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Volumn 81, Issue 1, 2007, Pages 30-34

In silico drug discovery: Solving the "target-rich and lead-poor" imbalance using the genome-to-drug-lead paradigm

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BOTULINUM TOXIN; CHYMOTRYPSIN LIKE CYSTEINE PROTEINASE; CHYMOTRYPSIN LIKE CYSTEINE PROTEINASE INHIBITOR; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; GLOBULAR PROTEIN; HUMAN SERUM ALBUMIN; NEW DRUG; PROTEIN; PROTEINASE INHIBITOR; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG; ZINC ENDOPEPTIDASE INHIBITOR;

EID: 33845971492     PISSN: 00099236     EISSN: 15326535     Source Type: Journal    
DOI: 10.1038/sj.clpt.6100030     Document Type: Review
Times cited : (25)

References (20)
  • 1
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter, J.C. et al. The sequence of the human genome. Science 291, 1304-1351 (2001).
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1
  • 2
    • 0034684425 scopus 로고    scopus 로고
    • Proteomics: New perspectives, new biomedical opportunities
    • Banks, R.E. et al. Proteomics: new perspectives, new biomedical opportunities. Lancet 356, 1749-1756 (2000).
    • (2000) Lancet , vol.356 , pp. 1749-1756
    • Banks, R.E.1
  • 3
    • 0032831070 scopus 로고    scopus 로고
    • Structural genomics: Beyond the Human Genome Project
    • Burley, S.K. et al. Structural genomics: beyond the Human Genome Project. Nat. Genet. 23, 151-157 (1999).
    • (1999) Nat. Genet , vol.23 , pp. 151-157
    • Burley, S.K.1
  • 4
    • 33845976443 scopus 로고    scopus 로고
    • Drug discovery - contemporary small molecule drug discovery - Tutorial: Stacking the deck in favor of drug-like leads
    • Chait, E.M. Drug discovery - contemporary small molecule drug discovery - Tutorial: stacking the deck in favor of drug-like leads. Genet. Eng. News 22, 34-37 (2002).
    • (2002) Genet. Eng. News , vol.22 , pp. 34-37
    • Chait, E.M.1
  • 5
    • 0034628541 scopus 로고    scopus 로고
    • Successful virtual screening of a chemical database for farnesyltransferase inhibitor leads
    • Perola, E. et al. Successful virtual screening of a chemical database for farnesyltransferase inhibitor leads. J. Med. Chem. 43, 401-408 (2000).
    • (2000) J. Med. Chem , vol.43 , pp. 401-408
    • Perola, E.1
  • 6
    • 0036491696 scopus 로고    scopus 로고
    • Chemical database techniques in drug discovery
    • Miller, M.A. Chemical database techniques in drug discovery. Nat. Rev. Drug Discov. 1, 220-227 (2002).
    • (2002) Nat. Rev. Drug Discov , vol.1 , pp. 220-227
    • Miller, M.A.1
  • 7
    • 33748276474 scopus 로고    scopus 로고
    • Protein-ligand docking: Current status and future challenges
    • Sousa, S.F., Fernandes, P.A. & Ramos, M.J. Protein-ligand docking: current status and future challenges. Proteins 65, 15-26 (2006).
    • (2006) Proteins , vol.65 , pp. 15-26
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 8
    • 33646520592 scopus 로고    scopus 로고
    • Receptor-ligand binding sites and virtual screening
    • Hattotuwagama, C.K., Davies, M.N. & Flower, D.R. Receptor-ligand binding sites and virtual screening. Curr Med Chem 13, 1283-1304 (2006).
    • (2006) Curr Med Chem , vol.13 , pp. 1283-1304
    • Hattotuwagama, C.K.1    Davies, M.N.2    Flower, D.R.3
  • 9
    • 0035976367 scopus 로고    scopus 로고
    • EUDOC: A computer program for identification of drug interaction sites in macromolecules and drug leads from chemical databases
    • Pang, Y.-P., Perola, E., Xu, K. & Prendergast, F.G. EUDOC: A computer program for identification of drug interaction sites in macromolecules and drug leads from chemical databases. J. Comp. Chem. 22, 1750-1771 (2001).
    • (2001) J. Comp. Chem , vol.22 , pp. 1750-1771
    • Pang, Y.-P.1    Perola, E.2    Xu, K.3    Prendergast, F.G.4
  • 10
    • 24944493938 scopus 로고    scopus 로고
    • Toward high-resolution de novo structure prediction for small proteins
    • Bradley, P., Misura, K.M. & Baker, D. Toward high-resolution de novo structure prediction for small proteins. Science 309, 1868-1871 (2005).
    • (2005) Science , vol.309 , pp. 1868-1871
    • Bradley, P.1    Misura, K.M.2    Baker, D.3
  • 11
    • 30344480804 scopus 로고    scopus 로고
    • From genome to drug lead: Identification of a small-molecule inhibitor of the SARS virus
    • Dooley, A.J., Shindo, N., Taggart, B., Park, J.G. & Pang, Y.-P. From genome to drug lead: identification of a small-molecule inhibitor of the SARS virus. Bioorg. Med. Chem. Lett. 16, 830-833 (2006).
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , pp. 830-833
    • Dooley, A.J.1    Shindo, N.2    Taggart, B.3    Park, J.G.4    Pang, Y.-P.5
  • 12
    • 0031910020 scopus 로고    scopus 로고
    • Locally accessible conformations of proteins -multiple molecular dynamics simulations of crambin
    • Caves, L.S.D., Evanseck, J.D. & Karplus, M. Locally accessible conformations of proteins -multiple molecular dynamics simulations of crambin. Protein Sci. 7, 649-666 (1998).
    • (1998) Protein Sci , vol.7 , pp. 649-666
    • Caves, L.S.D.1    Evanseck, J.D.2    Karplus, M.3
  • 13
    • 0037103003 scopus 로고    scopus 로고
    • Assessing equilibration and convergence in biomolecular simulations
    • Smith, L.J., Daura, X. & van Gunsteren, W.F. Assessing equilibration and convergence in biomolecular simulations. Proteins 48, 487-496 (2002).
    • (2002) Proteins , vol.48 , pp. 487-496
    • Smith, L.J.1    Daura, X.2    van Gunsteren, W.F.3
  • 14
    • 0037038372 scopus 로고    scopus 로고
    • Absolute comparison of simulated and experimental protein-folding dynamics
    • Snow, C.D., Nguyen, N., Pande, V.S. & Gruebele, M. Absolute comparison of simulated and experimental protein-folding dynamics. Nature 420, 102-106 (2002).
    • (2002) Nature , vol.420 , pp. 102-106
    • Snow, C.D.1    Nguyen, N.2    Pande, V.S.3    Gruebele, M.4
  • 15
    • 0036428782 scopus 로고    scopus 로고
    • Simulation of folding of a small alpha-helical protein in atomistic detail using worldwide-distributed computing
    • Zagrovic, B., Snow, C.D., Shirts, M.R. & Pande, V.S. Simulation of folding of a small alpha-helical protein in atomistic detail using worldwide-distributed computing. J. Mol. Biol. 323, 927-937 (2002).
    • (2002) J. Mol. Biol , vol.323 , pp. 927-937
    • Zagrovic, B.1    Snow, C.D.2    Shirts, M.R.3    Pande, V.S.4
  • 16
    • 0042666843 scopus 로고    scopus 로고
    • Modeling domino effects in enzymes: Molecular basis of the substrate specificity of the bacterial metallo-beta-lactamases IMP-1 and IMP-6
    • Oelschlaeger, P., Schmid, R.D. & Pleiss, J. Modeling domino effects in enzymes: molecular basis of the substrate specificity of the bacterial metallo-beta-lactamases IMP-1 and IMP-6. Biochemistry 42, 8945-8956 (2003).
    • (2003) Biochemistry , vol.42 , pp. 8945-8956
    • Oelschlaeger, P.1    Schmid, R.D.2    Pleiss, J.3
  • 17
    • 10344222619 scopus 로고    scopus 로고
    • Three-dimensional model of a substrate-bound SARS chymotrypsin-like cysteine proteinase predicted by multiple molecular dynamics simulations: Catalytic efficiency regulated by substrate binding
    • Pang, Y.-P. Three-dimensional model of a substrate-bound SARS chymotrypsin-like cysteine proteinase predicted by multiple molecular dynamics simulations: catalytic efficiency regulated by substrate binding. Proteins. 57, 747-757 (2004).
    • (2004) Proteins , vol.57 , pp. 747-757
    • Pang, Y.-P.1
  • 18
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos, O., Alam, S.L., Davis, D.R. & Sundquist, W.I. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nat. Struct. Biol. 9, 812-817 (2002).
    • (2002) Nat. Struct. Biol , vol.9 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 19
    • 33744945316 scopus 로고    scopus 로고
    • Only one protomer is active in the dimer of SARS 3C-like proteinase
    • Chen, H. et al. Only one protomer is active in the dimer of SARS 3C-like proteinase. J. Biol. Chem. 281, 13894-13898 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 13894-13898
    • Chen, H.1
  • 20
    • 28844505096 scopus 로고    scopus 로고
    • Serotype-selective, small-molecule inhibitors of the zinc endopeptidase of botulinum neurotoxin serotype A
    • Park, J.G. et al. Serotype-selective, small-molecule inhibitors of the zinc endopeptidase of botulinum neurotoxin serotype A. Bioorg. Med. Chem. 14, 395-408 (2006).
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 395-408
    • Park, J.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.