메뉴 건너뛰기




Volumn 105, Issue 2-3, 2003, Pages 361-370

Structural genomics of Mycobacterium tuberculosis: A preliminary report of progress at UCLA

Author keywords

Bioinformatics; Structural genomics; Tuberculosis

Indexed keywords

85B ANTIGEN; BACTERIAL ANTIGEN; BACTERIAL PROTEIN; GLUTAMATE SYNTHASE; MPT 63 ANTIGEN; RV 2878C; UNCLASSIFIED DRUG;

EID: 10744228030     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(03)00101-7     Document Type: Article
Times cited : (32)

References (33)
  • 3
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole S.T., Brosch R., Parkhill J., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 393:1998;537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3
  • 4
    • 85031070654 scopus 로고    scopus 로고
    • http://www.doe-mbi.ucla.edu/TB/.
  • 6
    • 0032169271 scopus 로고    scopus 로고
    • Conservation of gene order: A fingerprint of proteins that physically interact
    • Dandekar T., Snel B., Huynen M., Bork P. Conservation of gene order: a fingerprint of proteins that physically interact. Trends Biochem. Sci. 23:1998;324-328.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 324-328
    • Dandekar, T.1    Snel, B.2    Huynen, M.3    Bork, P.4
  • 8
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte E.M., Pellegrini M., Ng H.L., Rice D.W., Yeates T.O., Eisenberg D. Detecting protein function and protein-protein interactions from genome sequences. Science. 285:1999;751-753.
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1    Pellegrini, M.2    Ng, H.L.3    Rice, D.W.4    Yeates, T.O.5    Eisenberg, D.6
  • 13
    • 0034717008 scopus 로고    scopus 로고
    • Granuloma-specific expression of Mycobacterium virulence proteins from the glycine-rich PE-PGRS family
    • Ramakrishnan L., Federspiel N.A., Falkow S. Granuloma-specific expression of Mycobacterium virulence proteins from the glycine-rich PE-PGRS family. Science. 288:2000;1436-1439.
    • (2000) Science , vol.288 , pp. 1436-1439
    • Ramakrishnan, L.1    Federspiel, N.A.2    Falkow, S.3
  • 14
    • 0034646354 scopus 로고    scopus 로고
    • Selecting protein targets for structural genomics of Pyrobaculum aerophilium: Validating automated fold assignment methods by using binary hypothesis testing
    • Mallick P., Goodwill K.E., Fitz-Gibbon S., Miller J.H., Eisenberg D. Selecting protein targets for structural genomics of Pyrobaculum aerophilium: validating automated fold assignment methods by using binary hypothesis testing. Proc. Natl. Acad. Sci. USA. 97:2000;2450-2455.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2450-2455
    • Mallick, P.1    Goodwill, K.E.2    Fitz-Gibbon, S.3    Miller, J.H.4    Eisenberg, D.5
  • 15
    • 0029962977 scopus 로고    scopus 로고
    • Increased cloning efficiency by temperature-cycle ligation
    • Lund A.H., Duch M., Pedersen F.S. Increased cloning efficiency by temperature-cycle ligation. Nucl. Acids Res. 24:1996;800-801.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 800-801
    • Lund, A.H.1    Duch, M.2    Pedersen, F.S.3
  • 16
    • 0035951410 scopus 로고    scopus 로고
    • Protein aggregation as bacterial inclusion bodies is reversible
    • Carrio M.M., Villaverde A. Protein aggregation as bacterial inclusion bodies is reversible. FEBS Lett. 489:2001;29-33.
    • (2001) FEBS Lett. , vol.489 , pp. 29-33
    • Carrio, M.M.1    Villaverde, A.2
  • 17
    • 0035477627 scopus 로고    scopus 로고
    • Screening for soluble expression of recombinant proteins in a 96-well format
    • Knaust R.K., Nordlund P. Screening for soluble expression of recombinant proteins in a 96-well format. Anal. Biochem. 297:2001;79-85.
    • (2001) Anal. Biochem. , vol.297 , pp. 79-85
    • Knaust, R.K.1    Nordlund, P.2
  • 18
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli E., Dobeli H., Schacher A. New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J. Chromatogr. 411:1987;177-184.
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0035997129 scopus 로고    scopus 로고
    • Ab initio crystallographic structure determination of insulin from protein to electron density without crystal handling
    • Gavira J.A., Toh D., Lopez-Jaramillo J., Garcia-Ruiz J.M., Ng J.D. Ab initio crystallographic structure determination of insulin from protein to electron density without crystal handling. Acta Crystallogr. D: Biol. Crystallogr. 58:2002;1147-1154.
    • (2002) Acta Crystallogr. D: Biol. Crystallogr. , vol.58 , pp. 1147-1154
    • Gavira, J.A.1    Toh, D.2    Lopez-Jaramillo, J.3    Garcia-Ruiz, J.M.4    Ng, J.D.5
  • 21
    • 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 (Camb.). 10:2002;147-151.
    • (2002) Structure (Camb.) , vol.10 , pp. 147-151
    • Rayment, I.1
  • 22
    • 0035937258 scopus 로고    scopus 로고
    • An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30-kDa major secretory protein (antigen 85B), a mycolyl transferase
    • Anderson D.H., Harth G., Horwitz M.A., Eisenberg D. An interfacial mechanism and a class of inhibitors inferred from two crystal structures of the Mycobacterium tuberculosis 30-kDa major secretory protein (antigen 85B), a mycolyl transferase. J. Mol. Biol. 307:2001;671-681.
    • (2001) J. Mol. Biol. , vol.307 , pp. 671-681
    • Anderson, D.H.1    Harth, G.2    Horwitz, M.A.3    Eisenberg, D.4
  • 23
    • 0028136469 scopus 로고
    • Glutamine synthetase of Mycobacterium tuberculosis: Extracellular release and characterization of its enzymatic activity
    • Harth G., Clemens D.L., Horwitz M.A. Glutamine synthetase of Mycobacterium tuberculosis: extracellular release and characterization of its enzymatic activity. PNAS. 91:1994;9342-9346.
    • (1994) PNAS , vol.91 , pp. 9342-9346
    • Harth, G.1    Clemens, D.L.2    Horwitz, M.A.3
  • 24
    • 0037031287 scopus 로고    scopus 로고
    • Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation
    • Gill H.S., Pfluegl G.M., Eisenberg D. Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation. Biochemistry. 41:2002;9863-9872.
    • (2002) Biochemistry , vol.41 , pp. 9863-9872
    • Gill, H.S.1    Pfluegl, G.M.2    Eisenberg, D.3
  • 25
    • 0034663990 scopus 로고    scopus 로고
    • The structure and function of the beta 2-adaptin appendage domain
    • Owen D.J., Vallis Y., Pearse B.M., McMahon H.T., Evans P.R. The structure and function of the beta 2-adaptin appendage domain. EMBO J. 19:2000;4216-4227.
    • (2000) EMBO J. , vol.19 , pp. 4216-4227
    • Owen, D.J.1    Vallis, Y.2    Pearse, B.M.3    McMahon, H.T.4    Evans, P.R.5
  • 26
    • 0033948978 scopus 로고    scopus 로고
    • Structural insights into clathrin-mediated endocytosis
    • Owen D.J., Luzio J.P. Structural insights into clathrin-mediated endocytosis. Curr. Opin. Cell Biol. 12:2000;467-474.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 467-474
    • Owen, D.J.1    Luzio, J.P.2
  • 27
    • 0033574274 scopus 로고    scopus 로고
    • The 2.8-Å crystal structure of visual arrestin: A model for arrestin's regulation
    • Hirsch J.A., Schubert C., Gurevich V.V., Sigler P.B. The 2.8-Å crystal structure of visual arrestin: a model for arrestin's regulation. Cell. 97:1999;257-269.
    • (1999) Cell , vol.97 , pp. 257-269
    • Hirsch, J.A.1    Schubert, C.2    Gurevich, V.V.3    Sigler, P.B.4
  • 28
    • 0033536633 scopus 로고    scopus 로고
    • Crystal structure of invasin: A bacterial integrin-binding protein
    • Hamburger Z.A., Brown M.S., Isberg R.R., Bjorkman P.J. Crystal structure of invasin: a bacterial integrin-binding protein. Science. 286:1999;291-295.
    • (1999) Science , vol.286 , pp. 291-295
    • Hamburger, Z.A.1    Brown, M.S.2    Isberg, R.R.3    Bjorkman, P.J.4
  • 29
    • 0032066057 scopus 로고    scopus 로고
    • Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus
    • Hennig M., D'Arcy A., Hampele I.C., Page M.G., Oefner C., Dale G.E. Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus. Nat. Struct. Biol. 5:1998;357-362.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 357-362
    • Hennig, M.1    D'Arcy, A.2    Hampele, I.C.3    Page, M.G.4    Oefner, C.5    Dale, G.E.6
  • 30
    • 0033617383 scopus 로고    scopus 로고
    • Structure/function analysis of a dUTPase: Catalytic mechanism of a potential chemotherapeutic target
    • Harris J.M., McIntosh E.M., Muscat G.E. Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target. J. Mol. Biol. 288:1999;275-287.
    • (1999) J. Mol. Biol. , vol.288 , pp. 275-287
    • Harris, J.M.1    McIntosh, E.M.2    Muscat, G.E.3
  • 31
    • 0035980265 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of Mycobacterium tuberculosis pantothenate synthetase
    • Zheng R., Blanchard J.S. Steady-state and pre-steady-state kinetic analysis of Mycobacterium tuberculosis pantothenate synthetase. Biochemistry. 40:2001;12904-12912.
    • (2001) Biochemistry , vol.40 , pp. 12904-12912
    • Zheng, R.1    Blanchard, J.S.2
  • 33
    • 0037407932 scopus 로고    scopus 로고
    • Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate
    • Wang S., Eisenberg D. Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate. Protein Sci. 13:2003;1097-1108.
    • (2003) Protein Sci. , vol.13 , pp. 1097-1108
    • Wang, S.1    Eisenberg, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.