메뉴 건너뛰기




Volumn 119, Issue 1, 2015, Pages 2-9

Flexibility and small pockets at protein-protein interfaces: New insights into druggability

Author keywords

Hotspots; Inhibitors druggability; Protein protein interfaces

Indexed keywords

PROTEIN;

EID: 84940893103     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2015.01.009     Document Type: Review
Times cited : (122)

References (104)
  • 1
    • 84909587217 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: progressing toward the reality
    • Arkin M.R., Tang Y., Wells J.A. Small-molecule inhibitors of protein-protein interactions: progressing toward the reality. Chem. Biol. 2014, 21:1102-1114.
    • (2014) Chem. Biol. , vol.21 , pp. 1102-1114
    • Arkin, M.R.1    Tang, Y.2    Wells, J.A.3
  • 3
    • 77956171332 scopus 로고    scopus 로고
    • Computational mapping of anchoring spots on protein surfaces
    • Ben-Shimon A., Eisenstein M. Computational mapping of anchoring spots on protein surfaces. J. Mol. Biol. 2010, 402:259-277.
    • (2010) J. Mol. Biol. , vol.402 , pp. 259-277
    • Ben-Shimon, A.1    Eisenstein, M.2
  • 6
    • 79960884702 scopus 로고    scopus 로고
    • Comprehensive, atomic-level characterization of structurally characterized protein-protein interactions: the PICCOLO database
    • Bickerton G.R., Higueruelo A.P., Blundell T.L. Comprehensive, atomic-level characterization of structurally characterized protein-protein interactions: the PICCOLO database. BMC Bioinforma. 2011, 12:313.
    • (2011) BMC Bioinforma. , vol.12 , pp. 313
    • Bickerton, G.R.1    Higueruelo, A.P.2    Blundell, T.L.3
  • 9
    • 0018382972 scopus 로고
    • Conformation and molecular-biology of polypeptide hormones .2. Glucagon
    • Blundell T. Conformation and molecular-biology of polypeptide hormones .2. Glucagon. Trends Biochem. Sci. 1979, 4:80-83.
    • (1979) Trends Biochem. Sci. , vol.4 , pp. 80-83
    • Blundell, T.1
  • 10
    • 0020016306 scopus 로고
    • The conformation, flexibility, and dynamics of polypeptide hormones
    • Blundell T., Wood S. The conformation, flexibility, and dynamics of polypeptide hormones. Annu. Rev. Biochem. 1982, 51:123-154.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 123-154
    • Blundell, T.1    Wood, S.2
  • 12
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell T.L., Jhoti H., Abell C. High-throughput crystallography for lead discovery in drug design. Nat. Rev. Drug Discov. 2002, 1:45-54.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 14
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan A.A., Thorn K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 1998, 280:1-9.
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 16
    • 0028224359 scopus 로고
    • Nuclear-magnetic-resonance solution structure of the arc repressor using relaxation matrix calculations
    • Bonvin A.M.J.J., Vis H., Breg J.N., Burgering M.J.M., Boelens R., Kaptein R. Nuclear-magnetic-resonance solution structure of the arc repressor using relaxation matrix calculations. J. Mol. Biol. 1994, 236:328-341.
    • (1994) J. Mol. Biol. , vol.236 , pp. 328-341
    • Bonvin, A.M.J.J.1    Vis, H.2    Breg, J.N.3    Burgering, M.J.M.4    Boelens, R.5    Kaptein, R.6
  • 17
    • 77949743743 scopus 로고    scopus 로고
    • Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database
    • Bourgeas R., Basse M.J., Morelli X., Roche P. Atomic analysis of protein-protein interfaces with known inhibitors: the 2P2I database. PLoS One 2010, 5.
    • (2010) PLoS One , vol.5
    • Bourgeas, R.1    Basse, M.J.2    Morelli, X.3    Roche, P.4
  • 18
    • 0021095726 scopus 로고
    • Conformation of glucagon in a lipid water interphase by H-1 nuclear magnetic-resonance
    • Braun W., Wider G., Lee K.H., Wuthrich K. Conformation of glucagon in a lipid water interphase by H-1 nuclear magnetic-resonance. J. Mol. Biol. 1983, 169:921-948.
    • (1983) J. Mol. Biol. , vol.169 , pp. 921-948
    • Braun, W.1    Wider, G.2    Lee, K.H.3    Wuthrich, K.4
  • 19
    • 0015840363 scopus 로고
    • Angiotensin-II blockade in man by sar1-ala8-angiotensin II for understanding and treatment of high blood-pressure
    • Brunner H.R., Gavras H., Laragh J.H. Angiotensin-II blockade in man by sar1-ala8-angiotensin II for understanding and treatment of high blood-pressure. Lancet 1973, 2:1045-1048.
    • (1973) Lancet , vol.2 , pp. 1045-1048
    • Brunner, H.R.1    Gavras, H.2    Laragh, J.H.3
  • 20
    • 0035912757 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibodies to hepatocyte growth factor/scatter factor (HGF/SF) display antitumor activity in animal models
    • Cao B., Su Y., Oskarsson M., Zhao P., Kort E.J., Fisher R.J., Wang L.M., Vande Woude G.F. Neutralizing monoclonal antibodies to hepatocyte growth factor/scatter factor (HGF/SF) display antitumor activity in animal models. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:7443-7448.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7443-7448
    • Cao, B.1    Su, Y.2    Oskarsson, M.3    Zhao, P.4    Kort, E.J.5    Fisher, R.J.6    Wang, L.M.7    Vande Woude, G.F.8
  • 22
    • 34250212118 scopus 로고    scopus 로고
    • DAPID: a 3D-domain annotated protein-protein interaction database
    • Chen Y.C., Chen H.C., Yang J.M. DAPID: a 3D-domain annotated protein-protein interaction database. Genome Inf. 2006, 17:206-215.
    • (2006) Genome Inf. , vol.17 , pp. 206-215
    • Chen, Y.C.1    Chen, H.C.2    Yang, J.M.3
  • 23
    • 0032957467 scopus 로고    scopus 로고
    • Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding
    • Chirgadze D.Y., Hepple J.P., Zhou H., Byrd R.A., Blundell T.L., Gherardi E. Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding. Nat. Struct. Biol. 1999, 6:72-79.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 72-79
    • Chirgadze, D.Y.1    Hepple, J.P.2    Zhou, H.3    Byrd, R.A.4    Blundell, T.L.5    Gherardi, E.6
  • 24
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T., Wells J.A. A hot spot of binding energy in a hormone-receptor interface. Science 1995, 267:383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 28
    • 27744564465 scopus 로고    scopus 로고
    • Protein surface recognition and proteomimetics: mimics of protein surface structure and function
    • Fletcher S., Hamilton A.D. Protein surface recognition and proteomimetics: mimics of protein surface structure and function. Curr. Opin. Chem. Biol. 2005, 9:632-638.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 632-638
    • Fletcher, S.1    Hamilton, A.D.2
  • 29
    • 58849145512 scopus 로고    scopus 로고
    • Predicting druggable binding sites at the protein-protein interface
    • Fuller J.C., Burgoyne N.J., Jackson R.M. Predicting druggable binding sites at the protein-protein interface. Drug Discov. Today 2009, 14:155-161.
    • (2009) Drug Discov. Today , vol.14 , pp. 155-161
    • Fuller, J.C.1    Burgoyne, N.J.2    Jackson, R.M.3
  • 31
    • 84899964275 scopus 로고    scopus 로고
    • Hot spot-based design of small-molecule inhibitors for protein-protein interactions
    • Guo W., Wisniewski J.A., Ji H. Hot spot-based design of small-molecule inhibitors for protein-protein interactions. Bioorg. Med. Chem. Lett. 2014.
    • (2014) Bioorg. Med. Chem. Lett.
    • Guo, W.1    Wisniewski, J.A.2    Ji, H.3
  • 32
    • 33847381100 scopus 로고    scopus 로고
    • A decade of fragment-based drug design: strategic advances and lessons learned
    • Hajduk P.J., Greer J. A decade of fragment-based drug design: strategic advances and lessons learned. Nat. Rev. Drug Discov. 2007, 6:211-219.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 211-219
    • Hajduk, P.J.1    Greer, J.2
  • 36
    • 0031370977 scopus 로고    scopus 로고
    • LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins
    • 389
    • Hendlich M., Rippmann F., Barnickel G. LIGSITE: automatic and efficient detection of potential small molecule-binding sites in proteins. J. Mol. Graph Model 1997, 15:359-363. 389.
    • (1997) J. Mol. Graph Model , vol.15 , pp. 359-363
    • Hendlich, M.1    Rippmann, F.2    Barnickel, G.3
  • 37
    • 84974712878 scopus 로고    scopus 로고
    • Multiprotein assemblies: modulating cell activity through targeting protein-protein interfaces
    • IISc Press and World Scientific, M. Ed Nansal, N. Srinivasan (Eds.)
    • Higueruelo A.P., Jubb H., Blundell A. Multiprotein assemblies: modulating cell activity through targeting protein-protein interfaces. Biomolecular Forms and Functions: a Celebration of 50 Years of the Ramachandran Map 2013, 1-13. IISc Press and World Scientific. M. Ed Nansal, N. Srinivasan (Eds.).
    • (2013) Biomolecular Forms and Functions: a Celebration of 50 Years of the Ramachandran Map , pp. 1-13
    • Higueruelo, A.P.1    Jubb, H.2    Blundell, A.3
  • 38
  • 39
    • 84871126379 scopus 로고    scopus 로고
    • What can we learn from the evolution of protein-ligand interactions to aid the design of new therapeutics?
    • Higueruelo A.P., Schreyer A., Bickerton G.R., Blundell T.L., Pitt W.R. What can we learn from the evolution of protein-ligand interactions to aid the design of new therapeutics?. PLoS One 2012, 7:e51742.
    • (2012) PLoS One , vol.7 , pp. e51742
    • Higueruelo, A.P.1    Schreyer, A.2    Bickerton, G.R.3    Blundell, T.L.4    Pitt, W.R.5
  • 41
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P., Hudson P.J. Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 2005, 23:1126-1136.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 42
    • 33847152551 scopus 로고    scopus 로고
    • Insights into the structure/function of hepatocyte growth factor/scatter factor from studies with individual domains
    • Holmes O., Pillozzi S., Deakin J.A., Carafoli F., Kemp L., Butler P.J.G., Lyon M., Gherardi E. Insights into the structure/function of hepatocyte growth factor/scatter factor from studies with individual domains. J. Mol. Biol. 2007, 367:395-408.
    • (2007) J. Mol. Biol. , vol.367 , pp. 395-408
    • Holmes, O.1    Pillozzi, S.2    Deakin, J.A.3    Carafoli, F.4    Kemp, L.5    Butler, P.J.G.6    Lyon, M.7    Gherardi, E.8
  • 44
    • 80755150215 scopus 로고    scopus 로고
    • Thermodynamic properties of water molecules at a protein-protein interaction surface
    • Huggins D.J., Marsh M., Payne M.C. Thermodynamic properties of water molecules at a protein-protein interaction surface. J. Chem. Theory Comput. 2011, 7:3514-3522.
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 3514-3522
    • Huggins, D.J.1    Marsh, M.2    Payne, M.C.3
  • 46
  • 48
    • 37349061824 scopus 로고    scopus 로고
    • PocketDepth: a new depth based algorithm for identification of ligand binding sites in proteins
    • Kalidas Y., Chandra N. PocketDepth: a new depth based algorithm for identification of ligand binding sites in proteins. J. Struct. Biol. 2008, 161:31-42.
    • (2008) J. Struct. Biol. , vol.161 , pp. 31-42
    • Kalidas, Y.1    Chandra, N.2
  • 49
    • 84872225092 scopus 로고    scopus 로고
    • On the binding affinity of macromolecular interactions: daring to ask why proteins interact
    • Kastritis P.L., Bonvin A.M. On the binding affinity of macromolecular interactions: daring to ask why proteins interact. J. R. Soc. Interface 2013, 10:20120835.
    • (2013) J. R. Soc. Interface , vol.10 , pp. 20120835
    • Kastritis, P.L.1    Bonvin, A.M.2
  • 50
    • 77951217659 scopus 로고    scopus 로고
    • Detection of multiscale pockets on protein surfaces using mathematical morphology
    • Kawabata T. Detection of multiscale pockets on protein surfaces using mathematical morphology. Proteins 2010, 78:1195-1211.
    • (2010) Proteins , vol.78 , pp. 1195-1211
    • Kawabata, T.1
  • 54
    • 84864451527 scopus 로고    scopus 로고
    • PocketQuery: protein-protein interaction inhibitor starting points from protein-protein interaction structure
    • Koes D.R., Camacho C.J. PocketQuery: protein-protein interaction inhibitor starting points from protein-protein interaction structure. Nucleic Acids Res. 2012, 40:W387-W392.
    • (2012) Nucleic Acids Res. , vol.40 , pp. W387-W392
    • Koes, D.R.1    Camacho, C.J.2
  • 55
    • 84864133078 scopus 로고    scopus 로고
    • Small-molecule inhibitor starting points learned from protein-protein interaction inhibitor structure
    • Koes D.R., Camacho C.J. Small-molecule inhibitor starting points learned from protein-protein interaction inhibitor structure. Bioinformatics 2012, 28:784-791.
    • (2012) Bioinformatics , vol.28 , pp. 784-791
    • Koes, D.R.1    Camacho, C.J.2
  • 57
    • 84912572423 scopus 로고    scopus 로고
    • Which three-dimensional characteristics make efficient inhibitors of protein-protein interactions?
    • Kuenemann M.A., Bourbon L.M., Labbe C.M., Villoutreix B.O., Sperandio O. Which three-dimensional characteristics make efficient inhibitors of protein-protein interactions?. J. Chem. Inf. Model 2014, 54:3067-3079.
    • (2014) J. Chem. Inf. Model , vol.54 , pp. 3067-3079
    • Kuenemann, M.A.1    Bourbon, L.M.2    Labbe, C.M.3    Villoutreix, B.O.4    Sperandio, O.5
  • 58
    • 18744394070 scopus 로고    scopus 로고
    • Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites
    • Laurie A.T., Jackson R.M. Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites. Bioinformatics 2005, 21:1908-1916.
    • (2005) Bioinformatics , vol.21 , pp. 1908-1916
    • Laurie, A.T.1    Jackson, R.M.2
  • 60
    • 84863209627 scopus 로고    scopus 로고
    • Antibody-enabled small-molecule drug discovery
    • Lawson A.D.G. Antibody-enabled small-molecule drug discovery. Nat. Rev. Drug Discov. 2012, 11:519-525.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 519-525
    • Lawson, A.D.G.1
  • 61
    • 44949231368 scopus 로고    scopus 로고
    • Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling
    • Li W., Bengtson M.H., Ulbrich A., Matsuda A., Reddy V.A., Orth A., Chanda S.K., Batalov S., Joazeiro C.A. Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling. PLoS One 2008, 3:e1487.
    • (2008) PLoS One , vol.3 , pp. e1487
    • Li, W.1    Bengtson, M.H.2    Ulbrich, A.3    Matsuda, A.4    Reddy, V.A.5    Orth, A.6    Chanda, S.K.7    Batalov, S.8    Joazeiro, C.A.9
  • 62
    • 1542358785 scopus 로고    scopus 로고
    • Highly discriminating protein-protein interaction specificities in the context of a conserved binding energy hotspot
    • Li W., Keeble A.H., Giffard C., James R., Moore G.R., Kleanthous C. Highly discriminating protein-protein interaction specificities in the context of a conserved binding energy hotspot. J. Mol. Biol. 2004, 337:743-759.
    • (2004) J. Mol. Biol. , vol.337 , pp. 743-759
    • Li, W.1    Keeble, A.H.2    Giffard, C.3    James, R.4    Moore, G.R.5    Kleanthous, C.6
  • 63
    • 7944225979 scopus 로고    scopus 로고
    • Protein-protein interactions: hot spots and structurally conserved residues often locate in complemented pockets that pre-organized in the unbound states: implications for docking
    • Li X., Keskin O., Ma B., Nussinov R., Liang J. Protein-protein interactions: hot spots and structurally conserved residues often locate in complemented pockets that pre-organized in the unbound states: implications for docking. J. Mol. Biol. 2004, 344:781-795.
    • (2004) J. Mol. Biol. , vol.344 , pp. 781-795
    • Li, X.1    Keskin, O.2    Ma, B.3    Nussinov, R.4    Liang, J.5
  • 64
    • 0026734672 scopus 로고
    • Structure-function analysis of hepatocyte growth factor - identification of variants that lack mitogenic activity yet retain high affinity receptor binding
    • Lokker N.A., Mark M.R., Luis E.A., Bennett G.L., Robbins K.A., Baker J.B., Godowski P.J. Structure-function analysis of hepatocyte growth factor - identification of variants that lack mitogenic activity yet retain high affinity receptor binding. EMBO J. 1992, 11:2503-2510.
    • (1992) EMBO J. , vol.11 , pp. 2503-2510
    • Lokker, N.A.1    Mark, M.R.2    Luis, E.A.3    Bennett, G.L.4    Robbins, K.A.5    Baker, J.B.6    Godowski, P.J.7
  • 65
    • 77957947345 scopus 로고    scopus 로고
    • Can self-inhibitory peptides be derived from the interfaces of globular protein-protein interactions?
    • London N., Raveh B., Movshovitz-Attias D., Schueler-Furman O. Can self-inhibitory peptides be derived from the interfaces of globular protein-protein interactions?. Proteins 2010, 78:3140-3149.
    • (2010) Proteins , vol.78 , pp. 3140-3149
    • London, N.1    Raveh, B.2    Movshovitz-Attias, D.3    Schueler-Furman, O.4
  • 66
    • 84890137047 scopus 로고    scopus 로고
    • Druggable protein-protein interactions-from hot spots to hot segments
    • London N., Raveh B., Schueler-Furman O. Druggable protein-protein interactions-from hot spots to hot segments. Curr. Opin. Chem. Biol. 2013, 17:952-959.
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 952-959
    • London, N.1    Raveh, B.2    Schueler-Furman, O.3
  • 67
    • 84905454868 scopus 로고    scopus 로고
    • Structure-based druggability assessment of the mammalian structural proteome with inclusion of light protein flexibility
    • Loving K.A., Lin A., Cheng A.C. Structure-based druggability assessment of the mammalian structural proteome with inclusion of light protein flexibility. PLoS Comput Biol. 2014, 10:e1003741.
    • (2014) PLoS Comput Biol. , vol.10 , pp. e1003741
    • Loving, K.A.1    Lin, A.2    Cheng, A.C.3
  • 69
    • 52249097805 scopus 로고    scopus 로고
    • Highly accurate method for ligand-binding site prediction in unbound state (apo) protein structures
    • Morita M., Nakamura S., Shimizu K. Highly accurate method for ligand-binding site prediction in unbound state (apo) protein structures. Proteins 2008, 73:468-479.
    • (2008) Proteins , vol.73 , pp. 468-479
    • Morita, M.1    Nakamura, S.2    Shimizu, K.3
  • 70
    • 77955982439 scopus 로고    scopus 로고
    • Structural biology in fragment-based drug design
    • Murray C.W., Blundell T.L. Structural biology in fragment-based drug design. Curr. Opin. Struct. Biol. 2010, 20:497-507.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 497-507
    • Murray, C.W.1    Blundell, T.L.2
  • 71
    • 0028168145 scopus 로고
    • Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans S., Atarhouch T., Saldanha J., Barbosa J.A., Hamers R. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 1994, 7:1129-1135.
    • (1994) Protein Eng. , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.4    Hamers, R.5
  • 72
    • 34648833340 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction inhibitors by chemoinformatics and machine learning methods
    • Neugebauer A., Hartmann R.W., Klein C.D. Prediction of protein-protein interaction inhibitors by chemoinformatics and machine learning methods. J. Med. Chem. 2007, 50:4665-4668.
    • (2007) J. Med. Chem. , vol.50 , pp. 4665-4668
    • Neugebauer, A.1    Hartmann, R.W.2    Klein, C.D.3
  • 76
    • 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, 300:445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 79
    • 84893298981 scopus 로고    scopus 로고
    • MCSM: predicting the effects of mutations in proteins using graph-based signatures
    • Pires D.E., Ascher D.B., Blundell T.L. mCSM: predicting the effects of mutations in proteins using graph-based signatures. Bioinformatics 2014, 30:335-342.
    • (2014) Bioinformatics , vol.30 , pp. 335-342
    • Pires, D.E.1    Ascher, D.B.2    Blundell, T.L.3
  • 80
    • 84879020527 scopus 로고    scopus 로고
    • Plucking the high hanging fruit: a systematic approach for targeting protein-protein interactions
    • Raj M., Bullock B.N., Arora P.S. Plucking the high hanging fruit: a systematic approach for targeting protein-protein interactions. Bioorg. Med. Chem. 2013, 21:4051-4057.
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 4051-4057
    • Raj, M.1    Bullock, B.N.2    Arora, P.S.3
  • 83
    • 0016709043 scopus 로고
    • X-ray analysis of glucagon and its relationship to receptor binding
    • Sasaki K., Dockerill S., Adamiak D.A., Tickle I.J., Blundell T. X-ray analysis of glucagon and its relationship to receptor binding. Nature 1975, 257:751-757.
    • (1975) Nature , vol.257 , pp. 751-757
    • Sasaki, K.1    Dockerill, S.2    Adamiak, D.A.3    Tickle, I.J.4    Blundell, T.5
  • 84
    • 84961490006 scopus 로고
    • Hormone-receptor interactions - study of the binding of hormone-substituted tobacco mosaic-virus to membrane-vesicles by dynamic light-scattering and by transient electric birefringence
    • Schwyzer R., Kriwaczek V.M., Baumann K., Haller H.R., Wider G., Wiltzius P. Hormone-receptor interactions - study of the binding of hormone-substituted tobacco mosaic-virus to membrane-vesicles by dynamic light-scattering and by transient electric birefringence. Pure Appl. Chem. 1979, 51:831-835.
    • (1979) Pure Appl. Chem. , vol.51 , pp. 831-835
    • Schwyzer, R.1    Kriwaczek, V.M.2    Baumann, K.3    Haller, H.R.4    Wider, G.5    Wiltzius, P.6
  • 87
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker S.B., Hajduk P.J., Meadows R.P., Fesik S.W. Discovering high-affinity ligands for proteins: SAR by NMR. Science 1996, 274:1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 89
    • 3142595278 scopus 로고    scopus 로고
    • Crystal structure of the HGF beta-chain in complex with the sema domain of the met receptor
    • Stamos J., Lazarus R.A., Yao X., Kirchhofer D., Wiesmann C. Crystal structure of the HGF beta-chain in complex with the sema domain of the met receptor. EMBO J. 2004, 23:2325-2335.
    • (2004) EMBO J. , vol.23 , pp. 2325-2335
    • Stamos, J.1    Lazarus, R.A.2    Yao, X.3    Kirchhofer, D.4    Wiesmann, C.5
  • 90
    • 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. 2011, 39:D718-D723.
    • (2011) Nucleic Acids Res. , vol.39 , pp. D718-D723
    • Stein, A.1    Ceol, A.2    Aloy, P.3
  • 91
    • 77955891885 scopus 로고    scopus 로고
    • The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer
    • Stewart M.L., Fire E., Keating A.E., Walensky L.D. The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer. Nat. Chem. Biol. 2010, 6:595-601.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 595-601
    • Stewart, M.L.1    Fire, E.2    Keating, A.E.3    Walensky, L.D.4
  • 94
    • 65549157572 scopus 로고    scopus 로고
    • A survey of available tools and web servers for analysis of protein-protein interactions and interfaces
    • Tuncbag N., Kar G., Keskin O., Gursoy A., Nussinov R. A survey of available tools and web servers for analysis of protein-protein interactions and interfaces. Brief. Bioinform. 2009, 10:217-232.
    • (2009) Brief. Bioinform. , vol.10 , pp. 217-232
    • Tuncbag, N.1    Kar, G.2    Keskin, O.3    Gursoy, A.4    Nussinov, R.5
  • 95
    • 0032533765 scopus 로고    scopus 로고
    • Crystal structure of the NK1 fragment of human hepatocyte growth factor at 2.0 Å resolution
    • Ultsch M., Lokker N.A., Godowski P.J., Vos A.M.d Crystal structure of the NK1 fragment of human hepatocyte growth factor at 2.0 Å resolution. Structure 1998, 6:1383-1393.
    • (1998) Structure , vol.6 , pp. 1383-1393
    • Ultsch, M.1    Lokker, N.A.2    Godowski, P.J.3    Vos, A.4
  • 97
    • 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., Miteva M.A. One hundred thousand mouse clicks down the road: selected online resources supporting drug discovery collected over a decade. Drug Discov. Today 2013, 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
  • 98
    • 84906254338 scopus 로고    scopus 로고
    • Anatomy of beta-strands at protein-protein interfaces
    • Watkins A.M., Arora P.S. Anatomy of beta-strands at protein-protein interfaces. ACS Chem. Biol. 2014, 9:1747-1754.
    • (2014) ACS Chem. Biol. , vol.9 , pp. 1747-1754
    • Watkins, A.M.1    Arora, P.S.2
  • 99
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • Wells J.A., McClendon C.L. Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 2007, 450:1001-1009.
    • (2007) Nature , vol.450 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 100
    • 84870810902 scopus 로고    scopus 로고
    • Biophysical and computational fragment-based approaches to targeting protein-protein interactions: applications in structure-guided drug discovery
    • Winter A., Higueruelo A.P., Marsh M., Sigurdardottir A., Pitt W.R., Blundell T.L. Biophysical and computational fragment-based approaches to targeting protein-protein interactions: applications in structure-guided drug discovery. Q. Rev. Biophys. 2012, 45:383-426.
    • (2012) Q. Rev. Biophys. , vol.45 , pp. 383-426
    • Winter, A.1    Higueruelo, A.P.2    Marsh, M.3    Sigurdardottir, A.4    Pitt, W.R.5    Blundell, T.L.6
  • 101
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 1999, 293:321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 104
    • 84865494461 scopus 로고    scopus 로고
    • Relationship between hot spot residues and ligand binding hot spots in protein-protein interfaces
    • Zerbe B.S., Hall D.R., Vajda S., Whitty A., Kozakov D. Relationship between hot spot residues and ligand binding hot spots in protein-protein interfaces. J. Chem. Inf. Model 2012, 52:2236-2244.
    • (2012) J. Chem. Inf. Model , vol.52 , pp. 2236-2244
    • Zerbe, B.S.1    Hall, D.R.2    Vajda, S.3    Whitty, A.4    Kozakov, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.