메뉴 건너뛰기




Volumn 7, Issue 3, 2003, Pages 340-345

High-throughput crystallography to enhance drug discovery

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 0038198865     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(03)00062-0     Document Type: Review
Times cited : (79)

References (41)
  • 1
    • 0036558207 scopus 로고    scopus 로고
    • Structure-based screening of low-affinity compounds
    • Carr R., Jhoti H. Structure-based screening of low-affinity compounds. Drug Discov Today. 7:2003;522-527.
    • (2003) Drug Discov Today , vol.7 , pp. 522-527
    • Carr, R.1    Jhoti, H.2
  • 2
    • 0002822987 scopus 로고    scopus 로고
    • High-throughput structural proteomics using X-rays
    • Jhoti H. High-throughput structural proteomics using X-rays. Trends Biotechnol. 19:2001;S67-S71.
    • (2001) Trends Biotechnol , vol.19
    • Jhoti, H.1
  • 4
    • 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
  • 5
    • 0028297112 scopus 로고
    • Application of the three-dimensional structures of protein target molecules in structure-based drug design
    • Greer J., Erickson J.W., Baldwin J.J., Varney M.D. Application of the three-dimensional structures of protein target molecules in structure-based drug design. J Med Chem. 37:1994;1035-1054.
    • (1994) J Med Chem , vol.37 , pp. 1035-1054
    • Greer, J.1    Erickson, J.W.2    Baldwin, J.J.3    Varney, M.D.4
  • 6
    • 0032996584 scopus 로고    scopus 로고
    • Development of neuraminidase inhibitors as anti-influenza virus drugs
    • Varghese J.N. Development of neuraminidase inhibitors as anti-influenza virus drugs. Drug Dev Res. 46:1999;176-196.
    • (1999) Drug Dev Res , vol.46 , pp. 176-196
    • Varghese, J.N.1
  • 7
    • 0033757822 scopus 로고    scopus 로고
    • An overview of structural genomics
    • Burley S.K. An overview of structural genomics. Nat Struct Biol. 7(suppl):2000;932-934.
    • (2000) Nat Struct Biol , vol.7 , Issue.SUPPL. , pp. 932-934
    • Burley, S.K.1
  • 8
    • 0033757870 scopus 로고    scopus 로고
    • Structural genomics in North America
    • Terwilliger T.C. Structural genomics in North America. Nat Struct Biol. 7:2000;935-939.
    • (2000) Nat Struct Biol , vol.7 , pp. 935-939
    • Terwilliger, T.C.1
  • 9
    • 0033757915 scopus 로고    scopus 로고
    • Structural genomics in Europe: Slow start, strong finish?
    • Heinemann U. Structural genomics in Europe: slow start, strong finish? Nat Struct Biol. 7:2000;940-942.
    • (2000) Nat Struct Biol , vol.7 , pp. 940-942
    • Heinemann, U.1
  • 12
    • 0035424346 scopus 로고    scopus 로고
    • High-throughput three-dimensional protein structure determination
    • Heinemann U., Illing G., Oschkinat H. High-throughput three-dimensional protein structure determination. Curr Opin Biotechnol. 12:2001;348-354.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 348-354
    • Heinemann, U.1    Illing, G.2    Oschkinat, H.3
  • 13
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • A comprehensive review of how advances in process automation and informatics have facilitated the development of high-throughput X-ray crystallography
    • Blundell T.L., Jhoti H., Abell C. High-throughput crystallography for lead discovery in drug design. Nat Rev Drug Disc. 1:2002;45-54 A comprehensive review of how advances in process automation and informatics have facilitated the development of high-throughput X-ray crystallography.
    • (2002) Nat Rev Drug Disc , vol.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 15
    • 0033787344 scopus 로고    scopus 로고
    • Science, art and drug discovery: A personal perspective
    • Campbell S.F. Science, art and drug discovery: a personal perspective. Clin Sci. 99:2000;255-260.
    • (2000) Clin Sci , vol.99 , pp. 255-260
    • Campbell, S.F.1
  • 16
    • 0033762915 scopus 로고    scopus 로고
    • Structural genomics programs at the US National Institute of General Medical Sciences
    • Norvell J.C., Machalek A.Z. Structural genomics programs at the US National Institute of General Medical Sciences. Nat Struct Biol. 7:2000;931.
    • (2000) Nat Struct Biol , vol.7 , pp. 931
    • Norvell, J.C.1    Machalek, A.Z.2
  • 17
    • 0033761962 scopus 로고    scopus 로고
    • Structural genomics in the biotechnology sector
    • Dry S., McCarthy S., Harris T. Structural genomics in the biotechnology sector. Nat Struct Biol. 7:2000;946-949.
    • (2000) Nat Struct Biol , vol.7 , pp. 946-949
    • Dry, S.1    McCarthy, S.2    Harris, T.3
  • 18
    • 0034665455 scopus 로고    scopus 로고
    • Design of high-throughput methods of protein production for structural biology
    • Stevens R. Design of high-throughput methods of protein production for structural biology. Structure. 8:2000;177-185.
    • (2000) Structure , vol.8 , pp. 177-185
    • Stevens, R.1
  • 19
    • 0034957669 scopus 로고    scopus 로고
    • High throughput proteomics: Protein expression and purification in the post-genomic world
    • Lesley S.A. High throughput proteomics: protein expression and purification in the post-genomic world. Protein Exp Purif. 22:2001;159-164.
    • (2001) Protein Exp Purif , vol.22 , pp. 159-164
    • Lesley, S.A.1
  • 21
    • 0036830410 scopus 로고    scopus 로고
    • Structural genomics. Tapping DNA for structures produces a trickle
    • Service R.F. Structural genomics. Tapping DNA for structures produces a trickle. Science. 298:2002;948-950.
    • (2002) Science , vol.298 , pp. 948-950
    • Service, R.F.1
  • 22
    • 0003026698 scopus 로고
    • New developments of the IMPAX small volume automated crystallisation system
    • Chayen N.E., Shaw Stewart P., Baldock P. New developments of the IMPAX small volume automated crystallisation system. Acta Crystallogr. D50:1994;456-458.
    • (1994) Acta Crystallogr , vol.D50 , pp. 456-458
    • Chayen, N.E.1    Shaw Stewart, P.2    Baldock, P.3
  • 24
    • 0001011919 scopus 로고    scopus 로고
    • High-throughput X-ray crystallography for structure-based drug design
    • Goodwill K.E., Tennant M.G., Stevens R.C. High-throughput X-ray crystallography for structure-based drug design. Drug Discov Today. 6:2001;S113-S118.
    • (2001) Drug Discov Today , vol.6
    • Goodwill, K.E.1    Tennant, M.G.2    Stevens, R.C.3
  • 25
    • 0036804362 scopus 로고    scopus 로고
    • The genesis of high-throughput structure-based drug discovery using protein crystallography
    • Advances in sub-microliter, automated protein crystallisation systems and automatic crystal visualisation systems have enabled direct integration into the drug-discovery process and led to significant increases in throughput
    • Kuhn P., Wilson K., Patch M.G., Stevens R.C. The genesis of high-throughput structure-based drug discovery using protein crystallography. Curr Opin Chem Biol. 6:2002;704-710 Advances in sub-microliter, automated protein crystallisation systems and automatic crystal visualisation systems have enabled direct integration into the drug-discovery process and led to significant increases in throughput.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 704-710
    • Kuhn, P.1    Wilson, K.2    Patch, M.G.3    Stevens, R.C.4
  • 26
    • 0033794367 scopus 로고    scopus 로고
    • High-throughput crystallisation
    • A review of efforts at automation and miniaturisation of protein crystallisation
    • Stevens R.C. High-throughput crystallisation. Curr Opin Struct Biol. 10:2000;558-563 A review of efforts at automation and miniaturisation of protein crystallisation.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 558-563
    • Stevens, R.C.1
  • 27
    • 0032793833 scopus 로고    scopus 로고
    • Microdispensing technologies in drug discovery
    • Rose D. Microdispensing technologies in drug discovery. Drug Discov Today. 4:1999;411-419.
    • (1999) Drug Discov Today , vol.4 , pp. 411-419
    • Rose, D.1
  • 28
    • 0037168508 scopus 로고    scopus 로고
    • A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion
    • Hansen C.L., Skordalakes E., Berger J.M., Quake S.R. A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion. Proc Natl Acad Sci USA. 99:2002;16531-16536.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16531-16536
    • Hansen, C.L.1    Skordalakes, E.2    Berger, J.M.3    Quake, S.R.4
  • 30
    • 0036847774 scopus 로고    scopus 로고
    • Towards the automated evaluation of crystallisation trials
    • Wilson J. Towards the automated evaluation of crystallisation trials. Acta Crystallogr. D58:2002;1907-1914.
    • (2002) Acta Crystallogr , vol.D58 , pp. 1907-1914
    • Wilson, J.1
  • 31
    • 0036793549 scopus 로고    scopus 로고
    • Semi-automatic protein crystallisation system that allows in situ observation of X-ray diffraction from crystals in the drop
    • Watanabe N. Semi-automatic protein crystallisation system that allows in situ observation of X-ray diffraction from crystals in the drop. Acta Crystallogr. D58:2002;1527-1530.
    • (2002) Acta Crystallogr , vol.D58 , pp. 1527-1530
    • Watanabe, N.1
  • 32
    • 0034476897 scopus 로고    scopus 로고
    • Automated crystal mounting and data collection in protein crystallography
    • Development and use of an in-house automated crystal sample changer
    • Muchmore S.W., Olson J., Jones R., Pan J., Blum M., Greer J., Merrick S.M., Magdalinos P., Nienaber N.L. Automated crystal mounting and data collection in protein crystallography. Structure. 58:2000;243-246 Development and use of an in-house automated crystal sample changer.
    • (2000) Structure , vol.58 , pp. 243-246
    • Muchmore, S.W.1    Olson, J.2    Jones, R.3    Pan, J.4    Blum, M.5    Greer, J.6    Merrick, S.M.7    Magdalinos, P.8    Nienaber, N.L.9
  • 33
    • 12344313512 scopus 로고    scopus 로고
    • High Throughput Crystallography on an in-house source, using ACTOR
    • in press
    • Sharff AJ: High Throughput Crystallography on an in-house source, using ACTOR. Rigaku Journal 2003, in press.
    • (2003) Rigaku Journal
    • Sharff, A.J.1
  • 34
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger T.C., Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr. D55:1999;849-861.
    • (1999) Acta Crystallogr , vol.D55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 35
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.M. Maximum-likelihood density modification. Acta Crystallogr. D56:2000;965-972.
    • (2000) Acta Crystallogr , vol.D56 , pp. 965-972
    • Terwilliger, T.M.1
  • 36
    • 0036077402 scopus 로고    scopus 로고
    • ARP/wARP's model-building algorithms. I. The main chain
    • Morris R.J., Perrakis A., Lamzin V.S. ARP/wARP's model-building algorithms. I. The main chain. Acta Crystallogr. D58:2002;968-975.
    • (2002) Acta Crystallogr , vol.D58 , pp. 968-975
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 38
    • 0001928830 scopus 로고    scopus 로고
    • Antitrypanosomiasis drug development based on structures of glycolytic enzymes
    • Edited by Veerapandian P. New York: Marcel Dekker Inc
    • Verlinde CLMJ, Kim H, Bernstein BE, Mande SC, Hol WGJ: Antitrypanosomiasis drug development based on structures of glycolytic enzymes. In Structure-based Drug Design. Edited by Veerapandian P. New York: Marcel Dekker Inc; 1997:365-394.
    • (1997) Structure-based Drug Design , pp. 365-394
    • Verlinde, C.L.M.J.1    Kim, H.2    Bernstein, B.E.3    Mande, S.C.4    Hol, W.G.J.5
  • 39
    • 0033773899 scopus 로고    scopus 로고
    • Discovering novel ligands for macromolecules using X-ray crystallographic screening
    • How to use fragment based approach to high-throughput 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 Biotech. 18:2000;1105-1108 How to use fragment based approach to high-throughput X-ray crystallographic screening.
    • (2000) Nat Biotech , 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
  • 40
    • 0037030686 scopus 로고    scopus 로고
    • SAR and X-ray. A new approach combining fragment-based screening and rational drug design: Application to the discovery of nanomolar inhibitors of Src SH2
    • Lesuisse D., Lange G., Deprez P., Benard D., Schoot B., Delettre G., Marquette J.P., Broto P., Jean-Baptiste V., Bichet P.et al. SAR and X-ray. A new approach combining fragment-based screening and rational drug design: application to the discovery of nanomolar inhibitors of Src SH2. J Med Chem. 45:2002;2379-2387.
    • (2002) J Med Chem , vol.45 , pp. 2379-2387
    • Lesuisse, D.1    Lange, G.2    Deprez, P.3    Benard, D.4    Schoot, B.5    Delettre, G.6    Marquette, J.P.7    Broto, P.8    Jean-Baptiste, V.9    Bichet, P.10
  • 41
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimated solubility and permeability in drug discovery and development
    • Lipinski C.A., Lombardo F., Dominy B.W., Feeney P.J. Experimental and computational approaches to estimated solubility and permeability in drug discovery and development. Adv Drug Delivery Res. 46:2001;3-26.
    • (2001) Adv Drug Delivery Res , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.