메뉴 건너뛰기




Volumn 7, Issue 21, 2007, Pages 3919-3931

Membrane subproteomic analysis of Mycobacterium bovis bacillus Calmette-Guérin

Author keywords

Calmette Gu rin; Integral membrane protein; Membrane subproteome; Mycobacterium bovis bacillus; Shotgun; Transmembrane helix

Indexed keywords

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATASE; BCG VACCINE; CARBONATE DEHYDRATASE; CARRIER PROTEIN; HYDROGENASE; IRON SULFUR PROTEIN; MEMBRANE PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) TRANSHYDROGENASE; PROTEIN SERINE THREONINE KINASE; PROTEINASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SERINE PROTEINASE; SERINE THREONINE PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 36048982541     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700342     Document Type: Article
Times cited : (12)

References (72)
  • 2
    • 0029920827 scopus 로고    scopus 로고
    • Molecular analysis of genetic differences between Mycobacterium bovis BCG and virulent M. bovis
    • Mahairas, G., Sabo, P., Hickey, M., Singh, D. et al., ., Molecular analysis of genetic differences between Mycobacterium bovis BCG and virulent M. bovis. J. Bacteriol. 1996, 178, 1274-1282.
    • (1996) J. Bacteriol , vol.178 , pp. 1274-1282
    • Mahairas, G.1    Sabo, P.2    Hickey, M.3    Singh, D.4
  • 3
    • 0028153628 scopus 로고
    • Efficacy of BCG vaccine in the prevention of tuberculosis. Meta-analysis of the published literature
    • Colditz, G. A., Brewer, T. F., Berkey, C. S., Wilson, M. E. et al., Efficacy of BCG vaccine in the prevention of tuberculosis. Meta-analysis of the published literature. JAMA 1994, 271, 698-702.
    • (1994) JAMA , vol.271 , pp. 698-702
    • Colditz, G.A.1    Brewer, T.F.2    Berkey, C.S.3    Wilson, M.E.4
  • 4
    • 0034985066 scopus 로고    scopus 로고
    • Comparative genomics of BCG vaccines
    • Behr, M. A., Comparative genomics of BCG vaccines. Tuberculosis 2001, 81, 165-168.
    • (2001) Tuberculosis , vol.81 , pp. 165-168
    • Behr, M.A.1
  • 5
    • 27944472724 scopus 로고    scopus 로고
    • A review of vaccine research and development: Tuberculosis
    • Girard, M. P., Fruth, U., Kieny, M.-P., A review of vaccine research and development: Tuberculosis. Vaccine 2005, 23, 5725-5731.
    • (2005) Vaccine , vol.23 , pp. 5725-5731
    • Girard, M.P.1    Fruth, U.2    Kieny, M.-P.3
  • 6
    • 0033767941 scopus 로고    scopus 로고
    • New roles for structure in biology and drug discovery
    • Russell, R. B., Eggleston, D. S., New roles for structure in biology and drug discovery. Nat. Struct. Biol. 2000, 7, 928-930.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 928-930
    • Russell, R.B.1    Eggleston, D.S.2
  • 8
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni, V., Molloy, M., Rabilloud, T., Membrane proteins and proteomics: Un amour impossible? Electrophoresis 2000, 21, 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 9
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu, C. C., Yates, J. R., III, The application of mass spectrometry to membrane proteomics. Nat. Biotechnol. 2003, 21, 262-267.
    • (2003) Nat. Biotechnol , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 10
    • 0036936653 scopus 로고    scopus 로고
    • Proteome analysis of the plasma membrane of Mycobacterium tuberculosis
    • Sinha, S., Arora, S., Kosalai, K., Namane, A. et al.,., Proteome analysis of the plasma membrane of Mycobacterium tuberculosis. Comp. Funct. Genomics 2002, 3, 470-483.
    • (2002) Comp. Funct. Genomics , vol.3 , pp. 470-483
    • Sinha, S.1    Arora, S.2    Kosalai, K.3    Namane, A.4
  • 11
    • 11144329901 scopus 로고    scopus 로고
    • Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain
    • Gu, S., Chen, J., Dobos, K. M., Bradbury, E. M. et al., Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell. Proteomics 2003, 2, 1284-1296.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1284-1296
    • Gu, S.1    Chen, J.2    Dobos, K.M.3    Bradbury, E.M.4
  • 12
    • 20844432340 scopus 로고    scopus 로고
    • Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry
    • Xiong, Y., Chalmers, M. J., Gao, F. P., Cross, T. A., Marshall, A. G., Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry. J. Proteome Res. 2005, 4, 855-861.
    • (2005) J. Proteome Res , vol.4 , pp. 855-861
    • Xiong, Y.1    Chalmers, M.J.2    Gao, F.P.3    Cross, T.A.4    Marshall, A.G.5
  • 13
    • 11144293517 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling
    • Mawuenyega, K. G., Forst, C. V., Dobos, K. M., Belisle, J. T. et al., Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 2005, 16, 396-404.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 396-404
    • Mawuenyega, K.G.1    Forst, C.V.2    Dobos, K.M.3    Belisle, J.T.4
  • 14
    • 34249748332 scopus 로고    scopus 로고
    • An improved strategy for selective and efficient enrichment of integral plasma membrane proteins of mycobacteria
    • Mattow, J., Siejak, F., Hagens, K., Schmidt, F. et al., An improved strategy for selective and efficient enrichment of integral plasma membrane proteins of mycobacteria. Proteomics 2007, 7, 1687-1701.
    • (2007) Proteomics , vol.7 , pp. 1687-1701
    • Mattow, J.1    Siejak, F.2    Hagens, K.3    Schmidt, F.4
  • 15
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C., Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 1981, 256, 1604-1607.
    • (1981) J. Biol. Chem , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 16
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C., MacCoss, M. J., Howell, K. E., Yates, J. R., III, A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 2003, 21, 532-538.
    • (2003) Nat. Biotechnol , vol.21 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 18
    • 33747170862 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of Shigella flexneri 2a membrane proteins
    • Wei, C., Yang, J., Zhu, J., Zhang, X. et al., Comprehensive proteomic analysis of Shigella flexneri 2a membrane proteins. J. Proteome Res. 2006, 5, 1860-1865.
    • (2006) J. Proteome Res , vol.5 , pp. 1860-1865
    • Wei, C.1    Yang, J.2    Zhu, J.3    Zhang, X.4
  • 19
    • 0036828724 scopus 로고    scopus 로고
    • Probability-based validation of protein identifications using a modified SEQUEST algorithm
    • MacCoss, M. J., Wu, C. C., Yates, J. R., III, Probability-based validation of protein identifications using a modified SEQUEST algorithm. Anal. Chem. 2002, 74, 5593-5599.
    • (2002) Anal. Chem , vol.74 , pp. 5593-5599
    • MacCoss, M.J.1    Wu, C.C.2    Yates III, J.R.3
  • 20
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng, J., Elias, J. E., Thoreen, C. C., Licklider, L. J., Gygi, S. P., Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome. J. Proteome Res. 2003, 2, 43-50.
    • (2003) J. Proteome Res , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 21
    • 33750462019 scopus 로고    scopus 로고
    • Comparison of a proteomic approach with a microarray-based approach to detect exons in the mouse genome
    • Sheng, Q.-H., Wang, L.-S., Dai, J., Jiang, X.-S. et al., Comparison of a proteomic approach with a microarray-based approach to detect exons in the mouse genome. Nat. Genet. 2006, 38, 1223-1224.
    • (2006) Nat. Genet , vol.38 , pp. 1223-1224
    • Sheng, Q.-H.1    Wang, L.-S.2    Dai, J.3    Jiang, X.-S.4
  • 22
    • 0028302337 scopus 로고
    • Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions
    • Bjellqvist, B., Basse, B., Olsen, E., Celis, J. E., Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions. Electrophoresis 1994, 15, 529-539.
    • (1994) Electrophoresis , vol.15 , pp. 529-539
    • Bjellqvist, B.1    Basse, B.2    Olsen, E.3    Celis, J.E.4
  • 23
    • 0034899781 scopus 로고    scopus 로고
    • Evaluation of methods for the prediction of membrane-spanning regions
    • Moller, S., Croning, M. D. R., Apweiler, R., Evaluation of methods for the prediction of membrane-spanning regions. Bioinformatics 2001, 17, 646-653.
    • (2001) Bioinformatics , vol.17 , pp. 646-653
    • Moller, S.1    Croning, M.D.R.2    Apweiler, R.3
  • 24
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S. T., Brosch, R., Parkhill, J., Garnier, T. et al., Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998, 393, 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4
  • 25
    • 28444455281 scopus 로고    scopus 로고
    • Proteomic analysis of mouse liver plasma membrane: Use of differential extraction to enrich hydrophobic membrane proteins
    • Zhang, L., Xie, J., Wang, X. E., Liu, X. et al., Proteomic analysis of mouse liver plasma membrane: Use of differential extraction to enrich hydrophobic membrane proteins. Proteomics 2005, 5, 4510-4524.
    • (2005) Proteomics , vol.5 , pp. 4510-4524
    • Zhang, L.1    Xie, J.2    Wang, X.E.3    Liu, X.4
  • 26
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A., Fowler, S., Lazarow, P., Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum. J. Cell Biol. 1982, 93, 97-102.
    • (1982) J. Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.2    Fowler, S.3    Lazarow, P.4
  • 27
    • 0033673225 scopus 로고    scopus 로고
    • Complementing genomics with proteomics: The membrane subproteome of Pseudomonas aeruginosa PAO1
    • Nouwens, A. S., Cordwell, S. J., Larsen, M. R., Molloy, M. P. et al., Complementing genomics with proteomics: The membrane subproteome of Pseudomonas aeruginosa PAO1. Electrophoresis 2000, 21, 3797-3809.
    • (2000) Electrophoresis , vol.21 , pp. 3797-3809
    • Nouwens, A.S.1    Cordwell, S.J.2    Larsen, M.R.3    Molloy, M.P.4
  • 28
  • 29
    • 0032847036 scopus 로고    scopus 로고
    • Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: Towards functional genomics of microbial pathogens
    • Jungblut, P. R., Schaible, U. E., Mollenkopf, H.-J., Zimny-Arndt, U. et al., Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: Towards functional genomics of microbial pathogens. Mol. Microbiol. 1999, 33, 1103-1117.
    • (1999) Mol. Microbiol , vol.33 , pp. 1103-1117
    • Jungblut, P.R.1    Schaible, U.E.2    Mollenkopf, H.-J.3    Zimny-Arndt, U.4
  • 30
    • 9144263752 scopus 로고    scopus 로고
    • Comparative proteome analysis of Mycobacterium tuberculosis grown under aerobic and anaerobic conditions
    • Starck, J., Kallenius, G., Marklund, B.-I., Andersson, D. I., Akerlund, T., Comparative proteome analysis of Mycobacterium tuberculosis grown under aerobic and anaerobic conditions. Microbiology 2004, 150, 3821-3829.
    • (2004) Microbiology , vol.150 , pp. 3821-3829
    • Starck, J.1    Kallenius, G.2    Marklund, B.-I.3    Andersson, D.I.4    Akerlund, T.5
  • 31
    • 0032501402 scopus 로고    scopus 로고
    • Comparison of predicted and observed properties of proteins encoded in the genome of Mycobacterium Tuberculosis H37Rv
    • Urquhart, B. L., Cordwell, S. J., Humphery-Smith, I., Comparison of predicted and observed properties of proteins encoded in the genome of Mycobacterium Tuberculosis H37Rv. Biochem. Biophys. Res. Commun. 1998, 253, 70-79.
    • (1998) Biochem. Biophys. Res. Commun , vol.253 , pp. 70-79
    • Urquhart, B.L.1    Cordwell, S.J.2    Humphery-Smith, I.3
  • 32
    • 0034876416 scopus 로고    scopus 로고
    • Identification and characterization of mycobacterial proteins differentially expressed under standing and shaking culture conditions, including Rv2623 from a novel class of putative ATP-binding proteins
    • Florczyk, M. A., McCue, L. A., Stack, R. F., Hauer, C. R., McDonough, K. A., Identification and characterization of mycobacterial proteins differentially expressed under standing and shaking culture conditions, including Rv2623 from a novel class of putative ATP-binding proteins. Infect. Immun. 2001, 69, 5777-5785.
    • (2001) Infect. Immun , vol.69 , pp. 5777-5785
    • Florczyk, M.A.1    McCue, L.A.2    Stack, R.F.3    Hauer, C.R.4    McDonough, K.A.5
  • 33
    • 0035317807 scopus 로고    scopus 로고
    • Identification of acidic, low molecular mass proteins of Mycobacterium tuberculosis strain H37Rv by matrix-assisted laser/ionization and electrospray ionization mass spectrometry
    • Mattow, J., Jungblut, P. R., Müller, E.-C., Kaufmann, S. H. E., Identification of acidic, low molecular mass proteins of Mycobacterium tuberculosis strain H37Rv by matrix-assisted laser/ionization and electrospray ionization mass spectrometry. Proteomics 2001, 1, 494-507.
    • (2001) Proteomics , vol.1 , pp. 494-507
    • Mattow, J.1    Jungblut, P.R.2    Müller, E.-C.3    Kaufmann, S.H.E.4
  • 34
    • 0034855108 scopus 로고    scopus 로고
    • Identification of proteins from Mycobacterium tuber culosis missing in attenuated Mycobacterium bovis BCG strains
    • Mattow, J., Jungblut, P. R., Schaible, U. E., Mollenkopf, H.-J. et al., Identification of proteins from Mycobacterium tuber culosis missing in attenuated Mycobacterium bovis BCG strains. Electrophoresis 2001, 22, 2936-2946.
    • (2001) Electrophoresis , vol.22 , pp. 2936-2946
    • Mattow, J.1    Jungblut, P.R.2    Schaible, U.E.3    Mollenkopf, H.-J.4
  • 35
    • 0034031272 scopus 로고    scopus 로고
    • Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection
    • Rosenkrands, I., Weldingh, K., Jacobsen, S., Hansen, C. V. et al., Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Electrophoresis 2000, 21, 935-948.
    • (2000) Electrophoresis , vol.21 , pp. 935-948
    • Rosenkrands, I.1    Weldingh, K.2    Jacobsen, S.3    Hansen, C.V.4
  • 36
    • 0035836060 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption-ionization mass spectrometry peptide mass fingerprinting for proteome analysis: Identification efficiency after on-blot or in-gel digestion with and without desalting procedures
    • Lamer, S., Jungblut, P. R., Matrix-assisted laser desorption-ionization mass spectrometry peptide mass fingerprinting for proteome analysis: Identification efficiency after on-blot or in-gel digestion with and without desalting procedures. J. Chromatogr. B 2001, 752, 311-322.
    • (2001) J. Chromatogr. B , vol.752 , pp. 311-322
    • Lamer, S.1    Jungblut, P.R.2
  • 37
    • 0035319968 scopus 로고    scopus 로고
    • The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis
    • Covert, B. A., Spencer, J. S., Orme, I. M., Belisle, J. T., The application of proteomics in defining the T cell antigens of Mycobacterium tuberculosis. Proteomics 2001, 1, 574-586.
    • (2001) Proteomics , vol.1 , pp. 574-586
    • Covert, B.A.1    Spencer, J.S.2    Orme, I.M.3    Belisle, J.T.4
  • 38
  • 39
    • 30744459634 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of drug-induced changes in mycobacteria
    • Hughes, M. A., Silva, J. C., Geromanos, S. J., Townsend, C. A., Quantitative proteomic analysis of drug-induced changes in mycobacteria. J. Proteome Res. 2006, 5, 54-63.
    • (2006) J. Proteome Res , vol.5 , pp. 54-63
    • Hughes, M.A.1    Silva, J.C.2    Geromanos, S.J.3    Townsend, C.A.4
  • 40
    • 7944226058 scopus 로고    scopus 로고
    • Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components
    • Sutcliffe, I. C., Harrington, D. J., Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components. FEMS Microbiol. Rev. 2004, 28, 645-659.
    • (2004) FEMS Microbiol. Rev , vol.28 , pp. 645-659
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 41
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J. P., Locher, K. P., Structure of a bacterial multidrug ABC transporter. Nature 2006, 443, 180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.P.1    Locher, K.P.2
  • 42
    • 33846303898 scopus 로고    scopus 로고
    • Our research on proton pumping ATPases over three decades: Their biochemistry, molecular biology and cell biology
    • Futai, M., Our research on proton pumping ATPases over three decades: Their biochemistry, molecular biology and cell biology. Proc. Jpn. Acad., Ser. B 2006, 82, 416-438.
    • (2006) Proc. Jpn. Acad., Ser. B , vol.82 , pp. 416-438
    • Futai, M.1
  • 43
    • 0142071834 scopus 로고    scopus 로고
    • Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction
    • Zito, C. R., Oliver, D., Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction. J. Biol. Chem. 2003, 278, 40640-40646.
    • (2003) J. Biol. Chem , vol.278 , pp. 40640-40646
    • Zito, C.R.1    Oliver, D.2
  • 44
    • 22144496081 scopus 로고    scopus 로고
    • Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics
    • Sinha, S., Kosalai, K., Arora, S., Namane, A. et al., Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics. Microbiology 2005, 151, 2411-2419.
    • (2005) Microbiology , vol.151 , pp. 2411-2419
    • Sinha, S.1    Kosalai, K.2    Arora, S.3    Namane, A.4
  • 45
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., Doolittle, R. F., A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157, 105-132.
    • (1982) J. Mol. Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 47
    • 0034744173 scopus 로고    scopus 로고
    • Whole proteome p/values correlate with subcellular localizations of proteins for organisms within the three domains of life
    • Schwartz, R., Ting, C. S., King, J., Whole proteome p/values correlate with subcellular localizations of proteins for organisms within the three domains of life. Genome Res. 2001, 11, 703-709.
    • (2001) Genome Res , vol.11 , pp. 703-709
    • Schwartz, R.1    Ting, C.S.2    King, J.3
  • 48
    • 0031862229 scopus 로고    scopus 로고
    • Multidrug-resistant Mycobacterium tuberculosis: Molecular perspectives
    • Rattan, A., Kalia, A., Ahmad, N., Multidrug-resistant Mycobacterium tuberculosis: Molecular perspectives. Emerg. Infect. Dis. 1998, 4, 195-209.
    • (1998) Emerg. Infect. Dis , vol.4 , pp. 195-209
    • Rattan, A.1    Kalia, A.2    Ahmad, N.3
  • 49
    • 0030913996 scopus 로고    scopus 로고
    • The emb Operon, a gene cluster of Mycobacterium tuberculosis involved in resistance to ethambutol
    • Telenti, A., Philipp, W. J., Sreevatsan, S., Bernasconi, C. et al., The emb Operon, a gene cluster of Mycobacterium tuberculosis involved in resistance to ethambutol. Nat. Med. 1997, 3, 567-570.
    • (1997) Nat. Med , vol.3 , pp. 567-570
    • Telenti, A.1    Philipp, W.J.2    Sreevatsan, S.3    Bernasconi, C.4
  • 50
    • 0029908204 scopus 로고    scopus 로고
    • The embAB genes of Mycobacterium avium encode an arabinosyl transferase involved in cell wall arabinan biosynthesis that is the target for the antimycobacterial drug ethambutol
    • Belanger, A. E., Besra, G. S., Ford, M. E., Mikusovádagger, K. et al., The embAB genes of Mycobacterium avium encode an arabinosyl transferase involved in cell wall arabinan biosynthesis that is the target for the antimycobacterial drug ethambutol. Proc. Natl. Acad. Sci. USA 1996, 93, 11919-11924.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11919-11924
    • Belanger, A.E.1    Besra, G.S.2    Ford, M.E.3    Mikusovádagger, K.4
  • 51
    • 0024084857 scopus 로고
    • Divergent promoters, a common form of gene organization
    • Beck, C. F., Warren, R. A. J., Divergent promoters, a common form of gene organization. Microbiol. Rev. 1988, 52, 318-326.
    • (1988) Microbiol. Rev , vol.52 , pp. 318-326
    • Beck, C.F.1    Warren, R.A.J.2
  • 52
    • 0034194181 scopus 로고    scopus 로고
    • The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis
    • Av-Gay, Y., Everett, M., The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis. Trends Microbiol. 2000, 8, 238-244.
    • (2000) Trends Microbiol , vol.8 , pp. 238-244
    • Av-Gay, Y.1    Everett, M.2
  • 53
    • 0032728879 scopus 로고    scopus 로고
    • Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB
    • Av-Gay, Y., Jamil, S., Drews, S. J., Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB. Infect. Immun. 1999, 67, 5676-5682.
    • (1999) Infect. Immun , vol.67 , pp. 5676-5682
    • Av-Gay, Y.1    Jamil, S.2    Drews, S.J.3
  • 54
    • 23044488472 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: Substrate identification and regulation of cell shape
    • Kang, C.-M., Abbott, D. W., Park, S. T., Dascher, C. C. et al., The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: Substrate identification and regulation of cell shape. Genes Dev. 2005, 19, 1692-1704.
    • (2005) Genes Dev , vol.19 , pp. 1692-1704
    • Kang, C.-M.1    Abbott, D.W.2    Park, S.T.3    Dascher, C.C.4
  • 55
    • 31844451502 scopus 로고    scopus 로고
    • Recent advances in our knowledge of Mycobacterium bovis: A feeling for the organism
    • Hewinson, R. G., Vordermeier, H. M., Smith, N. H., Gordon, S. V., Recent advances in our knowledge of Mycobacterium bovis: A feeling for the organism. Vet. Microbiol. 2006, 112, 127-139.
    • (2006) Vet. Microbiol , vol.112 , pp. 127-139
    • Hewinson, R.G.1    Vordermeier, H.M.2    Smith, N.H.3    Gordon, S.V.4
  • 56
    • 0027516419 scopus 로고
    • Control of glycolytic enzymes through binding to cell structures and by glucose 1,6-bisphosphate under different conditions. The role of Ca2q and calmodulin
    • Beitner, R., Control of glycolytic enzymes through binding to cell structures and by glucose 1,6-bisphosphate under different conditions. The role of Ca2q and calmodulin. Int. J. Biochem. 1993, 25, 297-305.
    • (1993) Int. J. Biochem , vol.25 , pp. 297-305
    • Beitner, R.1
  • 57
    • 16244381720 scopus 로고    scopus 로고
    • The pyruvate requirement of some members of the Mycobacterium tuberculosis complex is due to an inactive pyruvate kinase: Implications for in vivo growth
    • Keating, L. A., Wheeler, P. R., Mansoor, H., K. Inwald, J. et al., The pyruvate requirement of some members of the Mycobacterium tuberculosis complex is due to an inactive pyruvate kinase: Implications for in vivo growth. Mol. Microbiol. 2005, 56, 163-174.
    • (2005) Mol. Microbiol , vol.56 , pp. 163-174
    • Keating, L.A.1    Wheeler, P.R.2    Mansoor, H.K.3    Inwald, J.4
  • 58
    • 33750056032 scopus 로고    scopus 로고
    • Comparative genomics of metabolic pathways in Mycobacterium species: Gene duplication, gene decayand lateral gene transfer
    • Marri, P. R., Bannantine, J. P., Golding, G. B., Comparative genomics of metabolic pathways in Mycobacterium species: Gene duplication, gene decayand lateral gene transfer. FEMS Microbiol. Rev. 2006, 30, 906-925.
    • (2006) FEMS Microbiol. Rev , vol.30 , pp. 906-925
    • Marri, P.R.1    Bannantine, J.P.2    Golding, G.B.3
  • 60
    • 0035823134 scopus 로고    scopus 로고
    • The xyz of ABC transporters
    • Higgins, C. F., Linton, K. J., The xyz of ABC transporters. Science 2001, 293, 1782-1784.
    • (2001) Science , vol.293 , pp. 1782-1784
    • Higgins, C.F.1    Linton, K.J.2
  • 61
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A. L., Chen, J., ATP-binding cassette transporters in bacteria. Annu. Rev. Biochem. 2004, 73, 241-268.
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 62
    • 0028061607 scopus 로고
    • Mycobacterial cell wall: Structure and role in natural resistance to antibiotics
    • Jarlier, V., Nikaido, H., Mycobacterial cell wall: Structure and role in natural resistance to antibiotics. FEMS Microbiol. Lett. 1994, 123, 11-18.
    • (1994) FEMS Microbiol. Lett , vol.123 , pp. 11-18
    • Jarlier, V.1    Nikaido, H.2
  • 63
    • 0033819143 scopus 로고    scopus 로고
    • The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis
    • Braibant, M., Gilot, P., Content, J., The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. FEMS Microbiol. Rev. 2000, 24, 449-467.
    • (2000) FEMS Microbiol. Rev , vol.24 , pp. 449-467
    • Braibant, M.1    Gilot, P.2    Content, J.3
  • 64
    • 0034445202 scopus 로고    scopus 로고
    • Molecular properties of bacterial multidrug transporters
    • Putman, M., Veen, H. W. V., Konings, W. N., Molecular properties of bacterial multidrug transporters. Microbiol. Mol. Biol. Rev. 2000, 64, 672-693.
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 672-693
    • Putman, M.1    Veen, H.W.V.2    Konings, W.N.3
  • 65
    • 19744376797 scopus 로고    scopus 로고
    • Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance
    • Domenech, P., Reed, M. B., Barry, C. E., III, Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance. Infect. Immun. 2005, 73, 3492-3501.
    • (2005) Infect. Immun , vol.73 , pp. 3492-3501
    • Domenech, P.1    Reed, M.B.2    Barry III, C.E.3
  • 66
    • 0033523971 scopus 로고    scopus 로고
    • Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice
    • Cox, J. S., Chen, B., McNeil, M., Jacobs, W. R., Jr., Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature 1999, 42, 79-83.
    • (1999) Nature , vol.42 , pp. 79-83
    • Cox, J.S.1    Chen, B.2    McNeil, M.3    Jacobs Jr., W.R.4
  • 67
    • 0038623770 scopus 로고    scopus 로고
    • MmpL8 is required for sulfolipid-1 biosynthesis and Mycobacterium tuberculosis virulence
    • Converse, S. E., Mougous, J. D., Leavell, M. D., Leary, J. A. et al., MmpL8 is required for sulfolipid-1 biosynthesis and Mycobacterium tuberculosis virulence. Proc. Natl. Acad. Sci. USA 2003, 100, 6121-6126.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6121-6126
    • Converse, S.E.1    Mougous, J.D.2    Leavell, M.D.3    Leary, J.A.4
  • 68
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-Type ATPase superfamily
    • Axelsen, K. B., Palmgren, M. G., Evolution of substrate specificities in the P-Type ATPase superfamily. J. Mol. Evol. 1998, 46, 84-101.
    • (1998) J. Mol. Evol , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 69
    • 0025823848 scopus 로고
    • Lipoprotein antigens of Mycobacterium tuberculosis
    • Young, D. B., Garbe, T. R., Lipoprotein antigens of Mycobacterium tuberculosis. Microbiol. Res. 1991, 142, 55-65.
    • (1991) Microbiol. Res , vol.142 , pp. 55-65
    • Young, D.B.1    Garbe, T.R.2
  • 70
    • 0035865232 scopus 로고    scopus 로고
    • Microbial lipopeptides stimulate dendritic cell maturation via Toll-like receptor 2
    • Hertz, C. J., Kiertscher, S. M., Godowski, P. J., Bouis, D. A. et al., Microbial lipopeptides stimulate dendritic cell maturation via Toll-like receptor 2. J. Immunol. 2001, 166, 2444-2450.
    • (2001) J. Immunol , vol.166 , pp. 2444-2450
    • Hertz, C.J.1    Kiertscher, S.M.2    Godowski, P.J.3    Bouis, D.A.4
  • 71
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti, C. M., Boyd, D. H., Rubin, E. J., Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 2003, 48, 77-84.
    • (2003) Mol. Microbiol , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 72
    • 8244238391 scopus 로고    scopus 로고
    • Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG
    • Lefevre, P., Braibant, M., Wit, L. d., Kalai, M. et al., Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG. J. Bacteriol. 1997, 179, 2900-2906.
    • (1997) J. Bacteriol , vol.179 , pp. 2900-2906
    • Lefevre, P.1    Braibant, M.2    Wit, L.D.3    Kalai, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.