메뉴 건너뛰기




Volumn 11, Issue 1, 2012, Pages 119-130

Characterization of the mycobacterium tuberculosis proteome by liquid chromatography mass spectrometry-based proteomics techniques: A comprehensive resource for tuberculosis research

Author keywords

enrichment; mass spectrometry; membrane proteins; Mycobacterium tuberculosis; protein localization; WGA

Indexed keywords

30S RIBOSOMAL PROTEIN S5; 50S RIBOSOMAL PROTEIN L19; 50S RIBOSOMAL PROTEIN L2; ACYL COA SYNTHETASE PROTEIN; AMIDASE; BACTERIAL PROTEIN; BACTERIUM LYSATE; CONSERVED HYPOTHETICAL PROTEIN CFP17; DNA DIRECTED RNA POLYMERASE SUBUNIT BETA; F0F1 ATP SYNTHASE SUBUNIT A; F0F1 ATP SYNTHASE SUBUNIT ALPHA; HYPOTHETICAL PROTEIN RV1194C; HYPOTHETICAL PROTEIN RV2298; HYPOTHETICAL PROTEIN RV2449C; HYPOTHETICAL PROTEIN RV3130C; MEMBRANE PROTEIN; METHIONINE ADENOSYLTRANSFERASE; MYCOBACTERIUM ANTIGEN; POSSIBLE LIPOPROTEIN LPRC; PROBABLE CONSERVED TRANSMEMBRANE PROTEIN; PROBABLE CYTOCHROME C OXIDASE POLYPEPTIDE I CTAD; PROBABLE METAL CATION TRANSPORTER P-TYPE ATPASE CTPV; PROBABLE TRANSMEMBRANE CYTOCHROME C OXIDASE SUBUNIT II CTAC; PROBABLE UBIQUINOL CYTOCHROME C REDUCTASE QCRB; PUTATIVE TUBERCULIN RELATED PEPTIDE; UNCLASSIFIED DRUG; WHEAT GERM AGGLUTININ;

EID: 84862908770     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr2007939     Document Type: Article
Times cited : (63)

References (80)
  • 3
    • 77951518283 scopus 로고    scopus 로고
    • Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv
    • Malen, H.; Pathak, S.; Softeland, T.; de Souza, G. A.; Wiker, H. G. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv BMC Microbiol. 2010, 10, 132
    • (2010) BMC Microbiol. , vol.10 , pp. 132
    • Malen, H.1    Pathak, S.2    Softeland, T.3    De Souza, G.A.4    Wiker, H.G.5
  • 4
    • 0026015735 scopus 로고
    • Purification of rat liver plasma membranes by wheat-germ-agglutinin affinity partitioning
    • Persson, A.; Johansson, B.; Olsson, H.; Jergil, B. Purification of rat liver plasma membranes by wheat-germ-agglutinin affinity partitioning Biochem. J. 1991, 273 (Pt 1) 173-7
    • (1991) Biochem. J. , vol.273 , Issue.PART 1 , pp. 173-7
    • Persson, A.1    Johansson, B.2    Olsson, H.3    Jergil, B.4
  • 5
    • 33644663350 scopus 로고    scopus 로고
    • Proteomic analysis of brain plasma membranes isolated by affinity two-phase partitioning
    • DOI 10.1074/mcp.T500017-MCP200
    • Schindler, J.; Lewandrowski, U.; Sickmann, A.; Friauf, E.; Nothwang, H. G. Proteomic analysis of brain plasma membranes isolated by affinity two-phase partitioning Mol. Cell. Proteomics 2006, 5 (2) 390-400 (Pubitemid 43329316)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.2 , pp. 390-400
    • Schindler, J.1    Lewandrowski, U.2    Sickmann, A.3    Friauf, E.4    Nothwang, H.G.5
  • 6
    • 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 (4) 574-86 (Pubitemid 33588310)
    • (2001) Proteomics , vol.1 , Issue.4 , pp. 574-586
    • Covert, B.A.1    Spencer, J.S.2    Orme, I.M.3    Belisle, J.T.4
  • 7
    • 77957192821 scopus 로고    scopus 로고
    • Using a label-free proteomics method to identify differentially abundant proteins in closely related hypo- and hypervirulent clinical Mycobacterium tuberculosis Beijing isolates
    • de Souza, G. A.; Fortuin, S.; Aguilar, D.; Pando, R. H.; McEvoy, C. R.; van Helden, P. D.; Koehler, C. J.; Thiede, B.; Warren, R. M.; Wiker, H. G. Using a label-free proteomics method to identify differentially abundant proteins in closely related hypo- and hypervirulent clinical Mycobacterium tuberculosis Beijing isolates Mol. Cell. Proteomics 2010, 9 (11) 2414-23
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.11 , pp. 2414-23
    • De Souza, G.A.1    Fortuin, S.2    Aguilar, D.3    Pando, R.H.4    McEvoy, C.R.5    Van Helden, P.D.6    Koehler, C.J.7    Thiede, B.8    Warren, R.M.9    Wiker, H.G.10
  • 9
    • 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.; Belisle, J. T.; Chen, X. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain Mol. Cell. Proteomics 2003, 2 (12) 1284-96
    • (2003) Mol. Cell. Proteomics , vol.2 , Issue.12 , pp. 1284-96
    • Gu, S.1    Chen, J.2    Dobos, K.M.3    Bradbury, E.M.4    Belisle, J.T.5    Chen, X.6
  • 10
    • 0032847036 scopus 로고    scopus 로고
    • Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: Towards functional genomics of microbial pathogens
    • DOI 10.1046/j.1365-2958.1999.01549.x
    • Jungblut, P. R.; Schaible, U. E.; Mollenkopf, H. J.; Zimny-Arndt, U.; Raupach, B.; Mattow, J.; Halada, P.; Lamer, S.; Hagens, K.; Kaufmann, S. H. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens Mol. Microbiol. 1999, 33 (6) 1103-17 (Pubitemid 29433617)
    • (1999) Molecular Microbiology , vol.33 , Issue.6 , pp. 1103-1117
    • Jungblut, P.R.1    Schaible, U.E.2    Mollenkopf, H.-J.3    Zimny-Arndt, U.4    Raupach, B.5    Mattow, J.6    Halada, P.7    Lamer, S.8    Hagens, K.9    Kaufmann, S.H.E.10
  • 11
    • 34249701192 scopus 로고    scopus 로고
    • Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv
    • DOI 10.1002/pmic.200600853
    • Malen, H.; Berven, F. S.; Fladmark, K. E.; Wiker, H. G. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv Proteomics 2007, 7 (10) 1702-18 (Pubitemid 46841830)
    • (2007) Proteomics , vol.7 , Issue.10 , pp. 1702-1718
    • Malen, H.1    Berven, F.S.2    Fladmark, K.E.3    Wiker, H.G.4
  • 12
    • 78751645686 scopus 로고    scopus 로고
    • Comparison of membrane proteins of Mycobacterium tuberculosis H37Rv and H37Ra strains
    • Malen, H.; De Souza, G. A.; Pathak, S.; Softeland, T.; Wiker, H. G. Comparison of membrane proteins of Mycobacterium tuberculosis H37Rv and H37Ra strains BMC Microbiol. 2011, 11, 18
    • (2011) BMC Microbiol. , vol.11 , pp. 18
    • Malen, H.1    De Souza, G.A.2    Pathak, S.3    Softeland, T.4    Wiker, H.G.5
  • 14
    • 77952344404 scopus 로고    scopus 로고
    • Descriptive proteomic analysis shows protein variability between closely related clinical isolates of Mycobacterium tuberculosis
    • Mehaffy, C.; Hess, A.; Prenni, J. E.; Mathema, B.; Kreiswirth, B.; Dobos, K. M. Descriptive proteomic analysis shows protein variability between closely related clinical isolates of Mycobacterium tuberculosis Proteomics 2010, 10 (10) 1966-84
    • (2010) Proteomics , vol.10 , Issue.10 , pp. 1966-84
    • Mehaffy, C.1    Hess, A.2    Prenni, J.E.3    Mathema, B.4    Kreiswirth, B.5    Dobos, K.M.6
  • 16
    • 2542574741 scopus 로고    scopus 로고
    • Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology
    • DOI 10.1074/mcp.M300074-MCP200
    • Schmidt, F.; Donahoe, S.; Hagens, K.; Mattow, J.; Schaible, U. E.; Kaufmann, S. H.; Aebersold, R.; Jungblut, P. R. Complementary analysis of the Mycobacterium tuberculosis proteome by two-dimensional electrophoresis and isotope-coded affinity tag technology Mol. Cell. Proteomics 2004, 3 (1) 24-42 (Pubitemid 38697102)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.1 , pp. 24-42
    • Schmidt, F.1    Donahoe, S.2    Hagens, K.3    Mattow, J.4    Schaible, U.E.5    Kaufmann, S.H.E.6    Aebersold, R.7    Jungblut, P.R.8
  • 17
    • 22144496081 scopus 로고    scopus 로고
    • Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics
    • DOI 10.1099/mic.0.27799-0
    • Sinha, S.; Kosalai, K.; Arora, S.; Namane, A.; Sharma, P.; Gaikwad, A. N.; Brodin, P.; Cole, S. T. Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics Microbiology 2005, 151 (Pt 7) 2411-9 (Pubitemid 40984314)
    • (2005) Microbiology , vol.151 , Issue.7 , pp. 2411-2419
    • Sinha, S.1    Kosalai, K.2    Arora, S.3    Namane, A.4    Sharma, P.5    Gaikwad, A.N.6    Brodin, P.7    Cole, S.T.8
  • 18
    • 0030862226 scopus 로고    scopus 로고
    • Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and electrospray mass spectrometry
    • Sonnenberg, M. G.; Belisle, J. T. Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and electrospray mass spectrometry Infect. Immun. 1997, 65 (11) 4515-24 (Pubitemid 27463220)
    • (1997) Infection and Immunity , vol.65 , Issue.11 , pp. 4515-4524
    • Sonnenberg, M.G.1    Belisle, J.T.2
  • 19
    • 78149386742 scopus 로고    scopus 로고
    • Proteomic definition of the cell wall of Mycobacterium tuberculosis
    • Wolfe, L. M.; Mahaffey, S. B.; Kruh, N. A.; Dobos, K. M. Proteomic definition of the cell wall of Mycobacterium tuberculosis J. Proteome Res. 2010, 9 (11) 5816-26
    • (2010) J. Proteome Res. , vol.9 , Issue.11 , pp. 5816-26
    • Wolfe, L.M.1    Mahaffey, S.B.2    Kruh, N.A.3    Dobos, K.M.4
  • 20
    • 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
    • DOI 10.1021/pr0500049
    • 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 (3) 855-61 (Pubitemid 40863274)
    • (2005) Journal of Proteome Research , vol.4 , Issue.3 , pp. 855-861
    • Xiong, Y.1    Chalmers, M.J.2    Gao, F.P.3    Cross, T.A.4    Marshall, A.G.5
  • 21
    • 79960461488 scopus 로고    scopus 로고
    • A protemics view of mycobacteria
    • de Souza, G. A.; Wiker, H. G. A protemics view of mycobacteria Proteomics 2011, 11 (15) 3118-27
    • (2011) Proteomics , vol.11 , Issue.15 , pp. 3118-27
    • De Souza, G.A.1    Wiker, H.G.2
  • 23
    • 0026720807 scopus 로고
    • Purification of plasma membranes by aqueous two-phase affinity partitioning
    • Persson, A.; Jergil, B. Purification of plasma membranes by aqueous two-phase affinity partitioning Anal. Biochem. 1992, 204 (1) 131-6
    • (1992) Anal. Biochem. , vol.204 , Issue.1 , pp. 131-6
    • Persson, A.1    Jergil, B.2
  • 24
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • DOI 10.1021/ac010617e
    • Wolters, D. A.; Washburn, M. P.; Yates, J. R., 3rd An automated multidimensional protein identification technology for shotgun proteomics Anal. Chem. 2001, 73 (23) 5683-90 (Pubitemid 33126725)
    • (2001) Analytical Chemistry , vol.73 , Issue.23 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 25
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn, M. P.; Wolters, D.; Yates, J. R., 3rd Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 2001, 19 (3) 242-7 (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 26
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 2001, 305 (3) 567-80 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 28
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: A software Environment for integrated models of biomolecular interaction networks
    • DOI 10.1101/gr.1239303
    • Shannon, P.; Markiel, A.; Ozier, O.; Baliga, N. S.; Wang, J. T.; Ramage, D.; Amin, N.; Schwikowski, B.; Ideker, T. Cytoscape: a software environment for integrated models of biomolecular interaction networks Genome Res. 2003, 13 (11) 2498-504 (Pubitemid 37428274)
    • (2003) Genome Research , vol.13 , Issue.11 , pp. 2498-2504
    • Shannon, P.1    Markiel, A.2    Ozier, O.3    Baliga, N.S.4    Wang, J.T.5    Ramage, D.6    Amin, N.7    Schwikowski, B.8    Ideker, T.9
  • 29
    • 33751419295 scopus 로고    scopus 로고
    • Disease state differentiation and identification of tuberculosis biomarkers via native antigen array profiling
    • DOI 10.1074/mcp.M600089-MCP200
    • Sartain, M. J.; Slayden, R. A.; Singh, K. K.; Laal, S.; Belisle, J. T. Disease state differentiation and identification of tuberculosis biomarkers via native antigen array profiling Mol. Cell. Proteomics 2006, 5 (11) 2102-13 (Pubitemid 44817022)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.11 , pp. 2102-2113
    • Sartain, M.J.1    Slayden, R.A.2    Singh, K.K.3    Laal, S.4    Belisle, J.T.5
  • 30
    • 76749100307 scopus 로고    scopus 로고
    • Preparation of stable isotope-labeled peripheral cannabinoid receptor CB2 by bacterial fermentation
    • Berger, C.; Ho, J. T.; Kimura, T.; Hess, S.; Gawrisch, K.; Yeliseev, A. Preparation of stable isotope-labeled peripheral cannabinoid receptor CB2 by bacterial fermentation Protein Expr. Purif. 2010, 70 (2) 236-47
    • (2010) Protein Expr. Purif. , vol.70 , Issue.2 , pp. 236-47
    • Berger, C.1    Ho, J.T.2    Kimura, T.3    Hess, S.4    Gawrisch, K.5    Yeliseev, A.6
  • 31
    • 41549121540 scopus 로고    scopus 로고
    • Analysis of a G protein-coupled receptor for neurotensin by liquid chromatography-electrospray ionization-mass spectrometry
    • Ho, J. T.; White, J. F.; Grisshammer, R.; Hess, S. Analysis of a G protein-coupled receptor for neurotensin by liquid chromatography-electrospray ionization-mass spectrometry Anal. Biochem. 2008, 376 (1) 13-24
    • (2008) Anal. Biochem. , vol.376 , Issue.1 , pp. 13-24
    • Ho, J.T.1    White, J.F.2    Grisshammer, R.3    Hess, S.4
  • 32
    • 55749092578 scopus 로고    scopus 로고
    • Bacterial membrane proteomics
    • Poetsch, A.; Wolters, D. Bacterial membrane proteomics Proteomics 2008, 8 (19) 4100-22
    • (2008) Proteomics , vol.8 , Issue.19 , pp. 4100-22
    • Poetsch, A.1    Wolters, D.2
  • 33
    • 0024397663 scopus 로고
    • Identification, isolation and partial characterization of Mycobacterium tuberculosis glycoprotein antigens
    • Espitia, C.; Mancilla, R. Identification, isolation and partial characterization of Mycobacterium tuberculosis glycoprotein antigens Clin. Exp. Immunol. 1989, 77 (3) 378-83 (Pubitemid 19234386)
    • (1989) Clinical and Experimental Immunology , vol.77 , Issue.3 , pp. 378-383
    • Espitia, C.1    Mancilla, R.2
  • 34
    • 84862947059 scopus 로고    scopus 로고
    • The Analysis of Subcellular Fractions from Mycobacterium tuberculosis glycoprotein antigens
    • Smith, G. T.; Bell, C.; Sweredoski, M. J.; Hess, S., The Analysis of Subcellular Fractions from Mycobacterium tuberculosis glycoprotein antigens. Proc. 59th ASMS Conf, Denver CO, 2011.
    • (2011) Proc. 59th ASMS Conf, Denver CO
    • Smith, G.T.1    Bell, C.2    Sweredoski, M.J.3    Hess, S.4
  • 37
    • 57649185429 scopus 로고    scopus 로고
    • N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC
    • Sartain, M. J.; Belisle, J. T. N-Terminal clustering of the O-glycosylation sites in the Mycobacterium tuberculosis lipoprotein SodC Glycobiology 2009, 19 (1) 38-51
    • (2009) Glycobiology , vol.19 , Issue.1 , pp. 38-51
    • Sartain, M.J.1    Belisle, J.T.2
  • 38
    • 0035477410 scopus 로고    scopus 로고
    • Lipid modification of the Cu,Zn superoxide dismutase from Mycobacterium tuberculosis
    • DOI 10.1042/0264-6021:3590017
    • D'Orazio, M.; Folcarelli, S.; Mariani, F.; Colizzi, V.; Rotilio, G.; Battistoni, A. Lipid modification of the Cu,Zn superoxide dismutase from Mycobacterium tuberculosis Biochem. J. 2001, 359 (Pt 1) 17-22 (Pubitemid 32939203)
    • (2001) Biochemical Journal , vol.359 , Issue.1 , pp. 17-22
    • D'Orazio, M.1    Folcarelli, S.2    Mariani, F.3    Colizzi, V.4    Rotilio, G.5    Battistoni, A.6
  • 39
    • 0032515092 scopus 로고    scopus 로고
    • Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis
    • DOI 10.1016/S0014-5793(98)01373-8, PII S0014579398013738
    • Wu, C. H.; Tsai-Wu, J. J.; Huang, Y. T.; Lin, C. Y.; Lioua, G. G.; Lee, F. J. Identification and subcellular localization of a novel Cu,Zn superoxide dismutase of Mycobacterium tuberculosis FEBS Lett. 1998, 439 (1-2) 192-6 (Pubitemid 28537890)
    • (1998) FEBS Letters , vol.439 , Issue.1-2 , pp. 192-196
    • Wu, C.H.H.1    Tsai-Wu, J.-J.2    Huang, Y.-T.3    Lin, C.-Y.4    Lioua, G.-G.5    Lee, F.-J.S.6
  • 40
    • 0034685684 scopus 로고    scopus 로고
    • Analysis of post-translational modification of mycobacterial proteins using a cassette expression system
    • DOI 10.1016/S0014-5793(00)01553-2, PII S0014579300015532
    • Herrmann, J. L.; Delahay, R.; Gallagher, A.; Robertson, B.; Young, D. Analysis of post-translational modification of mycobacterial proteins using a cassette expression system FEBS Lett. 2000, 473 (3) 358-62 (Pubitemid 30249154)
    • (2000) FEBS Letters , vol.473 , Issue.3 , pp. 358-362
    • Herrmann, J.L.1    Delahay, R.2    Gallagher, A.3    Robertson, B.4    Young, D.5
  • 41
    • 70349333832 scopus 로고    scopus 로고
    • Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes
    • Kung, L. A.; Tao, S. C.; Qian, J.; Smith, M. G.; Snyder, M.; Zhu, H. Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes Mol. Syst. Biol. 2009, 5, 308
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 308
    • Kung, L.A.1    Tao, S.C.2    Qian, J.3    Smith, M.G.4    Snyder, M.5    Zhu, H.6
  • 42
    • 0027025528 scopus 로고
    • The participation of ribosomes in protein glycosylation. Interaction of the ribosome-UDP-N-acetyl-glucosamine complex with dolichol phosphate
    • Paszkiewicz-Gadek, A.; Porowska, H.; Galasinski, W. The participation of ribosomes in protein glycosylation. Interaction of the ribosome-UDP-N-acetyl- glucosamine complex with dolichol phosphate Acta Biochim. Pol. 1992, 39 (3) 251-64
    • (1992) Acta Biochim. Pol. , vol.39 , Issue.3 , pp. 251-64
    • Paszkiewicz-Gadek, A.1    Porowska, H.2    Galasinski, W.3
  • 43
    • 0034804919 scopus 로고    scopus 로고
    • Lipid biosynthesis as a target for antibacterial agents
    • DOI 10.1016/S0163-7827(01)00012-1, PII S0163782701000121
    • Heath, R. J.; White, S. W.; Rock, C. O. Lipid biosynthesis as a target for antibacterial agents Prog. Lipid Res. 2001, 40 (6) 467-97 (Pubitemid 32929968)
    • (2001) Progress in Lipid Research , vol.40 , Issue.6 , pp. 467-497
    • Heath, R.J.1    White, S.W.2    Rock, C.O.3
  • 44
    • 33846605483 scopus 로고    scopus 로고
    • Pyrazinoic acid and its n-propyl ester inhibit fatty acid synthase type I in replicating tubercle bacilli
    • DOI 10.1128/AAC.01369-06
    • Zimhony, O.; Vilcheze, C.; Arai, M.; Welch, J. T.; Jacobs, W. R., Jr. Pyrazinoic acid and its n-propyl ester inhibit fatty acid synthase type I in replicating tubercle bacilli Antimicrob. Agents Chemother. 2007, 51 (2) 752-4 (Pubitemid 46185301)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.2 , pp. 752-754
    • Zimhony, O.1    Vilcheze, C.2    Arai, M.3    Welch, J.T.4    Jacobs Jr., W.R.5
  • 45
    • 33847747061 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis virulence: Lipids inside and out
    • DOI 10.1038/nm0307-284, PII NM0307284
    • Ehrt, S.; Schnappinger, D. Mycobacterium tuberculosis virulence: lipids inside and out Nat. Med. 2007, 13 (3) 284-5 (Pubitemid 46376670)
    • (2007) Nature Medicine , vol.13 , Issue.3 , pp. 284-285
    • Ehrt, S.1    Schnappinger, D.2
  • 46
    • 0029150920 scopus 로고
    • Cloning, sequencing, and expression of the apa gene coding for the Mycobacterium tuberculosis 45/47-kilodalton secreted antigen complex
    • Laqueyrerie, A.; Militzer, P.; Romain, F.; Eiglmeier, K.; Cole, S.; Marchal, G. Cloning, sequencing, and expression of the apa gene coding for the Mycobacterium tuberculosis 45/47-kilodalton secreted antigen complex Infect. Immun. 1995, 63 (10) 4003-10
    • (1995) Infect. Immun. , vol.63 , Issue.10 , pp. 4003-10
    • Laqueyrerie, A.1    Militzer, P.2    Romain, F.3    Eiglmeier, K.4    Cole, S.5    Marchal, G.6
  • 47
    • 0029154710 scopus 로고
    • Evidence for glycosylation sites on the 45-kilodalton glycoprotein of Mycobacterium tuberculosis
    • Dobos, K. M.; Swiderek, K.; Khoo, K. H.; Brennan, P. J.; Belisle, J. T. Evidence for glycosylation sites on the 45-kilodalton glycoprotein of Mycobacterium tuberculosis Infect. Immun. 1995, 63 (8) 2846-53
    • (1995) Infect. Immun. , vol.63 , Issue.8 , pp. 2846-53
    • Dobos, K.M.1    Swiderek, K.2    Khoo, K.H.3    Brennan, P.J.4    Belisle, J.T.5
  • 48
    • 34247162754 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis cell-surface glycoprotein apa as a potential adhesin to colonize target cells via the innate immune system pulmonary C-type lectin surfactant protein A
    • DOI 10.1074/jbc.M610183200
    • Ragas, A.; Roussel, L.; Puzo, G.; Riviere, M. The Mycobacterium tuberculosis cell-surface glycoprotein apa as a potential adhesin to colonize target cells via the innate immune system pulmonary C-type lectin surfactant protein A J. Biol. Chem. 2007, 282 (8) 5133-42 (Pubitemid 47093750)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5133-5142
    • Ragas, A.1    Roussel, L.2    Puzo, G.3    Riviere, M.4
  • 49
    • 0032757323 scopus 로고    scopus 로고
    • Deglycosylation of the 45/47-kilodalton antigen complex of Mycobacterium tuberculosis decreases its capacity to elicit in vivo or in vitro cellular immune responses
    • Romain, F.; Horn, C.; Pescher, P.; Namane, A.; Riviere, M.; Puzo, G.; Barzu, O.; Marchal, G. Deglycosylation of the 45/47-kilodalton antigen complex of Mycobacterium tuberculosis decreases its capacity to elicit in vivo or in vitro cellular immune responses Infect. Immun. 1999, 67 (11) 5567-72 (Pubitemid 29508071)
    • (1999) Infection and Immunity , vol.67 , Issue.11 , pp. 5567-5572
    • Romain, F.1    Horn, C.2    Pescher, P.3    Namane, A.4    Riviere, M.5    Puzo, G.6    Barzu, O.7    Marchal, G.8
  • 50
    • 0033527568 scopus 로고    scopus 로고
    • Decreased capacity of recombinant 45/47-kDa molecules (Apa) of Mycobacterium tuberculosis to stimulate T lymphocyte responses related to changes in their mannosylation pattern
    • Horn, C.; Namane, A.; Pescher, P.; Riviere, M.; Romain, F.; Puzo, G.; Barzu, O.; Marchal, G. Decreased capacity of recombinant 45/47-kDa molecules (Apa) of Mycobacterium tuberculosis to stimulate T lymphocyte responses related to changes in their mannosylation pattern J. Biol. Chem. 1999, 274 (45) 32023-30
    • (1999) J. Biol. Chem. , vol.274 , Issue.45 , pp. 32023-30
    • Horn, C.1    Namane, A.2    Pescher, P.3    Riviere, M.4    Romain, F.5    Puzo, G.6    Barzu, O.7    Marchal, G.8
  • 52
    • 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
    • DOI 10.1006/jmbi.2001.4461
    • 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. 2001, 307 (2) 671-81 (Pubitemid 33027684)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.2 , pp. 671-681
    • Anderson, D.H.1    Harth, G.2    Horwitz, M.A.3    Eisenberg, D.4
  • 53
    • 0346996696 scopus 로고    scopus 로고
    • The Structure of Mycobacterium tuberculosis MPT51 (FbpC1) Defines a New Family of Non-catalytic α/β Hydrolases
    • DOI 10.1016/j.jmb.2003.11.001
    • Wilson, R. A.; Maughan, W. N.; Kremer, L.; Besra, G. S.; Futterer, K. The structure of Mycobacterium tuberculosis MPT51 (FbpC1) defines a new family of non-catalytic alpha/beta hydrolases J. Mol. Biol. 2004, 335 (2) 519-30 (Pubitemid 37532653)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.2 , pp. 519-530
    • Wilson, R.A.1    Maughan, W.N.2    Kremer, L.3    Besra, G.S.4    Futterer, K.5
  • 54
    • 0023689742 scopus 로고
    • Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG
    • Abou-Zeid, C.; Ratliff, T. L.; Wiker, H. G.; Harboe, M.; Bennedsen, J.; Rook, G. A. Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG Infect. Immun. 1988, 56 (12) 3046-51
    • (1988) Infect. Immun. , vol.56 , Issue.12 , pp. 3046-51
    • Abou-Zeid, C.1    Ratliff, T.L.2    Wiker, H.G.3    Harboe, M.4    Bennedsen, J.5    Rook, G.A.6
  • 55
    • 0033733477 scopus 로고    scopus 로고
    • Fibronectin-binding proteins secreted by Mycobacterium avium
    • Kitaura, H.; Ohara, N.; Naito, M.; Kobayashi, K.; Yamada, T. Fibronectin-binding proteins secreted by Mycobacterium avium Apmis 2000, 108 (9) 558-64
    • (2000) Apmis , vol.108 , Issue.9 , pp. 558-64
    • Kitaura, H.1    Ohara, N.2    Naito, M.3    Kobayashi, K.4    Yamada, T.5
  • 56
    • 60049091769 scopus 로고    scopus 로고
    • Secretion systems and their role in host-pathogen interaction
    • Simeone, R.; Bottai, D.; Brosch, R.; ESX/type, V. I. I. secretion systems and their role in host-pathogen interaction Curr. Opin. Microbiol. 2009, 12 (1) 4-10
    • (2009) Curr. Opin. Microbiol. , vol.12 , Issue.1 , pp. 4-10
    • Simeone, R.1    Bottai, D.2    Brosch, R.3
  • 57
    • 5644281780 scopus 로고    scopus 로고
    • ESAT-6 proteins: Protective antigens and virulence factors?
    • DOI 10.1016/j.tim.2004.09.007, PII S0966842X04002112
    • Brodin, P.; Rosenkrands, I.; Andersen, P.; Cole, S. T.; Brosch, R. ESAT-6 proteins: protective antigens and virulence factors? Trends Microbiol. 2004, 12 (11) 500-8 (Pubitemid 39370732)
    • (2004) Trends in Microbiology , vol.12 , Issue.11 , pp. 500-508
    • Brodin, P.1    Rosenkrands, I.2    Andersen, P.3    Cole, S.T.4    Brosch, R.5
  • 59
    • 0036784680 scopus 로고    scopus 로고
    • Epitope mapping of the immunodominant antigen TB10.4 and the two homologous proteins TB10.3 and TB12.9, which constitute a subfamily of the esat-6 gene family
    • Skjot, R. L.; Brock, I.; Arend, S. M.; Munk, M. E.; Theisen, M.; Ottenhoff, T. H.; Andersen, P. Epitope mapping of the immunodominant antigen TB10.4 and the two homologous proteins TB10.3 and TB12.9, which constitute a subfamily of the esat-6 gene family Infect. Immun. 2002, 70 (10) 5446-53
    • (2002) Infect. Immun. , vol.70 , Issue.10 , pp. 5446-53
    • Skjot, R.L.1    Brock, I.2    Arend, S.M.3    Munk, M.E.4    Theisen, M.5    Ottenhoff, T.H.6    Andersen, P.7
  • 61
    • 0036081140 scopus 로고    scopus 로고
    • IdeR, an essential gene in Mycobacterium tuberculosis: Role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response
    • DOI 10.1128/IAI.70.7.3371-3381.2002
    • Rodriguez, G. M.; Voskuil, M. I.; Gold, B.; Schoolnik, G. K.; Smith, I. ideR, An essential gene in mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response Infect. Immun. 2002, 70 (7) 3371-81 (Pubitemid 34665972)
    • (2002) Infection and Immunity , vol.70 , Issue.7 , pp. 3371-3381
    • Rodriguez, G.M.1    Voskuil, M.I.2    Gold, B.3    Schoolnik, G.K.4    Smith, I.5
  • 63
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • DOI 10.1046/j.1365-2958.2003.03425.x
    • Sassetti, C. M.; Boyd, D. H.; Rubin, E. J. Genes required for mycobacterial growth defined by high density mutagenesis Mol. Microbiol. 2003, 48 (1) 77-84 (Pubitemid 36411469)
    • (2003) Molecular Microbiology , vol.48 , Issue.1 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 66
    • 0036231045 scopus 로고    scopus 로고
    • Are the PE-PGRS proteins of Mycobacterium tuberculosis variable surface antigens?
    • DOI 10.1046/j.1365-2958.2002.02813.x
    • Banu, S.; Honore, N.; Saint-Joanis, B.; Philpott, D.; Prevost, M. C.; Cole, S. T. Are the PE-PGRS proteins of Mycobacterium tuberculosis variable surface antigens? Mol. Microbiol. 2002, 44 (1) 9-19 (Pubitemid 34429761)
    • (2002) Molecular Microbiology , vol.44 , Issue.1 , pp. 9-19
    • Banu, S.1    Honore, N.2    Saint-Joanis, B.3    Philpott, D.4    Prevost, M.-C.5    Cole, S.T.6
  • 67
    • 0025776531 scopus 로고
    • Heat shock proteins and antigens of Mycobacterium tuberculosis
    • Young, D. B.; Garbe, T. R. Heat shock proteins and antigens of Mycobacterium tuberculosis Infect. Immun. 1991, 59 (9) 3086-93
    • (1991) Infect. Immun. , vol.59 , Issue.9 , pp. 3086-93
    • Young, D.B.1    Garbe, T.R.2
  • 68
    • 77951967352 scopus 로고    scopus 로고
    • The development and preliminary evaluation of a new Mycobacterium tuberculosis vaccine comprising Ag85b, HspX and CFP-10:ESAT-6 fusion protein with CpG DNA and aluminum hydroxide adjuvants
    • Chen, L.; Xu, M.; Wang, Z. Y.; Chen, B. W.; Du, W. X.; Su, C.; Shen, X. B.; Zhao, A. H.; Dong, N.; Wang, Y. J.; Wang, G. Z. The development and preliminary evaluation of a new Mycobacterium tuberculosis vaccine comprising Ag85b, HspX and CFP-10:ESAT-6 fusion protein with CpG DNA and aluminum hydroxide adjuvants FEMS Immunol. Med. Microbiol. 2010, 59 (1) 42-52
    • (2010) FEMS Immunol. Med. Microbiol. , vol.59 , Issue.1 , pp. 42-52
    • Chen, L.1    Xu, M.2    Wang, Z.Y.3    Chen, B.W.4    Du, W.X.5    Su, C.6    Shen, X.B.7    Zhao, A.H.8    Dong, N.9    Wang, Y.J.10    Wang, G.Z.11
  • 69
    • 79953151566 scopus 로고    scopus 로고
    • Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG
    • Carroll, M. V.; Sim, R. B.; Bigi, F.; Jakel, A.; Antrobus, R.; Mitchell, D. A. Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG Protein Cell 2010, 1 (9) 859-70
    • (2010) Protein Cell , vol.1 , Issue.9 , pp. 859-70
    • Carroll, M.V.1    Sim, R.B.2    Bigi, F.3    Jakel, A.4    Antrobus, R.5    Mitchell, D.A.6
  • 70
    • 7944226058 scopus 로고    scopus 로고
    • Lipoproteins of Mycobacterium tuberculosis: An abundant and functionally diverse class of cell envelope components
    • DOI 10.1016/j.femsre.2004.06.002, PII S0168644504000476
    • 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 (5) 645-59 (Pubitemid 39469923)
    • (2004) FEMS Microbiology Reviews , vol.28 , Issue.5 , pp. 645-659
    • Sutcliffe, I.C.1    Harrington, D.J.2
  • 71
    • 33947413501 scopus 로고    scopus 로고
    • Lipoprotein synthesis in mycobacteria
    • DOI 10.1099/mic.0.2006/000216-0
    • Rezwan, M.; Grau, T.; Tschumi, A.; Sander, P. Lipoprotein synthesis in mycobacteria Microbiology 2007, 153 (Pt 3) 652-8 (Pubitemid 46444362)
    • (2007) Microbiology , vol.153 , Issue.3 , pp. 652-658
    • Rezwan, M.1    Grau, T.2    Tschumi, A.3    Sander, P.4
  • 72
    • 0029896457 scopus 로고    scopus 로고
    • Bacterial glycoproteins: A link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis
    • Herrmann, J. L.; O'Gaora, P.; Gallagher, A.; Thole, J. E.; Young, D. B. Bacterial glycoproteins: a link between glycosylation and proteolytic cleavage of a 19 kDa antigen from Mycobacterium tuberculosis EMBO J. 1996, 15 (14) 3547-54 (Pubitemid 26239767)
    • (1996) EMBO Journal , vol.15 , Issue.14 , pp. 3547-3554
    • Herrmann, J.L.1    O'Gaora, P.2    Gallagher, A.3    Thole, J.E.R.4    Young, D.B.5
  • 73
    • 0027514448 scopus 로고
    • Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: Immunological analysis and evidence of glycosylation
    • Garbe, T.; Harris, D.; Vordermeier, M.; Lathigra, R.; Ivanyi, J.; Young, D. Expression of the Mycobacterium tuberculosis 19-kilodalton antigen in Mycobacterium smegmatis: immunological analysis and evidence of glycosylation Infect. Immun. 1993, 61 (1) 260-7 (Pubitemid 23015425)
    • (1993) Infection and Immunity , vol.61 , Issue.1 , pp. 260-267
    • Garbe, T.1    Harris, D.2    Vordermeier, M.3    Lathigra, R.4    Ivanyi, J.5    Young, D.6
  • 74
    • 0037530648 scopus 로고    scopus 로고
    • Inhibition of IFN-γ-induced class II transactivator expression by a 19-kDa lipoprotein from Mycobacterium tuberculosis: A potential mechanism for immune evasion
    • Pai, R. K.; Convery, M.; Hamilton, T. A.; Boom, W. H.; Harding, C. V. Inhibition of IFN-gamma-induced class II transactivator expression by a 19-kDa lipoprotein from Mycobacterium tuberculosis: a potential mechanism for immune evasion J. Immunol. 2003, 171 (1) 175-84 (Pubitemid 36745286)
    • (2003) Journal of Immunology , vol.171 , Issue.1 , pp. 175-184
    • Pai, R.K.1    Convery, M.2    Hamilton, T.A.3    Henry Boom, W.4    Harding, C.V.5
  • 76
    • 77949550080 scopus 로고    scopus 로고
    • Regulation of antigen presentation by Mycobacterium tuberculosis: A role for Toll-like receptors
    • Harding, C. V.; Boom, W. H. Regulation of antigen presentation by Mycobacterium tuberculosis: a role for Toll-like receptors Nat. Rev. Microbiol. 2010, 8 (4) 296-307
    • (2010) Nat. Rev. Microbiol. , vol.8 , Issue.4 , pp. 296-307
    • Harding, C.V.1    Boom, W.H.2
  • 77
    • 33745298718 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis LprA is a lipoprotein agonist of TLR2 that regulates innate immunity and APC function
    • Pecora, N. D.; Gehring, A. J.; Canaday, D. H.; Boom, W. H.; Harding, C. V. Mycobacterium tuberculosis LprA is a lipoprotein agonist of TLR2 that regulates innate immunity and APC function J. Immunol. 2006, 177 (1) 422-9 (Pubitemid 43939154)
    • (2006) Journal of Immunology , vol.177 , Issue.1 , pp. 422-429
    • Pecora, N.D.1    Gehring, A.J.2    Canaday, D.H.3    Boom, W.H.4    Harding, C.V.5
  • 79
    • 0343920728 scopus 로고    scopus 로고
    • Cloning of the gene encoding a 22-kilodalton cell surface antigen of Mycobacterium bovis BCG and analysis of its potential for DNA vaccination against tuberculosis
    • DOI 10.1128/IAI.68.3.1040-1047.2000
    • Lefevre, P.; Denis, O.; De Wit, L.; Tanghe, A.; Vandenbussche, P.; Content, J.; Huygen, K. Cloning of the gene encoding a 22-kilodalton cell surface antigen of Mycobacterium bovis BCG and analysis of its potential for DNA vaccination against tuberculosis Infect. Immun. 2000, 68 (3) 1040-7 (Pubitemid 30108489)
    • (2000) Infection and Immunity , vol.68 , Issue.3 , pp. 1040-1047
    • Lefevre, P.1    Denis, O.2    De Wit, L.3    Tanghe, A.4    Vandenbussche, P.5    Content, J.6    Huygen, K.7
  • 80
    • 0035827613 scopus 로고    scopus 로고
    • Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier
    • Camacho, L. R.; Constant, P.; Raynaud, C.; Laneelle, M. A.; Triccas, J. A.; Gicquel, B.; Daffe, M.; Guilhot, C. Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier J. Biol. Chem. 2001, 276 (23) 19845-54
    • (2001) J. Biol. Chem. , vol.276 , Issue.23 , pp. 19845-54
    • Camacho, L.R.1    Constant, P.2    Raynaud, C.3    Laneelle, M.A.4    Triccas, J.A.5    Gicquel, B.6    Daffe, M.7    Guilhot, C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.