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Volumn 6, Issue 5, 2002, Pages 704-710

The genesis of high-throughput structure-based drug discovery using protein crystallography

Author keywords

[No Author keywords available]

Indexed keywords

AMPRENAVIR; DRUG; LIGAND; NELFINAVIR; OSELTAMIVIR; PROTEINASE; PROTEINASE INHIBITOR; SIALIDASE; SIALIDASE INHIBITOR; ZANAMIVIR;

EID: 0036804362     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(02)00361-7     Document Type: Review
Times cited : (111)

References (73)
  • 2
    • 0028846226 scopus 로고
    • Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme
    • Kim E.E., Baker C.T., Dwyer M.D., Murcko M.A., Rao B.G., Tung R.D., Navia M.A. Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme. J Am Chem Soc. 117:1995;1181-1182.
    • (1995) J Am Chem Soc , vol.117 , pp. 1181-1182
    • Kim, E.E.1    Baker, C.T.2    Dwyer, M.D.3    Murcko, M.A.4    Rao, B.G.5    Tung, R.D.6    Navia, M.A.7
  • 4
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: Design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • Kim C.U., Lew W., Williams M.A., Liu H.T., Zhang L.J., Swaminathan S., Bischofberger N., Chen M.S., Mendel D.B., Tai C.Y., et al. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J Am Chem Soc. 119:1997;681-690.
    • (1997) J Am Chem Soc , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3    Liu, H.T.4    Zhang, L.J.5    Swaminathan, S.6    Bischofberger, N.7    Chen, M.S.8    Mendel, D.B.9    Tai, C.Y.10
  • 5
    • 0036468948 scopus 로고    scopus 로고
    • Accelerating code to function: Sizing up the protein production line
    • Gilbert M., Albala J.S. Accelerating code to function: sizing up the protein production line. Curr Opin Chem Biol. 6:2002;102-105.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 102-105
    • Gilbert, M.1    Albala, J.S.2
  • 6
    • 0034957669 scopus 로고    scopus 로고
    • High-throughput proteomics: Protein expression and purification in the postgenomic world
    • Lesley S.A. High-throughput proteomics: protein expression and purification in the postgenomic world. Protein Expr Purif. 22:2001;159-164. The instrumentation and data analysis described in this paper exemplifies the critical aspects of automated sample preparation that are required for HT structural biology and structural genomics efforts.
    • (2001) Protein Expr Purif , vol.22 , pp. 159-164
    • Lesley, S.A.1
  • 7
    • 0034665455 scopus 로고    scopus 로고
    • Design of high-throughput methods of protein production for structural biology
    • Stevens R.C. Design of high-throughput methods of protein production for structural biology. Struct Fold Des. 8:2000;R177-R185.
    • (2000) Struct Fold Des , vol.8
    • Stevens, R.C.1
  • 9
    • 0024285044 scopus 로고
    • Phase determination by multiple-wavelength X-ray diffraction: Crystal structure of a basic "blue" copper protein from cucumbers
    • Guss J.M., Merritt E.A., Phizackerley R.P., Hedman B., Murata M., Hodgson K.O., Freeman H.C. Phase determination by multiple-wavelength X-ray diffraction: crystal structure of a basic "blue" copper protein from cucumbers. Science. 241:1988;806-811.
    • (1988) Science , vol.241 , pp. 806-811
    • Guss, J.M.1    Merritt, E.A.2    Phizackerley, R.P.3    Hedman, B.4    Murata, M.5    Hodgson, K.O.6    Freeman, H.C.7
  • 10
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson W.A., Horton J.R., LeMaster D.M. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9:1990;1665-1672.
    • (1990) EMBO J , vol.9 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 11
    • 0033213464 scopus 로고    scopus 로고
    • Cool data: Quantity AND quality
    • Garman E. Cool data: quantity AND quality. Acta Crystallogr D. 55:1999;1641-1653.
    • (1999) Acta Crystallogr D , vol.55 , pp. 1641-1653
    • Garman, E.1
  • 14
    • 0033789124 scopus 로고    scopus 로고
    • Recent developments in software for the automation of crystallographic macromolecular structure determination
    • Adams P.D., Grosse-Kunstleve R.W. Recent developments in software for the automation of crystallographic macromolecular structure determination. Curr Opin Struct Biol. 10:2000;564-568. Automation and software integration of the entire structure determination and refinement process is a critical enabling technology, for which new approaches are discussed in this paper.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 564-568
    • Adams, P.D.1    Grosse-Kunstleve, R.W.2
  • 15
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat Struct Biol. 6:1999;458-463. Perhaps one the most important breakthroughs in crystallographic structure determination has been the use of ARP/wARP in the automatic tracing of high-resolution phased diffraction data and rebuilding of partial models.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 16
    • 0033794367 scopus 로고    scopus 로고
    • High-throughput protein crystallization
    • Stevens R.C. High-throughput protein crystallization. Curr Opin Struct Biol. 10:2000;558-563.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 558-563
    • Stevens, R.C.1
  • 17
    • 0001011919 scopus 로고    scopus 로고
    • High-throughput X-ray crystallography for structure-based drug design
    • Goodwill KE, Tennant MG, Stevens RC: High-throughput X-ray crystallography for structure-based drug design. Drug Discovery Today 2001, 6 (Genomics Suppl):S113-118.
    • (2001) Drug Discovery Today , vol.6 , Issue.GENOMICS SUPPL.
    • Goodwill, K.E.1    Tennant, M.G.2    Stevens, R.C.3
  • 22
    • 0344027274 scopus 로고    scopus 로고
    • Drug discovery tutorial: High-throughput protein crystallization
    • Long A. Drug discovery tutorial: high-throughput protein crystallization. Gen Eng News. 21:(34):2001;62.
    • (2001) Gen Eng News , vol.21 , Issue.34 , pp. 62
    • Long, A.1
  • 23
    • 0035222401 scopus 로고    scopus 로고
    • The Berlin "protein structure factory" initiative: A technology-oriented approach to structural genomics
    • Heinemann U. The Berlin "protein structure factory" initiative: a technology-oriented approach to structural genomics. Ernst Schering Res Found Workshop. 34:2001;101-121.
    • (2001) Ernst Schering Res Found Workshop , vol.34 , pp. 101-121
    • Heinemann, U.1
  • 24
    • 0033915678 scopus 로고    scopus 로고
    • Recent developments in structure-based drug design
    • Klebe G. Recent developments in structure-based drug design. J Mol Med. 78:2000;269-281.
    • (2000) J Mol Med , vol.78 , pp. 269-281
    • Klebe, G.1
  • 25
    • 0035416126 scopus 로고    scopus 로고
    • High-throughput docking for lead generation
    • Abagyan R., Totrov M. High-throughput docking for lead generation. Curr Opin Chem Biol. 5:2001;375-382.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 375-382
    • Abagyan, R.1    Totrov, M.2
  • 26
    • 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. 1:2002;45-54.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 27
    • 0033576680 scopus 로고    scopus 로고
    • Consensus scoring: A method for obtaining improved hit rates from docking databases of three-dimensional structures into proteins
    • Charifson P.S., Corkery J.J., Murcko M.A., Walters W.P. Consensus scoring: a method for obtaining improved hit rates from docking databases of three-dimensional structures into proteins. J Med Chem. 42:1999;5100-5109. Individual docking algorithms appear to have biases towards certain biological target families and they all suffer from not being able to prioritize consistently. Using consensus scoring (multiple docking algorithms used at once), common hits are elevated above the others.
    • (1999) J Med Chem , vol.42 , pp. 5100-5109
    • Charifson, P.S.1    Corkery, J.J.2    Murcko, M.A.3    Walters, W.P.4
  • 28
    • 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. 274:1996;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
  • 29
    • 0033773899 scopus 로고    scopus 로고
    • Discovering novel ligands for macromolecules using X-ray crystallographic screening
    • Nienaber V.L., Richardson P.L., Klighofer V., Bouska J.J., Giranda V.L., Greer J. Discovering novel ligands for macromolecules using X-ray crystallographic screening. Nat Biotechnol. 18:2000;1105-1108. Althoughcomputational screening has made significant advances, experimental screens are still more robust. This paper describes a novel method to experimentally screen compound libraries using crystallographic methods.
    • (2000) Nat Biotechnol , vol.18 , pp. 1105-1108
    • Nienaber, V.L.1    Richardson, P.L.2    Klighofer, V.3    Bouska, J.J.4    Giranda, V.L.5    Greer, J.6
  • 30
    • 0031804609 scopus 로고    scopus 로고
    • Inhibitors of HIV-1 protease: A major success of structure-assisted drug design
    • Wlodawer A., Vondrasek J. Inhibitors of HIV-1 protease: a major success of structure-assisted drug design. Annu Rev Biophys Biomol Struct. 27:1998;249-284.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 249-284
    • Wlodawer, A.1    Vondrasek, J.2
  • 32
    • 0035382791 scopus 로고    scopus 로고
    • The use of 3D structural data in the design of specific factor Xa inhibitors
    • Maignan S., Mikol V. The use of 3D structural data in the design of specific factor Xa inhibitors. Curr Top Med Chem. 1:2001;161-174.
    • (2001) Curr Top Med Chem , vol.1 , pp. 161-174
    • Maignan, S.1    Mikol, V.2
  • 33
    • 0037075838 scopus 로고    scopus 로고
    • PRO_SELECT: Combining structure-based drug design and array-based chemistry for rapid lead discovery. 2. The development of a series of highly potent and selective factor Xa inhibitors
    • Liebeschuetz J.W., Jones S.D., Morgan P.J., Murray C.W., Rimmer A.D., Roscoe J.M., Waszkowycz B., Welsh P.M., Wylie W.A., Young S.C., et al. PRO_SELECT: combining structure-based drug design and array-based chemistry for rapid lead discovery. 2. The development of a series of highly potent and selective factor Xa inhibitors. J Med Chem. 45:2002;1221-1232.
    • (2002) J Med Chem , vol.45 , pp. 1221-1232
    • Liebeschuetz, J.W.1    Jones, S.D.2    Morgan, P.J.3    Murray, C.W.4    Rimmer, A.D.5    Roscoe, J.M.6    Waszkowycz, B.7    Welsh, P.M.8    Wylie, W.A.9    Young, S.C.10
  • 34
    • 0033985723 scopus 로고    scopus 로고
    • The crystal structures of human alpha-thrombin complexed with active site-directed diamino benzo[b]thiophene derivatives: A binding mode for a structurally novel class of inhibitors
    • Chirgadze N.Y., Sall D.J., Briggs S.L., Clawson D.K., Zhang M., Smith G.F., Schevitz R.W. The crystal structures of human alpha-thrombin complexed with active site-directed diamino benzo[b]thiophene derivatives: a binding mode for a structurally novel class of inhibitors. Protein Sci. 9:2000;29-36.
    • (2000) Protein Sci , vol.9 , pp. 29-36
    • Chirgadze, N.Y.1    Sall, D.J.2    Briggs, S.L.3    Clawson, D.K.4    Zhang, M.5    Smith, G.F.6    Schevitz, R.W.7
  • 37
    • 0035899191 scopus 로고    scopus 로고
    • Development of serine protease inhibitors displaying a multicentered short (2.3 Å) hydrogen bond binding mode: Inhibitors of urokinase-type plasminogen activator and factor Xa
    • Verner E., Katz B.A., Spencer J.R., Allen D., Hataye J., Hruzewicz W., Hui H.C., Kolesnikov A., Li Y., Luong C., et al. Development of serine protease inhibitors displaying a multicentered short (2.3 Å) hydrogen bond binding mode: inhibitors of urokinase-type plasminogen activator and factor Xa. J Med Chem. 44:2001;2753-2771.
    • (2001) J Med Chem , vol.44 , pp. 2753-2771
    • Verner, E.1    Katz, B.A.2    Spencer, J.R.3    Allen, D.4    Hataye, J.5    Hruzewicz, W.6    Hui, H.C.7    Kolesnikov, A.8    Li, Y.9    Luong, C.10
  • 41
    • 0035927192 scopus 로고    scopus 로고
    • Modeling of the binding mode of a non-covalent inhibitor of the 20S proteasome. Application to structure-based analogue design
    • Furet P., Imbach P., Furst P., Lang M., Noorani M., Zimmermann J., Garcia-Echeverria C. Modeling of the binding mode of a non-covalent inhibitor of the 20S proteasome. Application to structure-based analogue design. Bioorg Med Chem Lett. 11:2001;1321-1324.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 1321-1324
    • Furet, P.1    Imbach, P.2    Furst, P.3    Lang, M.4    Noorani, M.5    Zimmermann, J.6    Garcia-Echeverria, C.7
  • 47
    • 0035428019 scopus 로고    scopus 로고
    • Rational design of potent and selective EGFR tyrosine kinase inhibitors as anticancer agents
    • Ghosh S., Liu X.-P., Zheng Y., Uckun F.M. Rational design of potent and selective EGFR tyrosine kinase inhibitors as anticancer agents. Curr Cancer Drug Targets. 1:2001;129-140.
    • (2001) Curr Cancer Drug Targets , vol.1 , pp. 129-140
    • Ghosh, S.1    Liu, X.-P.2    Zheng, Y.3    Uckun, F.M.4
  • 48
    • 0033152210 scopus 로고    scopus 로고
    • Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors
    • Zhu X., Kim J.L., Newcomb J.R., Rose P.E., Stover D.R., Toledo L.M., Zhao H., Morgenstern K.A. Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors. Structure. 7:1999;651-661.
    • (1999) Structure , vol.7 , pp. 651-661
    • Zhu, X.1    Kim, J.L.2    Newcomb, J.R.3    Rose, P.E.4    Stover, D.R.5    Toledo, L.M.6    Zhao, H.7    Morgenstern, K.A.8
  • 50
    • 0033667937 scopus 로고    scopus 로고
    • Structure-based design of compounds inhibiting Grb2-SH2 mediated protein-protein interactions in signal transduction pathways
    • Fretz H., Furet P., Garcia-Echeverria C., Schoepfer J., Rahuel J. Structure-based design of compounds inhibiting Grb2-SH2 mediated protein-protein interactions in signal transduction pathways. Curr Pharm Des. 6:2000;1777-1796.
    • (2000) Curr Pharm Des , vol.6 , pp. 1777-1796
    • Fretz, H.1    Furet, P.2    Garcia-Echeverria, C.3    Schoepfer, J.4    Rahuel, J.5
  • 51
    • 0034548887 scopus 로고    scopus 로고
    • Protein structure-based de novo design and synthesis of aldose reductase inhibitors
    • Iwata Y., Naito S., Itai A., Miyamoto S. Protein structure-based de novo design and synthesis of aldose reductase inhibitors. Drug Des Discov. 17:2001;349-359.
    • (2001) Drug Des Discov , vol.17 , pp. 349-359
    • Iwata, Y.1    Naito, S.2    Itai, A.3    Miyamoto, S.4
  • 52
    • 0032701132 scopus 로고    scopus 로고
    • Structure-based design of a new class of anti-inflammatory drugs: Secretory phospholipase A(2) inhibitors, SPI
    • Mihelich E.D., Schevitz R.W. Structure-based design of a new class of anti-inflammatory drugs: secretory phospholipase A(2) inhibitors, SPI. Biochim Biophys Acta. 1441:1999;223-228.
    • (1999) Biochim Biophys Acta , vol.1441 , pp. 223-228
    • Mihelich, E.D.1    Schevitz, R.W.2
  • 53
    • 0034722896 scopus 로고    scopus 로고
    • STAT proteins: Novel molecular targets for cancer drug discovery
    • Turkson J., Jove R. STAT proteins: novel molecular targets for cancer drug discovery. Oncogene. 19:2000;6613-6626.
    • (2000) Oncogene , vol.19 , pp. 6613-6626
    • Turkson, J.1    Jove, R.2
  • 55
    • 0034699492 scopus 로고    scopus 로고
    • BCX-1812 (RWJ-270201): Discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design
    • Babu Y.S., Chand P., Bantia S., Kotian P., Dehghani A., El-Kattan Y., Lin T.H., Hutchison T.L., Elliott A.J., Parker C.D., et al. BCX-1812 (RWJ-270201): discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design. J Med Chem. 43:2000;3482-3486.
    • (2000) J Med Chem , vol.43 , pp. 3482-3486
    • Babu, Y.S.1    Chand, P.2    Bantia, S.3    Kotian, P.4    Dehghani, A.5    El-Kattan, Y.6    Lin, T.H.7    Hutchison, T.L.8    Elliott, A.J.9    Parker, C.D.10
  • 58
    • 0027403420 scopus 로고
    • Design of thymidylate synthase inhibitors using protein crystal structures: The synthesis and biological evaluation of a novel class of 5-substituted quinazolines
    • Webber S.E., Bleckman T.M., Attard J., Deal J.G., Kathardekar V., Welsh K.M., Webber S., Janson C.A., Matthews D.A., et al. Design of thymidylate synthase inhibitors using protein crystal structures: the synthesis and biological evaluation of a novel class of 5-substituted quinazolines. J Med Chem. 36:1993;733-746.
    • (1993) J Med Chem , vol.36 , pp. 733-746
    • Webber, S.E.1    Bleckman, T.M.2    Attard, J.3    Deal, J.G.4    Kathardekar, V.5    Welsh, K.M.6    Webber, S.7    Janson, C.A.8    Matthews, D.A.9
  • 61
    • 0035935669 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of prostaglandin-F alkylphosphinic acid derivatives as bone anabolic agents for the treatment of osteoporosis
    • Soper D.L., Milbank J.B., Mieling G.E., Dirr M.J., Kende A.S., Cooper R., Jee W.S., Yao W., Chen J.L., Bodman M., et al. Synthesis and biological evaluation of prostaglandin-F alkylphosphinic acid derivatives as bone anabolic agents for the treatment of osteoporosis. J Med Chem. 44:2001;4157-4169.
    • (2001) J Med Chem , vol.44 , pp. 4157-4169
    • Soper, D.L.1    Milbank, J.B.2    Mieling, G.E.3    Dirr, M.J.4    Kende, A.S.5    Cooper, R.6    Jee, W.S.7    Yao, W.8    Chen, J.L.9    Bodman, M.10
  • 62
    • 0035959994 scopus 로고    scopus 로고
    • Structure-based design and synthesis of potent matrix metalloproteinase inhibitors derived from a 6H-1,3,4-thiadiazine scaffold
    • Schroder J., Henke A., Wenzel H., Brandstetter H., Stammler H.G., Stammler A., Pfeiffer W.D., Tschesche H. Structure-based design and synthesis of potent matrix metalloproteinase inhibitors derived from a 6H-1,3,4-thiadiazine scaffold. J Med Chem. 44:2001;3231-3243.
    • (2001) J Med Chem , vol.44 , pp. 3231-3243
    • Schroder, J.1    Henke, A.2    Wenzel, H.3    Brandstetter, H.4    Stammler, H.G.5    Stammler, A.6    Pfeiffer, W.D.7    Tschesche, H.8
  • 63
    • 0035152282 scopus 로고    scopus 로고
    • Structures of trihydroxynaphthalene reductase-fungicide complexes: Implications for structure-based design and catalysis
    • Liao D., Basarab G.S., Gatenby A.A., Valent B., Jordan D.B. Structures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis. Structure. 9:2001;19-27.
    • (2001) Structure , vol.9 , pp. 19-27
    • Liao, D.1    Basarab, G.S.2    Gatenby, A.A.3    Valent, B.4    Jordan, D.B.5
  • 64
    • 0037011895 scopus 로고    scopus 로고
    • Pharmacophore mapping of a series of 2,4-diamino-5-deazapteridine inhibitors of Mycobacterium avium complex dihydrofolate reductase
    • Debnath A.K. Pharmacophore mapping of a series of 2,4-diamino-5-deazapteridine inhibitors of Mycobacterium avium complex dihydrofolate reductase. J Med Chem. 45:2002;41-53.
    • (2002) J Med Chem , vol.45 , pp. 41-53
    • Debnath, A.K.1
  • 67
    • 0035829450 scopus 로고    scopus 로고
    • Novel lead generation through hypothetical pharmacophore three-dimensional database searching: Discovery of isoflavonoids as nonsteroidal inhibitors of rat 5 alpha-reductase
    • Chen G.S., Chang C.S., Kan W.M., Chang C.L., Wang K.C., Chern J.W. Novel lead generation through hypothetical pharmacophore three-dimensional database searching: discovery of isoflavonoids as nonsteroidal inhibitors of rat 5 alpha-reductase. J Med Chem. 44:2001;3759-3763.
    • (2001) J Med Chem , vol.44 , pp. 3759-3763
    • Chen, G.S.1    Chang, C.S.2    Kan, W.M.3    Chang, C.L.4    Wang, K.C.5    Chern, J.W.6
  • 68
    • 0034844699 scopus 로고    scopus 로고
    • A 3D QSAR study of monoamino oxidase-B inhibitors using the chemical function based pharmacophore generation approach
    • Gritsch S., Guccione S., Hoffmann R., Cambria A., Raciti G., Langer T. A 3D QSAR study of monoamino oxidase-B inhibitors using the chemical function based pharmacophore generation approach. J Enzyme Inhib. 16:2001;199-215.
    • (2001) J Enzyme Inhib , vol.16 , pp. 199-215
    • Gritsch, S.1    Guccione, S.2    Hoffmann, R.3    Cambria, A.4    Raciti, G.5    Langer, T.6
  • 69
    • 0035246393 scopus 로고    scopus 로고
    • A feature based pharmacophore for Candida albicans myristoylCoA: Protein N-myristoyltransferase inhibitors
    • Karki R.G., Kulkarni V.M. A feature based pharmacophore for Candida albicans myristoylCoA: protein N-myristoyltransferase inhibitors. Eur J Med Chem. 36:2001;147-163.
    • (2001) Eur J Med Chem , vol.36 , pp. 147-163
    • Karki, R.G.1    Kulkarni, V.M.2
  • 70
    • 0034712714 scopus 로고    scopus 로고
    • Rational design of selective submicromolar inhibitors of Tritrichomonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase
    • Aronov A.M., Munagala N.R., Ortiz De Montellano P.R., Kuntz I.D., Wang C.C. Rational design of selective submicromolar inhibitors of Tritrichomonas foetus hypoxanthine-guanine-xanthine phosphoribosyltransferase. Biochemistry. 39:2000;4684-4691.
    • (2000) Biochemistry , vol.39 , pp. 4684-4691
    • Aronov, A.M.1    Munagala, N.R.2    Ortiz De Montellano, P.R.3    Kuntz, I.D.4    Wang, C.C.5
  • 71
    • 1642288258 scopus 로고    scopus 로고
    • Novel inhibitors of DNA gyrase: 3D structure based biased needle screening, hit validation by biophysical methods, and 3D guided optimization. A promising alternative to random screening
    • Boehm H.J., Boehringer M., Bur D., Gmuender H., Huber W., Klaus W., Kostrewa D., Kuehne H., Luebbers T., Meunier-Keller N., Mueller F. Novel inhibitors of DNA gyrase: 3D structure based biased needle screening, hit validation by biophysical methods, and 3D guided optimization. A promising alternative to random screening. J Med Chem. 43:2000;2664-2674.
    • (2000) J Med Chem , vol.43 , pp. 2664-2674
    • Boehm, H.J.1    Boehringer, M.2    Bur, D.3    Gmuender, H.4    Huber, W.5    Klaus, W.6    Kostrewa, D.7    Kuehne, H.8    Luebbers, T.9    Meunier-Keller, N.10    Mueller, F.11
  • 73
    • 0036077847 scopus 로고    scopus 로고
    • The Crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: A platform for the structure-based design of antibacterial agents
    • Guilloteau J.-P., Mathieu M., Giglione C., Blanc V., Dupuy A., Chevrier M., Gil P., Famechon A., Meinnel T., Mikol V. The Crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: A platform for the structure-based design of antibacterial agents. J Molec Biol. 320:2002;951-962.
    • (2002) J Molec Biol , vol.320 , pp. 951-962
    • Guilloteau, J.-P.1    Mathieu, M.2    Giglione, C.3    Blanc, V.4    Dupuy, A.5    Chevrier, M.6    Gil, P.7    Famechon, A.8    Meinnel, T.9    Mikol, V.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.