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Volumn 85, Issue 7, 2003, Pages 878-885

Structural genomics of microbial pathogens - An Indian programme

Author keywords

[No Author keywords available]

Indexed keywords

LACUNA; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS;

EID: 4444381512     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (3)

References (26)
  • 1
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J. S., The anatomy and taxonomy of protein structure. Adv. Protein Chem., 1981, 34, 168-339.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 168-339
    • Richardson, J.S.1
  • 3
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, T. and Chothia, C., SCOP: A structural classification of proteins database for the investigation of sequences and structures. J. Mol. Bol., 1995, 247, 536-540.
    • (1995) J. Mol. Bol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 4
    • 0033954256 scopus 로고    scopus 로고
    • The Protein Data Bank
    • Berman, H. M. et al., The Protein Data Bank. Nucleic Acids Res., 2000, 28, 235-242.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 235-242
    • Berman, H.M.1
  • 5
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F. C. et al., The Protein Data Bank: A computer-based archival file for macromolecular structures. J. Mol. Biol., 1977, 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1
  • 8
    • 0034671684 scopus 로고    scopus 로고
    • Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-A1F(4): Implications for decreased ATPase activity and molecular aggregation
    • Datta, S. et al., Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-A1F(4): Implications for decreased ATPase activity and molecular aggregation. Nucleic Acid Res., 2000, 28, 4964-4973.
    • (2000) Nucleic Acid Res. , vol.28 , pp. 4964-4973
    • Datta, S.1
  • 9
    • 0037441480 scopus 로고    scopus 로고
    • Structural studies on MtRecA-nucleotide complexes: Insights into DNA and nucleotide binding and the structural signature of NTP recognition
    • Datta, S., Ganesh, N., Chandra, N. R., Muniyappa, K. and Vijayan, M., Structural studies on MtRecA-nucleotide complexes: Insights into DNA and nucleotide binding and the structural signature of NTP recognition. Proteins: Struct. Funct. Genet., 2003, 50, 474-485.
    • (2003) Proteins: Struct. Funct. Genet. , vol.50 , pp. 474-485
    • Datta, S.1    Ganesh, N.2    Chandra, N.R.3    Muniyappa, K.4    Vijayan, M.5
  • 10
    • 0030029470 scopus 로고    scopus 로고
    • Functional characterization of the precursor and spliced forms of RecA protein of Mycobacterium tuberculosis
    • Kumar, R. A., Vaze, M. B., Chandra, N. R., Vijayan, M. and Muniyappa, K., Functional characterization of the precursor and spliced forms of RecA protein of Mycobacterium tuberculosis. Biochemistry, 1996, 35, 1793-1802.
    • (1996) Biochemistry , vol.35 , pp. 1793-1802
    • Kumar, R.A.1    Vaze, M.B.2    Chandra, N.R.3    Vijayan, M.4    Muniyappa, K.5
  • 11
    • 0038153902 scopus 로고    scopus 로고
    • Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes
    • Datta, S., Krishna, R., Ganesh, N., Chandra, N. R., Muniyappa, K. and Vijayan, M., Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes. J. Bacteriol., 2003, 185, 4280-4284.
    • (2003) J. Bacteriol. , vol.185 , pp. 4280-4284
    • Datta, S.1    Krishna, R.2    Ganesh, N.3    Chandra, N.R.4    Muniyappa, K.5    Vijayan, M.6
  • 12
    • 0041819759 scopus 로고    scopus 로고
    • Mycobacterium smegmatis RecA protein is structurally similar to but functionally distinct from Mycobacterium tuberculosis RecA
    • in press
    • Ganesh, N. and Muniyappa, K., Mycobacterium smegmatis RecA protein is structurally similar to but functionally distinct from Mycobacterium tuberculosis RecA. Proteins: Struct. Funct. Genet., 2003 (in press).
    • (2003) Proteins: Struct. Funct. Genet.
    • Ganesh, N.1    Muniyappa, K.2
  • 13
    • 0036008519 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray studies of the single-stranded DNA-binding protein from Mycobacterium tuberculosis
    • Saikrishnan, K. et al., Crystallization and preliminary X-ray studies of the single-stranded DNA-binding protein from Mycobacterium tuberculosis. Acta Crystallogr., 2002, D58, 327-329.
    • (2002) Acta Crystallogr. , vol.D58 , pp. 327-329
    • Saikrishnan, K.1
  • 14
    • 0041347886 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications
    • Saikrishnan, K. et al., Structure of Mycobacterium tuberculosis single-stranded DNA-binding protein. Variability in quaternary structure and its implications. J. Mol. Biol., 2003, 331, 385-393.
    • (2003) J. Mol. Biol. , vol.331 , pp. 385-393
    • Saikrishnan, K.1
  • 15
    • 0036008510 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 Å resolution
    • Taneja, B. and Mande, S. C., Structure of Mycobacterium tuberculosis chaperonin-10 at 3.5 Å resolution. Acta Crystallogr., 2002, D58, 260-266.
    • (2002) Acta Crystallogr. , vol.D58 , pp. 260-266
    • Taneja, B.1    Mande, S.C.2
  • 16
    • 0035860329 scopus 로고    scopus 로고
    • Crystal structure of Rv2118c: An AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv
    • Gupta, A., Kumar, P. H., Dineshkumar, T. K., Varshney, U. and Subramanya, H. S., Crystal structure of Rv2118c: An AdoMet-dependent methyltransferase from Mycobacterium tuberculosis H37Rv. J. Mol. Biol., 2001, 312, 381-391.
    • (2001) J. Mol. Biol. , vol.312 , pp. 381-391
    • Gupta, A.1    Kumar, P.H.2    Dineshkumar, T.K.3    Varshney, U.4    Subramanya, H.S.5
  • 19
    • 0041347544 scopus 로고    scopus 로고
    • Determination of the structure of the recombinant T = 1 capsid of sesbania mosaic virus
    • Sangita, V. et al., Determination of the structure of the recombinant T = 1 capsid of sesbania mosaic virus. Curr. Sci., 2002, 82, 1123-1131.
    • (2002) Curr. Sci. , vol.82 , pp. 1123-1131
    • Sangita, V.1
  • 20
    • 0037458571 scopus 로고    scopus 로고
    • Mutation of interfacial residues disrupts subunit folding and particle assembly of physalis mottle tymovirus
    • Uma Shankar, M., Murthy, M. R. N. and Savithri, H. S., Mutation of interfacial residues disrupts subunit folding and particle assembly of physalis mottle tymovirus. J. Biol. Chem., 2003, 278, 6145-6152.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6145-6152
    • Uma Shankar, M.1    Murthy, M.R.N.2    Savithri, H.S.3
  • 21
    • 0035314020 scopus 로고    scopus 로고
    • 1.9 Å X-ray study shows closed flap conformation in crystals of tethered HIV-1 PR
    • Pillai, B., Kannan, K. K. and Hosur, M. V., 1.9 Å X-ray study shows closed flap conformation in crystals of tethered HIV-1 PR. Proteins: Struct. Funct. Genet., 2001, 43, 57-64.
    • (2001) Proteins: Struct. Funct. Genet. , vol.43 , pp. 57-64
    • Pillai, B.1    Kannan, K.K.2    Hosur, M.V.3
  • 22
    • 0031570683 scopus 로고    scopus 로고
    • Triosephosphate isomerase from Plasmodium falciparum: The crystal structure provides insights into antimalarial drug design
    • Velankar, S. S. et al., Triosephosphate isomerase from Plasmodium falciparum: The crystal structure provides insights into antimalarial drug design. Structure, 1997, 5, 751-761.
    • (1997) Structure , vol.5 , pp. 751-761
    • Velankar, S.S.1
  • 23
    • 0037336247 scopus 로고    scopus 로고
    • Structure of a gametocyte protein essential for sexual development in Plasmodium falciparum
    • Sharma, A., Sharma, I., Kogkasuriyachai, D. and Kumar, N., Structure of a gametocyte protein essential for sexual development in Plasmodium falciparum. Nature Struct. Biol., 2003, 10, 197-203.
    • (2003) Nature Struct. Biol. , vol.10 , pp. 197-203
    • Sharma, A.1    Sharma, I.2    Kogkasuriyachai, D.3    Kumar, N.4
  • 24
    • 0036795477 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of cyclophilin from Leishmania donovani
    • Banerjee, R., Datta, M., Sen, M. and Datta, A. K., Crystallization and preliminary X-ray analysis of cyclophilin from Leishmania donovani. Acta Crystallogr., 2002, D58, 1846-1847.
    • (2002) Acta Crystallogr. , vol.D58 , pp. 1846-1847
    • Banerjee, R.1    Datta, M.2    Sen, M.3    Datta, A.K.4
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 1991, 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 26
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. and Honnig, B., Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet., 1991, 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honnig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.