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Volumn 88, Issue 6, 2008, Pages 526-544

Identification of outer membrane proteins of Mycobacterium tuberculosis

Author keywords

Amphiphilicity; Beta strand; Exported; Inner membrane; Periplasmic; Prediction; Secondary structure; Secreted proteins

Indexed keywords

BACTERIAL PROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN MCE1A; PROTEIN MCE1B; PROTEIN MCE1C; PROTEIN MCE1D; PROTEIN MCE1F; PROTEIN MCE2A; PROTEIN MCE2B; PROTEIN MCE2D; PROTEIN MCE2F; PROTEIN MCE3A; PROTEIN MCE3B; PROTEIN MCE3C; PROTEIN MCE3D; PROTEIN MCE3F; PROTEIN MCE4A; PROTEIN MCE4B; PROTEIN MCE4C; PROTEIN MCE4D; PROTEIN MCE4F; PROTEINASE K; UNCLASSIFIED DRUG;

EID: 54449088847     PISSN: 14729792     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tube.2008.02.004     Document Type: Article
Times cited : (134)

References (89)
  • 2
    • 0035339954 scopus 로고    scopus 로고
    • Interpreting cell wall 'virulence factors' of Mycobacterium tuberculosis
    • Barry C.E. Interpreting cell wall 'virulence factors' of Mycobacterium tuberculosis. Trends Microbiol 9 (2001) 237-241
    • (2001) Trends Microbiol , vol.9 , pp. 237-241
    • Barry, C.E.1
  • 3
    • 0002259015 scopus 로고
    • Lipids: complex lipids, their chemistry, biosynthesis and roles
    • Ratledge C., and Stanford J. (Eds), Academic Press, London
    • Minnikin D.E. Lipids: complex lipids, their chemistry, biosynthesis and roles. In: Ratledge C., and Stanford J. (Eds). The biology of the mycobacteria: physiology, identification and classification (1982), Academic Press, London 95-184
    • (1982) The biology of the mycobacteria: physiology, identification and classification , pp. 95-184
    • Minnikin, D.E.1
  • 4
    • 0027222842 scopus 로고
    • Physical organization of lipids in the cell wall of Mycobacterium chelonae
    • Nikaido H., Kim S.H., and Rosenberg E.Y. Physical organization of lipids in the cell wall of Mycobacterium chelonae. Mol Microbiol 8 (1993) 1025-1030
    • (1993) Mol Microbiol , vol.8 , pp. 1025-1030
    • Nikaido, H.1    Kim, S.H.2    Rosenberg, E.Y.3
  • 5
    • 41649116701 scopus 로고    scopus 로고
    • Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure
    • Hoffmann C., Leis L., Niederweis M., Plitzko J.M., and Engelhardt H. Disclosure of the mycobacterial outer membrane: Cryo-electron tomography and vitreous sections reveal the lipid bilayer structure. Proc Natl Acad Sci USA 105 (2008) 3963-3967
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3963-3967
    • Hoffmann, C.1    Leis, L.2    Niederweis, M.3    Plitzko, J.M.4    Engelhardt, H.5
  • 7
    • 0035028415 scopus 로고    scopus 로고
    • MspA provides the main hydrophilic pathway through the cell wall of Mycobacterium smegmatis
    • (authors' correction appeared in Mol Microbiol 2005;57:1509)
    • Stahl C., Kubetzko S., Kaps I., Seeber S., Engelhardt H., and Niederweis M. MspA provides the main hydrophilic pathway through the cell wall of Mycobacterium smegmatis. Mol Microbiol 40 (2001) 451-464 (authors' correction appeared in Mol Microbiol 2005;57:1509)
    • (2001) Mol Microbiol , vol.40 , pp. 451-464
    • Stahl, C.1    Kubetzko, S.2    Kaps, I.3    Seeber, S.4    Engelhardt, H.5    Niederweis, M.6
  • 8
    • 27444443072 scopus 로고    scopus 로고
    • The growth rate of Mycobacterium smegmatis depends on sufficient porin-mediated influx of nutrients
    • Stephan J., Bender J., Wolschendorf F., Hoffmann C., Roth E., Mailänder C., et al. The growth rate of Mycobacterium smegmatis depends on sufficient porin-mediated influx of nutrients. Mol Microbiol 58 (2005) 714-730
    • (2005) Mol Microbiol , vol.58 , pp. 714-730
    • Stephan, J.1    Bender, J.2    Wolschendorf, F.3    Hoffmann, C.4    Roth, E.5    Mailänder, C.6
  • 9
    • 1242352009 scopus 로고    scopus 로고
    • The structure of a mycobacterial outer-membrane channel
    • Faller M., Niederweis M., and Schulz G.E. The structure of a mycobacterial outer-membrane channel. Science 303 (2004) 1189-1192
    • (2004) Science , vol.303 , pp. 1189-1192
    • Faller, M.1    Niederweis, M.2    Schulz, G.E.3
  • 10
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67 (2003) 593-656
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 11
    • 0032457522 scopus 로고    scopus 로고
    • Expression of a gene for a porin-like protein of the OmpA family from Mycobacterium tuberculosis H37Rv
    • Senaratne R.H., Mobasheri H., Papavinasasundaram K.G., Jenner P., Lea E.J., and Draper P. Expression of a gene for a porin-like protein of the OmpA family from Mycobacterium tuberculosis H37Rv. J Bacteriol 180 (1998) 3541-3547
    • (1998) J Bacteriol , vol.180 , pp. 3541-3547
    • Senaratne, R.H.1    Mobasheri, H.2    Papavinasasundaram, K.G.3    Jenner, P.4    Lea, E.J.5    Draper, P.6
  • 13
    • 33748302014 scopus 로고    scopus 로고
    • pH-dependent pore-forming activity of OmpATb from Mycobacterium tuberculosis and characterization of the channel by peptidic dissection
    • Molle V., Saint N., Campagna S., Kremer L., Lea E., Draper P., et al. pH-dependent pore-forming activity of OmpATb from Mycobacterium tuberculosis and characterization of the channel by peptidic dissection. Mol Microbiol 61 (2006) 826-837
    • (2006) Mol Microbiol , vol.61 , pp. 826-837
    • Molle, V.1    Saint, N.2    Campagna, S.3    Kremer, L.4    Lea, E.5    Draper, P.6
  • 14
    • 34548475774 scopus 로고    scopus 로고
    • The N-terminal domain of OmpATb is required for membrane translocation and pore-forming activity in mycobacteria
    • Alahari A., Saint N., Campagna S., Molle V., Molle G., and Kremer L. The N-terminal domain of OmpATb is required for membrane translocation and pore-forming activity in mycobacteria. J Bacteriol 189 (2007) 6351-6358
    • (2007) J Bacteriol , vol.189 , pp. 6351-6358
    • Alahari, A.1    Saint, N.2    Campagna, S.3    Molle, V.4    Molle, G.5    Kremer, L.6
  • 16
    • 0019448664 scopus 로고
    • Isolation and partial characterization of outer and inner membranes from encapsulated Haemophilus influenzae type b
    • Loeb M.R., Zachary A.L., and Smith D.H. Isolation and partial characterization of outer and inner membranes from encapsulated Haemophilus influenzae type b. J Bacteriol 145 (1981) 596-604
    • (1981) J Bacteriol , vol.145 , pp. 596-604
    • Loeb, M.R.1    Zachary, A.L.2    Smith, D.H.3
  • 17
    • 0016439201 scopus 로고
    • Isolation and characterization of two outer membrane preparations from Escherichia coli
    • Mizushima S., and Yamada H. Isolation and characterization of two outer membrane preparations from Escherichia coli. Biochim Biophys Acta 375 (1975) 44-53
    • (1975) Biochim Biophys Acta , vol.375 , pp. 44-53
    • Mizushima, S.1    Yamada, H.2
  • 18
    • 0025105113 scopus 로고
    • Analysis of the subcellular location of pullulanase produced by Escherichia coli carrying the pulA gene from Klebsiella pneumoniae strain UNF5023
    • Pugsley A.P., Kornacker M.G., and Ryter A. Analysis of the subcellular location of pullulanase produced by Escherichia coli carrying the pulA gene from Klebsiella pneumoniae strain UNF5023. Mol Microbiol 4 (1990) 59-72
    • (1990) Mol Microbiol , vol.4 , pp. 59-72
    • Pugsley, A.P.1    Kornacker, M.G.2    Ryter, A.3
  • 20
    • 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., Chen J., Bradbury E.M., et al. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol Biol Cell 16 (2005) 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    Chen, J.5    Bradbury, E.M.6
  • 21
    • 0035109170 scopus 로고    scopus 로고
    • MPtopo: a database of membrane protein topology
    • Jayasinghe S., Hristova K., and White S.H. MPtopo: a database of membrane protein topology. Protein Sci 10 (2001) 455-458
    • (2001) Protein Sci , vol.10 , pp. 455-458
    • Jayasinghe, S.1    Hristova, K.2    White, S.H.3
  • 22
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: barrels in a nutshell
    • Koebnik R., Locher K.P., and van Gelder P. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol Microbiol 37 (2000) 239-253
    • (2000) Mol Microbiol , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    van Gelder, P.3
  • 23
    • 0037569526 scopus 로고    scopus 로고
    • Fishing new proteins in the twilight zone of genomes: the test case of outer membrane proteins in Escherichia coli K12, Escherichia coli O157:H7, and other Gram-negative bacteria
    • Casadio R., Fariselli P., Finocchiaro G., and Martelli P.L. Fishing new proteins in the twilight zone of genomes: the test case of outer membrane proteins in Escherichia coli K12, Escherichia coli O157:H7, and other Gram-negative bacteria. Protein Sci 12 (2003) 1158-1168
    • (2003) Protein Sci , vol.12 , pp. 1158-1168
    • Casadio, R.1    Fariselli, P.2    Finocchiaro, G.3    Martelli, P.L.4
  • 24
    • 13244259253 scopus 로고    scopus 로고
    • Evaluation of methods for predicting the topology of beta-barrel outer membrane proteins and a consensus prediction method
    • Bagos P.G., Liakopoulos T.D., and Hamodrakas S.J. Evaluation of methods for predicting the topology of beta-barrel outer membrane proteins and a consensus prediction method. BMC Bioinformatics 6 (2005) 7
    • (2005) BMC Bioinformatics , vol.6 , pp. 7
    • Bagos, P.G.1    Liakopoulos, T.D.2    Hamodrakas, S.J.3
  • 25
    • 33746783675 scopus 로고    scopus 로고
    • Computational identification of beta-barrel outer-membrane proteins in Mycobacterium tuberculosis predicted proteomes as putative vaccine candidates
    • Pajon R., Yero D., Lage A., Llanes A., and Borroto C.J. Computational identification of beta-barrel outer-membrane proteins in Mycobacterium tuberculosis predicted proteomes as putative vaccine candidates. Tuberculosis (Edinb) 86 (2006) 290-302
    • (2006) Tuberculosis (Edinb) , vol.86 , pp. 290-302
    • Pajon, R.1    Yero, D.2    Lage, A.3    Llanes, A.4    Borroto, C.J.5
  • 26
    • 0025976068 scopus 로고
    • Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein
    • Struyvé M., Moons M., and Tommassen J. Carboxy-terminal phenylalanine is essential for the correct assembly of a bacterial outer membrane protein. J Mol Biol 218 (1991) 141-148
    • (1991) J Mol Biol , vol.218 , pp. 141-148
    • Struyvé, M.1    Moons, M.2    Tommassen, J.3
  • 27
    • 4544384204 scopus 로고    scopus 로고
    • Lipoprotein trafficking in Escherichia coli
    • Narita S., Matsuyama S., and Tokuda H. Lipoprotein trafficking in Escherichia coli. Arch Microbiol 182 (2004) 1-6
    • (2004) Arch Microbiol , vol.182 , pp. 1-6
    • Narita, S.1    Matsuyama, S.2    Tokuda, H.3
  • 30
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy S.R. Profile hidden Markov models. Bioinformatics 14 (1998) 755-763
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 31
    • 3242891670 scopus 로고    scopus 로고
    • SledgeHMMER: a web server for batch searching the Pfam database
    • Chukkapalli G., Guda C., and Subramaniam S. SledgeHMMER: a web server for batch searching the Pfam database. Nucleic Acids Res 32 (2004) W542-W544
    • (2004) Nucleic Acids Res , vol.32
    • Chukkapalli, G.1    Guda, C.2    Subramaniam, S.3
  • 32
  • 33
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches for the prediction of signal peptides and other protein sorting signals
    • Nielsen H., Brunak S., and von Heijne G. Machine learning approaches for the prediction of signal peptides and other protein sorting signals. Protein Eng 12 (1999) 3-9
    • (1999) Protein Eng , vol.12 , pp. 3-9
    • Nielsen, H.1    Brunak, S.2    von Heijne, G.3
  • 34
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh A., Larsson B., von Heijne G., and Sonnhammer E.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305 (2001) 567-580
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 35
    • 0344406716 scopus 로고    scopus 로고
    • Reliability measures for membrane protein topology prediction algorithms
    • Melen K., Krogh A., and von Heijne G. Reliability measures for membrane protein topology prediction algorithms. J Mol Biol 327 (2003) 735-744
    • (2003) J Mol Biol , vol.327 , pp. 735-744
    • Melen, K.1    Krogh, A.2    von Heijne, G.3
  • 36
    • 0033106244 scopus 로고    scopus 로고
    • Evaluation and improvement of multiple sequence methods for protein secondary structure prediction
    • Cuff J.A., and Barton G.J. Evaluation and improvement of multiple sequence methods for protein secondary structure prediction. Proteins 34 (1999) 508-519
    • (1999) Proteins , vol.34 , pp. 508-519
    • Cuff, J.A.1    Barton, G.J.2
  • 37
    • 0034663597 scopus 로고    scopus 로고
    • Application of multiple sequence alignment profiles to improve protein secondary structure prediction
    • Cuff J.A., and Barton G.J. Application of multiple sequence alignment profiles to improve protein secondary structure prediction. Proteins 40 (2000) 502-511
    • (2000) Proteins , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 38
    • 0022517918 scopus 로고
    • Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods
    • Vogel H., and Jahnig F. Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods. J Mol Biol 190 (1986) 191-199
    • (1986) J Mol Biol , vol.190 , pp. 191-199
    • Vogel, H.1    Jahnig, F.2
  • 39
    • 0021112868 scopus 로고
    • Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure
    • Sweet R.M., and Eisenberg D. Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. J Mol Biol 171 (1983) 479-488
    • (1983) J Mol Biol , vol.171 , pp. 479-488
    • Sweet, R.M.1    Eisenberg, D.2
  • 40
    • 3242891271 scopus 로고    scopus 로고
    • ConPred II: a consensus prediction method for obtaining transmembrane topology models with high reliability
    • Arai M., Mitsuke H., Ikeda M., Xia J.X., Kikuchi T., Satake M., et al. ConPred II: a consensus prediction method for obtaining transmembrane topology models with high reliability. Nucleic Acids Res 32 (2004) W390-W393
    • (2004) Nucleic Acids Res , vol.32
    • Arai, M.1    Mitsuke, H.2    Ikeda, M.3    Xia, J.X.4    Kikuchi, T.5    Satake, M.6
  • 41
    • 0038739294 scopus 로고    scopus 로고
    • High level expression of the mycobacterial porin MspA in Escherichia coli and purification of the recombinant protein
    • Heinz C., Karosi S., and Niederweis M. High level expression of the mycobacterial porin MspA in Escherichia coli and purification of the recombinant protein. J Chromatogr B 790 (2003) 337-348
    • (2003) J Chromatogr B , vol.790 , pp. 337-348
    • Heinz, C.1    Karosi, S.2    Niederweis, M.3
  • 42
    • 0035980619 scopus 로고    scopus 로고
    • Energy transfer between fluorescent proteins using a co-expression system in Mycobacterium smegmatis
    • Kaps I., Ehrt S., Seeber S., Schnappinger D., Martin C., Riley L.W., et al. Energy transfer between fluorescent proteins using a co-expression system in Mycobacterium smegmatis. Gene 278 (2001) 115-124
    • (2001) Gene , vol.278 , pp. 115-124
    • Kaps, I.1    Ehrt, S.2    Seeber, S.3    Schnappinger, D.4    Martin, C.5    Riley, L.W.6
  • 43
    • 0025173980 scopus 로고
    • Peptidoglycan-associated polypeptides of Mycobacterium tuberculosis
    • Hirschfield G.R., McNeil M., and Brennan P.J. Peptidoglycan-associated polypeptides of Mycobacterium tuberculosis. J Bacteriol 172 (1990) 1005-1013
    • (1990) J Bacteriol , vol.172 , pp. 1005-1013
    • Hirschfield, G.R.1    McNeil, M.2    Brennan, P.J.3
  • 45
    • 33947132562 scopus 로고    scopus 로고
    • Porins are required for uptake of phosphates by Mycobacterium smegmatis
    • Wolschendorf F., Mahfoud M., and Niederweis M. Porins are required for uptake of phosphates by Mycobacterium smegmatis. J Bacteriol 189 (2007) 2435-2442
    • (2007) J Bacteriol , vol.189 , pp. 2435-2442
    • Wolschendorf, F.1    Mahfoud, M.2    Niederweis, M.3
  • 46
    • 2442515282 scopus 로고    scopus 로고
    • Rv1818c-encoded PE_PGRS protein of Mycobacterium tuberculosis is surface exposed and influences bacterial cell structure
    • Delogu G., Pusceddu C., Bua A., Fadda G., Brennan M.J., and Zanetti S. Rv1818c-encoded PE_PGRS protein of Mycobacterium tuberculosis is surface exposed and influences bacterial cell structure. Mol Microbiol 52 (2004) 725-733
    • (2004) Mol Microbiol , vol.52 , pp. 725-733
    • Delogu, G.1    Pusceddu, C.2    Bua, A.3    Fadda, G.4    Brennan, M.J.5    Zanetti, S.6
  • 47
    • 0036902040 scopus 로고    scopus 로고
    • OmpA membrane domain as a tight-binding anchor for lipid bilayers
    • Ringler P., and Schulz G.E. OmpA membrane domain as a tight-binding anchor for lipid bilayers. Chembiochem 3 (2002) 463-466
    • (2002) Chembiochem , vol.3 , pp. 463-466
    • Ringler, P.1    Schulz, G.E.2
  • 48
    • 0141677886 scopus 로고    scopus 로고
    • Mycobacterial porins - new channel proteins in unique outer membranes
    • Niederweis M. Mycobacterial porins - new channel proteins in unique outer membranes. Mol Microbiol 49 (2003) 1167-1177
    • (2003) Mol Microbiol , vol.49 , pp. 1167-1177
    • Niederweis, M.1
  • 49
    • 0242320522 scopus 로고    scopus 로고
    • The bacterial translocase: a dynamic protein channel complex
    • de Keyzer J., van der Does C., and Driessen A.J. The bacterial translocase: a dynamic protein channel complex. Cell Mol Life Sci 60 (2003) 2034-2052
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2034-2052
    • de Keyzer, J.1    van der Does, C.2    Driessen, A.J.3
  • 51
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley A.P. The complete general secretory pathway in gram-negative bacteria. Microbiol Rev 57 (1993) 50-108
    • (1993) Microbiol Rev , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 52
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • Wimley W.C. The versatile beta-barrel membrane protein. Curr Opin Struct Biol 13 (2003) 404-411
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 53
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E. coli porins
    • Cowan S.W., Schirmer T., Rummel G., Steiert M., Ghosh R., Pauptit R.A., et al. Crystal structures explain functional properties of two E. coli porins. Nature 358 (1992) 727-733
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Schirmer, T.2    Rummel, G.3    Steiert, M.4    Ghosh, R.5    Pauptit, R.A.6
  • 54
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • Schulz G.E. The structure of bacterial outer membrane proteins. Biochim Biophys Acta 1565 (2002) 308-317
    • (2002) Biochim Biophys Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 55
    • 2942522711 scopus 로고    scopus 로고
    • A Hidden Markov Model method, capable of predicting and discriminating beta-barrel outer membrane proteins
    • Bagos P.G., Liakopoulos T.D., Spyropoulos I.C., and Hamodrakas S.J. A Hidden Markov Model method, capable of predicting and discriminating beta-barrel outer membrane proteins. BMC Bioinformatics 5 (2004) 29
    • (2004) BMC Bioinformatics , vol.5 , pp. 29
    • Bagos, P.G.1    Liakopoulos, T.D.2    Spyropoulos, I.C.3    Hamodrakas, S.J.4
  • 56
    • 0036708003 scopus 로고    scopus 로고
    • The beta-barrel finder (BBF) program, allowing identification of outer membrane beta-barrel proteins encoded within prokaryotic genomes
    • Zhai Y., and Saier Jr. M.H. The beta-barrel finder (BBF) program, allowing identification of outer membrane beta-barrel proteins encoded within prokaryotic genomes. Protein Sci 11 (2002) 2196-2207
    • (2002) Protein Sci , vol.11 , pp. 2196-2207
    • Zhai, Y.1    Saier Jr., M.H.2
  • 57
    • 0026096589 scopus 로고
    • The structure of porin from Rhodobacter capsulatus at 1.8 A resolution
    • Weiss M.S., Kreusch A., Schiltz E., Nestel U., Welte W., Weckesser J., et al. The structure of porin from Rhodobacter capsulatus at 1.8 A resolution. FEBS Lett 280 (1991) 379-382
    • (1991) FEBS Lett , vol.280 , pp. 379-382
    • Weiss, M.S.1    Kreusch, A.2    Schiltz, E.3    Nestel, U.4    Welte, W.5    Weckesser, J.6
  • 58
    • 0025865958 scopus 로고
    • Primary structure of porin from Rhodobacter capsulatus
    • Schiltz E., Kreusch A., Nestel U., and Schulz G.E. Primary structure of porin from Rhodobacter capsulatus. Eur J Biochem 199 (1991) 587-594
    • (1991) Eur J Biochem , vol.199 , pp. 587-594
    • Schiltz, E.1    Kreusch, A.2    Nestel, U.3    Schulz, G.E.4
  • 59
    • 0036105803 scopus 로고    scopus 로고
    • Electrostatic properties of the anion selective porin Omp32 from Delftia acidovorans and of the arginine cluster of bacterial porins
    • Zachariae U., Koumanov A., Engelhardt H., and Karshikoff A. Electrostatic properties of the anion selective porin Omp32 from Delftia acidovorans and of the arginine cluster of bacterial porins. Protein Sci 11 (2002) 1309-1319
    • (2002) Protein Sci , vol.11 , pp. 1309-1319
    • Zachariae, U.1    Koumanov, A.2    Engelhardt, H.3    Karshikoff, A.4
  • 60
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: a comprehensive database of protein domain families based on seed alignments
    • Sonnhammer E.L., Eddy S.R., and Durbin R. Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins 28 (1997) 405-420
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 61
    • 33646845510 scopus 로고    scopus 로고
    • Topology of the porin MspA in the outer membrane of Mycobacterium smegmatis
    • Mahfoud M., Sukumaran S., Hülsmann P., Grieger K., and Niederweis M. Topology of the porin MspA in the outer membrane of Mycobacterium smegmatis. J Biol Chem 281 (2006) 5908-5915
    • (2006) J Biol Chem , vol.281 , pp. 5908-5915
    • Mahfoud, M.1    Sukumaran, S.2    Hülsmann, P.3    Grieger, K.4    Niederweis, M.5
  • 62
    • 0025836761 scopus 로고
    • Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm
    • Derman A.I., and Beckwith J. Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm. J Bacteriol 173 (1991) 7719-7722
    • (1991) J Bacteriol , vol.173 , pp. 7719-7722
    • Derman, A.I.1    Beckwith, J.2
  • 63
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome
    • Tjalsma H., Bolhuis A., Jongbloed J.D., Bron S., and van Dijl J.M. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol Mol Biol Rev 64 (2000) 515-547
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    van Dijl, J.M.5
  • 65
    • 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., Churcher C., Harris D., 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    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 66
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., et al. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390 (1997) 249-256
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5    Azevedo, V.6
  • 67
    • 34249701192 scopus 로고    scopus 로고
    • Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv
    • Malen H., Berven F.S., Fladmark K.E., and Wiker H.G. Comprehensive analysis of exported proteins from Mycobacterium tuberculosis H37Rv. Proteomics 7 (2007) 1702-1718
    • (2007) Proteomics , vol.7 , pp. 1702-1718
    • Malen, H.1    Berven, F.S.2    Fladmark, K.E.3    Wiker, H.G.4
  • 69
    • 25444484398 scopus 로고    scopus 로고
    • TMB-Hunt: an amino acid composition based method to screen proteomes for beta-barrel transmembrane proteins
    • Garrow A.G., Agnew A., and Westhead D.R. TMB-Hunt: an amino acid composition based method to screen proteomes for beta-barrel transmembrane proteins. BMC Bioinformatics 6 (2005) 56
    • (2005) BMC Bioinformatics , vol.6 , pp. 56
    • Garrow, A.G.1    Agnew, A.2    Westhead, D.R.3
  • 71
    • 0034819306 scopus 로고    scopus 로고
    • High extracellular levels of Mycobacterium tuberculosis glutamine synthetase and superoxide dismutase in actively growing cultures are due to high expression and extracellular stability rather than to a protein-specific export mechanism
    • Tullius M.V., Harth G., and Horwitz M.A. High extracellular levels of Mycobacterium tuberculosis glutamine synthetase and superoxide dismutase in actively growing cultures are due to high expression and extracellular stability rather than to a protein-specific export mechanism. Infect Immun 69 (2001) 6348-6363
    • (2001) Infect Immun , vol.69 , pp. 6348-6363
    • Tullius, M.V.1    Harth, G.2    Horwitz, M.A.3
  • 72
    • 0014073070 scopus 로고
    • Autolysis and secondary growth of Mycobacterium tuberculosis in submerged culture
    • Wayne L.G., and Diaz G.A. Autolysis and secondary growth of Mycobacterium tuberculosis in submerged culture. J Bacteriol 93 (1967) 1374-1381
    • (1967) J Bacteriol , vol.93 , pp. 1374-1381
    • Wayne, L.G.1    Diaz, G.A.2
  • 73
    • 33646918848 scopus 로고    scopus 로고
    • Membrane vesicles shed by Legionella pneumophila inhibit fusion of phagosomes with lysosomes
    • Fernandez-Moreira E., Helbig J.H., and Swanson M.S. Membrane vesicles shed by Legionella pneumophila inhibit fusion of phagosomes with lysosomes. Infect Immun 74 (2006) 3285-3295
    • (2006) Infect Immun , vol.74 , pp. 3285-3295
    • Fernandez-Moreira, E.1    Helbig, J.H.2    Swanson, M.S.3
  • 74
    • 0031663159 scopus 로고    scopus 로고
    • Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria
    • Li Z., Clarke A.J., and Beveridge T.J. Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria. J Bacteriol 180 (1998) 5478-5483
    • (1998) J Bacteriol , vol.180 , pp. 5478-5483
    • Li, Z.1    Clarke, A.J.2    Beveridge, T.J.3
  • 75
    • 11144222920 scopus 로고    scopus 로고
    • Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end
    • Akama H., Kanemaki M., Yoshimura M., Tsukihara T., Kashiwagi T., Yoneyama H., et al. Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: dual modes of membrane anchoring and occluded cavity end. J Biol Chem 279 (2004) 52816-52819
    • (2004) J Biol Chem , vol.279 , pp. 52816-52819
    • Akama, H.1    Kanemaki, M.2    Yoshimura, M.3    Tsukihara, T.4    Kashiwagi, T.5    Yoneyama, H.6
  • 76
    • 0027424110 scopus 로고
    • Cloning of an M. tuberculosis DNA fragment associated with entry and survival inside cells
    • Arruda S., Bomfim G., Knights R., Huima Byron T., and Riley L.W. Cloning of an M. tuberculosis DNA fragment associated with entry and survival inside cells. Science 261 (1993) 1454-1457
    • (1993) Science , vol.261 , pp. 1454-1457
    • Arruda, S.1    Bomfim, G.2    Knights, R.3    Huima Byron, T.4    Riley, L.W.5
  • 77
    • 33847775356 scopus 로고    scopus 로고
    • A phylogenomic analysis of the Actinomycetales mce operons
    • Casali N., and Riley L.W. A phylogenomic analysis of the Actinomycetales mce operons. BMC Genomics 8 (2007) 60
    • (2007) BMC Genomics , vol.8 , pp. 60
    • Casali, N.1    Riley, L.W.2
  • 78
    • 0346734118 scopus 로고    scopus 로고
    • Hypervirulent mutant of Mycobacterium tuberculosis resulting from disruption of the mce1 operon
    • Shimono N., Morici L., Casali N., Cantrell S., Sidders B., Ehrt S., et al. Hypervirulent mutant of Mycobacterium tuberculosis resulting from disruption of the mce1 operon. Proc Natl Acad Sci USA 100 (2003) 15918-15923
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15918-15923
    • Shimono, N.1    Morici, L.2    Casali, N.3    Cantrell, S.4    Sidders, B.5    Ehrt, S.6
  • 79
    • 0242268400 scopus 로고    scopus 로고
    • Genetic requirements for mycobacterial survival during infection
    • Sassetti C.M., and Rubin E.J. Genetic requirements for mycobacterial survival during infection. Proc Natl Acad Sci USA 100 (2003) 12989-12994
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12989-12994
    • Sassetti, C.M.1    Rubin, E.J.2
  • 82
    • 0032240715 scopus 로고    scopus 로고
    • Analysis of the genome of Mycobacterium tuberculosis H37Rv
    • (discussion 72-77)
    • Cole S.T., and Barrell B.G. Analysis of the genome of Mycobacterium tuberculosis H37Rv. Novartis Found Symp 217 (1998) 160-172 (discussion 72-77)
    • (1998) Novartis Found Symp , vol.217 , pp. 160-172
    • Cole, S.T.1    Barrell, B.G.2
  • 83
    • 33751323180 scopus 로고    scopus 로고
    • Gey van Pittius NC, Sampson SL, Lee H, Kim Y, van Helden PD, Warren RM. Evolution and expansion of the Mycobacterium tuberculosis PE and PPE multigene families and their association with the duplication of the ESAT-6 (esx) gene cluster regions
    • Gey van Pittius NC, Sampson SL, Lee H, Kim Y, van Helden PD, Warren RM. Evolution and expansion of the Mycobacterium tuberculosis PE and PPE multigene families and their association with the duplication of the ESAT-6 (esx) gene cluster regions. BMC Evol Biol 6 (2006) 95
    • (2006) BMC Evol Biol , vol.6 , pp. 95
  • 84
    • 0035177858 scopus 로고    scopus 로고
    • Evidence that mycobacterial PE_PGRS proteins are cell surface constituents that influence interactions with other cells
    • Brennan M.J., Delogu G., Chen Y., Bardarov S., Kriakov J., Alavi M., et al. Evidence that mycobacterial PE_PGRS proteins are cell surface constituents that influence interactions with other cells. Infect Immun 69 (2001) 7326-7333
    • (2001) Infect Immun , vol.69 , pp. 7326-7333
    • Brennan, M.J.1    Delogu, G.2    Chen, Y.3    Bardarov, S.4    Kriakov, J.5    Alavi, M.6
  • 86
    • 36549015553 scopus 로고    scopus 로고
    • PE is a functional domain responsible for protein translocation and localization on mycobacterial cell wall
    • Cascioferro A., Delogu G., Colone M., Sali M., Stringaro A., Arancia G., et al. PE is a functional domain responsible for protein translocation and localization on mycobacterial cell wall. Mol Microbiol 66 (2007) 1536-1547
    • (2007) Mol Microbiol , vol.66 , pp. 1536-1547
    • Cascioferro, A.1    Delogu, G.2    Colone, M.3    Sali, M.4    Stringaro, A.5    Arancia, G.6
  • 87
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong M., Sawaya M.R., Wang S., Phillips M., Cascio D., and Eisenberg D. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc Natl Acad Sci USA 103 (2006) 8060-8065
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 88
    • 0035699903 scopus 로고    scopus 로고
    • Antigenicity and immunogenicity of synthetic peptides
    • Van Regenmortel M.H. Antigenicity and immunogenicity of synthetic peptides. Biologicals 29 (2001) 209-213
    • (2001) Biologicals , vol.29 , pp. 209-213
    • Van Regenmortel, M.H.1
  • 89
    • 0042532056 scopus 로고    scopus 로고
    • Identification of a regulated alkaline phosphatase, a cell surface-associated lipoprotein, in Mycobacterium smegmatis
    • Kriakov J., Lee S., and Jacobs Jr. W.R. Identification of a regulated alkaline phosphatase, a cell surface-associated lipoprotein, in Mycobacterium smegmatis. J Bacteriol 185 (2003) 4983-4991
    • (2003) J Bacteriol , vol.185 , pp. 4983-4991
    • Kriakov, J.1    Lee, S.2    Jacobs Jr., W.R.3


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