메뉴 건너뛰기




Volumn 11, Issue 11, 2011, Pages 1305-1319

Modulators of protein-protein interactions - novel approaches in targeting protein kinases and other pharmaceutically relevant biomolecules

Author keywords

Molecular modeling; Protein kinases; Protein protein interaction modulators; Protein protein interactions; Rational drug design; Virtual screening

Indexed keywords

AUROTHIOMALATE; BETA CATENIN; CYCLIN A; CYCLIN DEPENDENT KINASE 2; ENFUVIRTIDE; GLYCOPROTEIN GP 120; GLYCOPROTEIN GP 41; INTERLEUKIN 2; INTERLEUKIN 2 RECEPTOR ALPHA; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MARAVIROC; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; POLO LIKE KINASE 1; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN KINASE C EPSILON; PROTEIN KINASE C LAMBDA; PROTEIN MDM2; PROTEIN P300; PROTEIN P53; PROTEIN P56; PROTEIN P62; PROTEIN S100B; SURVIVIN; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR; VICRIVIROC;

EID: 79958143460     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/156802611795589610     Document Type: Review
Times cited : (18)

References (200)
  • 1
    • 23044496736 scopus 로고    scopus 로고
    • Protein-protein interactions in human disease
    • Ryan, D.P.; Matthews, J.M. Protein-protein interactions in human disease. Curr. Opin. Struct. Biol., 2005, 15, 441-446.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 441-446
    • Ryan, D.P.1    Matthews, J.M.2
  • 4
    • 33846919627 scopus 로고    scopus 로고
    • The protein network as a tool for finding novel drug targets
    • Strong, M.; Eisenberg, D. The protein network as a tool for finding novel drug targets. Prog. Drug. Res., 2007, 64, 193-215.
    • (2007) Prog. Drug. Res , vol.64 , pp. 193-215
    • Strong, M.1    Eisenberg, D.2
  • 5
    • 33845594315 scopus 로고    scopus 로고
    • Protein-protein interactions as targets for small molecule drug discovery
    • Fry, D.C. Protein-protein interactions as targets for small molecule drug discovery. Biopolymers, 2006, 84, 535-552.
    • (2006) Biopolymers , vol.84 , pp. 535-552
    • Fry, D.C.1
  • 8
    • 22144454687 scopus 로고    scopus 로고
    • Strategies for targeting protein-protein interactions with synthetic agents
    • Yin, H.; Hamilton, A.D. Strategies for targeting protein-protein interactions with synthetic agents. Angew. Chem., Int. Ed., 2005, 44, 4130-4163.
    • (2005) Angew. Chem., Int. Ed , vol.44 , pp. 4130-4163
    • Yin, H.1    Hamilton, A.D.2
  • 9
    • 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
  • 10
    • 20444376940 scopus 로고    scopus 로고
    • Protein-protein interactions and cancer: Small molecules going in for the kill
    • Arkin, M. Protein-protein interactions and cancer: small molecules going in for the kill. Curr. Opin. Chem. Biol., 2005, 9, 317-324.
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 317-324
    • Arkin, M.1
  • 11
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of proteinprotein interactions: Progressing towards the dream
    • Arkin, M.R.; Wells, J.A. Small-molecule inhibitors of proteinprotein interactions: progressing towards the dream. Nat. Rev. Drug Discov., 2004, 3, 301-317.
    • (2004) Nat. Rev. Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 12
    • 0142087554 scopus 로고    scopus 로고
    • Antibodies as therapeutic agents: Vive la renaissance!
    • Stockwin, L.H.; Holmes, S. Antibodies as therapeutic agents: vive la renaissance! Expert Opin. Biol. Ther., 2003, 3, 1133-1152.
    • (2003) Expert Opin. Biol. Ther , vol.3 , pp. 1133-1152
    • Stockwin, L.H.1    Holmes, S.2
  • 13
    • 0034754136 scopus 로고    scopus 로고
    • Epidermal growth factor receptor biology (IMC-C225)
    • Kim, E.S.; Khuri, F.R.; Herbst, R.S. Epidermal growth factor receptor biology (IMC-C225). Curr. Opin. Oncol., 2001, 13, 506-513.
    • (2001) Curr. Opin. Oncol , vol.13 , pp. 506-513
    • Kim, E.S.1    Khuri, F.R.2    Herbst, R.S.3
  • 14
    • 52649096967 scopus 로고    scopus 로고
    • Antibody-based therapy for solid tumors
    • Yan, L.; Hsu, K.; Beckman, R.A. Antibody-based therapy for solid tumors. Cancer J., 2008, 14, 178-183.
    • (2008) Cancer J , vol.14 , pp. 178-183
    • Yan, L.1    Hsu, K.2    Beckman, R.A.3
  • 15
    • 0036468670 scopus 로고    scopus 로고
    • Evolutionary predictions of binding surfaces and interactions
    • Lichtarge, O.; Sowa, M.E. Evolutionary predictions of binding surfaces and interactions. Curr. Opin. Struct. Biol., 2002, 12, 21-27.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 21-27
    • Lichtarge, O.1    Sowa, M.E.2
  • 17
    • 34548779127 scopus 로고    scopus 로고
    • Hot spots-a review of the protein-protein interface determinant amino-acid residues
    • Moreira, I.S.; Fernandes, P.A.; Ramos, M.J. Hot spots-a review of the protein-protein interface determinant amino-acid residues. Proteins: Struct., Funct., Bioinf., 2007, 68, 803-812.
    • (2007) Proteins: Struct., Funct., Bioinf , vol.68 , pp. 803-812
    • Moreira, I.S.1    Fernandes, P.A.2    Ramos, M.J.3
  • 18
    • 34249079980 scopus 로고    scopus 로고
    • Molecular modeling of hydration in drug design
    • Mancera, R.L. Molecular modeling of hydration in drug design. Curr. Opin. Drug Discov. Dev., 2007, 10, 275-280.
    • (2007) Curr. Opin. Drug Discov. Dev , vol.10 , pp. 275-280
    • Mancera, R.L.1
  • 19
    • 33748578600 scopus 로고    scopus 로고
    • Targeting protein-protein interactions with small molecules: Challenges and perspectives for computational binding epitope detection and ligand finding
    • Gonzalez-Ruiz, D.; Gohlke, H. Targeting protein-protein interactions with small molecules: challenges and perspectives for computational binding epitope detection and ligand finding. Curr. Med. Chem., 2006, 13, 2607-2625.
    • (2006) Curr. Med. Chem , vol.13 , pp. 2607-2625
    • Gonzalez-Ruiz, D.1    Gohlke, H.2
  • 20
    • 65549157572 scopus 로고    scopus 로고
    • A survey of available tools and web servers for analysis of proteinprotein interactions and interfaces
    • Tuncbag, N.; Kar, G.; Keskin, O.; Gursoy, A.; Nussinov, R. A survey of available tools and web servers for analysis of proteinprotein interactions and interfaces. Briefings Bioinform., 2009, 10, 217-232.
    • (2009) Briefings Bioinform , vol.10 , pp. 217-232
    • Tuncbag, N.1    Kar, G.2    Keskin, O.3    Gursoy, A.4    Nussinov, R.5
  • 21
    • 57149136433 scopus 로고    scopus 로고
    • The Protein Data Bank (PDB), its related services and software tools as key components for in silico guided drug discovery
    • Kirchmair, J.; Markt, P.; Distinto, S.; Schuster, D.; Spitzer, G.M.; Liedl, K.R.; Langer, T.; Wolber, G. The Protein Data Bank (PDB), its related services and software tools as key components for in silico guided drug discovery. J. Med. Chem., 2008, 51, 7021-7040.
    • (2008) J. Med. Chem , vol.51 , pp. 7021-7040
    • Kirchmair, J.1    Markt, P.2    Distinto, S.3    Schuster, D.4    Spitzer, G.M.5    Liedl, K.R.6    Langer, T.7    Wolber, G.8
  • 22
    • 28544446811 scopus 로고    scopus 로고
    • Targeting protein-protein interactions for cancer therapy
    • Fry, D.C.; Vassilev, L.T. Targeting protein-protein interactions for cancer therapy. J. Mol. Med., 2005, 83, 955-963.
    • (2005) J. Mol. Med , vol.83 , pp. 955-963
    • Fry, D.C.1    Vassilev, L.T.2
  • 24
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of proteinprotein recognition sites
    • Conte, L.L.; Chothia, C.; Janin, J. The atomic structure of proteinprotein recognition sites. J. Mol. Biol., 1999, 285, 2177-2198.
    • (1999) J. Mol. Biol , vol.285 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 25
    • 33645827371 scopus 로고    scopus 로고
    • Targeting protein-protein interactions by rational design: Mimicry of protein surfaces
    • Fletcher, S.; Hamilton, A.D. Targeting protein-protein interactions by rational design: mimicry of protein surfaces. J. R. Soc. Interface, 2006, 3, 215-233.
    • (2006) J. R. Soc. Interface , vol.3 , pp. 215-233
    • Fletcher, S.1    Hamilton, A.D.2
  • 28
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin, J.; Chothia, C. The structure of protein-protein recognition sites. J. Biol. Chem., 1990, 265, 16027-16030.
    • (1990) J. Biol. Chem , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 29
    • 0033613904 scopus 로고    scopus 로고
    • Protein surface roughness and small molecular binding sites
    • Pettit, F.K.; Bowie, J.U. Protein surface roughness and small molecular binding sites. J. Mol. Biol., 1999, 285, 1377-1382.
    • (1999) J. Mol. Biol , vol.285 , pp. 1377-1382
    • Pettit, F.K.1    Bowie, J.U.2
  • 30
    • 70349756972 scopus 로고    scopus 로고
    • Atomic interactions and profile of small molecules disrupting protein-protein interfaces: The TIMBAL database
    • Higueruelo, A.P.; Schreyer, A.; Bickerton, G.R.J.; Pitt, W.R.; Groom, C.R.; Blundell, T.L. Atomic interactions and profile of small molecules disrupting protein-protein interfaces: the TIMBAL database. Chem. Biol. Drug Des., 2009, 74, 457-467.
    • (2009) Chem. Biol. Drug Des , vol.74 , pp. 457-467
    • Higueruelo, A.P.1    Schreyer, A.2    Bickerton, G.R.J.3    Pitt, W.R.4    Groom, C.R.5    Blundell, T.L.6
  • 31
    • 1342302339 scopus 로고    scopus 로고
    • Conformational changes associated with protein-protein interactions
    • Goh, C.S.; Milburn, D.; Gerstein, M. Conformational changes associated with protein-protein interactions. Curr. Opin. Struct. Biol., 2004, 14, 104-109.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 104-109
    • Goh, C.S.1    Milburn, D.2    Gerstein, M.3
  • 32
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano, W.L.; Ultsch, M.H.; de Vos, A.M.; Wells, J.A. Convergent solutions to binding at a protein-protein interface. Science, 2000, 287, 1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • de Lano, W.L.1    Ultsch, M.H.2    de Vos, A.M.3    Wells, J.A.4
  • 33
    • 0034660904 scopus 로고    scopus 로고
    • Luxury accommodations: The expanding role of structural plasticity in protein-protein interactions
    • Sundberg, E.J.; Mariuzza, R.A. Luxury accommodations: the expanding role of structural plasticity in protein-protein interactions. Structure, 2000, 8, R137-R142.
    • (2000) Structure , vol.8
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 34
    • 33746076877 scopus 로고    scopus 로고
    • Effects of conformational dynamics on predicted protein druggability
    • Scott, P.B.; Philip, J.H. Effects of conformational dynamics on predicted protein druggability. ChemMedChem, 2006, 1, 70-72.
    • (2006) ChemMedChem , vol.1 , pp. 70-72
    • Scott, P.B.1    Philip, J.H.2
  • 35
    • 34547583152 scopus 로고    scopus 로고
    • Transient pockets on protein surfaces involved in protein-protein interaction
    • Eyrisch, S.; Helms, V. Transient pockets on protein surfaces involved in protein-protein interaction. J. Med. Chem., 2007, 50, 3457-3464.
    • (2007) J. Med. Chem , vol.50 , pp. 3457-3464
    • Eyrisch, S.1    Helms, V.2
  • 36
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young, L.; Jernigan, R.L.; Covell, D.G. A role for surface hydrophobicity in protein-protein recognition. Protein Sci., 1994, 3, 717-729.
    • (1994) Protein Sci , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 37
    • 0026079134 scopus 로고
    • Distribution and complementarity of hydropathy in multisubunit proteins
    • Korn, A.P.; Burnett, R.M. Distribution and complementarity of hydropathy in multisubunit proteins. Proteins: Struct., Funct., Genet., 1991, 9, 37-55.
    • (1991) Proteins: Struct., Funct., Genet , vol.9 , pp. 37-55
    • Korn, A.P.1    Burnett, R.M.2
  • 38
    • 0037422589 scopus 로고    scopus 로고
    • Insufficiently dehydrated hydrogen bonds as determinants of protein interactions
    • Fernandez, A.; Scheraga, H.A. Insufficiently dehydrated hydrogen bonds as determinants of protein interactions. Proc. Natl. Acad. Sci. U. S. A., 2003, 100, 113-118.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 113-118
    • Fernandez, A.1    Scheraga, H.A.2
  • 40
    • 0032981961 scopus 로고    scopus 로고
    • Free energy landscapes of encounter complexes in protein-protein association
    • Camacho, C.J.; Weng, Z.P.; Vajda, S.; DeLisi, C. Free energy landscapes of encounter complexes in protein-protein association. Biophys. J., 1999, 76, 1166-1178.
    • (1999) Biophys. J , vol.76 , pp. 1166-1178
    • Camacho, C.J.1    Weng, Z.P.2    Vajda, S.3    de Lisi, C.4
  • 41
    • 0034039797 scopus 로고    scopus 로고
    • Electrostatic aspects of protein-protein interactions
    • Sheinerman, F.B.; Norel, R.; Honig, B. Electrostatic aspects of protein-protein interactions. Curr. Opin. Struct. Biol., 2000, 10, 153-159.
    • (2000) Curr. Opin. Struct. Biol , vol.10 , pp. 153-159
    • Sheinerman, F.B.1    Norel, R.2    Honig, B.3
  • 42
    • 0032557503 scopus 로고    scopus 로고
    • Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
    • Vijayakumar, M.; Wong, K.Y.; Schreiber, G.; Fersht, A.R.; Szabo, A.; Zhou, H.X. Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar. J. Mol. Biol., 1998, 278, 1015-1024.
    • (1998) J. Mol. Biol , vol.278 , pp. 1015-1024
    • Vijayakumar, M.1    Wong, K.Y.2    Schreiber, G.3    Fersht, A.R.4    Szabo, A.5    Zhou, H.X.6
  • 43
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu, D.; Lin, S.L.; Nussinov, R. Protein binding versus protein folding: the role of hydrophilic bridges in protein associations. J. Mol. Biol., 1997, 265, 68-84.
    • (1997) J. Mol. Biol , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 44
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu, D.; Tsai, C.J.; Nussinov, R. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng., 1997, 10, 999-1012.
    • (1997) Protein Eng , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 45
    • 0011909346 scopus 로고    scopus 로고
    • Macromolecular therapeutics: Emerging strategies for drug discovery in the postgenome era
    • Juliano, R.L.; Astriab-Fisher, A.; Falke, D. Macromolecular therapeutics: emerging strategies for drug discovery in the postgenome era. Mol. Interv., 2001, 1, 40-53.
    • (2001) Mol. Interv , vol.1 , pp. 40-53
    • Juliano, R.L.1    Astriab-Fisher, A.2    Falke, D.3
  • 46
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • Lipinski, C.A. Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods, 2000, 44, 235-249.
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1
  • 47
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C.A.; Lombardo, F.; Dominy, B.W.; Feeney, P.J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev., 1997, 23, 3-25.
    • (1997) Adv. Drug Deliv. Rev , vol.23 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 48
    • 0037609791 scopus 로고    scopus 로고
    • Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces
    • Ma, B.Y.; Elkayam, T.; Wolfson, H.; Nussinov, R. Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces. Proc. Natl. Acad. Sci. USA, 2003, 100, 5772-5777.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5772-5777
    • Ma, B.Y.1    Elkayam, T.2    Wolfson, H.3    Nussinov, R.4
  • 49
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: Progress and challenges
    • DeLano, W.L. Unraveling hot spots in binding interfaces: progress and challenges. Curr. Opin. Struct. Biol., 2002, 12, 14-20.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 14-20
    • de Lano, W.L.1
  • 50
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormonereceptor interface
    • Clackson, T.; Wells, J. A hot spot of binding energy in a hormonereceptor interface. Science, 1995, 267, 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.2
  • 51
    • 0032540358 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone:Receptor complex reveals the molecular basis for receptor affinity
    • Clackson, T.; Ultsch, M.H.; Wells, J.A.; de Vos, A.M. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J. Mol. Biol., 1998, 277, 1111-1128.
    • (1998) J. Mol. Biol , vol.277 , pp. 1111-1128
    • Clackson, T.1    Ultsch, M.H.2    Wells, J.A.3    de Vos, A.M.4
  • 52
    • 0030795733 scopus 로고    scopus 로고
    • Vascular endothelial growth factor: Crystal structure and functional mapping of the kinase domain receptor binding-site
    • Muller, Y.A.; Li, B.; Christinger, H.W.; Wells, J.A.; Cunningham, B.C.; de Vos, A.M. Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding-site. Proc. Natl. Acad. Sci. U. S. A., 1997, 94, 7192-7197.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 7192-7197
    • Muller, Y.A.1    Li, B.2    Christinger, H.W.3    Wells, J.A.4    Cunningham, B.C.5    de Vos, A.M.6
  • 53
    • 33750303565 scopus 로고    scopus 로고
    • Hot-spot mimicry of a cytokine receptor by a small molecule
    • Thanos, C.D.; DeLano, W.L.; Wells, J.A. Hot-spot mimicry of a cytokine receptor by a small molecule. Proc. Natl. Acad. Sci. U. S. A., 2006, 103, 15422-15427.
    • (2006) Proc. Natl. Acad. Sci. U. S. A , vol.103 , pp. 15422-15427
    • Thanos, C.D.1    de Lano, W.L.2    Wells, J.A.3
  • 55
    • 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
  • 56
    • 34447286664 scopus 로고    scopus 로고
    • Trp/Met/Phe hot spots in protein-protein interactions: Potential targets in drug design
    • Ma, B.; Nussinov, R. Trp/Met/Phe hot spots in protein-protein interactions: potential targets in drug design. Curr. Top. Med. Chem. (Sharjah, United Arab Emirates), 2007, 7, 999-1005.
    • (2007) Curr. Top. Med. Chem. (Sharjah, United Arab Emirates) , vol.7 , pp. 999-1005
    • Ma, B.1    Nussinov, R.2
  • 57
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • Ofran, Y.; Rost, B. Analysing six types of protein-protein interfaces. J. Mol. Biol., 2003, 325, 377-387.
    • (2003) J. Mol. Biol , vol.325 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 58
    • 34547573955 scopus 로고    scopus 로고
    • Protein-protein interaction hotspots carved into sequences
    • Ofran, Y.; Rost, B. Protein-protein interaction hotspots carved into sequences. PLoS Comput. Biol., 2007, 3, 1169-1176.
    • (2007) PLoS Comput. Biol , vol.3 , pp. 1169-1176
    • Ofran, Y.1    Rost, B.2
  • 59
    • 0035630691 scopus 로고    scopus 로고
    • Protein-protein interfaces: Mimics and inhibitors
    • Cochran, A.G. Protein-protein interfaces: mimics and inhibitors. Curr. Opin. Chem. Biol., 2001, 5, 654-659.
    • (2001) Curr. Opin. Chem. Biol , vol.5 , pp. 654-659
    • Cochran, A.G.1
  • 61
    • 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
  • 62
    • 70350176700 scopus 로고    scopus 로고
    • From peptides to non-peptide alpha-helix inducers and mimetics
    • Haridas, V. From peptides to non-peptide alpha-helix inducers and mimetics. Eur. J. Org. Chem., 2009, 30, 5112-5128.
    • (2009) Eur. J. Org. Chem , vol.30 , pp. 5112-5128
    • Haridas, V.1
  • 63
    • 84891302493 scopus 로고    scopus 로고
    • Protein secondary structure mimetics as modulators of protein-protein and protein-ligand interactions
    • Yin, H.; Hamilton, A.D. Protein secondary structure mimetics as modulators of protein-protein and protein-ligand interactions. Chem. Biol., 2007, 1, 250-269.
    • (2007) Chem. Biol , vol.1 , pp. 250-269
    • Yin, H.1    Hamilton, A.D.2
  • 64
    • 33745181229 scopus 로고    scopus 로고
    • Development of small molecules designed to modulate protein-protein interactions
    • Che, Y.; Brooks, B.R.; Marshall, G.R. Development of small molecules designed to modulate protein-protein interactions. J. Comput.-Aided Mol. Des., 2006, 20, 109-130.
    • (2006) J. Comput.-Aided Mol. Des , vol.20 , pp. 109-130
    • Che, Y.1    Brooks, B.R.2    Marshall, G.R.3
  • 65
    • 0034801374 scopus 로고    scopus 로고
    • Toward proteomimetics: Terphenyl derivatives as structural and functional mimics of extended regions of an alpha-helix
    • Orner, B.P.; Ernst, J.T.; Hamilton, A.D. Toward proteomimetics: terphenyl derivatives as structural and functional mimics of extended regions of an alpha-helix. J. Am. Chem. Soc., 2001, 123, 5382-5383.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 5382-5383
    • Orner, B.P.1    Ernst, J.T.2    Hamilton, A.D.3
  • 66
  • 71
    • 53349142711 scopus 로고    scopus 로고
    • Enhancing drug discovery through in-silico screening: Strategies to increase true positives retrieval rates
    • Kirchmair, J.; Distinto, S.; Schuster, D.; Spitzer, G.; Langer, T.; Wolber, G. Enhancing drug discovery through in-silico screening: strategies to increase true positives retrieval rates. Curr. Med. Chem., 2008, 15, 2040-2053.
    • (2008) Curr. Med. Chem , vol.15 , pp. 2040-2053
    • Kirchmair, J.1    Distinto, S.2    Schuster, D.3    Spitzer, G.4    Langer, T.5    Wolber, G.6
  • 72
    • 67649124670 scopus 로고    scopus 로고
    • Docking and scoring: Applications to drug discovery in the interactomics era
    • Grosdidier, S.; Fernandez-Recio, J. Docking and scoring: applications to drug discovery in the interactomics era. Expert Opin. Drug Discovery, 2009, 4, 673-686.
    • (2009) Expert Opin. Drug Discovery , vol.4 , pp. 673-686
    • Grosdidier, S.1    Fernandez-Recio, J.2
  • 73
    • 18344382014 scopus 로고    scopus 로고
    • Comparative analysis of protein-bound ligand conformations with respect to Catalyst's conformational space subsampling algorithms
    • Kirchmair, J.; Laggner, C.; Wolber, G.; Langer, T. Comparative analysis of protein-bound ligand conformations with respect to Catalyst's conformational space subsampling algorithms. J. Chem. Inf. Model., 2005, 45, 422-430.
    • (2005) J. Chem. Inf. Model , vol.45 , pp. 422-430
    • Kirchmair, J.1    Laggner, C.2    Wolber, G.3    Langer, T.4
  • 74
    • 37249016887 scopus 로고    scopus 로고
    • Fast and efficient in silico 3D screening: Toward maximum computational efficiency of pharmacophore-based and shape-based approaches
    • Kirchmair, J.; Ristic, S.; Eder, K.; Markt, P.; Wolber, G.; Laggner, C.; Langer, T. Fast and efficient in silico 3D screening: toward maximum computational efficiency of pharmacophore-based and shape-based approaches. J. Chem. Inf. Model., 2007, 47, 2182-2196.
    • (2007) J. Chem. Inf. Model , vol.47 , pp. 2182-2196
    • Kirchmair, J.1    Ristic, S.2    Eder, K.3    Markt, P.4    Wolber, G.5    Laggner, C.6    Langer, T.7
  • 75
    • 33746921247 scopus 로고    scopus 로고
    • Comparative performance assessment of the conformational model generators Omega and Catalyst: A large-scale survey on the retrieval of protein-bound ligand conformations
    • Kirchmair, J.; Wolber, G.; Laggner, C.; Langer, T. Comparative performance assessment of the conformational model generators Omega and Catalyst: a large-scale survey on the retrieval of protein-bound ligand conformations. J. Chem. Inf. Model., 2006, 46, 1848-1861.
    • (2006) J. Chem. Inf. Model , vol.46 , pp. 1848-1861
    • Kirchmair, J.1    Wolber, G.2    Laggner, C.3    Langer, T.4
  • 76
    • 35248863951 scopus 로고    scopus 로고
    • CAESAR: A new conformer generation algorithm based on recursive buildup and local rotational symmetry consideration
    • Li, J.; Ehlers, T.; Sutter, J.; Varma-O'Brien, S.; Kirchmair, J. CAESAR: a new conformer generation algorithm based on recursive buildup and local rotational symmetry consideration. J. Chem. Inf. Model., 2007, 47, 1923-1932.
    • (2007) J. Chem. Inf. Model , vol.47 , pp. 1923-1932
    • Li, J.1    Ehlers, T.2    Sutter, J.3    Varma-O'Brien, S.4    Kirchmair, J.5
  • 77
    • 0032961895 scopus 로고    scopus 로고
    • The particle concept: Placing discrete water molecules during protein-ligand docking predictions
    • Rarey, M.; Kramer, B.; Lengauer, T. The particle concept: placing discrete water molecules during protein-ligand docking predictions. Proteins: Struct., Funct., Genet., 1999, 34, 17-28.
    • (1999) Proteins: Struct., Funct., Genet , vol.34 , pp. 17-28
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3
  • 79
    • 50249094315 scopus 로고    scopus 로고
    • Exploiting ordered waters in molecular docking
    • Huang, N.; Shoichet, B.K. Exploiting ordered waters in molecular docking. J. Med. Chem., 2008, 51, 4862-4865.
    • (2008) J. Med. Chem , vol.51 , pp. 4862-4865
    • Huang, N.1    Shoichet, B.K.2
  • 84
    • 0033674405 scopus 로고    scopus 로고
    • Virtual screening with solvation and ligand-induced complementarity
    • Schnecke, V.; Kuhn, L.A. Virtual screening with solvation and ligand-induced complementarity. Perspect. Drug Discov. Des., 2000, 20, 171-190.
    • (2000) Perspect. Drug Discov. Des , vol.20 , pp. 171-190
    • Schnecke, V.1    Kuhn, L.A.2
  • 85
    • 33750014560 scopus 로고    scopus 로고
    • Solvated docking: Introducing water into the modelling of biomolecular complexes
    • van Dijk, A.D.J.; Bonvin, A. Solvated docking: introducing water into the modelling of biomolecular complexes. Bioinformatics, 2006, 22, 2340-2347.
    • (2006) Bioinformatics , vol.22 , pp. 2340-2347
    • van Dijk, A.D.J.1    Bonvin, A.2
  • 86
    • 56449104546 scopus 로고    scopus 로고
    • Evaluation of different virtual screening programs for docking in a charged binding pocket
    • Deng, W.; Verlinde, C. Evaluation of different virtual screening programs for docking in a charged binding pocket. J. Chem. Inf. Model., 2008, 48, 2010-2020.
    • (2008) J. Chem. Inf. Model , vol.48 , pp. 2010-2020
    • Deng, W.1    Verlinde, C.2
  • 87
    • 67650077384 scopus 로고    scopus 로고
    • Docking ligands into flexible and solvated macromolecules. 4. Are popular scoring functions accurate for this class of proteins?
    • Englebienne, P.; Moitessier, N. Docking ligands into flexible and solvated macromolecules. 4. Are popular scoring functions accurate for this class of proteins? J. Chem. Inf. Model., 2009, 49, 1568-1580.
    • (2009) J. Chem. Inf. Model , vol.49 , pp. 1568-1580
    • Englebienne, P.1    Moitessier, N.2
  • 88
    • 34247197110 scopus 로고    scopus 로고
    • Docking ligands into flexible and solvated macromolecules. 1. Development and validation of FITTED 1.0
    • Corbeil, C.R.; Englebienne, P.; Moitessier, N. Docking ligands into flexible and solvated macromolecules. 1. Development and validation of FITTED 1.0. J. Chem. Inf. Model., 2007, 47, 435-449.
    • (2007) J. Chem. Inf. Model , vol.47 , pp. 435-449
    • Corbeil, C.R.1    Englebienne, P.2    Moitessier, N.3
  • 89
    • 0141907191 scopus 로고    scopus 로고
    • WaterScore: A novel method for distinguishing between bound and displaceable water molecules in the crystal structure of the binding site of proteinligand complexes
    • Garcia-Sosa, A.T.; Mancera, R.L.; Dean, P.M. WaterScore: a novel method for distinguishing between bound and displaceable water molecules in the crystal structure of the binding site of proteinligand complexes. J. Mol. Model., 2003, 9, 172-182.
    • (2003) J. Mol. Model , vol.9 , pp. 172-182
    • Garcia-Sosa, A.T.1    Mancera, R.L.2    Dean, P.M.3
  • 90
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding-sites on biologically important macromolecules
    • Goodford, P.J. A computational procedure for determining energetically favorable binding-sites on biologically important macromolecules. J. Med. Chem., 1985, 28, 849-857.
    • (1985) J. Med. Chem , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 91
    • 0343517556 scopus 로고    scopus 로고
    • Hydrophobicity: Is LogP(o/w) more than the sum of its parts?
    • Kellogg, G.E.; Abraham, D.J. Hydrophobicity: is LogP(o/w) more than the sum of its parts? Eur. J. Med. Chem., 2000, 35, 651-661.
    • (2000) Eur. J. Med. Chem , vol.35 , pp. 651-661
    • Kellogg, G.E.1    Abraham, D.J.2
  • 92
    • 4143131457 scopus 로고    scopus 로고
    • The importance of being exhaustive. Optimization of bridging structural water molecules and water networks in models of biological systems
    • Kellogg, G.E.; Chen, D.L. The importance of being exhaustive. Optimization of bridging structural water molecules and water networks in models of biological systems. Chem. Biodivers., 2004, 1, 98-105.
    • (2004) Chem. Biodivers , vol.1 , pp. 98-105
    • Kellogg, G.E.1    Chen, D.L.2
  • 94
    • 0031592453 scopus 로고    scopus 로고
    • Predicting conserved water-mediated and polar ligand interactions in proteins using a K-nearestneighbors genetic algorithm
    • Raymer, M.L.; Sanschagrin, P.C.; Punch, W.F.; Venkataraman, S.; Goodman, E.D.; Kuhn, L.A. Predicting conserved water-mediated and polar ligand interactions in proteins using a K-nearestneighbors genetic algorithm. J. Mol. Biol., 1997, 265, 445-464.
    • (1997) J. Mol. Biol , vol.265 , pp. 445-464
    • Raymer, M.L.1    Sanschagrin, P.C.2    Punch, W.F.3    Venkataraman, S.4    Goodman, E.D.5    Kuhn, L.A.6
  • 96
    • 0033047007 scopus 로고    scopus 로고
    • SuperStar: A knowledgebased approach for identifying interaction sites in proteins
    • Verdonk, M.L.; Cole, J.C.; Taylor, R. SuperStar: a knowledgebased approach for identifying interaction sites in proteins. J. Mol. Biol., 1999, 289, 1093-1108.
    • (1999) J. Mol. Biol , vol.289 , pp. 1093-1108
    • Verdonk, M.L.1    Cole, J.C.2    Taylor, R.3
  • 97
    • 0035970295 scopus 로고    scopus 로고
    • SuperStar: Improved knowledge-based interaction fields for protein binding sites
    • Verdonk, M.L.; Cole, J.C.; Watson, P.; Gillet, V.; Willett, P. SuperStar: improved knowledge-based interaction fields for protein binding sites. J. Mol. Biol., 2001, 307, 841-859.
    • (2001) J. Mol. Biol , vol.307 , pp. 841-859
    • Verdonk, M.L.1    Cole, J.C.2    Watson, P.3    Gillet, V.4    Willett, P.5
  • 98
    • 35449002345 scopus 로고    scopus 로고
    • Analytical ULTracentrifugation: Sedimentation Velocity and Sedimentation Equilibrium
    • In, Elsevier Academic Press Inc: San Diego
    • Cole, J.L.; Lary, J.W.; Moody, T.P.; Laue, T.M. Analytical ULTracentrifugation: Sedimentation Velocity and Sedimentation Equilibrium. In Biophysical Tools for Biologists: Vol 1 in Vitro Techniques; Elsevier Academic Press Inc: San Diego, 2008; Vol. 84, pp. 143-179.
    • (2008) Biophysical Tools for Biologists: Vol 1 in Vitro Techniques , vol.84 , pp. 143-179
    • Cole, J.L.1    Lary, J.W.2    Moody, T.P.3    Laue, T.M.4
  • 99
    • 33750565735 scopus 로고    scopus 로고
    • Biomolecular interaction analysis in drug discovery using surface plasmon resonance technology
    • Huber, W.; Mueller, F. Biomolecular interaction analysis in drug discovery using surface plasmon resonance technology. Curr. Pharm. Des., 2006, 12, 3999-4021.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 3999-4021
    • Huber, W.1    Mueller, F.2
  • 100
    • 47549106882 scopus 로고    scopus 로고
    • Applications of isothermal titration calorimetry in protein science
    • Liang, Y. Applications of isothermal titration calorimetry in protein science. Acta Biochim. Biophys. Sin., 2008, 40, 565-576.
    • (2008) Acta Biochim. Biophys. Sin , vol.40 , pp. 565-576
    • Liang, Y.1
  • 101
    • 33846070699 scopus 로고    scopus 로고
    • Discovery of inhibitors of protein-protein interactions from combinatorial libraries
    • Vicent, M.J.; Perez-Paya, E.; Orzaez, M. Discovery of inhibitors of protein-protein interactions from combinatorial libraries. Curr. Top. Med. Chem., 2007, 7, 83-95.
    • (2007) Curr. Top. Med. Chem , vol.7 , pp. 83-95
    • Vicent, M.J.1    Perez-Paya, E.2    Orzaez, M.3
  • 103
    • 0034687234 scopus 로고    scopus 로고
    • Discovery of novel p-arylthio cinnamides as antagonists of leukocyte function-associated antigen-1/intracellular adhesion molecule-1 interaction. 1. Identification of an additional binding pocket based on an anilino diaryl sulfide lead
    • Liu, G.; Link, J.T.; Pei, Z.; Reilly, E.B.; Leitza, S.; Nguyen, B.; Marsh, K.C.; Okasinski, G.F.; von Geldern, T.W.; Ormes, M.; Fowler, K.; Gallatin, M. Discovery of novel p-arylthio cinnamides as antagonists of leukocyte function-associated antigen-1/intracellular adhesion molecule-1 interaction. 1. Identification of an additional binding pocket based on an anilino diaryl sulfide lead. J. Med. Chem., 2000, 43, 4025-4040.
    • (2000) J. Med. Chem , vol.43 , pp. 4025-4040
    • Liu, G.1    Link, J.T.2    Pei, Z.3    Reilly, E.B.4    Leitza, S.5    Nguyen, B.6    Marsh, K.C.7    Okasinski, G.F.8    von Geldern, T.W.9    Ormes, M.10    Fowler, K.11    Gallatin, M.12
  • 105
    • 2942597981 scopus 로고    scopus 로고
    • The design of drug candidate molecules as selective inhibitors of therapeutically relevant protein kinases
    • Fischer, P.M. The design of drug candidate molecules as selective inhibitors of therapeutically relevant protein kinases. Curr. Med. Chem., 2004, 11, 1563-1583.
    • (2004) Curr. Med. Chem , vol.11 , pp. 1563-1583
    • Fischer, P.M.1
  • 106
    • 0030031766 scopus 로고    scopus 로고
    • Inhibition of the Abl protein-tyrosine kinase in vitro and in vivo by a 2-phenylaminopyrimidine derivative
    • Buchdunger, E.; Zimmermann, J.; Mett, H.; Meyer, T.; Muller, M.; Druker, B.J.; Lydon, N.B. Inhibition of the Abl protein-tyrosine kinase in vitro and in vivo by a 2-phenylaminopyrimidine derivative. Cancer Res., 1996, 56, 100-104.
    • (1996) Cancer Res , vol.56 , pp. 100-104
    • Buchdunger, E.1    Zimmermann, J.2    Mett, H.3    Meyer, T.4    Muller, M.5    Druker, B.J.6    Lydon, N.B.7
  • 107
    • 0033816156 scopus 로고    scopus 로고
    • Abl protein-tyrosine kinase inhibitor STI571 inhibits in vitro signal transduction mediated by c-Kit and platelet-derived growth factor receptors
    • Buchdunger, E.; Cioffi, C.L.; Law, N.; Stover, D.; Ohno-Jones, S.; Druker, B.J.; Lydon, N.B. Abl protein-tyrosine kinase inhibitor STI571 inhibits in vitro signal transduction mediated by c-Kit and platelet-derived growth factor receptors. J. Pharmacol. Exp. Ther., 2000, 295, 139-145.
    • (2000) J. Pharmacol. Exp. Ther , vol.295 , pp. 139-145
    • Buchdunger, E.1    Cioffi, C.L.2    Law, N.3    Stover, D.4    Ohno-Jones, S.5    Druker, B.J.6    Lydon, N.B.7
  • 108
    • 70450197345 scopus 로고    scopus 로고
    • Sunitinib: A multitargeted receptor tyrosine kinase inhibitor in the era of molecular cancer therapies
    • Papaetis, G.S.; Syrigos, K.N. Sunitinib: a multitargeted receptor tyrosine kinase inhibitor in the era of molecular cancer therapies. BioDrugs, 2009, 23, 377-389.
    • (2009) BioDrugs , vol.23 , pp. 377-389
    • Papaetis, G.S.1    Syrigos, K.N.2
  • 110
    • 64049093006 scopus 로고    scopus 로고
    • Non-ATP competitive protein kinase inhibitors as anti-tumor therapeutics
    • Kirkland, L.O.; McInnes, C. Non-ATP competitive protein kinase inhibitors as anti-tumor therapeutics. Biochem. Pharmacol., 2009, 77, 1561-1571.
    • (2009) Biochem. Pharmacol , vol.77 , pp. 1561-1571
    • Kirkland, L.O.1    McInnes, C.2
  • 111
    • 0033021061 scopus 로고    scopus 로고
    • MEK Wars, a new front in the battle against cancer
    • Duesbery, N.S.; Webb, C.P.; Woude, G.F.V. MEK Wars, a new front in the battle against cancer. Nat. Med., 1999, 5, 736-737.
    • (1999) Nat. Med , vol.5 , pp. 736-737
    • Duesbery, N.S.1    Webb, C.P.2    Woude, G.F.V.3
  • 112
    • 0036400204 scopus 로고    scopus 로고
    • Ras-MAP kinase signaling pathways and control of cell proliferation: Relevance to cancer therapy
    • Shapiro, P. Ras-MAP kinase signaling pathways and control of cell proliferation: Relevance to cancer therapy. Crit. Rev. Clin. Lab. Sci., 2002, 39, 285-330.
    • (2002) Crit. Rev. Clin. Lab. Sci , vol.39 , pp. 285-330
    • Shapiro, P.1
  • 113
    • 22244490088 scopus 로고    scopus 로고
    • Identification of novel extracellular signal-regulated kinase docking domain inhibitors
    • Hancock, C.N.; Macias, A.; Lee, E.K.; Yu, S.Y.; MacKerell, A.D.; Shapiro, P. Identification of novel extracellular signal-regulated kinase docking domain inhibitors. J. Med. Chem., 2005, 48, 4586-4595.
    • (2005) J. Med. Chem , vol.48 , pp. 4586-4595
    • Hancock, C.N.1    Macias, A.2    Lee, E.K.3    Yu, S.Y.4    McKerell, A.D.5    Shapiro, P.6
  • 115
    • 71749119790 scopus 로고    scopus 로고
    • Structure-activity relationship (SAR) studies of 3-(2-amino-ethyl)-5-(4-ethoxybenzylidene)-thiazolidine-2,4-dione: Development of potential substrate-specific ERK1/2 inhibitors
    • Li, Q.; Al-Ayoubi, A.; Guo, T.; Zheng, H.; Sarkar, A.; Nguyen, T.; Eblen, S.T.; Grant, S.; Kellogg, G.E.; Zhang, S. Structure-activity relationship (SAR) studies of 3-(2-amino-ethyl)-5-(4-ethoxybenzylidene)-thiazolidine-2,4-dione: development of potential substrate-specific ERK1/2 inhibitors. Bioorg. Med. Chem. Lett., 2009, 19, 6042-6046.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , pp. 6042-6046
    • Li, Q.1    Al-Ayoubi, A.2    Guo, T.3    Zheng, H.4    Sarkar, A.5    Nguyen, T.6    Eblen, S.T.7    Grant, S.8    Kellogg, G.E.9    Zhang, S.10
  • 116
    • 45849109148 scopus 로고    scopus 로고
    • Src family kinases as potential therapeutic targets for malignancies and immunological disorders
    • Benati, D.; Baldari, C.T. Src family kinases as potential therapeutic targets for malignancies and immunological disorders. Curr. Med. Chem., 2008, 15, 1154-1165.
    • (2008) Curr. Med. Chem , vol.15 , pp. 1154-1165
    • Benati, D.1    Baldari, C.T.2
  • 117
    • 0030472640 scopus 로고    scopus 로고
    • Determination of affinities for lck SH2 binding peptides using a sensitive fluorescence assay: Comparison between the pYEEIP and pYQPQP consensus sequences reveals context-dependent binding specificity
    • Cousins-Wasti, R.C.; Ingraham, R.H.; Morelock, M.M.; Grygon, C.A. Determination of affinities for lck SH2 binding peptides using a sensitive fluorescence assay: Comparison between the pYEEIP and pYQPQP consensus sequences reveals context-dependent binding specificity. Biochemistry, 1996, 35, 16746-16752.
    • (1996) Biochemistry , vol.35 , pp. 16746-16752
    • Cousins-Wasti, R.C.1    Ingraham, R.H.2    Morelock, M.M.3    Grygon, C.A.4
  • 118
    • 3042590341 scopus 로고    scopus 로고
    • Identification of non-phosphate-containing small molecular weight inhibitors of the tyrosine kinase p56 Lck SH2 domain via in silico screening against the pY+3 binding site
    • Huang, N.; Nagarsekar, A.; Xia, G.J.; Hayashi, J.; MacKerell, A.D. Identification of non-phosphate-containing small molecular weight inhibitors of the tyrosine kinase p56 Lck SH2 domain via in silico screening against the pY+3 binding site. J. Med. Chem., 2004, 47, 3502-3511.
    • (2004) J. Med. Chem , vol.47 , pp. 3502-3511
    • Huang, N.1    Nagarsekar, A.2    Xia, G.J.3    Hayashi, J.4    McKerell, A.D.5
  • 119
    • 28944440837 scopus 로고    scopus 로고
    • Lead validation and SAR development via chemical similarity searching: Application to compounds targeting the pY+3 site of the SH2 domain of p56(lck)
    • Macias, A.T.; Mia, M.Y.; Xia, G.J.; Hayashi, J.; MacKerell, A.D. Lead validation and SAR development via chemical similarity searching: application to compounds targeting the pY+3 site of the SH2 domain of p56(lck). J. Chem. Inf. Model., 2005, 45, 1759-1766.
    • (2005) J. Chem. Inf. Model , vol.45 , pp. 1759-1766
    • Macias, A.T.1    Mia, M.Y.2    Xia, G.J.3    Hayashi, J.4    McKerell, A.D.5
  • 120
    • 0038068134 scopus 로고    scopus 로고
    • Rosmarinic acid inhibits TCR-induced T cell activation and proliferation in an Lck-dependent manner
    • Won, J.; Hur, Y.G.; Hur, E.M.; Park, S.H.; Kang, M.A.; Choi, Y.; Park, C.; Lee, K.H.; Yun, Y. Rosmarinic acid inhibits TCR-induced T cell activation and proliferation in an Lck-dependent manner. Eur. J. Immunol., 2003, 33, 870-879.
    • (2003) Eur. J. Immunol , vol.33 , pp. 870-879
    • Won, J.1    Hur, Y.G.2    Hur, E.M.3    Park, S.H.4    Kang, M.A.5    Choi, Y.6    Park, C.7    Lee, K.H.8    Yun, Y.9
  • 121
    • 34247503274 scopus 로고    scopus 로고
    • The structure-activity relationship of the series of nonpeptide small antagonists for p561ck SH2 domain
    • Park, S.H.; Oh, H.S.; Kang, M.A.; Cho, H.J.; Prasad, J.B.; Won, J.; Lee, K.H. The structure-activity relationship of the series of nonpeptide small antagonists for p561ck SH2 domain. Bioorg. Med. Chem., 2007, 15, 3938-3950.
    • (2007) Bioorg. Med. Chem , vol.15 , pp. 3938-3950
    • Park, S.H.1    Oh, H.S.2    Kang, M.A.3    Cho, H.J.4    Prasad, J.B.5    Won, J.6    Lee, K.H.7
  • 122
    • 43149093993 scopus 로고    scopus 로고
    • Inhibition of polo-like kinase 1 by blocking polo-box domaindependent protein-protein interactions
    • Reindl, W.G.; Yuan, J.P.; Kramer, A.; Strebhardt, K.; Berg, T. Inhibition of polo-like kinase 1 by blocking polo-box domaindependent protein-protein interactions. Chem. Biol., 2008, 15, 459-466.
    • (2008) Chem. Biol , vol.15 , pp. 459-466
    • Reindl, W.G.1    Yuan, J.P.2    Kramer, A.3    Strebhardt, K.4    Berg, T.5
  • 123
    • 67650472492 scopus 로고    scopus 로고
    • Inhibition of polo-like kinase 1 by blocking polo-box domain-dependent protein-protein interactions
    • Reindl, W.; Yuan, J.P.; Kramer, A.; Strebhardt, K.; Berg, T. Inhibition of polo-like kinase 1 by blocking polo-box domain-dependent protein-protein interactions. ChemBioChem, 2009, 10, 1145-1148.
    • (2009) ChemBioChem , vol.10 , pp. 1145-1148
    • Reindl, W.1    Yuan, J.P.2    Kramer, A.3    Strebhardt, K.4    Berg, T.5
  • 124
    • 59049093510 scopus 로고    scopus 로고
    • Deficiency in chromosome congression by the inhibition of Plk1 polo box domain-dependent recognition
    • Watanabe, N.; Sekine, T.; Takagi, M.; Iwasaki, J.; Imamoto, N.; Kawasaki, H.; Osada, H. Deficiency in chromosome congression by the inhibition of Plk1 polo box domain-dependent recognition. J. Biol. Chem., 2009, 284, 2344-2353.
    • (2009) J. Biol. Chem , vol.284 , pp. 2344-2353
    • Watanabe, N.1    Sekine, T.2    Takagi, M.3    Iwasaki, J.4    Imamoto, N.5    Kawasaki, H.6    Osada, H.7
  • 126
    • 0025885070 scopus 로고
    • Isolation of the human cdk2 gene that encodes the cyclin A-and adenovirus E1A-associated p33 kinase
    • Tsai, L.H.; Harlow, E.; Meyerson, M. Isolation of the human cdk2 gene that encodes the cyclin A-and adenovirus E1A-associated p33 kinase. Nature, 1991, 353, 174-177.
    • (1991) Nature , vol.353 , pp. 174-177
    • Tsai, L.H.1    Harlow, E.2    Meyerson, M.3
  • 127
    • 0036830109 scopus 로고    scopus 로고
    • Highly potent p21(WAF1)-derived peptide inhibitors of CDK-mediated pRb phosphorylation: Delineation and structural insight into their interactions with cyclin A
    • Zheleva, D.I.; McInnes, C.; Gavine, A.L.; Zhelev, N.Z.; Fischer, P.M.; Lane, D.P. Highly potent p21(WAF1)-derived peptide inhibitors of CDK-mediated pRb phosphorylation: delineation and structural insight into their interactions with cyclin A. J. Pept. Res., 2002, 60, 257-270.
    • (2002) J. Pept. Res , vol.60 , pp. 257-270
    • Zheleva, D.I.1    McInnes, C.2    Gavine, A.L.3    Zhelev, N.Z.4    Fischer, P.M.5    Lane, D.P.6
  • 128
    • 0037212102 scopus 로고    scopus 로고
    • LigandFit: A novel method for the shape-directed rapid docking of ligands to protein active sites
    • Venkatachalam, C.M.; Jiang, X.; Oldfield, T.; Waldman, M. LigandFit: a novel method for the shape-directed rapid docking of ligands to protein active sites. J. Mol. Graph. Modell., 2003, 21, 289-307.
    • (2003) J. Mol. Graph. Modell , vol.21 , pp. 289-307
    • Venkatachalam, C.M.1    Jiang, X.2    Oldfield, T.3    Waldman, M.4
  • 129
    • 36749037936 scopus 로고    scopus 로고
    • Targeting the oncogenic protein kinase C-l signalling pathway for the treatment of cancer
    • Fields, A.P.; Frederick, L.A.; Regala, R.P. Targeting the oncogenic protein kinase C-l signalling pathway for the treatment of cancer. Biochem. Soc. Trans., 2007, 35, 996-1000.
    • (2007) Biochem. Soc. Trans , vol.35 , pp. 996-1000
    • Fields, A.P.1    Frederick, L.A.2    Regala, R.P.3
  • 130
    • 70350236536 scopus 로고    scopus 로고
    • Atypical protein kinase C iota is required for bronchioalveolar stem cell expansion and lung tumorigenesis
    • Regala, R.P.; Davis, R.K.; Kunz, A.; Khoor, A.; Leitges, M.; Fields, A.P. Atypical protein kinase C iota is required for bronchioalveolar stem cell expansion and lung tumorigenesis. Cancer Res., 2009, 69, 7603-7611.
    • (2009) Cancer Res , vol.69 , pp. 7603-7611
    • Regala, R.P.1    Davis, R.K.2    Kunz, A.3    Khoor, A.4    Leitges, M.5    Fields, A.P.6
  • 132
    • 32944470373 scopus 로고    scopus 로고
    • A novel small-molecule inhibitor of protein kinase C iota blocks transformed growth of non-small-cell lung cancer cells
    • Stallings-Mann, M.; Jamieson, L.; Regala, R.P.; Weems, C.; Murray, N.R.; Fields, A.P. A novel small-molecule inhibitor of protein kinase C iota blocks transformed growth of non-small-cell lung cancer cells. Cancer Res., 2006, 66, 1767-1774.
    • (2006) Cancer Res , vol.66 , pp. 1767-1774
    • Stallings-Mann, M.1    Jamieson, L.2    Regala, R.P.3    Weems, C.4    Murray, N.R.5    Fields, A.P.6
  • 134
    • 0027418816 scopus 로고
    • Overexpression of protein kinase C-delta and-epsilon in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity
    • Mischak, H.; Goodnight, J.; Kolch, W.; Martinybaron, G.; Schaechtle, C.; Kazanietz, M.G.; Blumberg, P.M.; Pierce, J.H.; Mushinski, J.F. Overexpression of protein kinase C-delta and-epsilon in NIH 3T3 cells induces opposite effects on growth, morphology, anchorage dependence, and tumorigenicity. J. Biol. Chem., 1993, 268, 6090-6096.
    • (1993) J. Biol. Chem , vol.268 , pp. 6090-6096
    • Mischak, H.1    Goodnight, J.2    Kolch, W.3    Martinybaron, G.4    Schaechtle, C.5    Kazanietz, M.G.6    Blumberg, P.M.7    Pierce, J.H.8    Mushinski, J.F.9
  • 135
    • 0030784596 scopus 로고    scopus 로고
    • Experimental diabetes is associated with functional activation of protein kinase C epsilon and phosphorylation of troponin I in the heart, which are prevented by angiotensin II receptor blockade
    • Malhotra, A.; Reich, D.; Nakouzi, A.; Sanghi, V.; Geenen, D.L.; Buttrick, P.M. Experimental diabetes is associated with functional activation of protein kinase C epsilon and phosphorylation of troponin I in the heart, which are prevented by angiotensin II receptor blockade. Circ. Res., 1997, 81, 1027-1033.
    • (1997) Circ. Res , vol.81 , pp. 1027-1033
    • Malhotra, A.1    Reich, D.2    Nakouzi, A.3    Sanghi, V.4    Geenen, D.L.5    Buttrick, P.M.6
  • 137
    • 0034705485 scopus 로고    scopus 로고
    • Transgenic overexpression of constitutively active protein kinase C epsilon causes concentric cardiac hypertrophy
    • Takeishi, Y.; Ping, P.; Bolli, R.; Kirkpatrick, D.L.; Hoit, B.D.; Walsh, R.A. Transgenic overexpression of constitutively active protein kinase C epsilon causes concentric cardiac hypertrophy Circ. Res., 2000, 86, 1218-1223.
    • (2000) Circ. Res , vol.86 , pp. 1218-1223
    • Takeishi, Y.1    Ping, P.2    Bolli, R.3    Kirkpatrick, D.L.4    Hoit, B.D.5    Walsh, R.A.6
  • 138
    • 0033166535 scopus 로고    scopus 로고
    • Specific involvement of PKC-epsilon in sensitization of the neuronal response to painful heat
    • Cesare, P.; Dekker, L.V.; Sardini, A.; Parker, P.J.; McNaughton, P.A. Specific involvement of PKC-epsilon in sensitization of the neuronal response to painful heat. Neuron, 1999, 23, 617-624.
    • (1999) Neuron , vol.23 , pp. 617-624
    • Cesare, P.1    Dekker, L.V.2    Sardini, A.3    Parker, P.J.4    McNaughton, P.A.5
  • 140
    • 0034746792 scopus 로고    scopus 로고
    • Protein kinase C epsilon is required for macrophage activation and defense against bacterial infection
    • Castrillo, A.; Pennington, D.J.; Otto, F.; Parker, P.J.; Owen, M.J.; Bosca, L. Protein kinase C epsilon is required for macrophage activation and defense against bacterial infection. J. Exp. Med., 2001, 194, 1231-1242.
    • (2001) J. Exp. Med , vol.194 , pp. 1231-1242
    • Castrillo, A.1    Pennington, D.J.2    Otto, F.3    Parker, P.J.4    Owen, M.J.5    Bosca, L.6
  • 141
    • 0030670399 scopus 로고    scopus 로고
    • The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase C epsilon
    • Csukai, M.; Chen, C.H.; DeMatteis, M.A.; Mochly-Rosen, D. The coatomer protein beta'-COP, a selective binding protein (RACK) for protein kinase C epsilon. J. Biol. Chem., 1997, 272, 29200-29206.
    • (1997) J. Biol. Chem , vol.272 , pp. 29200-29206
    • Csukai, M.1    Chen, C.H.2    de Matteis, M.A.3    Mochly-Rosen, D.4
  • 142
    • 0029745535 scopus 로고    scopus 로고
    • A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function
    • Johnson, J.A.; Gray, M.O.; Chen, C.H.; Mochly-Rosen, D. A protein kinase C translocation inhibitor as an isozyme-selective antagonist of cardiac function. J. Biol. Chem., 1996, 271, 24962-24966.
    • (1996) J. Biol. Chem , vol.271 , pp. 24962-24966
    • Johnson, J.A.1    Gray, M.O.2    Chen, C.H.3    Mochly-Rosen, D.4
  • 143
    • 79952292102 scopus 로고    scopus 로고
    • Barbituric acid derivative BAS 02104951 inhibits PKCepsilon, PKCeta, PKCepsilon/RACK2 interaction, Elk-1 phosphorylation in HeLa and PKCepsilon and eta translocation in PC3 cells following TPA-induction
    • Gruber, P.; Rechfeld, F.; Kirchmair, J.; Hauser, N.; Boehler, M.; Garczarczyk, D.; Langer, T.; Hofmann, J. Barbituric acid derivative BAS 02104951 inhibits PKCepsilon, PKCeta, PKCepsilon/RACK2 interaction, Elk-1 phosphorylation in HeLa and PKCepsilon and eta translocation in PC3 cells following TPA-induction. J. Biochem., 2011, 149, 331-336.
    • (2011) J. Biochem , vol.149 , pp. 331-336
    • Gruber, P.1    Rechfeld, F.2    Kirchmair, J.3    Hauser, N.4    Boehler, M.5    Garczarczyk, D.6    Langer, T.7    Hofmann, J.8
  • 144
    • 0034177264 scopus 로고    scopus 로고
    • Antagonists of protein-protein interactions
    • Cochran, A.G. Antagonists of protein-protein interactions. Chem. Biol., 2000, 7, R85-R94.
    • (2000) Chem. Biol , vol.7
    • Cochran, A.G.1
  • 145
    • 33947173624 scopus 로고    scopus 로고
    • Inhibitors of protein-protein interactions as potential drugs
    • Veselovsky, A.V.; Archakov, A.I. Inhibitors of protein-protein interactions as potential drugs. Curr. Comput.-Aided Drug Des., 2007, 3, 51-58.
    • (2007) Curr. Comput.-Aided Drug Des , vol.3 , pp. 51-58
    • Veselovsky, A.V.1    Archakov, A.I.2
  • 146
    • 0141807008 scopus 로고
    • The CD4 and CD8 antigens are coupled to a proteintyrosine kinase (p56lck) that phosphorylates the CD3 complex
    • Barber, E.K.; Dasgupta, J.D.; Schlossman, S.F.; Trevillyan, J.M.; Rudd, C.E. The CD4 and CD8 antigens are coupled to a proteintyrosine kinase (p56lck) that phosphorylates the CD3 complex. Proc. Natl. Acad. Sci. U. S. A., 1989, 86, 3277-3281.
    • (1989) Proc. Natl. Acad. Sci. U. S. A , vol.86 , pp. 3277-3281
    • Barber, E.K.1    Dasgupta, J.D.2    Schlossman, S.F.3    Trevillyan, J.M.4    Rudd, C.E.5
  • 147
    • 0023521229 scopus 로고
    • Interaction between CD4 and class II MHC molecules mediates cell adhesion
    • Doyle, C.; Strominger, J.L. Interaction between CD4 and class II MHC molecules mediates cell adhesion. Nature, 1987, 330, 256-259.
    • (1987) Nature , vol.330 , pp. 256-259
    • Doyle, C.1    Strominger, J.L.2
  • 149
    • 0026563077 scopus 로고
    • MHC class II interaction with CD4 mediated by a region analogous to the MHC class I binding site for CD8
    • Konig, R.; Huang, L.Y.; Germain, R.N. MHC class II interaction with CD4 mediated by a region analogous to the MHC class I binding site for CD8. Nature, 1992, 356, 796-798.
    • (1992) Nature , vol.356 , pp. 796-798
    • Konig, R.1    Huang, L.Y.2    Germain, R.N.3
  • 150
    • 0023737931 scopus 로고
    • The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck
    • Veillette, A.; Bookman, M.A.; Horak, E.M.; Bolen, J.B. The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck. Cell, 1988, 55, 301-308.
    • (1988) Cell , vol.55 , pp. 301-308
    • Veillette, A.1    Bookman, M.A.2    Horak, E.M.3    Bolen, J.B.4
  • 152
    • 36048932729 scopus 로고    scopus 로고
    • J2 prolongs the corneal allograft survival through inhibition of the CD4(+) T cell-mediated response in vivo
    • Xiao, H.; Zhang, H.; Yu, Z.Y.; Zhang, L.; Yu, M.; Huang, Y.F.; Li, S.; Shen, B.F.; Li, Y. J2 prolongs the corneal allograft survival through inhibition of the CD4(+) T cell-mediated response in vivo. Transplant Immunol., 2007, 18, 130-137.
    • (2007) Transplant Immunol , vol.18 , pp. 130-137
    • Xiao, H.1    Zhang, H.2    Yu, Z.Y.3    Zhang, L.4    Yu, M.5    Huang, Y.F.6    Li, S.7    Shen, B.F.8    Li, Y.9
  • 154
    • 2542643984 scopus 로고    scopus 로고
    • Integrating fragment assembly and biophysical methods in the chemical advancement of small-molecule antagonists of IL-2: An approach for inhibiting protein-protein interactions
    • Raimundo, B.C.; Oslob, J.D.; Braisted, A.C.; Hyde, J.; McDowell, R.S.; Randal, M.; Waal, N.D.; Wilkinson, J.; Yu, C.H.; Arkin, M.R. Integrating fragment assembly and biophysical methods in the chemical advancement of small-molecule antagonists of IL-2: an approach for inhibiting protein-protein interactions. J. Med. Chem., 2004, 47, 3111-3130.
    • (2004) J. Med. Chem , vol.47 , pp. 3111-3130
    • Raimundo, B.C.1    Oslob, J.D.2    Braisted, A.C.3    Hyde, J.4    McDowell, R.S.5    Randal, M.6    Waal, N.D.7    Wilkinson, J.8    Yu, C.H.9    Arkin, M.R.10
  • 156
    • 33846036984 scopus 로고    scopus 로고
    • ICG-001, a novel small molecule regulator of TCF/beta-catenin transcription
    • Eguchi, M.; Nguyen, C.; Lee, S.C.; Kahn, M. ICG-001, a novel small molecule regulator of TCF/beta-catenin transcription. Med. Chem., 2005, 1, 467-472.
    • (2005) Med. Chem , vol.1 , pp. 467-472
    • Eguchi, M.1    Nguyen, C.2    Lee, S.C.3    Kahn, M.4
  • 158
    • 0031181346 scopus 로고    scopus 로고
    • QXP: Powerful, rapid computer algorithms for structure-based drug design
    • McMartin, C.; Bohacek, R.S. QXP: Powerful, rapid computer algorithms for structure-based drug design. J. Comput.-Aided Mol. Des., 1997, 11, 333-344.
    • (1997) J. Comput.-Aided Mol. Des , vol.11 , pp. 333-344
    • McMartin, C.1    Bohacek, R.S.2
  • 161
    • 0028899283 scopus 로고
    • Biochemical properties and biological effects of p53
    • Haffner, R.; Oren, M. Biochemical properties and biological effects of p53. Curr. Opin. Genet. Dev., 1995, 5, 84-90.
    • (1995) Curr. Opin. Genet. Dev , vol.5 , pp. 84-90
    • Haffner, R.1    Oren, M.2
  • 162
    • 33646807832 scopus 로고    scopus 로고
    • The P53 pathway: What questions remain to be explored?
    • Levine, A.J.; Hu, W.; Feng, Z. The P53 pathway: what questions remain to be explored? Cell Death Differ., 2006, 13, 1027-1036.
    • (2006) Cell Death Differ , vol.13 , pp. 1027-1036
    • Levine, A.J.1    Hu, W.2    Feng, Z.3
  • 168
    • 35048895357 scopus 로고    scopus 로고
    • Targeting protein-protein interactions: Lessons from p53/MDM2
    • Murray, J.K.; Gellman, S.H. Targeting protein-protein interactions: lessons from p53/MDM2. Biopolymers, 2007, 88, 657-686.
    • (2007) Biopolymers , vol.88 , pp. 657-686
    • Murray, J.K.1    Gellman, S.H.2
  • 169
    • 0033945124 scopus 로고    scopus 로고
    • Structure of the negative regulatory domain of p53 bound to S100B(beta beta)
    • Rustandi, R.R.; Baldisseri, D.M.; Weber, D.J. Structure of the negative regulatory domain of p53 bound to S100B(beta beta). Nat. Struct. Biol., 2000, 7, 570-574.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 570-574
    • Rustandi, R.R.1    Baldisseri, D.M.2    Weber, D.J.3
  • 170
    • 4744357517 scopus 로고    scopus 로고
    • Identification and characterization of small molecule inhibitors of the calcium dependent S100B-p53 tumor suppressor interaction
    • Markowitz, J.; Chen, J.; Gitti, R.; Baldisseri, D.M.; Pan, Y.P.; Udan, R.; Carrier, F.; MacKerell, A.D.; Weber, D.J. Identification and characterization of small molecule inhibitors of the calcium dependent S100B-p53 tumor suppressor interaction. J. Med. Chem., 2004, 47, 5085-5093.
    • (2004) J. Med. Chem , vol.47 , pp. 5085-5093
    • Markowitz, J.1    Chen, J.2    Gitti, R.3    Baldisseri, D.M.4    Pan, Y.P.5    Udan, R.6    Carrier, F.7    McKerell, A.D.8    Weber, D.J.9
  • 171
    • 0034722884 scopus 로고    scopus 로고
    • Bcl-2 family proteins as targets for anticancer drug design
    • Huang, Z.W. Bcl-2 family proteins as targets for anticancer drug design. Oncogene, 2000, 19, 6627-6631.
    • (2000) Oncogene , vol.19 , pp. 6627-6631
    • Huang, Z.W.1
  • 172
    • 0035154832 scopus 로고    scopus 로고
    • Death by design: The big debut of small molecules
    • Zheng, T.S. Death by design: the big debut of small molecules. Nat. Cell Biol., 2001, 3, E43-E46.
    • (2001) Nat. Cell Biol , vol.3
    • Zheng, T.S.1
  • 173
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams, J.M.; Cory, S. The Bcl-2 protein family: arbiters of cell survival. Science, 1998, 281, 1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 176
    • 0037344678 scopus 로고    scopus 로고
    • Therapeutic activation of caspases in cancer: A question of selectivity
    • Beauparlant, P.; Shore, G.C. Therapeutic activation of caspases in cancer: a question of selectivity. Curr. Opin. Drug Discov. Dev., 2003, 6, 179-187.
    • (2003) Curr. Opin. Drug Discov. Dev , vol.6 , pp. 179-187
    • Beauparlant, P.1    Shore, G.C.2
  • 179
    • 34447558127 scopus 로고    scopus 로고
    • Exploration of backbone space in foldamers containing alpha-and betaamino acid residues: Developing protease-resistant oligomers that bind tightly to the BH3-recognition cleft of Bcl-x(L)
    • Sadowsky, J.D.; Murray, J.K.; Tomita, Y.; Gellman, S.H. Exploration of backbone space in foldamers containing alpha-and betaamino acid residues: Developing protease-resistant oligomers that bind tightly to the BH3-recognition cleft of Bcl-x(L). ChemBioChem, 2007, 8, 903-916.
    • (2007) ChemBioChem , vol.8 , pp. 903-916
    • Sadowsky, J.D.1    Murray, J.K.2    Tomita, Y.3    Gellman, S.H.4
  • 182
    • 63149129655 scopus 로고    scopus 로고
    • Bcl-2 inhibitors: Targeting mitochondrial apoptotic pathways in cancer therapy
    • Kang, M.H.; Reynolds, C.P. Bcl-2 inhibitors: targeting mitochondrial apoptotic pathways in cancer therapy. Clin. Cancer Res., 2009, 15, 1126-1132.
    • (2009) Clin. Cancer Res , vol.15 , pp. 1126-1132
    • Kang, M.H.1    Reynolds, C.P.2
  • 183
    • 0030746636 scopus 로고    scopus 로고
    • A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
    • Ambrosini, G.; Adida, C.; Altieri, D.C. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat. Med., 1997, 3, 917-921.
    • (1997) Nat. Med , vol.3 , pp. 917-921
    • Ambrosini, G.1    Adida, C.2    Altieri, D.C.3
  • 184
    • 0142215849 scopus 로고    scopus 로고
    • Blocking survivin to kill cancer cells
    • Altieri, D.C. Blocking survivin to kill cancer cells. Methods Mol. Biol., 2003, 223, 533-542.
    • (2003) Methods Mol. Biol , vol.223 , pp. 533-542
    • Altieri, D.C.1
  • 185
    • 0642317016 scopus 로고    scopus 로고
    • Survivin in apoptosis control and cell cycle regulation in cancer
    • Altieri, D.C. Survivin in apoptosis control and cell cycle regulation in cancer. Prog. Cell Cycle Res., 2003, 5, 447-452.
    • (2003) Prog. Cell Cycle Res , vol.5 , pp. 447-452
    • Altieri, D.C.1
  • 188
    • 33847619355 scopus 로고    scopus 로고
    • Optimization and determination of the absolute configuration of a series of potent inhibitors of human papillomavirus type-11 E1-E2 protein-protein interaction: A combined medicinal chemistry, NMR and computational chemistry approach
    • Goudreau, N.; Cameron, D.R.; Deziel, R.; Hache, B.; Jakalian, A.; Malenfant, E.; Naud, J.; Ogilvie, W.W.; O'Meara, J.; White, P.W.; Yoakim, C. Optimization and determination of the absolute configuration of a series of potent inhibitors of human papillomavirus type-11 E1-E2 protein-protein interaction: a combined medicinal chemistry, NMR and computational chemistry approach. Bioorg. Med. Chem., 2007, 15, 2690-2700.
    • (2007) Bioorg. Med. Chem , vol.15 , pp. 2690-2700
    • Goudreau, N.1    Cameron, D.R.2    Deziel, R.3    Hache, B.4    Jakalian, A.5    Malenfant, E.6    Naud, J.7    Ogilvie, W.W.8    O'Meara, J.9    White, P.W.10    Yoakim, C.11
  • 192
    • 57449117704 scopus 로고    scopus 로고
    • In search of small molecules blocking interactions between HIV proteins and intracellular cofactors
    • Busschots, K.; De Rijck, J.; Christ, F.; Debyser, Z. In search of small molecules blocking interactions between HIV proteins and intracellular cofactors. Mol. Biosyst., 2009, 5, 21-31.
    • (2009) Mol. Biosyst , vol.5 , pp. 21-31
    • Busschots, K.1    de Rijck, J.2    Christ, F.3    Debyser, Z.4
  • 195
    • 40849098660 scopus 로고    scopus 로고
    • Molecular interactions of CCR5 with major classes of small-molecule anti-HIV CCR5 antagonists
    • Kondru, R.; Zhang, J.; Ji, C.; Mirzadegan, T.; Rotstein, D.; Sankuratri, S.; Dioszegi, M. Molecular interactions of CCR5 with major classes of small-molecule anti-HIV CCR5 antagonists. Mol. Pharmacol., 2008, 73, 789-800.
    • (2008) Mol. Pharmacol , vol.73 , pp. 789-800
    • Kondru, R.1    Zhang, J.2    Ji, C.3    Mirzadegan, T.4    Rotstein, D.5    Sankuratri, S.6    Dioszegi, M.7
  • 197
    • 56749182203 scopus 로고    scopus 로고
    • CCR5 inhibitors in HIV-1 therapy
    • Dorr, P.; Perros, M. CCR5 inhibitors in HIV-1 therapy. Expert Opin. Drug Discov., 2008, 3, 1345-1361.
    • (2008) Expert Opin. Drug Discov , vol.3 , pp. 1345-1361
    • Dorr, P.1    Perros, M.2
  • 200
    • 23844440296 scopus 로고    scopus 로고
    • N-phenyl-N'-(2,2,6,6-tetramethyl-piperidin-4-yl)-oxalamides as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4
    • Zhao, Q.; Ma, L.Y.; Jiang, S.B.; Lu, H.; Liu, S.W.; He, Y.X.; Strick, N.; Neamati, N.; Debnath, A.K. N-phenyl-N'-(2,2,6,6-tetramethyl-piperidin-4-yl)-oxalamides as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4. Virology, 2005, 339, 213-225.
    • (2005) Virology , vol.339 , pp. 213-225
    • Zhao, Q.1    Ma, L.Y.2    Jiang, S.B.3    Lu, H.4    Liu, S.W.5    He, Y.X.6    Strick, N.7    Neamati, N.8    Debnath, A.K.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.