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Volumn 10, Issue 10, 2002, Pages

Structural proteomics: The potential of high-throughput structure determination

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT;

EID: 0036791908     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0966-842X(02)02443-5     Document Type: Review
Times cited : (35)

References (38)
  • 1
    • 0036050539 scopus 로고    scopus 로고
    • Strategies in the design of antiviral drugs
    • De Clercq E. Strategies in the design of antiviral drugs. Nat. Rev. Drug Discov. 1:2002;13-25.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 13-25
    • De Clercq, E.1
  • 2
    • 0034331314 scopus 로고    scopus 로고
    • Transposon-based approaches to identify essential bacterial genes
    • Judson N., Mekalanos J.J. Transposon-based approaches to identify essential bacterial genes. Trends Microbiol. 8:2000;521-526.
    • (2000) Trends Microbiol. , vol.8 , pp. 521-526
    • Judson, N.1    Mekalanos, J.J.2
  • 3
    • 0032134269 scopus 로고    scopus 로고
    • Novel approaches to the discovery of antimicrobial agents
    • Schmid M.B. Novel approaches to the discovery of antimicrobial agents. Curr. Opin. Chem. Biol. 2:1998;529-534.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 529-534
    • Schmid, M.B.1
  • 4
    • 0036256037 scopus 로고    scopus 로고
    • An array of target-specific screening strains for antibacterial discovery
    • DeVito J.A., et al. An array of target-specific screening strains for antibacterial discovery. Nat. Biotechnol. 20:2002;478-483.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 478-483
    • DeVito, J.A.1
  • 5
    • 0034687158 scopus 로고    scopus 로고
    • Regulated gene expression in Staphylococcus aureus for identifying conditional lethal phenotypes and antibiotic mode of action
    • Zhang L., et al. Regulated gene expression in Staphylococcus aureus for identifying conditional lethal phenotypes and antibiotic mode of action. Gene. 255:2000;297-305.
    • (2000) Gene , vol.255 , pp. 297-305
    • Zhang, L.1
  • 6
    • 0035395224 scopus 로고    scopus 로고
    • Phage display for target-based antibacterial drug discovery
    • Christensen D.J., et al. Phage display for target-based antibacterial drug discovery. Drug Discov. Today. 6:2001;721-727.
    • (2001) Drug Discov. Today , vol.6 , pp. 721-727
    • Christensen, D.J.1
  • 7
    • 0036090929 scopus 로고    scopus 로고
    • Novel targets for the future development of antibacterial agents
    • McDevitt D., et al. Novel targets for the future development of antibacterial agents. J. Appl. Microbiol. 92:(Suppl):2002;S28-S34.
    • (2002) J. Appl. Microbiol. , vol.92 , Issue.SUPPL.
    • McDevitt, D.1
  • 8
    • 0035581737 scopus 로고    scopus 로고
    • Exploiting genomics to discover new antibiotics
    • McDevitt D., Rosenberg M. Exploiting genomics to discover new antibiotics. Trends Microbiol. 9:2001;611-617.
    • (2001) Trends Microbiol. , vol.9 , pp. 611-617
    • McDevitt, D.1    Rosenberg, M.2
  • 9
    • 0034995092 scopus 로고    scopus 로고
    • Completeness in structural genomics
    • Vitkup D., et al. Completeness in structural genomics. Nat. Struct. Biol. 8:2001;559-566.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 559-566
    • Vitkup, D.1
  • 10
    • 0035703310 scopus 로고    scopus 로고
    • Processing and evaluation of predictions in CASP4
    • Zemla A., et al. Processing and evaluation of predictions in CASP4. Proteins. 45:(Suppl. 5):2001;13-21.
    • (2001) Proteins , vol.45 , Issue.SUPPL. 5 , pp. 13-21
    • Zemla, A.1
  • 11
    • 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. Structure Fold Des. 8:2000;R177-R185.
    • (2000) Structure Fold Des. , vol.8
    • Stevens, R.C.1
  • 12
    • 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.
    • (2001) Protein Expr. Purif. , vol.22 , pp. 159-164
    • Lesley, S.A.1
  • 13
    • 0033768325 scopus 로고    scopus 로고
    • Protein production: Feeding the crystallographers and NMR spectroscopists
    • Edwards A.M., et al. Protein production: feeding the crystallographers and NMR spectroscopists. Nat. Struct. Biol. 7:(Suppl):2000;970-972.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 970-972
    • Edwards, A.M.1
  • 14
    • 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
  • 15
    • 0035812704 scopus 로고    scopus 로고
    • Global efforts in structural genomics
    • Stevens R.C., et al. Global efforts in structural genomics. Science. 294:2001;89-92.
    • (2001) Science , vol.294 , pp. 89-92
    • Stevens, R.C.1
  • 16
    • 0033785799 scopus 로고    scopus 로고
    • Structural proteomics of an archaeon
    • Christendat D., et al. Structural proteomics of an archaeon. Nat. Struct. Biol. 7:2000;903-909.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 903-909
    • Christendat, D.1
  • 17
    • 0036129154 scopus 로고    scopus 로고
    • Structural genomics: A pipeline for providing structures for the biologist
    • Chance M.R., et al. Structural genomics: a pipeline for providing structures for the biologist. Protein Sci. 11:2002;723-738.
    • (2002) Protein Sci. , vol.11 , pp. 723-738
    • Chance, M.R.1
  • 18
    • 18244366113 scopus 로고    scopus 로고
    • An NMR approach to structural proteomics
    • Yee A., et al. An NMR approach to structural proteomics. Proc. Natl. Acad. Sci. U. S. A. 99:2002;1825-1830.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1825-1830
    • Yee, A.1
  • 19
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • Hammarstrom M., et al. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 11:2002;313-321.
    • (2002) Protein Sci. , vol.11 , pp. 313-321
    • Hammarstrom, M.1
  • 20
    • 0036175235 scopus 로고    scopus 로고
    • Small-scale batch crystallization of proteins revisited: An underutilized way to grow large protein crystals
    • Rayment I. Small-scale batch crystallization of proteins revisited: an underutilized way to grow large protein crystals. Structure. 10:2002;147-151.
    • (2002) Structure , vol.10 , pp. 147-151
    • Rayment, I.1
  • 21
    • 0036075170 scopus 로고    scopus 로고
    • Protein crystallization for genomics: Towards high-throughput optimization techniques
    • Chayen N.E., Saridakis E. Protein crystallization for genomics: towards high-throughput optimization techniques. Acta Crystallogr. D. Biol. Crystallogr. 58:2002;921-927.
    • (2002) Acta Crystallogr. D. Biol. Crystallogr. , vol.58 , pp. 921-927
    • Chayen, N.E.1    Saridakis, E.2
  • 22
    • 0036137978 scopus 로고    scopus 로고
    • Fast drops: A high-throughput approach for setting up protein crystal screens
    • Villasenor A., et al. Fast drops: a high-throughput approach for setting up protein crystal screens. BioTechniques. 32:2002;184-189.
    • (2002) BioTechniques , vol.32 , pp. 184-189
    • Villasenor, A.1
  • 23
    • 0035394771 scopus 로고    scopus 로고
    • SPINE: An integrated tracking database and data mining approach for identifying feasible targets in high-throughput structural proteomics
    • Bertone P., et al. SPINE: an integrated tracking database and data mining approach for identifying feasible targets in high-throughput structural proteomics. Nucleic Acids Res. 29:2001;2884-2898.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2884-2898
    • Bertone, P.1
  • 24
    • 0033767365 scopus 로고    scopus 로고
    • Automation of X-ray crystallography
    • Abola E., et al. Automation of X-ray crystallography. Nat. Struct. Biol. 7:(Suppl):2000;973-977.
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 973-977
    • Abola, E.1
  • 25
    • 0033772589 scopus 로고    scopus 로고
    • Advances in multiple wavelength anomalous diffraction crystallography
    • Ealick S.E. Advances in multiple wavelength anomalous diffraction crystallography. Curr. Opin. Chem. Biol. 4:2000;495-499.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 495-499
    • Ealick, S.E.1
  • 26
    • 0036584359 scopus 로고    scopus 로고
    • Timeline: The march of structural biology
    • Campbell I.D. Timeline: the march of structural biology. Nat. Rev. Mol. Cell Biol. 3:2002;377-381.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 377-381
    • Campbell, I.D.1
  • 27
    • 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
  • 28
    • 0032705719 scopus 로고    scopus 로고
    • Mode of action of fluoroquinolones
    • Hooper D.C. Mode of action of fluoroquinolones. Drugs. 58:(Suppl. 2):1999;6-10.
    • (1999) Drugs , vol.58 , Issue.SUPPL. 2 , pp. 6-10
    • Hooper, D.C.1
  • 29
    • 0034792726 scopus 로고    scopus 로고
    • The role of combichem in antibiotic discovery
    • Trias J. The role of combichem in antibiotic discovery. Curr. Opin. Microbiol. 4:2001;520-525.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 520-525
    • Trias, J.1
  • 30
    • 0037130227 scopus 로고    scopus 로고
    • Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI)
    • Miller W.H., et al. Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI). J. Med. Chem. 45:2002;3246-3256.
    • (2002) J. Med. Chem. , vol.45 , pp. 3246-3256
    • Miller, W.H.1
  • 31
    • 0035805213 scopus 로고    scopus 로고
    • Crystal structure of the ribosome at 5.5 Å resolution
    • Yusupov M.M., et al. Crystal structure of the ribosome at 5.5 Å resolution. Science. 292:2001;883-896.
    • (2001) Science , vol.292 , pp. 883-896
    • Yusupov, M.M.1
  • 32
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., et al. The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science. 289:2000;905-920.
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1
  • 33
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • Murakami K.S., et al. Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution. Science. 296:2002;1280-1284.
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1
  • 34
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • Murakami K.S., et al. Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science. 296:2002;1285-1290.
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1
  • 35
    • 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., et al. 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. Mol. Biol. 320:2002;951-962.
    • (2002) J. Mol. Biol. , vol.320 , pp. 951-962
    • Guilloteau, J.P.1
  • 36
    • 0034322059 scopus 로고    scopus 로고
    • Identification of a potent peptide deformylase inhibitor from a rationally designed combinatorial library
    • Wei Y., et al. Identification of a potent peptide deformylase inhibitor from a rationally designed combinatorial library. J. Comb. Chem. 2:2000;650-657.
    • (2000) J. Comb. Chem. , vol.2 , pp. 650-657
    • Wei, Y.1
  • 37
    • 0035806083 scopus 로고    scopus 로고
    • Identification of novel potent hydroxamic acid inhibitors of peptidyl deformylase and the importance of the hydroxamic acid functionality on inhibition
    • Thorarensen A., et al. Identification of novel potent hydroxamic acid inhibitors of peptidyl deformylase and the importance of the hydroxamic acid functionality on inhibition. Bioorg. Med. Chem. Lett. 11:2001;1355-1358.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 1355-1358
    • Thorarensen, A.1
  • 38
    • 0035821593 scopus 로고    scopus 로고
    • 2-(2-Oxo-1,4-dihydro-2H-quinazolin-3-yl)- and 2-(2,2-dioxo-1,4-dihydro-2H-2(6-benzo[1,2,6]thiadiazin-3-yl)-N-hydrox y-acetamides as potent and selective peptide deformylase inhibitors
    • Apfel C., et al. 2-(2-Oxo-1,4-dihydro-2H-quinazolin-3-yl)- and 2-(2,2-dioxo-1,4-dihydro-2H-2(6-benzo [1,2,6] thiadiazin-3-yl)-N-hydrox y-acetamides as potent and selective peptide deformylase inhibitors. J. Med. Chem. 44:2001;1847-1852.
    • (2001) J. Med. Chem. , vol.44 , pp. 1847-1852
    • Apfel, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.