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Volumn 45, Issue W1, 2017, Pages W337-W343

Proteins Plus: A web portal for structure analysis of macromolecules

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; AUTOMATIC POCKET DETECTION; AUTOMATION; BINDING SITE; CLASSIFICATION; COMPUTER INTERFACE; DOGSITESCORER; EDIA; GENERALIZED WORKFLOW; HYPPI; MACHINE LEARNING; MACROMOLECULE; MOLECULAR MODEL; ONLINE SYSTEM; POSEVIEW; PRIORITY JOURNAL; PROCESS DESIGN; PROCESS OPTIMIZATION; PROTEIN DATABASE; PROTEIN PROTEIN INTERACTION; PROTOSS; QUALITY CONTROL; SOFTWARE; STRUCTURE ANALYSIS; STRUCTURE BASED MOLECULAR MODELING; WEB PORTAL; WORKFLOW; CHEMISTRY; INTERNET; PROTEIN ANALYSIS; PROTEIN CONFORMATION;

EID: 85023176527     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkx333     Document Type: Article
Times cited : (177)

References (63)
  • 1
    • 0345059376 scopus 로고    scopus 로고
    • Announcing the worldwide Protein Data Bank
    • Berman, H., Henrick, K., and Nakamura, H. (2003) Announcing the worldwide Protein Data Bank. Nat. Struct. Biol., 10, 980-980.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 980
    • Berman, H.1    Henrick, K.2    Nakamura, H.3
  • 6
    • 33747872588 scopus 로고    scopus 로고
    • Molecular complexes at a glance: Automated generation of two-dimensional complex diagrams
    • Stierand, K., Maab, P.C., and Rarey, M. (2006) Molecular complexes at a glance: automated generation of two-dimensional complex diagrams. Bioinformatics, 22, 1710-1716.
    • (2006) Bioinformatics , vol.22 , pp. 1710-1716
    • Stierand, K.1    Maab, P.C.2    Rarey, M.3
  • 7
    • 84865132980 scopus 로고    scopus 로고
    • DoGSiteScorer: A web-server for automatic binding site prediction, analysis, and druggability assessment
    • Volkamer, A., Kuhn, D., Rippmann, F., and Rarey, M. (2012) DoGSiteScorer: a web-server for automatic binding site prediction, analysis, and druggability assessment. Bioinformatics, 28, 2074-2075.
    • (2012) Bioinformatics , vol.28 , pp. 2074-2075
    • Volkamer, A.1    Kuhn, D.2    Rippmann, F.3    Rarey, M.4
  • 8
    • 84979865146 scopus 로고    scopus 로고
    • NGL Viewer: A web application for molecular visualization
    • Rose, A.S., and Hildebrand, P.W. (2015) NGL Viewer: a web application for molecular visualization. Nucleic Acids Res., 43, W576-W579.
    • (2015) Nucleic Acids Res. , vol.43 , pp. W576-W579
    • Rose, A.S.1    Hildebrand, P.W.2
  • 9
    • 0023965741 scopus 로고
    • SMILES, a chemical language and information system. 1. Introduction to methodology and encoding rules
    • Weininger, D. (1988) SMILES, a chemical language and information system. 1. introduction to methodology and encoding rules. J. Chem. Inf. Comput. Sci., 28, 31-36.
    • (1988) J. Chem. Inf. Comput. Sci. , vol.28 , pp. 31-36
    • Weininger, D.1
  • 10
    • 0345171487 scopus 로고    scopus 로고
    • Crystal structures of an archaeal class i CCA-Adding enzyme and its nucleotide complexes
    • Xiong, Y., Li, F., Wang, J., Weiner, A.M., and Steitz, T.A. (2003) Crystal structures of an archaeal class I CCA-Adding enzyme and its nucleotide complexes. Mol. Cell, 12, 1165-1172.
    • (2003) Mol. Cell , vol.12 , pp. 1165-1172
    • Xiong, Y.1    Li, F.2    Wang, J.3    Weiner, A.M.4    Steitz, T.A.5
  • 11
    • 0024250301 scopus 로고
    • Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison
    • Brunger, A.T., and Karplus, M. (1988) Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. Proteins, 4, 148-156.
    • (1988) Proteins , vol.4 , pp. 148-156
    • Brunger, A.T.1    Karplus, M.2
  • 12
    • 0026520305 scopus 로고
    • A method for determining the positions of polar hydrogens added to a protein structure that maximizes protein hydrogen bonding
    • Bass, M.B., Hopkins, D.F., Jaquysh, W. A.N., and Ornstein, R.L. (1992) A method for determining the positions of polar hydrogens added to a protein structure that maximizes protein hydrogen bonding. Proteins, 12, 266-277.
    • (1992) Proteins , vol.12 , pp. 266-277
    • Bass, M.B.1    Hopkins, D.F.2    Jaquysh, W.A.N.3    Ornstein, R.L.4
  • 13
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I.K., and Thornton, J.M. (1994) Satisfying hydrogen bonding potential in proteins. J. Mol. Biol., 238, 777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 14
    • 0029017638 scopus 로고
    • The application of hydrogen bonding analysis in X-ray crystallography to help orientate asparagine, glutamine and histidine side chains
    • McDonald, I.K., and Thornton, J.M. (1995) The application of hydrogen bonding analysis in X-ray crystallography to help orientate asparagine, glutamine and histidine side chains. Protein Eng., 8, 217-224.
    • (1995) Protein Eng. , vol.8 , pp. 217-224
    • McDonald, I.K.1    Thornton, J.M.2
  • 15
    • 0030442990 scopus 로고    scopus 로고
    • Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures
    • Hooft, R.W., Sander, C., and Vriend, G. (1996) Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures. Proteins, 26, 363-376.
    • (1996) Proteins , vol.26 , pp. 363-376
    • Hooft, R.W.1    Sander, C.2    Vriend, G.3
  • 16
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word, J.M., Lovell, S.C., Richardson, J.S., and Richardson, D.C. (1999) Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol., 285, 1735-1747.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 17
    • 33847034125 scopus 로고    scopus 로고
    • Assignment of polar states for protein amino acid residues using an interaction cluster decomposition algorithm and its application to high resolution protein structure modeling
    • Li, X., Jacobson, M.P., Zhu, K., Zhao, S., and Friesner, R.A. (2007) Assignment of polar states for protein amino acid residues using an interaction cluster decomposition algorithm and its application to high resolution protein structure modeling. Proteins, 66, 824-837.
    • (2007) Proteins , vol.66 , pp. 824-837
    • Li, X.1    Jacobson, M.P.2    Zhu, K.3    Zhao, S.4    Friesner, R.A.5
  • 18
    • 69249222839 scopus 로고    scopus 로고
    • Web application for studying the free energy of binding and protonation states of protein-ligand complexes based on HINT
    • Bayden, A.S., Fornabaio, M., Scarsdale, J.N., and Kellogg, G.E. (2009) Web application for studying the free energy of binding and protonation states of protein-ligand complexes based on HINT. J. Comput. Aided Mol. Des., 23, 621-632.
    • (2009) J. Comput. Aided Mol. Des. , vol.23 , pp. 621-632
    • Bayden, A.S.1    Fornabaio, M.2    Scarsdale, J.N.3    Kellogg, G.E.4
  • 19
    • 65249157397 scopus 로고    scopus 로고
    • Protonate3D: Assignment of ionization states and hydrogen coordinates to macromolecular structures
    • Labute, P. (2009) Protonate3D: assignment of ionization states and hydrogen coordinates to macromolecular structures. Proteins, 75, 187-205.
    • (2009) Proteins , vol.75 , pp. 187-205
    • Labute, P.1
  • 20
    • 84855945977 scopus 로고    scopus 로고
    • Assignment of protonation states in proteins and ligands: Combining pKa prediction with hydrogen bonding network optimization
    • Baron, R (ed Springer, NY
    • Krieger, E., Dunbrack, R.L. Jr, Hooft, R.W., and Krieger, B. (2012) Assignment of protonation states in proteins and ligands: combining pKa prediction with hydrogen bonding network optimization. In: Baron, R (ed). Computational Drug Discovery and Design. Springer, NY, pp. 405-421.
    • (2012) Computational Drug Discovery and Design. , pp. 405-421
    • Krieger, E.1    Dunbrack, R.L.2    Hooft, R.W.3    Krieger, B.4
  • 21
    • 74049110393 scopus 로고    scopus 로고
    • Fast automated placement of polar hydrogen atoms in protein-ligand complexes
    • Lippert, T., and Rarey, M. (2009) Fast automated placement of polar hydrogen atoms in protein-ligand complexes. J. Cheminf., 1, 13.
    • (2009) J. Cheminf. , vol.1 , pp. 13
    • Lippert, T.1    Rarey, M.2
  • 22
    • 84900532536 scopus 로고    scopus 로고
    • Protoss: A holistic approach to predict tautomers and protonation states in protein-ligand complexes
    • Bietz, S., Urbaczek, S., Schulz, B., and Rarey, M. (2014) Protoss: a holistic approach to predict tautomers and protonation states in protein-ligand complexes. J. Cheminf., 6, 12.
    • (2014) J. Cheminf. , vol.6 , pp. 12
    • Bietz, S.1    Urbaczek, S.2    Schulz, B.3    Rarey, M.4
  • 24
    • 35248846115 scopus 로고    scopus 로고
    • 2D depiction of protein-ligand complexes
    • Clark, A.M., and Labute, P. (2007) 2D depiction of protein-ligand complexes. J. Chem. Inf. Model., 47, 1933-1944.
    • (2007) J. Chem. Inf. Model. , vol.47 , pp. 1933-1944
    • Clark, A.M.1    Labute, P.2
  • 25
    • 84884376621 scopus 로고    scopus 로고
    • LeView: Automatic and interactive generation of 2D diagrams for biomacromolecule/ligand interactions
    • Caboche, S. (2013) LeView: automatic and interactive generation of 2D diagrams for biomacromolecule/ligand interactions. J. Cheminform., 5, 40.
    • (2013) J. Cheminform. , vol.5 , pp. 40
    • Caboche, S.1
  • 26
    • 80054911951 scopus 로고    scopus 로고
    • LigPlot+: Multiple ligand-protein interaction diagrams for drug discovery
    • Laskowski, R.A., and Swindells, M.B. (2011) LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J. Chem. Inf. Model., 51, 2778-2786.
    • (2011) J. Chem. Inf. Model. , vol.51 , pp. 2778-2786
    • Laskowski, R.A.1    Swindells, M.B.2
  • 27
    • 51049104888 scopus 로고    scopus 로고
    • From modeling to medicinal chemistry: Automatic generation of two-dimensional complex diagrams
    • Stierand, K., and Rarey, M. (2007) From modeling to medicinal chemistry: automatic generation of two-dimensional complex diagrams. Chemmedchem, 2, 853-860.
    • (2007) Chemmedchem , vol.2 , pp. 853-860
    • Stierand, K.1    Rarey, M.2
  • 28
    • 78650203607 scopus 로고    scopus 로고
    • Drawing the PDB: Protein-ligand complexes in two dimensions
    • Stierand, K., and Rarey, M. (2010) Drawing the PDB: protein-ligand complexes in two dimensions. ACS Med. Chem. Lett., 1, 540-545.
    • (2010) ACS Med. Chem. Lett. , vol.1 , pp. 540-545
    • Stierand, K.1    Rarey, M.2
  • 29
    • 0030841587 scopus 로고    scopus 로고
    • 10 Electron density map interpretation
    • Jones, T., and Kjeldgaard, M. (1997) [10] Electron density map interpretation. Methods Enzymol., 277, 173-208.
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.1    Kjeldgaard, M.2
  • 30
    • 84860305929 scopus 로고    scopus 로고
    • Statistical quality indicators for electron-density maps
    • Tickle, I.J. (2012) Statistical quality indicators for electron-density maps. Acta Crystallogr. D Biol. Crystallogr. , 68, 454-467.
    • (2012) Acta Crystallogr. D Biol. Crystallogr. , vol.68 , pp. 454-467
    • Tickle, I.J.1
  • 31
    • 84928689662 scopus 로고    scopus 로고
    • Evidence of water molecules-A statistical evaluation of water molecules based on electron density
    • Nittinger, E., Schneider, N., Lange, G., and Rarey, M. (2015) Evidence of water molecules-A statistical evaluation of water molecules based on electron density. J. Chem. Inf. Model., 55, 771-783.
    • (2015) J. Chem. Inf. Model. , vol.55 , pp. 771-783
    • Nittinger, E.1    Schneider, N.2    Lange, G.3    Rarey, M.4
  • 32
    • 84955572044 scopus 로고    scopus 로고
    • SIENA: Efficient compilation of selective protein binding site ensembles
    • Bietz, S., and Rarey, M. (2016) SIENA: efficient compilation of selective protein binding site ensembles. J. Chem. Inf. Model., 56, 248-259.
    • (2016) J. Chem. Inf. Model. , vol.56 , pp. 248-259
    • Bietz, S.1    Rarey, M.2
  • 33
    • 84940182462 scopus 로고    scopus 로고
    • ASCONA: Rapid detection and alignment of protein binding site conformations
    • Bietz, S., and Rarey, M. (2015) ASCONA: rapid detection and alignment of protein binding site conformations. J. Chem. Inf. Model., 55, 1747-1756.
    • (2015) J. Chem. Inf. Model. , vol.55 , pp. 1747-1756
    • Bietz, S.1    Rarey, M.2
  • 34
    • 79954426877 scopus 로고    scopus 로고
    • Crystal structure of E339K mutated human glucokinase reveals changes in the ATP binding site
    • Liu, Q., Shen, Y., Liu, S., Weng, J., and Liu, J. (2011) Crystal structure of E339K mutated human glucokinase reveals changes in the ATP binding site. FEBS Lett., 585, 1175-1179.
    • (2011) FEBS Lett. , vol.585 , pp. 1175-1179
    • Liu, Q.1    Shen, Y.2    Liu, S.3    Weng, J.4    Liu, J.5
  • 35
    • 84895469259 scopus 로고    scopus 로고
    • Exploiting structural information for drug-Target assessment
    • Volkamer, A., and Rarey, M. (2014) Exploiting structural information for drug-Target assessment. Future Med. Chem., 6, 319-331.
    • (2014) Future Med. Chem. , vol.6 , pp. 319-331
    • Volkamer, A.1    Rarey, M.2
  • 36
    • 67649422714 scopus 로고    scopus 로고
    • Fpocket: An open source platform for ligand pocket detection
    • Le Guilloux, V., Schmidtke, P., and Tuffery, P. (2009) Fpocket: an open source platform for ligand pocket detection. BMC Bioinformatics, 10, 168.
    • (2009) BMC Bioinformatics , vol.10 , pp. 168
    • Le Guilloux, V.1    Schmidtke, P.2    Tuffery, P.3
  • 37
    • 65249117514 scopus 로고    scopus 로고
    • Identifying and characterizing binding sites and assessing druggability
    • Halgren, T.A. (2009) Identifying and characterizing binding sites and assessing druggability. J. Chem. Inf. Model., 49, 377-389.
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 377-389
    • Halgren, T.A.1
  • 38
    • 84857531280 scopus 로고    scopus 로고
    • Combining global and local measures for structure-based druggability predictions
    • Volkamer, A., Kuhn, D., Grombacher, T., Rippmann, F., and Rarey, M. (2012) Combining global and local measures for structure-based druggability predictions. J. Chem. Inf. Model., 52, 360-372.
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 360-372
    • Volkamer, A.1    Kuhn, D.2    Grombacher, T.3    Rippmann, F.4    Rarey, M.5
  • 39
    • 78649499434 scopus 로고    scopus 로고
    • Analyzing the topology of active sites: On the prediction of pockets and subpockets
    • Volkamer, A., Griewel, A., Grombacher, T., and Rarey, M. (2010) Analyzing the topology of active sites: on the prediction of pockets and subpockets. J. Chem. Inf. Model., 50, 2041-2052.
    • (2010) J. Chem. Inf. Model. , vol.50 , pp. 2041-2052
    • Volkamer, A.1    Griewel, A.2    Grombacher, T.3    Rarey, M.4
  • 40
    • 34547341277 scopus 로고    scopus 로고
    • PocketPicker: Analysis of ligand binding-sites with shape descriptors
    • Weisel, M., Proschak, E., and Schneider, G. (2007) PocketPicker: analysis of ligand binding-sites with shape descriptors. Chem. Cent. J., 1, 7.
    • (2007) Chem. Cent. J. , vol.1 , pp. 7
    • Weisel, M.1    Proschak, E.2    Schneider, G.3
  • 41
    • 2542530042 scopus 로고    scopus 로고
    • The PDBbind database: Collection of binding affinities for protein-ligand complexes with known three-dimensional structures
    • Wang, R., Fang, X., Lu, Y. andWang, S. (2004) The PDBbind database: collection of binding affinities for protein-ligand complexes with known three-dimensional structures. J. Med. Chem., 47, 2977-2980.
    • (2004) J. Med. Chem. , vol.47 , pp. 2977-2980
    • Wang, R.1    Fang, X.2    Lu, Y.3    Wang, S.4
  • 42
    • 33646228824 scopus 로고    scopus 로고
    • Sc-PDB: An annotated database of druggable binding sites from the Protein Data Bank
    • Kellenberger, E., Muller, P., Schalon, C., Bret, G., Foata, N., and Rognan, D. (2006) sc-PDB: an annotated database of druggable binding sites from the Protein Data Bank. J. Chem. Inf. Model., 46, 717-727.
    • (2006) J. Chem. Inf. Model. , vol.46 , pp. 717-727
    • Kellenberger, E.1    Muller, P.2    Schalon, C.3    Bret, G.4    Foata, N.5    Rognan, D.6
  • 43
    • 77955397914 scopus 로고    scopus 로고
    • Understanding and predicting druggability. A high-Throughput method for detection of drug binding sites
    • Schmidtke, P., and Barril, X. (2010) Understanding and predicting druggability. A high-Throughput method for detection of drug binding sites. J. Med. Chem., 53, 5858-5867.
    • (2010) J. Med. Chem. , vol.53 , pp. 5858-5867
    • Schmidtke, P.1    Barril, X.2
  • 44
    • 84886950237 scopus 로고    scopus 로고
    • One hundred thousand mouse clicks down the road: Selected online resources supporting drug discovery collected over a decade
    • Villoutreix, B.O., Lagorce, D., Labbe, C.M., Sperandio, O., and Miteva, M.A. (2013) One hundred thousand mouse clicks down the road: selected online resources supporting drug discovery collected over a decade. Drug Discov. Today, 18, 1081-1089.
    • (2013) Drug Discov. Today , vol.18 , pp. 1081-1089
    • Villoutreix, B.O.1    Lagorce, D.2    Labbe, C.M.3    Sperandio, O.4    Miteva, M.A.5
  • 45
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells, J.A., and McClendon, C.L. (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature, 450, 1001-1009.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 46
    • 84879784821 scopus 로고    scopus 로고
    • Targeting protein-protein interactions as an anticancer strategy
    • Ivanov, A.A., Khuri, F.R., and Fu, H. (2013) Targeting protein-protein interactions as an anticancer strategy. Trends Pharmacol. Sci., 34, 393-400.
    • (2013) Trends Pharmacol. Sci. , vol.34 , pp. 393-400
    • Ivanov, A.A.1    Khuri, F.R.2    Fu, H.3
  • 48
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick, K., and Thornton, J.M. (1998) PQS: a protein quaternary structure file server. Trends Biochem. Sci., 23, 358-361.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.M.2
  • 50
    • 33750090686 scopus 로고    scopus 로고
    • Physicochemical descriptors to discriminate protein-protein interactions in permanent and transient complexes selected by means of machine learning algorithms
    • Block, P., Paern, J., H ullermeier, E., Sanschagrin, P., Sotriffer, C.A., and Klebe, G. (2006) Physicochemical descriptors to discriminate protein-protein interactions in permanent and transient complexes selected by means of machine learning algorithms. Proteins, 65, 607-622.
    • (2006) Proteins , vol.65 , pp. 607-622
    • Block, P.1    Paern, J.2    Hullermeier, E.3    Sanschagrin, P.4    Sotriffer, C.A.5    Klebe, G.6
  • 51
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol., 372, 774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 52
    • 40049091293 scopus 로고    scopus 로고
    • DiMoVo: A voronoi tessellation-based method for discriminating crystallographic and biological protein-protein interactions
    • Bernauer, J., Bahadur, R.P., Rodier, F., Janin, J., and Poupon, A. (2008) DiMoVo: a voronoi tessellation-based method for discriminating crystallographic and biological protein-protein interactions. Bioinformatics, 24, 652-658.
    • (2008) Bioinformatics , vol.24 , pp. 652-658
    • Bernauer, J.1    Bahadur, R.P.2    Rodier, F.3    Janin, J.4    Poupon, A.5
  • 53
    • 77955781875 scopus 로고    scopus 로고
    • CRK: An evolutionary approach for distinguishing biologically relevant interfaces from crystal contacts
    • Scharer, M.A., Gr utter, M.G., and Capitani, G. (2010) CRK: an evolutionary approach for distinguishing biologically relevant interfaces from crystal contacts. Proteins, 78, 2707-2713.
    • (2010) Proteins , vol.78 , pp. 2707-2713
    • Scharer, M.A.1    Grutter, M.G.2    Capitani, G.3
  • 54
    • 77949891473 scopus 로고    scopus 로고
    • Propensity vectors of low-ASA residue pairs in the distinction of protein interactions
    • Liu, Q., and Li, J. (2010) Propensity vectors of low-ASA residue pairs in the distinction of protein interactions. Proteins, 78, 589-602.
    • (2010) Proteins , vol.78 , pp. 589-602
    • Liu, Q.1    Li, J.2
  • 55
    • 79952478104 scopus 로고    scopus 로고
    • Combining Bayes classification and point group symmetry under Boolean framework for enhanced protein quaternary structure inference
    • Mitra, P., and Pal, D. (2011) Combining Bayes classification and point group symmetry under Boolean framework for enhanced protein quaternary structure inference. Structure, 19, 304-312.
    • (2011) Structure , vol.19 , pp. 304-312
    • Mitra, P.1    Pal, D.2
  • 56
    • 84942540332 scopus 로고    scopus 로고
    • IChemPIC: A
    • random forest classifier of biological and crystallographic protein-protein interfaces
    • Da Silva, F., Desaphy, J., Bret, G., and Rognan, D. (2015) IChemPIC: a random forest classifier of biological and crystallographic protein-protein interfaces. J. Chem. Inf. Model., 55, 2005-2014.
    • (2015) J. Chem. Inf. Model. , vol.55 , pp. 2005-2014
    • Da Silva, F.1    Desaphy, J.2    Bret, G.3    Rognan, D.4
  • 57
    • 84874111137 scopus 로고    scopus 로고
    • A consistent description of HYdrogen bond and DEhydration energies in protein-ligand complexes: Methods behind the HYDE scoring function
    • Schneider, N., Lange, G., Hindle, S., Klein, R., and Rarey, M. (2013) A consistent description of HYdrogen bond and DEhydration energies in protein-ligand complexes: methods behind the HYDE scoring function. J. Comput. Aided Mol. Des., 27, 15-29.
    • (2013) J. Comput. Aided Mol. Des. , vol.27 , pp. 15-29
    • Schneider, N.1    Lange, G.2    Hindle, S.3    Klein, R.4    Rarey, M.5
  • 58
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren, I. M.A., and Thornton, J.M. (2003) Structural characterisation and functional significance of transient protein-protein interactions. J. Mol. Biol., 325, 991-1018.
    • (2003) J. Mol. Biol. , vol.325 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 59
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-specific protein-protein interfaces
    • Bahadur, R.P., Chakrabarti, P., Rodier, F., and Janin, J. (2004) A dissection of specific and non-specific protein-protein interfaces. J. Mol. Biol., 336, 943-955.
    • (2004) J. Mol. Biol. , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 60
    • 24944549109 scopus 로고    scopus 로고
    • Interaction preferences across protein-protein interfaces of obligatory and non-obligatory components are different
    • De, S., Krishnadev, O., Srinivasan, N., and Rekha, N. (2005) Interaction preferences across protein-protein interfaces of obligatory and non-obligatory components are different. BMC Struct. Biol., 5, 15.
    • (2005) BMC Struct. Biol. , vol.5 , pp. 15
    • Krishnadev, O.1    Srinivasan, N.2    Rekha, N.3
  • 61
    • 58749108303 scopus 로고    scopus 로고
    • Common physical basis of macromolecule-binding sites in proteins
    • Chen, Y.C., and Lim, C. (2008) Common physical basis of macromolecule-binding sites in proteins. Nucleic Acids Res., 36, 7078-7087.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 7078-7087
    • Chen, Y.C.1    Lim, C.2
  • 62
    • 45549091203 scopus 로고    scopus 로고
    • Coevolution at protein complex interfaces can be detected by the complementarity trace with important impact for predictive docking
    • Madaoui, H., and Guerois, R. (2008) Coevolution at protein complex interfaces can be detected by the complementarity trace with important impact for predictive docking. Proc. Natl. Acad. Sci. U.S.A., 105, 7708-7713.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7708-7713
    • Madaoui, H.1    Guerois, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.