162
    • Aloy, P.1    Russell, R.B.2
  • 60
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen, M.Y. & Sali, A. Statistical potential for assessment and prediction of protein structures. Protein Sci. 15, 2507-2524 (2006).
    • (2006) Protein Sci. , vol.15 , pp. 2507-2524
    • Shen, M.Y.1    Sali, A.2
  • 61
    • 84858077472 scopus 로고    scopus 로고
    • The Pfam protein families database
    • Punta, M. et al. The Pfam protein families database. Nucleic Acids Res. 40, D290-D301 (2012).
    • (2012) Nucleic Acids Res. , vol.40
    • Punta, M.1
  • 62
    • 80055082271 scopus 로고    scopus 로고
    • Accelerated profile hmm searches
    • Eddy, S.R. Accelerated Profile HMM Searches. PLoS Comput. Biol. 7, e1002195 (2011).
    • (2011) PLoS Comput. Biol. , vol.7
    • Eddy, S.R.1
  • 63
    • 77955476975 scopus 로고    scopus 로고
    • Novel peptide-mediated interactions derived from high-resolution 3-dimensional structures
    • Stein, A. & Aloy, P. Novel peptide-mediated interactions derived from high-resolution 3-dimensional structures. PLoS Comput. Biol. 6, e1000789 (2010).
    • (2010) PLoS Comput. Biol. , vol.6
    • Stein, A.1    Aloy, P.2
  • 64
    • 35348976204 scopus 로고    scopus 로고
    • Broadening the horizonYlevel 2.5 of the HUPO-PSI format for molecular interactions
    • Kerrien, S. et al. Broadening the horizonYlevel 2.5 of the HUPO-PSI format for molecular interactions. BMC Biol. 5, 44 (2007).
    • (2007) BMC Biol. , vol.5 , pp. 44
    • Kerrien, S.1
  • 65
    • 0034060520 scopus 로고    scopus 로고
    • Protein domain interfaces: Characterization and comparison with oligomeric protein interfaces
    • Jones, S., Marin, A. & Thornton, J.M. Protein domain interfaces: Characterization and comparison with oligomeric protein interfaces. Protein Eng. 13, 77-82 (2000).
    • (2000) Protein Eng. , vol.13 , pp. 77-82
    • Jones, S.1    Marin, A.2    Thornton, J.M.3
  • 66
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller, S., Janin, J., Lesk, A.M. & Chothia, C. Interior and surface of monomeric proteins. J. Mol. Biol. 196, 641-656 (1987).
    • (1987) J. Mol. Biol. , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Chothia, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.