메뉴 건너뛰기




Volumn 9, Issue 7, 2013, Pages

Pathway-based Screening Strategy for Multitarget Inhibitors of Diverse Proteins in Metabolic Pathways

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGICAL SYSTEMS; DIAGNOSIS; DRUG THERAPY; PROTEINS;

EID: 84880848738     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1003127     Document Type: Article
Times cited : (23)

References (39)
  • 2
    • 0037107887 scopus 로고    scopus 로고
    • Structure-based virtual screening: an overview
    • Lyne PD, (2002) Structure-based virtual screening: an overview. Drug Discov Today 7: 1047-1055.
    • (2002) Drug Discov Today , vol.7 , pp. 1047-1055
    • Lyne, P.D.1
  • 3
    • 8844263008 scopus 로고    scopus 로고
    • Docking and scoring in virtual screening for drug discovery: methods and applications
    • Kitchen DB, Decornez H, Furr JR, Bajorath J, (2004) Docking and scoring in virtual screening for drug discovery: methods and applications. Nature Reviews Drug Discovery 3: 935-949.
    • (2004) Nature Reviews Drug Discovery , vol.3 , pp. 935-949
    • Kitchen, D.B.1    Decornez, H.2    Furr, J.R.3    Bajorath, J.4
  • 5
    • 33744551693 scopus 로고    scopus 로고
    • Structure-based virtual screening of chemical libraries for drug discovery Current Opinion in Chemical
    • Ghosh S, Nie AH, An J, Huang ZW, (2006) Structure-based virtual screening of chemical libraries for drug discovery Current Opinion in Chemical. Biology 10: 194-202.
    • (2006) Biology , vol.10 , pp. 194-202
    • Ghosh, S.1    Nie, A.H.2    An, J.3    Huang, Z.W.4
  • 6
    • 29144433925 scopus 로고    scopus 로고
    • Oseltamivir resistance - disabling our influenza defenses
    • Moscona A, (2005) Oseltamivir resistance- disabling our influenza defenses. N Engl J Med 353: 2633-2636.
    • (2005) N Engl J Med , vol.353 , pp. 2633-2636
    • Moscona, A.1
  • 7
    • 1842509978 scopus 로고    scopus 로고
    • Positive selection detection in 40,000 human immunodeficiency virus (HIV) type 1 sequences automatically identifies drug resistance and positive fitness mutations in HIV protease and reverse transcriptase
    • Chen LM, Perlina A, Lee CJ, (2004) Positive selection detection in 40,000 human immunodeficiency virus (HIV) type 1 sequences automatically identifies drug resistance and positive fitness mutations in HIV protease and reverse transcriptase. Journal of Virology 78: 3722-3732.
    • (2004) Journal of Virology , vol.78 , pp. 3722-3732
    • Chen, L.M.1    Perlina, A.2    Lee, C.J.3
  • 8
    • 57149112608 scopus 로고    scopus 로고
    • Double-edged swords as cancer therapeutics: simultaneously targeting p53 and NF-kappa B pathways
    • Dey A, Tergaonkar V, Lane DP, (2008) Double-edged swords as cancer therapeutics: simultaneously targeting p53 and NF-kappa B pathways. Nat Rev Drug Discov 7: 1031-1040.
    • (2008) Nat Rev Drug Discov , vol.7 , pp. 1031-1040
    • Dey, A.1    Tergaonkar, V.2    Lane, D.P.3
  • 9
    • 75149130051 scopus 로고    scopus 로고
    • Targeting the cancer kinome through polypharmacology
    • Knight ZA, Lin H, Shokat KM, (2010) Targeting the cancer kinome through polypharmacology. Nat Rev Cancer 10: 130-137.
    • (2010) Nat Rev Cancer , vol.10 , pp. 130-137
    • Knight, Z.A.1    Lin, H.2    Shokat, K.M.3
  • 11
    • 70349345898 scopus 로고    scopus 로고
    • Three-dimensional structural view of the central metabolic network of Thermotoga maritima
    • Zhang Y, Thiele I, Weekes D, Li ZW, Jaroszewski L, et al. (2009) Three-dimensional structural view of the central metabolic network of Thermotoga maritima. Science 325: 1544-1549.
    • (2009) Science , vol.325 , pp. 1544-1549
    • Zhang, Y.1    Thiele, I.2    Weekes, D.3    Li, Z.W.4    Jaroszewski, L.5
  • 12
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen RA, (1976) Enzyme recruitment in evolution of new function. Annu Rev Microbiol 30: 409-425.
    • (1976) Annu Rev Microbiol , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 13
    • 77954249073 scopus 로고    scopus 로고
    • SiMMap: a web server for inferring site-moiety map to recognize interaction preferences between protein pockets and compound moieties
    • Chen YF, Hsu KC, Lin SR, Wang WC, Huang YC, et al. (2010) SiMMap: a web server for inferring site-moiety map to recognize interaction preferences between protein pockets and compound moieties. Nucleic Acids Res 38: W424-W430.
    • (2010) Nucleic Acids Res , vol.38
    • Chen, Y.F.1    Hsu, K.C.2    Lin, S.R.3    Wang, W.C.4    Huang, Y.C.5
  • 14
    • 84863257777 scopus 로고    scopus 로고
    • Core site-moiety maps reveal inhibitors and binding mechanisms of orthologous proteins by screening compound libraries
    • Hsu KC, Cheng WC, Chen YF, Wang HJ, Li LT, et al. (2012) Core site-moiety maps reveal inhibitors and binding mechanisms of orthologous proteins by screening compound libraries. PLoS One 7: e32142.
    • (2012) PLoS One , vol.7
    • Hsu, K.C.1    Cheng, W.C.2    Chen, Y.F.3    Wang, H.J.4    Li, L.T.5
  • 15
    • 0030835739 scopus 로고    scopus 로고
    • The complete genome sequence of the gastric pathogen Helicobacter pylori
    • Tomb JF, White O, Kerlavage AR, Clayton RA, Sutton GG, et al. (1997) The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388: 539-547.
    • (1997) Nature , vol.388 , pp. 539-547
    • Tomb, J.F.1    White, O.2    Kerlavage, A.R.3    Clayton, R.A.4    Sutton, G.G.5
  • 16
    • 0033552961 scopus 로고    scopus 로고
    • Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori
    • Alm RA, Ling LSL, Moir DT, King BL, Brown ED, et al. (1999) Genomic-sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori. Nature 397: 176-180.
    • (1999) Nature , vol.397 , pp. 176-180
    • Alm, R.A.1    Ling, L.S.L.2    Moir, D.T.3    King, B.L.4    Brown, E.D.5
  • 17
    • 0032565968 scopus 로고    scopus 로고
    • Evidence for the shikimate pathway in apicomplexan parasites
    • Roberts F, Roberts CW, Johnson JJ, Kyle DE, Krell T, et al. (1998) Evidence for the shikimate pathway in apicomplexan parasites. Nature 393: 801-805.
    • (1998) Nature , vol.393 , pp. 801-805
    • Roberts, F.1    Roberts, C.W.2    Johnson, J.J.3    Kyle, D.E.4    Krell, T.5
  • 18
    • 33749396618 scopus 로고    scopus 로고
    • Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori
    • Han C, Wang L, Yu K, Chen L, Hu L, et al. (2006) Biochemical characterization and inhibitor discovery of shikimate dehydrogenase from Helicobacter pylori. FEBS J 273: 4682-4692.
    • (2006) FEBS J , vol.273 , pp. 4682-4692
    • Han, C.1    Wang, L.2    Yu, K.3    Chen, L.4    Hu, L.5
  • 19
    • 28044450588 scopus 로고    scopus 로고
    • Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase
    • Cheng WC, Chang YN, Wang WC, (2005) Structural basis for shikimate-binding specificity of Helicobacter pylori shikimate kinase. J Bacteriol 187: 8156-8163.
    • (2005) J Bacteriol , vol.187 , pp. 8156-8163
    • Cheng, W.C.1    Chang, Y.N.2    Wang, W.C.3
  • 21
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases
    • Ewing TJ, Makino S, Skillman AG, Kuntz ID, (2001) DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases. J Comput Aided Mol Des 15: 411-428.
    • (2001) J Comput Aided Mol Des , vol.15 , pp. 411-428
    • Ewing, T.J.1    Makino, S.2    Skillman, A.G.3    Kuntz, I.D.4
  • 22
    • 0032738842 scopus 로고    scopus 로고
    • Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking
    • Kramer B, Rarey M, Lengauer T, (1999) Evaluation of the FLEXX incremental construction algorithm for protein-ligand docking. Proteins 37: 228-241.
    • (1999) Proteins , vol.37 , pp. 228-241
    • Kramer, B.1    Rarey, M.2    Lengauer, T.3
  • 23
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R, (1997) Development and validation of a genetic algorithm for flexible docking. J Mol Biol 267: 727-748.
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 24
    • 16344377697 scopus 로고    scopus 로고
    • A pharmacophore-based evolutionary approach for screening selective estrogen receptor modulators
    • Yang JM, Shen TW, (2005) A pharmacophore-based evolutionary approach for screening selective estrogen receptor modulators. Proteins-Structure Function and Bioinformatics 59: 205-220.
    • (2005) Proteins-Structure Function and Bioinformatics , vol.59 , pp. 205-220
    • Yang, J.M.1    Shen, T.W.2
  • 25
    • 55849131743 scopus 로고    scopus 로고
    • Combinatorial computational approaches to identify tetracycline derivatives as flavivirus inhibitors
    • Yang JM, Chen YF, Tu YY, Yen KR, Yang YL, (2007) Combinatorial computational approaches to identify tetracycline derivatives as flavivirus inhibitors. PLoS One 2: e428.
    • (2007) PLoS One , vol.2
    • Yang, J.M.1    Chen, Y.F.2    Tu, Y.Y.3    Yen, K.R.4    Yang, Y.L.5
  • 26
    • 77949325119 scopus 로고    scopus 로고
    • The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris
    • Chin KH, Lee YC, Tu ZL, Chen CH, Tseng YH, et al. (2010) The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris. J Mol Biol 396: 646-662.
    • (2010) J Mol Biol , vol.396 , pp. 646-662
    • Chin, K.H.1    Lee, Y.C.2    Tu, Z.L.3    Chen, C.H.4    Tseng, Y.H.5
  • 27
    • 61549125031 scopus 로고    scopus 로고
    • Rational design for crystallization of beta-lactoglobulin and vitamin D-3 complex: revealing a secondary binding site
    • Yang MC, Guan HH, Yang JM, Ko CN, Liu MY, et al. (2008) Rational design for crystallization of beta-lactoglobulin and vitamin D-3 complex: revealing a secondary binding site. Cryst Growth Des 8: 4268-4276.
    • (2008) Cryst Growth Des , vol.8 , pp. 4268-4276
    • Yang, M.C.1    Guan, H.H.2    Yang, J.M.3    Ko, C.N.4    Liu, M.Y.5
  • 28
    • 34548861221 scopus 로고    scopus 로고
    • Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: Insights into the enzymatic mechanism
    • Bagautdinov B, Kunishima N, (2007) Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: Insights into the enzymatic mechanism. J Mol Biol 373: 424-438.
    • (2007) J Mol Biol , vol.373 , pp. 424-438
    • Bagautdinov, B.1    Kunishima, N.2
  • 29
    • 33751246776 scopus 로고    scopus 로고
    • Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis
    • Hartmann MD, Bourenkov GP, Oberschall A, Strizhov N, Bartunik HD, (2006) Mechanism of phosphoryl transfer catalyzed by shikimate kinase from Mycobacterium tuberculosis. J Mol Biol 364: 411-423.
    • (2006) J Mol Biol , vol.364 , pp. 411-423
    • Hartmann, M.D.1    Bourenkov, G.P.2    Oberschall, A.3    Strizhov, N.4    Bartunik, H.D.5
  • 30
    • 14844307853 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli
    • Lindner HA, Nadeau G, Matte A, Michel G, Menard R, et al. (2005) Site-directed mutagenesis of the active site region in the quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli. J Biol Chem 280: 7162-7169.
    • (2005) J Biol Chem , vol.280 , pp. 7162-7169
    • Lindner, H.A.1    Nadeau, G.2    Matte, A.3    Michel, G.4    Menard, R.5
  • 31
    • 84863378835 scopus 로고    scopus 로고
    • Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism
    • Cheng WC, Chen YF, Wang HJ, Hsu KC, Lin SC, et al. (2012) Structures of Helicobacter pylori shikimate kinase reveal a selective inhibitor-induced-fit mechanism. PLoS One7: e33481.
    • (2012) PLoS , vol.7
    • Cheng, W.C.1    Chen, Y.F.2    Wang, H.J.3    Hsu, K.C.4    Lin, S.C.5
  • 32
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures
    • Landau M, Mayrose I, Rosenberg Y, Glaser F, Martz E, et al. (2005) ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res 33: W299-302.
    • (2005) Nucleic Acids Res , vol.33
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5
  • 33
    • 0034687650 scopus 로고    scopus 로고
    • Explaining the high mutation rates of cancer cells to drug and multidrug resistance by chromosome reassortments that are catalyzed by aneuploidy
    • Duesberg P, Stindl R, Hehlmann R, (2000) Explaining the high mutation rates of cancer cells to drug and multidrug resistance by chromosome reassortments that are catalyzed by aneuploidy. Proc Natl Acad Sci U S A 97: 14295-14300.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14295-14300
    • Duesberg, P.1    Stindl, R.2    Hehlmann, R.3
  • 34
    • 0020067634 scopus 로고
    • Variation of Influenza-A, Influenza-B, and Influenza-C viruses
    • Palese P, Young JF, (1982) Variation of Influenza-A, Influenza-B, and Influenza-C viruses. Science 215: 1468-1474.
    • (1982) Science , vol.215 , pp. 1468-1474
    • Palese, P.1    Young, J.F.2
  • 35
    • 33751036696 scopus 로고    scopus 로고
    • Drug evaluation: VX-702, a MAP kinase inhibitor for rheumatoid arthritis and acute coronary syndrome
    • Ding CH, (2006) Drug evaluation: VX-702, a MAP kinase inhibitor for rheumatoid arthritis and acute coronary syndrome. Curr Opin Investig Drugs 7: 1020-1025.
    • (2006) Curr Opin Investig Drugs , vol.7 , pp. 1020-1025
    • Ding, C.H.1
  • 37
    • 0032537722 scopus 로고    scopus 로고
    • Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis
    • Carpenter EP, Hawkins AR, Frost JW, Brown KA, (1998) Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature 394: 299-302.
    • (1998) Nature , vol.394 , pp. 299-302
    • Carpenter, E.P.1    Hawkins, A.R.2    Frost, J.W.3    Brown, K.A.4
  • 38
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov IN, Bourne PE, (1998) Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng 11: 739-747.
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 39
    • 33746083227 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimic acid and an ATP analogue
    • Gan JH, Gu YJ, Li Y, Yan HG, Ji XH, (2006) Crystal structure of Mycobacterium tuberculosis shikimate kinase in complex with shikimic acid and an ATP analogue. Biochemistry 45: 8539-8545.
    • (2006) Biochemistry , vol.45 , pp. 8539-8545
    • Gan, J.H.1    Gu, Y.J.2    Li, Y.3    Yan, H.G.4    Ji, X.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.