메뉴 건너뛰기




Volumn 49, Issue 5, 2003, Pages 1167-1177

Mycobacterial porins - New channel proteins in unique outer membranes

Author keywords

[No Author keywords available]

Indexed keywords

CEPHALOSPORIN DERIVATIVE; ETHAMBUTOL; ISONIAZID; PENICILLIN DERIVATIVE; PYRAZINAMIDE;

EID: 0141677886     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03662.x     Document Type: Short Survey
Times cited : (163)

References (95)
  • 1
    • 0034695440 scopus 로고    scopus 로고
    • Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers
    • Arora, A., Rinehart, D., Szabo, G., and Tamm, L.K. (2000) Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers. J Biol Chem 275: 1594-1600.
    • (2000) J Biol Chem , vol.275 , pp. 1594-1600
    • Arora, A.1    Rinehart, D.2    Szabo, G.3    Tamm, L.K.4
  • 2
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora, A., Abildgaard, F., Bushweller, J.H., and Tamm, L.K. (2001) Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat Struct Biol 8: 334-338.
    • (2001) Nat Struct Biol , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 3
    • 0000769687 scopus 로고    scopus 로고
    • Mycobacterium smegmatis: An absurd model for tuberculosis?
    • Barry, C.E. III (2001) Mycobacterium smegmatis: an absurd model for tuberculosis? Trends Microbiol 9: 473.
    • (2001) Trends Microbiol , vol.9 , pp. 473
    • Barry C.E. III1
  • 5
    • 0024424616 scopus 로고
    • One single lysine residue is responsible for the special interaction between polyphosphate and the outer membrane porin PhoE of Escherichia coli
    • Bauer, K., Struyve, M., Bosch, D., Benz, R., and Tommassen, J. (1989) One single lysine residue is responsible for the special interaction between polyphosphate and the outer membrane porin PhoE of Escherichia coli. J Biol Chem 264: 16393-16398.
    • (1989) J Biol Chem , vol.264 , pp. 16393-16398
    • Bauer, K.1    Struyve, M.2    Bosch, D.3    Benz, R.4    Tommassen, J.5
  • 6
    • 0017648838 scopus 로고
    • Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein
    • Bavoil, P., Nikaido, H., and von Meyenburg, K. (1977) Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Mol Gen Genet 158: 23-33.
    • (1977) Mol Gen Genet , vol.158 , pp. 23-33
    • Bavoil, P.1    Nikaido, H.2    Von Meyenburg, K.3
  • 7
    • 0019312556 scopus 로고
    • Major heat-modifiable outer membrane protein in Gram-negative bacteria: Comparison with the OmpA protein of Escherichia coli
    • Beher, M.G., Schnaitman, C.A., and Pugsley, A.P. (1980) Major heat-modifiable outer membrane protein in Gram-negative bacteria: comparison with the OmpA protein of Escherichia coli. J Bacteriol 143: 906-913.
    • (1980) J Bacteriol , vol.143 , pp. 906-913
    • Beher, M.G.1    Schnaitman, C.A.2    Pugsley, A.P.3
  • 9
    • 0004104929 scopus 로고    scopus 로고
    • Global Tuberculosis control
    • Geneva, Switzerland: World Health Organization
    • Bleed, D., Watt, C., and Dye, C. (2001) Global Tuberculosis control. In WHO Report 2001. Geneva, Switzerland: World Health Organization.
    • (2001) WHO Report 2001
    • Bleed, D.1    Watt, C.2    Dye, C.3
  • 10
    • 0035996998 scopus 로고    scopus 로고
    • OmpA: A pore or not a pore? Simulation and modeling studies
    • Bond, P.J., Faraldo-Gomez, J.D., and Sansom, M.S. (2002) OmpA: a pore or not a pore? Simulation and modeling studies. Biophys J 83: 763-775.
    • (2002) Biophys J , vol.83 , pp. 763-775
    • Bond, P.J.1    Faraldo-Gomez, J.D.2    Sansom, M.S.3
  • 11
    • 0032946645 scopus 로고    scopus 로고
    • Bacterial solutions to the iron-supply problem
    • Braun, V., and Killmann, H. (1999) Bacterial solutions to the iron-supply problem. Trends Biochem Sci 24: 104-109.
    • (1999) Trends Biochem Sci , vol.24 , pp. 104-109
    • Braun, V.1    Killmann, H.2
  • 12
    • 0035212925 scopus 로고    scopus 로고
    • Two nonredundant SecA homologues function in mycobacteria
    • Braunstein, M., Brown, A.M., Kurtz, S., and Jacobs, W.R., Jr (2001) Two nonredundant SecA homologues function in mycobacteria. J Bacteriol 183: 6979-6990.
    • (2001) J Bacteriol , vol.183 , pp. 6979-6990
    • Braunstein, M.1    Brown, A.M.2    Kurtz, S.3    Jacobs W.R., Jr.4
  • 13
    • 0037844364 scopus 로고    scopus 로고
    • Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis
    • Brennan, P.J. (2003) Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis. Tuberculosis) 83: 91-97.
    • (2003) Tuberculosis , vol.83 , pp. 91-97
    • Brennan, P.J.1
  • 14
    • 0029061399 scopus 로고
    • The envelope of mycobacteria
    • Brennan, P.J., and Nikaido, H. (1995) The envelope of mycobacteria. Annu Rev Biochem 64: 29-63.
    • (1995) Annu Rev Biochem , vol.64 , pp. 29-63
    • Brennan, P.J.1    Nikaido, H.2
  • 16
    • 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. (1992) Crystal structures explain functional properties of two E. coli porins. Nature 358: 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
  • 17
    • 0032452982 scopus 로고    scopus 로고
    • The envelope layers of mycobacteria with reference to their pathogenicity
    • Daffé, M., and Draper, P. (1998) The envelope layers of mycobacteria with reference to their pathogenicity. Adv Microb Physiol 39: 131-203.
    • (1998) Adv Microb Physiol , vol.39 , pp. 131-203
    • Daffé, M.1    Draper, P.2
  • 18
    • 0040606207 scopus 로고    scopus 로고
    • Growth temperature dependence of channel size of the major outer-membrane protein (OprF) in psychrotrophic Pseudomonas fluorescens strains
    • De, E., Orange, N., Saint, N., Guerillon, J., De Mot, R., and Molle, G. (1997) Growth temperature dependence of channel size of the major outer-membrane protein (OprF) in psychrotrophic Pseudomonas fluorescens strains. Microbiology 143: 1029-1035.
    • (1997) Microbiology , vol.143 , pp. 1029-1035
    • De, E.1    Orange, N.2    Saint, N.3    Guerillon, J.4    De Mot, R.5    Molle, G.6
  • 19
    • 0028828533 scopus 로고
    • Cadaverine induces closing of E. coli porins
    • Dela Vega, A.L., and Delcour, A.H. (1995) Cadaverine induces closing of E. coli porins. EMBO J 14: 6058-6065.
    • (1995) EMBO J , vol.14 , pp. 6058-6065
    • Dela Vega, A.L.1    Delcour, A.H.2
  • 20
    • 0030841732 scopus 로고    scopus 로고
    • Function and modulation of bacterial porins: Insights from electrophysiology
    • Delcour, A.H. (1997) Function and modulation of bacterial porins: insights from electrophysiology. FEMS Microbiol Lett 151: 115-123.
    • (1997) FEMS Microbiol Lett , vol.151 , pp. 115-123
    • Delcour, A.H.1
  • 21
    • 0141585145 scopus 로고    scopus 로고
    • Solute uptake through general porins
    • Delcour, A.H. (2003) Solute uptake through general porins. Front Biosci 8: D1055-D1071.
    • (2003) Front Biosci , vol.8
    • Delcour, A.H.1
  • 22
    • 0033864778 scopus 로고    scopus 로고
    • Molecular mechanics of the mycobacterial cell wall: From horizontal layers to vertical scaffolds
    • Dmitriev, B.A., Ehlers, S., Rietschel, E.T., and Brennan, P.J. (2000) Molecular mechanics of the mycobacterial cell wall: from horizontal layers to vertical scaffolds. Int J Med Microbiol 290: 251-258.
    • (2000) Int J Med Microbiol , vol.290 , pp. 251-258
    • Dmitriev, B.A.1    Ehlers, S.2    Rietschel, E.T.3    Brennan, P.J.4
  • 23
    • 0032535516 scopus 로고    scopus 로고
    • The outer parts of the mycobacterial envelope as permeability barriers
    • Draper, P. (1998) The outer parts of the mycobacterial envelope as permeability barriers. Front Biosci 3: 1253-1261.
    • (1998) Front Biosci , vol.3 , pp. 1253-1261
    • Draper, P.1
  • 24
    • 0034733718 scopus 로고    scopus 로고
    • Sugar transport through maltoporin of Escherichia coli. Role of polar tracks
    • Dumas, F., Koebnik, R., Winterhalter, M., and van Gelder, P. (2000) Sugar transport through maltoporin of Escherichia coli. Role of polar tracks. J Biol Chem 275: 19747-19751.
    • (2000) J Biol Chem , vol.275 , pp. 19747-19751
    • Dumas, F.1    Koebnik, R.2    Winterhalter, M.3    Van Gelder, P.4
  • 25
    • 0037020168 scopus 로고    scopus 로고
    • A tetrameric porin limits the cell wall permeability of Mycobacterium smegmatis
    • Engelhardt, H., Heinz, C., and Niederweis, M. (2002) A tetrameric porin limits the cell wall permeability of Mycobacterium smegmatis. J Biol Chem 277: 37567-37572.
    • (2002) J Biol Chem , vol.277 , pp. 37567-37572
    • Engelhardt, H.1    Heinz, C.2    Niederweis, M.3
  • 26
    • 0033118890 scopus 로고    scopus 로고
    • Regulation by nutrient limitation
    • Ferenci, T. (1999) Regulation by nutrient limitation. Curr Opin Microbiol 2: 208-213.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 208-213
    • Ferenci, T.1
  • 27
    • 0036397455 scopus 로고    scopus 로고
    • Is Mycobacterium tuberculosis a closer relative to Gram-positive or Gram-negative bacterial pathogens?
    • Fu, L.M., and Fu-Liu, C.S. (2002) Is Mycobacterium tuberculosis a closer relative to Gram-positive or Gram-negative bacterial pathogens? Tuberculosis 82: 85-90.
    • (2002) Tuberculosis , vol.82 , pp. 85-90
    • Fu, L.M.1    Fu-Liu, C.S.2
  • 29
    • 0025862413 scopus 로고
    • Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli
    • Hancock, R.E., Farmer, S.W., Li, Z.S., and Peele, K. (1991) Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli. Antimicrob Agents Chemother 35: 1309-1314.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 1309-1314
    • Hancock, R.E.1    Farmer, S.W.2    Li, Z.S.3    Peele, K.4
  • 30
    • 0019814049 scopus 로고
    • Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the OmpF porin
    • Harder, K.J., Nikaido, H., and Matsuhashi, M. (1981) Mutants of Escherichia coli that are resistant to certain beta-lactam compounds lack the OmpF porin. Antimicrob Agents Chemother 20: 549-552.
    • (1981) Antimicrob Agents Chemother , vol.20 , pp. 549-552
    • Harder, K.J.1    Nikaido, H.2    Matsuhashi, M.3
  • 31
    • 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. (2003a) High level expression of the mycobacterial porin MspA in Escherichia coli and purification of the recombinant protein. J Chromatogr B 790: 337-348.
    • (2003) J Chromatogr B , vol.790 , pp. 337-348
    • Heinz, C.1    Karosi, S.2    Niederweis, M.3
  • 32
    • 0037424352 scopus 로고    scopus 로고
    • The core of the tetrameric mycobacterial porin MspA is an extremely stable beta-sheet domain
    • Heinz, C., Engelhardt, H., and Niederweis, M. (2003b) The core of the tetrameric mycobacterial porin MspA is an extremely stable beta-sheet domain. J Biol Chem 278: 8678-8685.
    • (2003) J Biol Chem , vol.278 , pp. 8678-8685
    • Heinz, C.1    Engelhardt, H.2    Niederweis, M.3
  • 33
    • 0034499999 scopus 로고    scopus 로고
    • The rapidly growing mycobacteria: Saprophytes and parasites
    • Howard, S.T., and Byrd, T.F. (2000) The rapidly growing mycobacteria: saprophytes and parasites. Microbes Infect 2: 1845-1853.
    • (2000) Microbes Infect , vol.2 , pp. 1845-1853
    • Howard, S.T.1    Byrd, T.F.2
  • 34
    • 0036301334 scopus 로고    scopus 로고
    • Ions and counterions in a biological channel: A molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1 M KCl aqueous salt solution
    • Im, W., and Roux, B. (2002) Ions and counterions in a biological channel: a molecular dynamics simulation of OmpF porin from Escherichia coli in an explicit membrane with 1 M KCl aqueous salt solution. J Mol Biol 319: 1177-1197.
    • (2002) J Mol Biol , vol.319 , pp. 1177-1197
    • Im, W.1    Roux, B.2
  • 35
    • 0034615780 scopus 로고    scopus 로고
    • Molecular basis for the polyamine-OmpF porin interactions: Inhibitor and mutant studies
    • Iyer, R., Wu, Z., Woster, P.M., and Delcour, A.H. (2000) Molecular basis for the polyamine-OmpF porin interactions: inhibitor and mutant studies. J Mol Biol 297: 933-945.
    • (2000) J Mol Biol , vol.297 , pp. 933-945
    • Iyer, R.1    Wu, Z.2    Woster, P.M.3    Delcour, A.H.4
  • 36
    • 0034730751 scopus 로고    scopus 로고
    • Phosphatidylinositol is an essential phosphelipid of mycobacteria
    • Jackson, M., Crick, D.C., and Brennan, P.J. (2000) Phosphatidylinositol is an essential phosphelipid of mycobacteria. J Biol Chem 275: 30092-30099.
    • (2000) J Biol Chem , vol.275 , pp. 30092-30099
    • Jackson, M.1    Crick, D.C.2    Brennan, P.J.3
  • 37
    • 0032982736 scopus 로고    scopus 로고
    • Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the Mycobacterium tuberculosis cell envelope
    • Jackson, M., Raynaud, C., Laneelle, M.A., Guilhot, C., Laurent-Winter, C., Ensergueix, D., et al. (1999) Inactivation of the antigen 85C gene profoundly affects the mycolate content and alters the permeability of the Mycobacterium tuberculosis cell envelope. Mol Microbiol 31: 1573-1587.
    • (1999) Mol Microbiol , vol.31 , pp. 1573-1587
    • Jackson, M.1    Raynaud, C.2    Laneelle, M.A.3    Guilhot, C.4    Laurent-Winter, C.5    Ensergueix, D.6
  • 38
    • 0025255458 scopus 로고
    • Permeability barrier to hydrophilic solutes in Mycobacterium chelonei
    • Jarlier, V., and Nikaido, H. (1990) Permeability barrier to hydrophilic solutes in Mycobacterium chelonei. J Bacteriol 172: 1418-1423.
    • (1990) J Bacteriol , vol.172 , pp. 1418-1423
    • Jarlier, V.1    Nikaido, H.2
  • 39
    • 0032718515 scopus 로고    scopus 로고
    • Porins in the cell wall of Mycobacterium tuberculosis
    • Authors' correction appeared in. J Bacteriol 181: 7650
    • Kartmann, B., Stenger, S., and Niederweis, M. (1999) Porins in the cell wall of Mycobacterium tuberculosis. J Bacteriol 181: 6543-6546. (Authors' correction appeared in. J Bacteriol 181: 7650).
    • (1999) J Bacteriol , vol.181 , pp. 6543-6546
    • Kartmann, B.1    Stenger, S.2    Niederweis, M.3
  • 40
    • 0024279245 scopus 로고
    • Naturally crystalline porin in the outer membrane of Bordetella pertussis
    • Kessel, M., Brennan, M.J., Trus, B.L., Bisher, M.E., and Steven, A.C. (1988) Naturally crystalline porin in the outer membrane of Bordetella pertussis. J Mol Biol 203: 275-278.
    • (1988) J Mol Biol , vol.203 , pp. 275-278
    • Kessel, M.1    Brennan, M.J.2    Trus, B.L.3    Bisher, M.E.4    Steven, A.C.5
  • 41
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J.A. (1998) Hydrophobic mismatch between proteins and lipids in membranes. Biochim Biophys Acta 1376: 401-415.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 401-415
    • Killian, J.A.1
  • 42
    • 0036441481 scopus 로고    scopus 로고
    • Secondary and tertiary structure formation of the beta-barrel membrane protein OmpA is synchronized and depends on membrane thickness
    • Kleinschmidt, J.H., and Tamm, L.K. (2002) Secondary and tertiary structure formation of the beta-barrel membrane protein OmpA is synchronized and depends on membrane thickness. J Mol Biol 324: 319-330.
    • (2002) J Mol Biol , vol.324 , pp. 319-330
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 43
    • 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. (2000) Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol Microbiol 37: 239-253.
    • (2000) Mol Microbiol , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 44
    • 0141585123 scopus 로고
    • Fine structure of intracytoplasmic organelles of mycobacteria
    • Koike, M., and Takeya, K. (1961) Fine structure of intracytoplasmic organelles of mycobacteria. J Biophys Biochem Cyt 9: 597-608.
    • (1961) J Biophys Biochem Cyt , vol.9 , pp. 597-608
    • Koike, M.1    Takeya, K.2
  • 45
    • 0036096326 scopus 로고    scopus 로고
    • Cellular impermeability and uptake of biocides and antibiotics in Gram-positive bacteria and mycobacteria
    • Lambert, P.A. (2002) Cellular impermeability and uptake of biocides and antibiotics in Gram-positive bacteria and mycobacteria. J Appl Microbiol 92: 46S-54S.
    • (2002) J Appl Microbiol , vol.92
    • Lambert, P.A.1
  • 46
    • 0032432632 scopus 로고    scopus 로고
    • Upregulation of a histone-like protein in dormant Mycobacterium smegmatis
    • Lee, B.H., Murugasu-Oei, B., and Dick, T. (1998) Upregulation of a histone-like protein in dormant Mycobacterium smegmatis. Mol Gen Genet 260: 475-479.
    • (1998) Mol Gen Genet , vol.260 , pp. 475-479
    • Lee, B.H.1    Murugasu-Oei, B.2    Dick, T.3
  • 47
    • 0032573030 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of the cell wall porin of Corynebacterium glutamicum: The channel is formed by a low molecular mass polypeptide
    • Lichtinger, T., Burkovski, A., Niederweis, M., Kramer, R., and Benz, R. (1998) Biochemical and biophysical characterization of the cell wall porin of Corynebacterium glutamicum: the channel is formed by a low molecular mass polypeptide. Biochemistry 37: 15024-15032.
    • (1998) Biochemistry , vol.37 , pp. 15024-15032
    • Lichtinger, T.1    Burkovski, A.2    Niederweis, M.3    Kramer, R.4    Benz, R.5
  • 48
    • 0032973863 scopus 로고    scopus 로고
    • Evidence for a small anion-selective channel in the cell wall of Mycobacterium bovis BCG besides a wide cation-selective pore
    • Lichtinger, T., Heym, B., Maier, E., Eichner, H., Cole, S.T., and Benz, R. (1999) Evidence for a small anion-selective channel in the cell wall of Mycobacterium bovis BCG besides a wide cation-selective pore. FEBS Lett 454: 349-355.
    • (1999) FEBS Lett , vol.454 , pp. 349-355
    • Lichtinger, T.1    Heym, B.2    Maier, E.3    Eichner, H.4    Cole, S.T.5    Benz, R.6
  • 49
    • 0031717824 scopus 로고    scopus 로고
    • Inhibitory effect of acidic pH on OmpC porin: Wild-type and mutant studies
    • Liu, N., and Delcour, A.H. (1998) Inhibitory effect of acidic pH on OmpC porin: wild-type and mutant studies. FEBS Lett 434: 160-164.
    • (1998) FEBS Lett , vol.434 , pp. 160-164
    • Liu, N.1    Delcour, A.H.2
  • 50
    • 0028820791 scopus 로고
    • Fluidity of the lipid domain of cell wall from Mycobacterium chelonae
    • Liu, J., Rosenberg, E.Y., and Nikaido, H. (1995) Fluidity of the lipid domain of cell wall from Mycobacterium chelonae. Proc Natl Acad Sci USA 92: 11254-11258.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11254-11258
    • Liu, J.1    Rosenberg, E.Y.2    Nikaido, H.3
  • 51
    • 0029862802 scopus 로고    scopus 로고
    • Mycolic acid structure determines the fluidity of the mycobacterial cell wall
    • Liu, J., Barry, C.E., III, Besra, G.S., and Nikaido, H. (1996) Mycolic acid structure determines the fluidity of the mycobacterial cell wall. J Biol Chem 271: 29545-29551.
    • (1996) J Biol Chem , vol.271 , pp. 29545-29551
    • Liu, J.1    Barry C.E. III2    Besra, G.S.3    Nikaido, H.4
  • 52
    • 0023852792 scopus 로고
    • Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site
    • Maier, C., Bremer, E., Schmid, A., and Benz, R. (1988) Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site. J Biol Chem 263: 2493-2499.
    • (1988) J Biol Chem , vol.263 , pp. 2493-2499
    • Maier, C.1    Bremer, E.2    Schmid, A.3    Benz, R.4
  • 53
    • 0016912108 scopus 로고
    • Thermotropic transitions in biomembranes
    • Melchior, D.L., and Steim, J.M. (1976) Thermotropic transitions in biomembranes. Annu Rev Biophys Bioeng 5: 205-238.
    • (1976) Annu Rev Biophys Bioeng , vol.5 , pp. 205-238
    • Melchior, D.L.1    Steim, J.M.2
  • 54
    • 0002259015 scopus 로고
    • Lipids: Complex lipids, their chemistry, biosynthesis and roles
    • Ratledge, C., and Stanford, J. (eds). London: Academic Press
    • Minnikin, D.E. (1982) Lipids: Complex lipids, their chemistry, biosynthesis and roles. In The Biology of the Mycobacteria: Physiology, Identification and Classification. Ratledge, C., and Stanford, J. (eds). London: Academic Press, pp. 95-184
    • (1982) The Biology of the Mycobacteria: Physiology, Identification and Classification , pp. 95-184
    • Minnikin, D.E.1
  • 55
    • 0025776357 scopus 로고
    • Chemical principles in the organization of lipid components in the mycobacterial cell envelope
    • Minnikin, D.E. (1991) Chemical principles in the organization of lipid components in the mycobacterial cell envelope. Res Microbiol 142: 423-427.
    • (1991) Res Microbiol , vol.142 , pp. 423-427
    • Minnikin, D.E.1
  • 56
    • 0030882980 scopus 로고    scopus 로고
    • Characterization of a porin from Mycobacterium smegmatis
    • Mukhopadhyay, S., Basu, D., and Chakrabarti, P. (1997) Characterization of a porin from Mycobacterium smegmatis. J Bacteriol 179: 6205-6207.
    • (1997) J Bacteriol , vol.179 , pp. 6205-6207
    • Mukhopadhyay, S.1    Basu, D.2    Chakrabarti, P.3
  • 58
    • 0028025336 scopus 로고
    • Porins and specific diffusion channels in bacterial outer membranes
    • Nikaido, H. (1994) Porins and specific diffusion channels in bacterial outer membranes. J Biol Chem 269: 3905-3908.
    • (1994) J Biol Chem , vol.269 , pp. 3905-3908
    • Nikaido, H.1
  • 59
    • 0020597554 scopus 로고
    • Porin channels in Escherichia coli: Studies with liposomes reconstituted from purified proteins
    • Nikaido, H., and Rosenberg, E.Y. (1983) Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins. J Bacteriol 153: 241-252.
    • (1983) J Bacteriol , vol.153 , pp. 241-252
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 60
    • 0017687155 scopus 로고
    • Outer membrane of Salmonella. XIV. Reduced transmembrane diffusion rates in porin-deficient mutants
    • Nikaido, H., Song, S.A., Shaltiel, L., and Nurminen, M. (1977) Outer membrane of Salmonella. XIV. Reduced transmembrane diffusion rates in porin-deficient mutants. Biochem Biophys Res Commun 76: 324-330.
    • (1977) Biochem Biophys Res Commun , vol.76 , pp. 324-330
    • Nikaido, H.1    Song, S.A.2    Shaltiel, L.3    Nurminen, M.4
  • 61
    • 0027222842 scopus 로고
    • Physical organization of lipids in the cell wall of Mycobacterium chelonae
    • Nikaido, H., Kim, S.H., and Rosenberg, E.Y. (1993) Physical organization of lipids in the cell wall of Mycobacterium chelonae. Mol Microbiol 8: 1025-1030.
    • (1993) Mol Microbiol , vol.8 , pp. 1025-1030
    • Nikaido, H.1    Kim, S.H.2    Rosenberg, E.Y.3
  • 62
    • 0030070034 scopus 로고    scopus 로고
    • Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species
    • Ortalo-Magne, A., Lemassu, A., Laneelle, M.A., Bardou, F., Silve, G., Gounon, P., et al. (1996) Identification of the surface-exposed lipids on the cell envelopes of Mycobacterium tuberculosis and other mycobacterial species. J Bacteriol 178: 456-461.
    • (1996) J Bacteriol , vol.178 , pp. 456-461
    • Ortalo-Magne, A.1    Lemassu, A.2    Laneelle, M.A.3    Bardou, F.4    Silve, G.5    Gounon, P.6
  • 63
    • 0026655895 scopus 로고
    • Reevaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols
    • Paul, T.R., and Beveridge, T.J. (1992) Reevaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols. J Bacteriol 174: 6508-6517.
    • (1992) J Bacteriol , vol.174 , pp. 6508-6517
    • Paul, T.R.1    Beveridge, T.J.2
  • 64
    • 0027691151 scopus 로고
    • Ultrastructure of mycobacterial surfaces by freeze-substitution
    • Paul, T.R., and Beveridge, T.J. (1993) Ultrastructure of mycobacterial surfaces by freeze-substitution. Zentralbl Bakteriol 279: 450-457.
    • (1993) Zentralbl Bakteriol , vol.279 , pp. 450-457
    • Paul, T.R.1    Beveridge, T.J.2
  • 65
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch, A., and Schulz, G.E. (1998) Structure of the outer membrane protein A transmembrane domain. Nat Struct Biol 5: 1013-1017.
    • (1998) Nat Struct Biol , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 66
    • 0035849873 scopus 로고    scopus 로고
    • The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination
    • Pethe, K., Alonso, S., Biet, F., Delogu, G., Brennan, M.J., Locht, C., and Menozzi, F.D. (2001) The heparin-binding haemagglutinin of M. tuberculosis is required for extrapulmonary dissemination. Nature 412: 190-194.
    • (2001) Nature , vol.412 , pp. 190-194
    • Pethe, K.1    Alonso, S.2    Biet, F.3    Delogu, G.4    Brennan, M.J.5    Locht, C.6    Menozzi, F.D.7
  • 67
    • 0035967529 scopus 로고    scopus 로고
    • Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation
    • Phale, P.S., Philippsen, A., Widmer, C., Phale, V.P., Rosenbusch, J.P., and Schirmer, T. (2001) Role of charged residues at the OmpF porin channel constriction probed by mutagenesis and simulation. Biochemistry 40: 6319-6325.
    • (2001) Biochemistry , vol.40 , pp. 6319-6325
    • Phale, P.S.1    Philippsen, A.2    Widmer, C.3    Phale, V.P.4    Rosenbusch, J.P.5    Schirmer, T.6
  • 69
    • 0029992419 scopus 로고    scopus 로고
    • From acids to osmZ: Multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli
    • Pratt, L.A., Hsing, W., Gibson, K.E., and Silhavy, T.J. (1996) From acids to osmZ: multiple factors influence synthesis of the OmpF and OmpC porins in Escherichia coli. Mol Microbiol 20: 911-917.
    • (1996) Mol Microbiol , vol.20 , pp. 911-917
    • Pratt, L.A.1    Hsing, W.2    Gibson, K.E.3    Silhavy, T.J.4
  • 70
    • 0027450561 scopus 로고
    • The complete general secretorypathway in gram-negative bacteria
    • Pugsley, A.P. (1993) The complete general secretorypathway in gram-negative bacteria. Microbiol Rev 57: 50-108.
    • (1993) Microbiol Rev , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 71
    • 0034043955 scopus 로고    scopus 로고
    • The Fusobacterium nucleatum porin FomA possesses the general topology of the non-specific porins
    • Puntervoll, P., Kleivdal, H., Dahl, K.O., Bitter, W., Tommassen, J., and Jensen, H.B. (2000) The Fusobacterium nucleatum porin FomA possesses the general topology of the non-specific porins. Microbiology 146: 1437-1445.
    • (2000) Microbiology , vol.146 , pp. 1437-1445
    • Puntervoll, P.1    Kleivdal, H.2    Dahl, K.O.3    Bitter, W.4    Tommassen, J.5    Jensen, H.B.6
  • 72
    • 0040162268 scopus 로고    scopus 로고
    • The mycobacteria: An introduction to nomenclature and pathogenesis
    • Rastogi, N., Legrand, E., and Sola, C. (2001) The mycobacteria: an introduction to nomenclature and pathogenesis. Rev Sci Tech 20: 21-54.
    • (2001) Rev Sci Tech , vol.20 , pp. 21-54
    • Rastogi, N.1    Legrand, E.2    Sola, C.3
  • 73
    • 0043284551 scopus 로고    scopus 로고
    • Mechanisms of pyrazinamide resistance in mycobacteria: Importance of lack of uptake in addition to lack of pyrazinamidase activity
    • Raynaud, C., Laneelle, M.A., Senaratne, R.H., Draper, P., Laneelle, G., and Daffé, M. (1999) Mechanisms of pyrazinamide resistance in mycobacteria: importance of lack of uptake in addition to lack of pyrazinamidase activity. Microbiology 145: 1359-1367.
    • (1999) Microbiology , vol.145 , pp. 1359-1367
    • Raynaud, C.1    Laneelle, M.A.2    Senaratne, R.H.3    Draper, P.4    Laneelle, G.5    Daffé, M.6
  • 75
  • 76
    • 0035477536 scopus 로고    scopus 로고
    • Mycobacterium smegmatis: An absurd model for tuberculosis?
    • Reyrat, J., and Kahn, D. (2001) Mycobacterium smegmatis: an absurd model for tuberculosis? Trends Microbiol 9: 472-473.
    • (2001) Trends Microbiol , vol.9 , pp. 472-473
    • Reyrat, J.1    Kahn, D.2
  • 77
    • 2142686080 scopus 로고    scopus 로고
    • Study of the properties of a channel-forming protein of the cell wall of the Gram-positive bacterium Mycobacterium phlei
    • Riess, F.G., Dorner, U., Schiffler, B., and Benz, R. (2001) Study of the properties of a channel-forming protein of the cell wall of the Gram-positive bacterium Mycobacterium phlei. J Membr Biol 182: 147-157.
    • (2001) J Membr Biol , vol.182 , pp. 147-157
    • Riess, F.G.1    Dorner, U.2    Schiffler, B.3    Benz, R.4
  • 78
    • 0031974203 scopus 로고    scopus 로고
    • Differentiation of phylogenetically related slowly growing mycobacteria based on 16S-23S rRNA gene internal transcribed spacer sequences
    • Roth, A., Fischer, M., Hamid, M.E., Michalke, S., Ludwig, W., and Mauch, H. (1998) Differentiation of phylogenetically related slowly growing mycobacteria based on 16S-23S rRNA gene internal transcribed spacer sequences. J Clin Microbiol 36: 139-147.
    • (1998) J Clin Microbiol , vol.36 , pp. 139-147
    • Roth, A.1    Fischer, M.2    Hamid, M.E.3    Michalke, S.4    Ludwig, W.5    Mauch, H.6
  • 79
    • 0034666641 scopus 로고    scopus 로고
    • Ion channel formation by N-terminal domain: A common feature of OprFs of Pseudomonas and OmpA of Escherichia coli
    • Saint, N., El Hamel, C., E., and Molle, G. (2000) Ion channel formation by N-terminal domain: a common feature of OprFs of Pseudomonas and OmpA of Escherichia coli. FEMS Microbiol Lett 190: 261-265.
    • (2000) FEMS Microbiol Lett , vol.190 , pp. 261-265
    • Saint, N.1    El Hamel, C.E.2    Molle, G.3
  • 80
    • 0031914958 scopus 로고    scopus 로고
    • Cytokine activation leads to acidification and increases maturation of Mycobacterium avium-containing phagosomes in murine macrophages
    • Schaible, U.E., Sturgill-Koszycki, S., Schlesinger, P.H., and Russell, D.G. (1998) Cytokine activation leads to acidification and increases maturation of Mycobacterium avium-containing phagosomes in murine macrophages. J Immunol 160: 1290-1296.
    • (1998) J Immunol , vol.160 , pp. 1290-1296
    • Schaible, U.E.1    Sturgill-Koszycki, S.2    Schlesinger, P.H.3    Russell, D.G.4
  • 81
    • 0025865958 scopus 로고
    • Primary structure of porin from Rhodobacter capsulatus
    • Schlitz, E., Kreusch, A., Nestel, U., and Schulz, G.E. (1991) Primary structure of porin from Rhodobacter capsulatus. Eur J Biochem 199: 587-594.
    • (1991) Eur J Biochem , vol.199 , pp. 587-594
    • Schlitz, E.1    Kreusch, A.2    Nestel, U.3    Schulz, G.E.4
  • 82
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • Schulz, G.E. (2002) The structure of bacterial outer membrane proteins. Biochim Biophys Acta 1565: 308-317.
    • (2002) Biochim Biophys Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 83
    • 0017330062 scopus 로고
    • Action of a major outer cell envelope membrane protein in conjugation of Escherichia coli K-12
    • Schweizer, M., and Henning, U. (1977) Action of a major outer cell envelope membrane protein in conjugation of Escherichia coli K-12. J Bacteriol 129: 1651-1652.
    • (1977) J Bacteriol , vol.129 , pp. 1651-1652
    • Schweizer, M.1    Henning, U.2
  • 84
    • 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. (1998) Expression of a gene for a porin-like protein of the OmpA family from Mycobacterium tuberculosis H37Rv. J Bacteriol 180: 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
  • 85
    • 0025081151 scopus 로고
    • Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis
    • Snapper, S.B., Melton, R.E., Mustafa, S., Kieser, T., and Jacobs, W.R., Jr (1990) Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol Microbiol 4: 1911-1919.
    • (1990) Mol Microbiol , vol.4 , pp. 1911-1919
    • Snapper, S.B.1    Melton, R.E.2    Mustafa, S.3    Kieser, T.4    Jacobs W.R., Jr.5
  • 86
    • 0018150270 scopus 로고
    • Cell envelope and shape of Escherichia coli: Multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins
    • Sonntag, I., Schwarz, H., Hirota, Y., and Henning, U. (1978) Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J Bacteriol 136: 280-285.
    • (1978) J Bacteriol , vol.136 , pp. 280-285
    • Sonntag, I.1    Schwarz, H.2    Hirota, Y.3    Henning, U.4
  • 87
    • 0035028415 scopus 로고    scopus 로고
    • MspA provides the main hydrophilic pathway through the cell wall of Mycobacterium smegmatis
    • Stahl, C., Kubetzko, S., Kaps, I., Seeber, S., Engelhardt, H., and Niederweis, M. (2001) MspA provides the main hydrophilic pathway through the cell wall of Mycobacterium smegmatis. Mol Microbiol 40: 451-464.
    • (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
  • 88
    • 0026785288 scopus 로고
    • Pore-forming activity of OmpA protein of Escherichia coli
    • Sugawara, E., and Nikaido, H. (1992) Pore-forming activity of OmpA protein of Escherichia coli. J Biol Chem 267: 2507-2511.
    • (1992) J Biol Chem , vol.267 , pp. 2507-2511
    • Sugawara, E.1    Nikaido, H.2
  • 89
    • 0028321391 scopus 로고
    • OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms
    • Sugawara, E., and Nikaido, H. (1994) OmpA protein of Escherichia coli outer membrane occurs in open and closed channel forms. J Biol Chem 269: 17981-17987.
    • (1994) J Biol Chem , vol.269 , pp. 17981-17987
    • Sugawara, E.1    Nikaido, H.2
  • 90
    • 0027418821 scopus 로고
    • Characterization of the channel formed by the mycobactedal porin in lipid bilayer membranes. Demonstration of voltage gating and of negative point charges at the channel mouth
    • Trias, J., and Benz, R. (1993) Characterization of the channel formed by the mycobactedal porin in lipid bilayer membranes. Demonstration of voltage gating and of negative point charges at the channel mouth. J Biol Chem 268: 6234-6240.
    • (1993) J Biol Chem , vol.268 , pp. 6234-6240
    • Trias, J.1    Benz, R.2
  • 91
    • 0028113382 scopus 로고
    • Permeability of the cell wall of Mycobacterium smegmatis
    • Trias, J., and Benz, R. (1994) Permeability of the cell wall of Mycobacterium smegmatis. Mol Microbiol 14: 283-290.
    • (1994) Mol Microbiol , vol.14 , pp. 283-290
    • Trias, J.1    Benz, R.2
  • 92
    • 0027064590 scopus 로고
    • Porins in the cell wall of mycobacteria
    • Trias, J., Jarlier, V., and Benz, R. (1992) Porins in the cell wall of mycobacteria. Science 258: 1479-1481.
    • (1992) Science , vol.258 , pp. 1479-1481
    • Trias, J.1    Jarlier, V.2    Benz, R.3
  • 93
    • 0036291172 scopus 로고    scopus 로고
    • The function of OmpA in Escherichia coli
    • Wang, Y. (2002) The function of OmpA in Escherichia coli. Biochem Biophys Res Commun 292: 396-401.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 396-401
    • Wang, Y.1
  • 94
    • 0034924433 scopus 로고    scopus 로고
    • Separation and characterization of individual mycolic acids in representative mycobacteria
    • Watanabe, M., Aoyagi, Y., Ridell, M., and Minnikin, D.E. (2001) Separation and characterization of individual mycolic acids in representative mycobacteria. Microbiology 147: 1825-1837.
    • (2001) Microbiology , vol.147 , pp. 1825-1837
    • Watanabe, M.1    Aoyagi, Y.2    Ridell, M.3    Minnikin, D.E.4
  • 95
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss, M.S., Abele, U., Weckesser, J., Welte, W., Schlitz, E., and Schulz, G.E. (1991) Molecular architecture and electrostatic properties of a bacterial porin. Science 254: 1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schlitz, E.5    Schulz, G.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.