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Volumn 13, Issue 4, 2004, Pages 1155-1163

An improved crystal form of Plasmodium falciparum peptide deformylase

Author keywords

Crystal engineering; Drug design; Malaria; PDF; Plasmodium

Indexed keywords

ANTIMALARIAL AGENT; ENZYME INHIBITOR; LIGAND; MONOMER; PEPTIDE DEFORMYLASE; TRIPEPTIDE;

EID: 1842611335     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03456404     Document Type: Article
Times cited : (28)

References (23)
  • 1
    • 0035084128 scopus 로고    scopus 로고
    • Peptide deformylase as an antibacterial drug target: Assays for detection of its inhibition in Escherichia coli cell homogenates and intact cells
    • Apfel, C.M., Evers, S., Hubschwerlen, C., Pirson, W., Page, M.G., and Keck, W. 2001a. Peptide deformylase as an antibacterial drug target: Assays for detection of its inhibition in Escherichia coli cell homogenates and intact cells. Antimicrob. Agents Chemother. 45: 1053-1057.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1053-1057
    • Apfel, C.M.1    Evers, S.2    Hubschwerlen, C.3    Pirson, W.4    Page, M.G.5    Keck, W.6
  • 9
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. 1991. Molscript - A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24: 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 10
    • 0036124280 scopus 로고    scopus 로고
    • Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design
    • Kumar, A., Nguyen, K.T., Srivathsan, S., Ornstein, B., Turley, S., Hirsh, I., Pei, D., and Hol, W.G. 2002. Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design. Structure 10: 357-367.
    • (2002) Structure , vol.10 , pp. 357-367
    • Kumar, A.1    Nguyen, K.T.2    Srivathsan, S.3    Ornstein, B.4    Turley, S.5    Hirsh, I.6    Pei, D.7    Hol, W.G.8
  • 11
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A. and Bacon, D.J. 1997. Raster3D: Photorealistic molecular graphics. Macromol. Crystal. Pt B 277: 505-524.
    • (1997) Macromol. Crystal. , vol.277 , Issue.PART B , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 13
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A., and Dodson, E.J. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53: 240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 14
    • 0042473206 scopus 로고    scopus 로고
    • Characterization of a human peptide deformylase: Implications for antibacterial drug design
    • Nguyen, K.T., Hu, X., Colton, C., Chakrabarti, R., Zhu, M.X., and Pei, D. 2003. Characterization of a human peptide deformylase: Implications for antibacterial drug design. Biochemistry 42: 9952-9958.
    • (2003) Biochemistry , vol.42 , pp. 9952-9958
    • Nguyen, K.T.1    Hu, X.2    Colton, C.3    Chakrabarti, R.4    Zhu, M.X.5    Pei, D.6
  • 15
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R.J. 1986. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42: 140-149.
    • (1986) Acta Crystallogr. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 16
    • 0037378039 scopus 로고    scopus 로고
    • In vitro activity of a new antibiotic, NVP-PDF386 (VRC4887), against Chlamydia pneumoniae
    • Roblin, P.M. and Hammerschlag, M.R. 2003. In vitro activity of a new antibiotic, NVP-PDF386 (VRC4887), against Chlamydia pneumoniae. Antimicrob. Agents Chemother. 47: 1447-1448.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 1447-1448
    • Roblin, P.M.1    Hammerschlag, M.R.2
  • 17
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. and Teplyakov, A. 1997. MOLREP: An automated program for molecular replacement. J. Appl. Cryst. 30: 1022-1025.
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 18
    • 0030158429 scopus 로고    scopus 로고
    • PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules
    • van Aalten, D.M., Bywater, R., Findlay, J.B., Hendlich, M., Hooft, R.W., and Vriend, G. 1996. PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. J. Comput. Aided Mol. Des. 10: 255-263.
    • (1996) J. Comput. Aided Mol. Des. , vol.10 , pp. 255-263
    • Van Aalten, D.M.1    Bywater, R.2    Findlay, J.B.3    Hendlich, M.4    Hooft, R.W.5    Vriend, G.6
  • 19
    • 0035066836 scopus 로고    scopus 로고
    • Global indicators of X-ray data quality
    • Weiss, M.S. 2001. Global indicators of X-ray data quality. J. Appl. Crystallogr. 34: 130-135.
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 130-135
    • Weiss, M.S.1
  • 22
    • 0036210712 scopus 로고    scopus 로고
    • In vitro activities of peptide deformylase inhibitors against gram-positive pathogens
    • Wise, R., Andrews, J.M., and Ashby, J. 2002. In vitro activities of peptide deformylase inhibitors against gram-positive pathogens. Antimicrob. Agents Chemother. 46: 1117-1118.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1117-1118
    • Wise, R.1    Andrews, J.M.2    Ashby, J.3
  • 23
    • 0032077212 scopus 로고    scopus 로고
    • A flash-annealing technique to improve diffraction limits and lower mosaicity in crystals of glycerol kinase
    • Yeh, J.I. and Hol, W.G. 1998. A flash-annealing technique to improve diffraction limits and lower mosaicity in crystals of glycerol kinase. Acta Crystallogr. D Biol. Crystallogr. 54: 479-480.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 479-480
    • Yeh, J.I.1    Hol, W.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.