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Volumn 11, Issue SUPPL. 1, 2006, Pages 2017-2027

Subcellular structures of mycoplasmas

Author keywords

Adherence; Attachment Organelle; Cytoskeleton; Mycoplasma; Review; Ultrastructure

Indexed keywords

BACTERIA (MICROORGANISMS); EUKARYOTA; MYCOPLASMA; MYCOPLASMA MOBILE; MYCOPLASMA PNEUMONIAE; MYCOPLASMATALES; PROKARYOTA;

EID: 33744739470     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1943     Document Type: Article
Times cited : (18)

References (120)
  • 2
    • 0002890882 scopus 로고
    • A motile organism of the pleuropneumonia group
    • Andrewes C.W. & F.V. Welch. A motile organism of the pleuropneumonia group. J Pathol Bacteriol 58, 578-580 (1946)
    • (1946) J Pathol Bacteriol , vol.58 , pp. 578-580
    • Andrewes, C.W.1    Welch, F.V.2
  • 3
    • 0014397430 scopus 로고
    • Motility and multiplication of Mycoplasma pneumoniae: A phase-contrast study
    • Bredt W. Motility and multiplication of Mycoplasma pneumoniae: a phase-contrast study. Pathol Microbiol 32, 321-326 (1968)
    • (1968) Pathol Microbiol , vol.32 , pp. 321-326
    • Bredt, W.1
  • 4
    • 0000761034 scopus 로고
    • Motility
    • Eds: Barile MF, Razin S, Academic Press, NY
    • W. Bredt: Motility. In: The Mycoplasmas. Eds: Barile MF, Razin S, Vol 1, Academic Press, NY, 141-155 (1979)
    • (1979) The Mycoplasmas , vol.1 , pp. 141-155
    • Bredt, W.1
  • 5
    • 0001927033 scopus 로고
    • Morphology and Ultrastructure of the Mycoplasmatales
    • Eds: Barile MF, Razin S, Academic Press, NY
    • E.S. Boatman: Morphology and Ultrastructure of the Mycoplasmatales. The Mycoplasmas. Eds: Barile MF, Razin S, Vol 1, Academic Press, NY, 63-102 (1979)
    • (1979) The Mycoplasmas , vol.1 , pp. 63-102
    • Boatman, E.S.1
  • 6
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent F., L.A. Amos & J. Lowe. Prokaryotic origin of the actin cytoskeleton. Nature 413, 39-44 (2001)
    • (2001) Nature , vol.413 , pp. 39-44
    • Van Den Ent, F.1    Amos, L.A.2    Lowe, J.3
  • 7
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones L.J., R. Carballido-Lopez & J. Errington. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104, 913-922 (2001)
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 8
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
    • Shih Y.L., T. Le & L.I. Rothfield. Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc Natl Acad Sci USA 100, 7865-7870 (2003)
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7865-7870
    • Shih, Y.L.1    Le, T.2    Rothfield, L.I.3
  • 9
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, coordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge R.M., A.V. Divakaruni & J.W. Gober. MreB, the cell shape-determining bacterial actin homologue, coordinates cell wall morphogenesis in Caulobacter crescentus. Mol Microbiol 51, 1321-1332 (2004)
    • (2004) Mol Microbiol , vol.51 , pp. 1321-1332
    • Figge, R.M.1    Divakaruni, A.V.2    Gober, J.W.3
  • 10
    • 0242381270 scopus 로고    scopus 로고
    • Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins
    • Soufo H.J. & P.L. Graumann. Actin-like proteins MreB and Mbl from Bacillus subtilis are required for bipolar positioning of replication origins. Curr Biol. 13, 1916-1920 (2003)
    • (2003) Curr Biol , vol.13 , pp. 1916-1920
    • Soufo, H.J.1    Graumann, P.L.2
  • 11
    • 0035114392 scopus 로고    scopus 로고
    • Cell division protein FtsZ: Running rings around bacteria, chloroplasts and mitochondria
    • Gilson P.R. & P.L. Beech. Cell division protein FtsZ: running rings around bacteria, chloroplasts and mitochondria. Res Microbiol 152, 3-10 (2001)
    • (2001) Res Microbiol , vol.152 , pp. 3-10
    • Gilson, P.R.1    Beech, P.L.2
  • 13
    • 0346020436 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: An intermediate filament-like function in cell shape
    • Ausmees N., J.R. Kuhn & C. Jacobs-Wagner. The bacterial cytoskeleton: an intermediate filament-like function in cell shape. Cell 115, 705-713 (2003)
    • (2003) Cell , vol.115 , pp. 705-713
    • Ausmees, N.1    Kuhn, J.R.2    Jacobs-Wagner, C.3
  • 14
    • 0001299065 scopus 로고
    • Relationships between Mycoplasma pneumoniae and human respiratory epithelium
    • Collier A.M. & W.A. Clyde, Jr. Relationships between Mycoplasma pneumoniae and human respiratory epithelium. Infect Immun 3, 694-701 (1971)
    • (1971) Infect Immun , vol.3 , pp. 694-701
    • Collier, A.M.1    Clyde Jr., W.A.2
  • 15
    • 0013951267 scopus 로고
    • The interaction of mycoplasmas with mammalian cells. I. HeLa cells, neutrophils, and eosinophils
    • Zucker-Franklin D., M. Davidson & L. Thomas. The interaction of mycoplasmas with mammalian cells. I. HeLa cells, neutrophils, and eosinophils. J Exp Med 124, 521-532 (1966)
    • (1966) J Exp Med , vol.124 , pp. 521-532
    • Zucker-Franklin, D.1    Davidson, M.2    Thomas, L.3
  • 16
    • 0019205331 scopus 로고
    • Intracellular structures of Mycoplasma pneumoniae revealed after membrane removal
    • Meng K.E. & R.M. Pfister. Intracellular structures of Mycoplasma pneumoniae revealed after membrane removal. J Bacteriol 144, 390-399 (1980)
    • (1980) J Bacteriol , vol.144 , pp. 390-399
    • Meng, K.E.1    Pfister, R.M.2
  • 17
    • 0019816823 scopus 로고
    • Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents
    • Gobel U., V. Speth & W. Bredt. Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents. J Cell Biol 91, 537-543 (1981)
    • (1981) J Cell Biol , vol.91 , pp. 537-543
    • Gobel, U.1    Speth, V.2    Bredt, W.3
  • 18
    • 0017759026 scopus 로고
    • Extraction of an actin-like protein from the prokaryote Mycoplasma pneumoniae
    • Neimark H.C. Extraction of an actin-like protein from the prokaryote Mycoplasma pneumoniae. Proc Natl Acad Sci USA 74, 4041-4045 (1977)
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 4041-4045
    • Neimark, H.C.1
  • 19
    • 0017838727 scopus 로고
    • Inhibition of mycoplasma division by cytochalasin B
    • Ghosh A., J. Maniloff & D.A. Gerling. Inhibition of mycoplasma division by cytochalasin B. Cell 13, 57-64 (1978)
    • (1978) Cell , vol.13 , pp. 57-64
    • Ghosh, A.1    Maniloff, J.2    Gerling, D.A.3
  • 21
    • 0035050279 scopus 로고    scopus 로고
    • Defining the mycoplasma 'cytoskeleton': The protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2-D gel electrophoresis and mass spectrometry
    • Regula J.T., G. Boguth, A. Gorg, J. Hegermann, F. Mayer, R. Frank & R. Herrmann. Defining the mycoplasma 'cytoskeleton': the protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2-D gel electrophoresis and mass spectrometry. Microbiology 147, 1045-1057 (2001).
    • (2001) Microbiology , vol.147 , pp. 1045-1057
    • Regula, J.T.1    Boguth, G.2    Gorg, A.3    Hegermann, J.4    Mayer, F.5    Frank, R.6    Herrmann, R.7
  • 22
    • 1442300837 scopus 로고    scopus 로고
    • Cellular engineering in a minimal microbe: Structure and assembly of the terminal organelle of Mycoplasma pneumoniae
    • Krause D.C. & M.F. Balish. Cellular engineering in a minimal microbe: structure and assembly of the terminal organelle of Mycoplasma pneumoniae. Mol Microbiol 51, 917-924 (2004)
    • (2004) Mol Microbiol , vol.51 , pp. 917-924
    • Krause, D.C.1    Balish, M.F.2
  • 23
    • 3042615587 scopus 로고    scopus 로고
    • Spike structure at the interface between gliding Mycoplasma mobile cells and glass surfaces visualized by rapid-freeze-and-fracture electron microscopy
    • Miyata M. & J.D. Petersen. Spike structure at the interface between gliding Mycoplasma mobile cells and glass surfaces visualized by rapid-freeze-and-fracture electron microscopy. J Bacteriol 186: 4382-4386 (2004)
    • (2004) J Bacteriol , vol.186 , pp. 4382-4386
    • Miyata, M.1    Petersen, J.D.2
  • 24
    • 0015830895 scopus 로고
    • Occurrence and ultrastructure of a variant (rho) form of Mycoplasma
    • Peterson J.E., A.W. Rodwell & E.S. Rodwell. Occurrence and ultrastructure of a variant (rho) form of Mycoplasma. J Bacteriol 115: 411-425 (1973)
    • (1973) J Bacteriol , vol.115 , pp. 411-425
    • Peterson, J.E.1    Rodwell, A.W.2    Rodwell, E.S.3
  • 25
    • 1242292243 scopus 로고    scopus 로고
    • Cell division gene cluster in Spiroplasma kunkelii: Functional characterization of ftsZ and the first report of ftsA in mollicutes
    • Zhao Y., R.W. Hammond, I.M. Lee, B.A. Roe, S. Lin & R.E. Davis. Cell division gene cluster in Spiroplasma kunkelii: functional characterization of ftsZ and the first report of ftsA in mollicutes. DNA Cell Biol 23, 127-134 (2004)
    • (2004) DNA Cell Biol , vol.23 , pp. 127-134
    • Zhao, Y.1    Hammond, R.W.2    Lee, I.M.3    Roe, B.A.4    Lin, S.5    Davis, R.E.6
  • 26
    • 21144450388 scopus 로고    scopus 로고
    • Transcriptional analysis of the conserved ftsZ gene cluster in Mycoplasma genitalium and Mycoplasma pneumoniae
    • Benders G.A., B.C. Powell & C.A. Hutchison III. Transcriptional analysis of the conserved ftsZ gene cluster in Mycoplasma genitalium and Mycoplasma pneumoniae. J Bacteriol 187, 4542-4551 (2005)
    • (2005) J Bacteriol , vol.187 , pp. 4542-4551
    • Benders, G.A.1    Powell, B.C.2    Hutchison III, C.A.3
  • 27
    • 0036809920 scopus 로고    scopus 로고
    • Cytoskeletal elements in the bacterium Mycoplasma pneumoniae
    • Hegermann J., F. Mayer & R. Herrmann. Cytoskeletal elements in the bacterium Mycoplasma pneumoniae. Naturwissenschaften 89, 453-458 (2002)
    • (2002) Naturwissenschaften , vol.89 , pp. 453-458
    • Hegermann, J.1    Mayer, F.2    Herrmann, R.3
  • 28
    • 0037221778 scopus 로고    scopus 로고
    • Localization of Mycoplasma pneumoniae cytadherence-associated protein HMW2 by fusion with green fluorescent protein: Implications for attachment organelle structure
    • Balish M.F., R.T. Santurri, A. Ricci, K.K. Lee & D.C. Krause. Localization of Mycoplasma pneumoniae cytadherence-associated protein HMW2 by fusion with green fluorescent protein: implications for attachment organelle structure. Mol Microbiol 47, 49-60 (2003)
    • (2003) Mol Microbiol , vol.47 , pp. 49-60
    • Balish, M.F.1    Santurri, R.T.2    Ricci, A.3    Lee, K.K.4    Krause, D.C.5
  • 29
    • 5644300391 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae and its role as a human pathogen
    • Waites K.B. & D.F. Talkington. Mycoplasma pneumoniae and its role as a human pathogen. Clin Microbiol Rev 17, 697-728 (2004)
    • (2004) Clin Microbiol Rev , vol.17 , pp. 697-728
    • Waites, K.B.1    Talkington, D.F.2
  • 30
    • 0014807002 scopus 로고
    • Ultrastructural features of Mycoplasma pneumoniae
    • Biberfeld G. & P. Biberfeld. Ultrastructural features of Mycoplasma pneumoniae. J Bacteriol 102, 855-861 (1970)
    • (1970) J Bacteriol , vol.102 , pp. 855-861
    • Biberfeld, G.1    Biberfeld, P.2
  • 31
    • 0018489241 scopus 로고
    • An ultrastructural study on the interaction of Mycoplasma gallisepticum with the chicken tracheal epithelium
    • Tajima M., T. Nunoya & T. Yagihashi. An ultrastructural study on the interaction of Mycoplasma gallisepticum with the chicken tracheal epithelium. Am J Vet Res 40, 1009-1014 (1979)
    • (1979) Am J Vet Res , vol.40 , pp. 1009-1014
    • Tajima, M.1    Nunoya, T.2    Yagihashi, T.3
  • 32
    • 0040782137 scopus 로고    scopus 로고
    • Avian mycoplasmosis (Mycoplasma gallisepticum)
    • Levisohn S. & S.H. Kleven. Avian mycoplasmosis (Mycoplasma gallisepticum). Rev Sci Tech 19, 425-442 (2000)
    • (2000) Rev Sci Tech , vol.19 , pp. 425-442
    • Levisohn, S.1    Kleven, S.H.2
  • 33
    • 0029182483 scopus 로고
    • Attachment of Mycoplasma mobile 163 K to piscine gill arches and rakers - Light, scanning and transmission electron microscopic findings
    • Stadtlander C.T. & H. Kirchhoff. Attachment of Mycoplasma mobile 163 K to piscine gill arches and rakers - light, scanning and transmission electron microscopic findings. Br Vet J 151, 89-100 (1995)
    • (1995) Br Vet J , vol.151 , pp. 89-100
    • Stadtlander, C.T.1    Kirchhoff, H.2
  • 34
    • 0021931565 scopus 로고
    • Interaction of Mycoplasma pneumoniae with erythrocyte glycolipids of I and i antigen types
    • Loomes L.M., K. Uemura & T. Feizi. Interaction of Mycoplasma pneumoniae with erythrocyte glycolipids of I and i antigen types. Infect Immun 47, 15-20 (1985)
    • (1985) Infect Immun , vol.47 , pp. 15-20
    • Loomes, L.M.1    Uemura, K.2    Feizi, T.3
  • 35
    • 0024517925 scopus 로고
    • Sialo-oligosaccharide receptors for Mycoplasma pneumoniae and related oligosaccharides of poly-N-acetyllactosamine series are polarized at the cilia and apical-microvillar domains of the ciliated cells in human bronchial epithelium
    • Loveless R.W. & T. Feizi. Sialo-oligosaccharide receptors for Mycoplasma pneumoniae and related oligosaccharides of poly-N-acetyllactosamine series are polarized at the cilia and apical-microvillar domains of the ciliated cells in human bronchial epithelium. Infect Immun 57, 1285-1289 (1989)
    • (1989) Infect Immun , vol.57 , pp. 1285-1289
    • Loveless, R.W.1    Feizi, T.2
  • 36
    • 0024409821 scopus 로고
    • Adhesion of Mycoplasma pneumoniae to sulfated glycolipids and inhibition by dextran sulfate
    • Krivan H.C., L.D. Olson, M.F. Barile, V. Ginsburg & D.D. Roberts. Adhesion of Mycoplasma pneumoniae to sulfated glycolipids and inhibition by dextran sulfate. J Biol Chem 264, 9283-9288 (1989)
    • (1989) J Biol Chem , vol.264 , pp. 9283-9288
    • Krivan, H.C.1    Olson, L.D.2    Barile, M.F.3    Ginsburg, V.4    Roberts, D.D.5
  • 37
    • 0036434714 scopus 로고    scopus 로고
    • Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae
    • Dallo S.F., T.R. Kannan, M.W. Blaylock & J.B. Baseman. Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae. Mol Microbiol 46, 1041-1051 (2002)
    • (2002) Mol Microbiol , vol.46 , pp. 1041-1051
    • Dallo, S.F.1    Kannan, T.R.2    Blaylock, M.W.3    Baseman, J.B.4
  • 38
    • 0038460041 scopus 로고    scopus 로고
    • Surface localized glyceraldehyde-3-phosphate dehydrogenase of Mycoplasma genitalium binds mucin
    • Alvarez R.A., M.W. Blaylock & J.B. Baseman. Surface localized glyceraldehyde-3-phosphate dehydrogenase of Mycoplasma genitalium binds mucin. Mol Microbiol 48, 1417-1425 (2003)
    • (2003) Mol Microbiol , vol.48 , pp. 1417-1425
    • Alvarez, R.A.1    Blaylock, M.W.2    Baseman, J.B.3
  • 39
    • 17644416114 scopus 로고    scopus 로고
    • Identification and characterization of human surfactant protein a binding protein of Mycoplasma pneumoniae
    • Kannan T.R., D. Provenzano, J.R. Wright & J.B. Baseman. Identification and characterization of human surfactant protein A binding protein of Mycoplasma pneumoniae. Infect Immun 73, 2828-2834 (2005)
    • (2005) Infect Immun , vol.73 , pp. 2828-2834
    • Kannan, T.R.1    Provenzano, D.2    Wright, J.R.3    Baseman, J.B.4
  • 40
    • 0842329803 scopus 로고    scopus 로고
    • Mycoplasma genitalium: The aetiological agent of urethritis and other sexually transmitted diseases
    • Jensen J.S. Mycoplasma genitalium: the aetiological agent of urethritis and other sexually transmitted diseases. J Eur Acad Dermatol Venereol 18, 1-11 (2004)
    • (2004) J Eur Acad Dermatol Venereol , vol.18 , pp. 1-11
    • Jensen, J.S.1
  • 41
    • 0014005529 scopus 로고
    • Sialic acid binding sites: Roles in hemagglutination by Mycoplasma gallisepticum
    • Gesner B. & L. Thomas. Sialic acid binding sites: roles in hemagglutination by Mycoplasma gallisepticum. Science 151, 590-591 (1966)
    • (1966) Science , vol.151 , pp. 590-591
    • Gesner, B.1    Thomas, L.2
  • 42
    • 0025718524 scopus 로고
    • Newly discovered mycoplasma isolated from patients infected with HIV
    • Lo S.C., M.M. Hayes, R.Y. Wang, P.F. Pierce, H. Kotani & J.W. Shih. Newly discovered mycoplasma isolated from patients infected with HIV. Lancet 338, 1415-1418 (1991)
    • (1991) Lancet , vol.338 , pp. 1415-1418
    • Lo, S.C.1    Hayes, M.M.2    Wang, R.Y.3    Pierce, P.F.4    Kotani, H.5    Shih, J.W.6
  • 44
    • 0027597861 scopus 로고
    • Adhesion onto and invasion into mammalian cells by Mycoplasma penetrans: A newly isolated mycoplasma from patients with AIDS
    • Lo S.C., M.M. Hayes, H. Kotani, P.F. Pierce, D.J. Wear, P.B. Newton III, J.G. Tully & J.W. Shih. Adhesion onto and invasion into mammalian cells by Mycoplasma penetrans: a newly isolated mycoplasma from patients with AIDS. Mod Pathol 6, 276-280 (1993)
    • (1993) Mod Pathol , vol.6 , pp. 276-280
    • Lo, S.C.1    Hayes, M.M.2    Kotani, H.3    Pierce, P.F.4    Wear, D.J.5    Newton III, P.B.6    Tully, J.G.7    Shih, J.W.8
  • 45
    • 0029055157 scopus 로고
    • Piscine gill epithelial cell necrosis due to Mycoplasma mobile strain 163 K: Comparison of in-vivo and in-vitro infection
    • Stadtlander C.T., W. Lotz, W. Korting & H. Kirchhoff. Piscine gill epithelial cell necrosis due to Mycoplasma mobile strain 163 K: comparison of in-vivo and in-vitro infection. J Comp Pathol 112, 351-359 (1995)
    • (1995) J Comp Pathol , vol.112 , pp. 351-359
    • Stadtlander, C.T.1    Lotz, W.2    Korting, W.3    Kirchhoff, H.4
  • 46
    • 0022327703 scopus 로고
    • Mycoplasma pulmonis-host relationships in a breeding colony of Sprague-Dawley rats with enzootic murine respiratory mycoplasmosis
    • Lindsey J.R., M.K. Davidson, T.R. Schoeb & G.H. Cassell. Mycoplasma pulmonis-host relationships in a breeding colony of Sprague-Dawley rats with enzootic murine respiratory mycoplasmosis. Lab Anim Sci 35, 597-608 (1985)
    • (1985) Lab Anim Sci , vol.35 , pp. 597-608
    • Lindsey, J.R.1    Davidson, M.K.2    Schoeb, T.R.3    Cassell, G.H.4
  • 47
    • 0019388279 scopus 로고
    • Adherence and colonization of Mycoplasma pulmonis to genital epithelium and spermatozoa in rats
    • Cassell G.H., W.H. Wilborn, S.H. Silvers & F.C. Minion. Adherence and colonization of Mycoplasma pulmonis to genital epithelium and spermatozoa in rats. Isr J Med Sci 17, 593-598 (1981)
    • (1981) Isr J Med Sci , vol.17 , pp. 593-598
    • Cassell, G.H.1    Wilborn, W.H.2    Silvers, S.H.3    Minion, F.C.4
  • 48
    • 0034769801 scopus 로고    scopus 로고
    • Bacterial gliding motility: Multiple mechanisms for cell movement over surfaces
    • McBride M.J. Bacterial gliding motility: multiple mechanisms for cell movement over surfaces. Annu Rev Microbiol 55, 49-75 (2001)
    • (2001) Annu Rev Microbiol , vol.55 , pp. 49-75
    • McBride, M.J.1
  • 49
    • 33744760555 scopus 로고
    • Phase contrast studies on living mycoplasmas
    • Bredt W. Phase contrast studies on living mycoplasmas. Med Microbiol Immunol 157, 169 (1972)
    • (1972) Med Microbiol Immunol , vol.157 , pp. 169
    • Bredt, W.1
  • 50
    • 0017686781 scopus 로고
    • Gliding motility of Mycoplasma pulmonis
    • Bredt W. & U. Radestock. Gliding motility of Mycoplasma pulmonis. J Bacteriol 130, 937-938 (1977)
    • (1977) J Bacteriol , vol.130 , pp. 937-938
    • Bredt, W.1    Radestock, U.2
  • 51
    • 0021739444 scopus 로고
    • Flask-shaped mycoplasmas: Properties and pathogenicity for man and animals
    • Kirchhoff H., R. Rosengarten, W. Lotz, M. Fischer & D. Lopatta. Flask-shaped mycoplasmas: properties and pathogenicity for man and animals. Isr J Med Sci 20, 848-853 (1984)
    • (1984) Isr J Med Sci , vol.20 , pp. 848-853
    • Kirchhoff, H.1    Rosengarten, R.2    Lotz, W.3    Fischer, M.4    Lopatta, D.5
  • 52
    • 0023176566 scopus 로고
    • Gliding motility of Mycoplasma sp. nov. strain 163K
    • Rosengarten R. & H. Kirchhoff. Gliding motility of Mycoplasma sp. nov. strain 163K. J Bacteriol 169, 1891-1898 (1987)
    • (1987) J Bacteriol , vol.169 , pp. 1891-1898
    • Rosengarten, R.1    Kirchhoff, H.2
  • 53
    • 24944547468 scopus 로고    scopus 로고
    • Mutant analysis reveals specific requirement for protein P30 in Mycoplasma pneumoniae gliding motility
    • Hasselbring B.M., J.L. Jordan & D.C. Krause. Mutant analysis reveals specific requirement for protein P30 in Mycoplasma pneumoniae gliding motility. J Bacteriol 187, 6281-6289 (2005)
    • (2005) J Bacteriol , vol.187 , pp. 6281-6289
    • Hasselbring, B.M.1    Jordan, J.L.2    Krause, D.C.3
  • 54
    • 1342304075 scopus 로고    scopus 로고
    • Identification of a 349-kilodalton protein (Gli349) responsible for cytadherence and glass binding during gliding of Mycoplasma mobile
    • Uenoyama A., A. Kusumoto & M. Miyata. Identification of a 349-kilodalton protein (Gli349) responsible for cytadherence and glass binding during gliding of Mycoplasma mobile. J Bacteriol 186, 1537-1545 (2004)
    • (2004) J Bacteriol , vol.186 , pp. 1537-1545
    • Uenoyama, A.1    Kusumoto, A.2    Miyata, M.3
  • 55
    • 18244379832 scopus 로고    scopus 로고
    • Identification of a 521-kilodalton protein (Gli521) involved in force generation or force transmission for Mycoplasma mobile gliding
    • Seto S., A. Uenoyama & M. Miyata. Identification of a 521-kilodalton protein (Gli521) involved in force generation or force transmission for Mycoplasma mobile gliding. J Bacteriol 187, 3502-3510 (2005)
    • (2005) J Bacteriol , vol.187 , pp. 3502-3510
    • Seto, S.1    Uenoyama, A.2    Miyata, M.3
  • 56
    • 3042515670 scopus 로고    scopus 로고
    • Energetics of gliding motility in Mycoplasma mobile
    • Jaffe J.D., M. Miyata & H. Berg. Energetics of gliding motility in Mycoplasma mobile. J Bacteriol 186, 4254-4261 (2004)
    • (2004) J Bacteriol , vol.186 , pp. 4254-4261
    • Jaffe, J.D.1    Miyata, M.2    Berg, H.3
  • 57
    • 0013901392 scopus 로고
    • Analysis of the life cycle of Mycoplasma gallisepticum
    • Morowitz H.J. & J. Maniloff. Analysis of the life cycle of Mycoplasma gallisepticum. J Bacteriol 91, 1638-1644 (1966)
    • (1966) J Bacteriol , vol.91 , pp. 1638-1644
    • Morowitz, H.J.1    Maniloff, J.2
  • 58
    • 0035113906 scopus 로고    scopus 로고
    • Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy
    • Seto S., G. Layh-Schmitt, T. Kenri & M. Miyata. Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy. J Bacteriol 183, 1621-1630 (2001)
    • (2001) J Bacteriol , vol.183 , pp. 1621-1630
    • Seto, S.1    Layh-Schmitt, G.2    Kenri, T.3    Miyata, M.4
  • 59
    • 0026720512 scopus 로고
    • Mycoplasma pneumoniae cytadherence phase-variabl protein HMW3 is a component of the attachment organelle
    • Stevens M.K. & D.C. Krause. Mycoplasma pneumoniae cytadherence phase-variabl protein HMW3 is a component of the attachment organelle. J Bacteriol 174, 4265-4274 (1992)
    • (1992) J Bacteriol , vol.174 , pp. 4265-4274
    • Stevens, M.K.1    Krause, D.C.2
  • 60
    • 0036094563 scopus 로고    scopus 로고
    • Characterization of a Mycoplasma pneumoniae hmw3 mutant: Implications for attachment organelle assembly
    • Willby M.J. & D.C. Krause. Characterization of a Mycoplasma pneumoniae hmw3 mutant: implications for attachment organelle assembly. J Bacteriol 184, 3061-3068 (2002)
    • (2002) J Bacteriol , vol.184 , pp. 3061-3068
    • Willby, M.J.1    Krause, D.C.2
  • 61
    • 0016201010 scopus 로고
    • Partial purification of a membrane-associated deoxyribonucleic acid complex from Mycoplasma gallisepticum
    • Maniloff J. & D.C. Quinlan. Partial purification of a membrane-associated deoxyribonucleic acid complex from Mycoplasma gallisepticum. J Bacteriol 120, 495-501 (1974)
    • (1974) J Bacteriol , vol.120 , pp. 495-501
    • Maniloff, J.1    Quinlan, D.C.2
  • 62
    • 0002084168 scopus 로고    scopus 로고
    • Cytadherence and the Cytoskeleton
    • Eds: Razin S, Herrmann R, Kluwer Academic/Plenum Publishers, NY
    • M.F. Balish & D.C. Krause: Cytadherence and the Cytoskeleton. In: Molecular Biology and Pathogenicity of Mycoplasmas. Eds: Razin S, Herrmann R, Kluwer Academic/Plenum Publishers, NY, 491-518 (2002)
    • (2002) Molecular Biology and Pathogenicity of Mycoplasmas , pp. 491-518
    • Balish, M.F.1    Krause, D.C.2
  • 63
    • 0020953929 scopus 로고
    • Supramolecular structures in mycoplasmas
    • Gobel U. Supramolecular structures in mycoplasmas. Yale J Biol Med 56, 695-700 (1983)
    • (1983) Yale J Biol Med , vol.56 , pp. 695-700
    • Gobel, U.1
  • 64
    • 0036407027 scopus 로고    scopus 로고
    • Suspected utility of enzymes with multiple activities in the small genome Mycoplasma species: The replacement of the missing "household" nucleoside diphosphate kinase gene and activity by glycolytic kinases
    • Pollack J.D., M.A. Myers, T. Dandekar & R. Herrmann. Suspected utility of enzymes with multiple activities in the small genome Mycoplasma species: the replacement of the missing "household" nucleoside diphosphate kinase gene and activity by glycolytic kinases. OMICS 6, 247-258 (2002)
    • (2002) OMICS , vol.6 , pp. 247-258
    • Pollack, J.D.1    Myers, M.A.2    Dandekar, T.3    Herrmann, R.4
  • 66
    • 0017641557 scopus 로고
    • Mycoplasma alvi, a new species from bovine intestinal and urogenital tracts
    • Gourlay R.N., S.G. Wyld & R.H. Leach. Mycoplasma alvi, a new species from bovine intestinal and urogenital tracts. Int J Syst Bacteriol 27, 86-96 (1977)
    • (1977) Int J Syst Bacteriol , vol.27 , pp. 86-96
    • Gourlay, R.N.1    Wyld, S.G.2    Leach, R.H.3
  • 67
    • 0021816518 scopus 로고
    • Mycoplasma pirum sp. nov., a terminal structured mollicute from cell cultures
    • Del Giudice R.A., J.G. Tully, D.L. Rose & R.M. Cole. Mycoplasma pirum sp. nov., a terminal structured mollicute from cell cultures. Int J Syst Bacteriol 35, 285-291 (1985)
    • (1985) Int J Syst Bacteriol , vol.35 , pp. 285-291
    • Del Giudice, R.A.1    Tully, J.G.2    Rose, D.L.3    Cole, R.M.4
  • 69
    • 0015830978 scopus 로고
    • Electron microscopy of ultrathin sections of Mycoplasma gallisepticum (Strain TT) organisms grown on glass surface
    • Bruch J. & K.K. Sethi. Electron microscopy of ultrathin sections of Mycoplasma gallisepticum (Strain TT) organisms grown on glass surface. Path Microbiol 39, 373-382 (1973)
    • (1973) Path Microbiol , vol.39 , pp. 373-382
    • Bruch, J.1    Sethi, K.K.2
  • 70
    • 0022377805 scopus 로고
    • Mycoplasma testudinis, a new species isolated from a tortoise
    • Hill A.C. Mycoplasma testudinis, a new species isolated from a tortoise. Int J Syst Bacteriol 35, 489-492 (1985)
    • (1985) Int J Syst Bacteriol , vol.35 , pp. 489-492
    • Hill, A.C.1
  • 72
    • 0018897644 scopus 로고
    • Mycoplasma fastidiosum: A new species from horses
    • Lemcke R.M. & J. Poland. Mycoplasma fastidiosum: a new species from horses. Int J Syst Bacteriol 30, 151-162 (1980)
    • (1980) Int J Syst Bacteriol , vol.30 , pp. 151-162
    • Lemcke, R.M.1    Poland, J.2
  • 73
    • 0021708079 scopus 로고
    • Mycoplasma cavipharyngis, a new species isolated from the nasopharynx of guinea-pigs
    • Hill A.C. Mycoplasma cavipharyngis, a new species isolated from the nasopharynx of guinea-pigs. J Gen Microbiol 130, 3183-3188 (1984)
    • (1984) J Gen Microbiol , vol.130 , pp. 3183-3188
    • Hill, A.C.1
  • 74
    • 2142751166 scopus 로고    scopus 로고
    • Hemotrophic mycoplasmas (hemoplasmas): A review and new insights into pathogenic potential
    • Messick J.B. Hemotrophic mycoplasmas (hemoplasmas): a review and new insights into pathogenic potential. Vet Clin Pathol 33, 2-13 (2004)
    • (2004) Vet Clin Pathol , vol.33 , pp. 2-13
    • Messick, J.B.1
  • 75
    • 23644442099 scopus 로고    scopus 로고
    • Identification of a 123-kilodalton protein (Gli123) involved in machinery for gliding motility of Mycoplasma mobile
    • Uenoyama A. & M. Miyata. Identification of a 123-kilodalton protein (Gli123) involved in machinery for gliding motility of Mycoplasma mobile. J Bacteriol 187, 5578-5584 (2005)
    • (2005) J Bacteriol , vol.187 , pp. 5578-5584
    • Uenoyama, A.1    Miyata, M.2
  • 77
    • 0034041197 scopus 로고    scopus 로고
    • Gliding mutants of Mycoplasma mobile: Relationships between motility and cell morphology, cell adhesion and microcolony formation
    • Miyata M., H. Yamamoto, T. Shimizu, A. Uenoyama, C. Citti & R. Rosengarten. Gliding mutants of Mycoplasma mobile: relationships between motility and cell morphology, cell adhesion and microcolony formation. Microbiology 146, 1311-1320 (2000)
    • (2000) Microbiology , vol.146 , pp. 1311-1320
    • Miyata, M.1    Yamamoto, H.2    Shimizu, T.3    Uenoyama, A.4    Citti, C.5    Rosengarten, R.6
  • 79
    • 0017735264 scopus 로고
    • Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium
    • Hu P.C., A.M. Collier & J.M. Baseman. Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium. J Exp Med 145, 1328-1343 (1977)
    • (1977) J Exp Med , vol.145 , pp. 1328-1343
    • Hu, P.C.1    Collier, A.M.2    Baseman, J.M.3
  • 80
    • 0020466617 scopus 로고
    • Molecular basis for cytadsorption of Mycoplasma pneumoniae
    • Baseman J.B., R.M. Cole, D.C. Krause & D.K. Leith. Molecular basis for cytadsorption of Mycoplasma pneumoniae. J Bacteriol 151, 1514-1522 (1982)
    • (1982) J Bacteriol , vol.151 , pp. 1514-1522
    • Baseman, J.B.1    Cole, R.M.2    Krause, D.C.3    Leith, D.K.4
  • 81
    • 0020003676 scopus 로고
    • Identification of Mycoplasma pneumoniae proteins associated with hemadsorption and virulence
    • Krause D.C., D.K. Leith, R.M. Wilson & J.B. Baseman. Identification of Mycoplasma pneumoniae proteins associated with hemadsorption and virulence. Infect Immun 35, 809-817 (1982)
    • (1982) Infect Immun , vol.35 , pp. 809-817
    • Krause, D.C.1    Leith, D.K.2    Wilson, R.M.3    Baseman, J.B.4
  • 82
    • 0014333230 scopus 로고
    • Adsorption of Mycoplasma pneumoniae to neuraminic acid receptors of various cells and possible role in virulence
    • Sobeslavsky O., B. Prescott & R.M. Chanock. Adsorption of Mycoplasma pneumoniae to neuraminic acid receptors of various cells and possible role in virulence. J Bacteriol 96, 695-705 (1968)
    • (1968) J Bacteriol , vol.96 , pp. 695-705
    • Sobeslavsky, O.1    Prescott, B.2    Chanock, R.M.3
  • 84
    • 0019954368 scopus 로고
    • Mycoplasma pneumoniae adhesin localized to tip structure by monoclonal antibody
    • Feldner J., U. Gobel & W. Bredt. Mycoplasma pneumoniae adhesin localized to tip structure by monoclonal antibody. Nature 298, 765-767 (1982)
    • (1982) Nature , vol.298 , pp. 765-767
    • Feldner, J.1    Gobel, U.2    Bredt, W.3
  • 85
    • 0027203167 scopus 로고
    • Properties of adhering and nonadhering populations of Mycoplasma genitalium
    • Mernaugh G.R., S.F. Dallo, S.C. Holt & J.B. Baseman. Properties of adhering and nonadhering populations of Mycoplasma genitalium. Clin Infect Dis 17, S69-S78 (1993)
    • (1993) Clin Infect Dis , vol.17
    • Mernaugh, G.R.1    Dallo, S.F.2    Holt, S.C.3    Baseman, J.B.4
  • 86
    • 0036893426 scopus 로고    scopus 로고
    • GapA and CrmA coexpression is essential for Mycoplasma gallisepticum cytadherence and virulence
    • Papazisi L., S. Frasca, Jr., M. Gladd, X. Liao, D. Yogev & S.J. Geary. GapA and CrmA coexpression is essential for Mycoplasma gallisepticum cytadherence and virulence. Infect Immun 70, 6839-6845 (2002)
    • (2002) Infect Immun , vol.70 , pp. 6839-6845
    • Papazisi, L.1    Frasca Jr., S.2    Gladd, M.3    Liao, X.4    Yogev, D.5    Geary, S.J.6
  • 88
    • 0022385669 scopus 로고
    • Detection of the major adhesin P1 in triton shells of virulent Mycoplasma pneumoniae
    • Kahane I., S. Tucker, D.K. Leith, J. Morrison-Plummer & J.B. Baseman. Detection of the major adhesin P1 in triton shells of virulent Mycoplasma pneumoniae. Infect Immun 50, 944-946 (1985)
    • (1985) Infect Immun , vol.50 , pp. 944-946
    • Kahane, I.1    Tucker, S.2    Leith, D.K.3    Morrison-Plummer, J.4    Baseman, J.B.5
  • 89
    • 0037307792 scopus 로고    scopus 로고
    • Attachment organelle formation represented by localization of cytadherence proteins and formation of the electron-dense core in wild-type and mutant strains of Mycoplasma pneumoniae
    • Seto S. & M. Miyata. Attachment organelle formation represented by localization of cytadherence proteins and formation of the electron-dense core in wild-type and mutant strains of Mycoplasma pneumoniae. J Bacteriol 185, 1082-1091 (2003)
    • (2003) J Bacteriol , vol.185 , pp. 1082-1091
    • Seto, S.1    Miyata, M.2
  • 90
    • 0346887117 scopus 로고    scopus 로고
    • Deletion analysis identifies key functional domains of the cytadherence-associated protein HMW2 of Mycoplasma pneumoniae
    • Balish M.F., S.M. Ross, M. Fisseha & D.C. Krause. Deletion analysis identifies key functional domains of the cytadherence-associated protein HMW2 of Mycoplasma pneumoniae. Mol Microbiol 50, 1507-1516 (2003)
    • (2003) Mol Microbiol , vol.50 , pp. 1507-1516
    • Balish, M.F.1    Ross, S.M.2    Fisseha, M.3    Krause, D.C.4
  • 91
    • 0036146065 scopus 로고    scopus 로고
    • Stability of cytadherence-related proteins P140/P110 in Mycoplasma genitalium requires MG218 and unidentified factors
    • Dhandayuthapani S., W.G. Rasmussen & J.B. Baseman. Stability of cytadherence-related proteins P140/P110 in Mycoplasma genitalium requires MG218 and unidentified factors. Arch Med Res 33, 1-5 (2002)
    • (2002) Arch Med Res , vol.33 , pp. 1-5
    • Dhandayuthapani, S.1    Rasmussen, W.G.2    Baseman, J.B.3
  • 92
    • 0026596904 scopus 로고
    • Mycoplasma adhesion
    • Razin S. & E. Jacobs. Mycoplasma adhesion. J Gen Microbiol 138, 407-422 (1992)
    • (1992) J Gen Microbiol , vol.138 , pp. 407-422
    • Razin, S.1    Jacobs, E.2
  • 93
    • 0024246572 scopus 로고
    • Analysis of the nucleotide sequence of the P1 operon of Mycoplasma pneumoniae
    • Inamine J.M., S. Loechel & P.C. Hu. Analysis of the nucleotide sequence of the P1 operon of Mycoplasma pneumoniae. Gene 73, 175-183 (1989)
    • (1989) Gene , vol.73 , pp. 175-183
    • Inamine, J.M.1    Loechel, S.2    Hu, P.C.3
  • 94
    • 0027957270 scopus 로고
    • Spatial arrangement of gene products of the P1 operon in the membrane of Mycoplasma pneumoniae
    • Layh-Schmitt G. & R. Herrmann. Spatial arrangement of gene products of the P1 operon in the membrane of Mycoplasma pneumoniae. Infect Immun 62, 974-979 (1994)
    • (1994) Infect Immun , vol.62 , pp. 974-979
    • Layh-Schmitt, G.1    Herrmann, R.2
  • 95
    • 0022447814 scopus 로고
    • Biological effects of anti-lipid and anti-protein monoclonal antibodies on Mycoplasma pneumoniae
    • Morrison-Plummer J., D.K. Leith & J.B. Baseman. Biological effects of anti-lipid and anti-protein monoclonal antibodies on Mycoplasma pneumoniae. Infect Immun 53, 398-403 (1986)
    • (1986) Infect Immun , vol.53 , pp. 398-403
    • Morrison-Plummer, J.1    Leith, D.K.2    Baseman, J.B.3
  • 97
    • 0033057626 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development
    • Romero-Arroyo C.E., J. Jordan, S.J. Peacock, M.J. Willby, M.A. Farmer & D.C. Krause. Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development. J Bacteriol 181, 1079-1087 (1999)
    • (1999) J Bacteriol , vol.181 , pp. 1079-1087
    • Romero-Arroyo, C.E.1    Jordan, J.2    Peacock, S.J.3    Willby, M.J.4    Farmer, M.A.5    Krause, D.C.6
  • 99
    • 0028786874 scopus 로고
    • Molecular cloning and characterization of an adherence-related operon of Mycoplasma genitalium
    • Reddy S.P., W.G. Rasmussen & J.B. Baseman. Molecular cloning and characterization of an adherence-related operon of Mycoplasma genitalium. J Bacteriol 177, 5943-5951 (1995)
    • (1995) J Bacteriol , vol.177 , pp. 5943-5951
    • Reddy, S.P.1    Rasmussen, W.G.2    Baseman, J.B.3
  • 100
    • 0031841218 scopus 로고    scopus 로고
    • Characterization of MGC2, a Mycoplasma gallisepticum cytadhesin with homology to the Mycoplasma pneumoniae 30-kilodalton protein P30 and Mycoplasma genitalium P32
    • Hnatow L.L., Keeler C.L. III, L.L. Tessmer, K. Czymmek & J.E. Dohms. Characterization of MGC2, a Mycoplasma gallisepticum cytadhesin with homology to the Mycoplasma pneumoniae 30-kilodalton protein P30 and Mycoplasma genitalium P32. Infect Immun 66, 3436-3442 (1998)
    • (1998) Infect Immun , vol.66 , pp. 3436-3442
    • Hnatow, L.L.1    Keeler III, C.L.2    Tessmer, L.L.3    Czymmek, K.4    Dohms, J.E.5
  • 101
    • 0033918467 scopus 로고    scopus 로고
    • Molecular characterization of the Mycoplasma gallisepticum pvpA gene which encodes a putative variable cytadhesin protein
    • Boguslavsky S., D. Menaker, I. Lysnyansky, T. Liu, S. Levisohn, R. Rosengarten, M. Garcia & D. Yogev. Molecular characterization of the Mycoplasma gallisepticum pvpA gene which encodes a putative variable cytadhesin protein. Infect Immun 68, 3958-3964 (2000)
    • (2000) Infect Immun , vol.68 , pp. 3958-3964
    • Boguslavsky, S.1    Menaker, D.2    Lysnyansky, I.3    Liu, T.4    Levisohn, S.5    Rosengarten, R.6    Garcia, M.7    Yogev, D.8
  • 102
    • 0344731371 scopus 로고    scopus 로고
    • Identification and complementation of frameshift mutations associated with loss of cytadherence in Mycoplasma pneumoniae
    • Fisseha M., H.W.H. Gohlmann, R. Herrmann & D.C. Krause. Identification and complementation of frameshift mutations associated with loss of cytadherence in Mycoplasma pneumoniae. J Bacteriol 181, 4404-4410 (1999)
    • (1999) J Bacteriol , vol.181 , pp. 4404-4410
    • Fisseha, M.1    Gohlmann, H.W.H.2    Herrmann, R.3    Krause, D.C.4
  • 103
    • 0030899710 scopus 로고    scopus 로고
    • Transposon mutagenesis reinforces the correlation between Mycoplasma pneumoniae cytoskeletal protein HMW2 and cytadherence
    • Krause D.C., T. Proft, C.T. Hedreyda, H. Hubert, H. Plagens & R. Herrmann. Transposon mutagenesis reinforces the correlation between Mycoplasma pneumoniae cytoskeletal protein HMW2 and cytadherence. J Bacteriol 179, 2668-2677 (1997)
    • (1997) J Bacteriol , vol.179 , pp. 2668-2677
    • Krause, D.C.1    Proft, T.2    Hedreyda, C.T.3    Hubert, H.4    Plagens, H.5    Herrmann, R.6
  • 104
    • 0028263463 scopus 로고
    • Identification and characterization of hitherto unknown Mycoplasma pneumoniae proteins
    • Proft T. & R. Herrmann. Identification and characterization of hitherto unknown Mycoplasma pneumoniae proteins. Mol Microbiol 13, 337-348 (1994)
    • (1994) Mol Microbiol , vol.13 , pp. 337-348
    • Proft, T.1    Herrmann, R.2
  • 105
    • 0031443659 scopus 로고    scopus 로고
    • Loss of HMW1 and HMW3 in noncytadhering mutants of Mycoplasma pneumoniae occurs post-translationally
    • Popham P.L., T.-W. Hahn, K.A. Krebes & D.C. Krause. Loss of HMW1 and HMW3 in noncytadhering mutants of Mycoplasma pneumoniae occurs post-translationally. Proc Natl Acad Sci USA 94, 13979-13984 (1997)
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 13979-13984
    • Popham, P.L.1    Hahn, T.-W.2    Krebes, K.A.3    Krause, D.C.4
  • 106
    • 0035212227 scopus 로고    scopus 로고
    • Stability and subcellular localization of cytadherence-associated protein P65 in Mycoplasma pneumoniae
    • Jordan J.L., K.M. Berry, M.F. Balish & D.C. Krause. Stability and subcellular localization of cytadherence-associated protein P65 in Mycoplasma pneumoniae. J Bacteriol 183, 7387-7391 (2001)
    • (2001) J Bacteriol , vol.183 , pp. 7387-7391
    • Jordan, J.L.1    Berry, K.M.2    Balish, M.F.3    Krause, D.C.4
  • 107
    • 0026064484 scopus 로고
    • Localization of the Mycoplasma pneumoniae cytadherence-accessory proteins HMW1 and HMW4 in the cytoskeletonlike triton shell
    • Stevens M.K. & D.C. Krause. Localization of the Mycoplasma pneumoniae cytadherence-accessory proteins HMW1 and HMW4 in the cytoskeletonlike triton shell. J Bacteriol 173, 1041-1050 (1991)
    • (1991) J Bacteriol , vol.173 , pp. 1041-1050
    • Stevens, M.K.1    Krause, D.C.2
  • 108
    • 0034986997 scopus 로고    scopus 로고
    • Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell
    • Balish M.F., T.-W. Hahn, P.L. Popham & D.C. Krause. Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell. J Bacteriol 183, 3680-3688 (2001)
    • (2001) J Bacteriol , vol.183 , pp. 3680-3688
    • Balish, M.F.1    Hahn, T.-W.2    Popham, P.L.3    Krause, D.C.4
  • 109
    • 10044248456 scopus 로고    scopus 로고
    • HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae
    • Willby M.J., M.F. Balish, S.M. Ross, K.K. Lee, J.L. Jordan & D.C. Krause. HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae. J Bacteriol 186, 8221-8228 (2004)
    • (2004) J Bacteriol , vol.186 , pp. 8221-8228
    • Willby, M.J.1    Balish, M.F.2    Ross, S.M.3    Lee, K.K.4    Jordan, J.L.5    Krause, D.C.6
  • 110
    • 0031934211 scopus 로고    scopus 로고
    • HMW1 is required for cytadhesin P1 trafficking to the attachment organelle in Mycoplasma pneumoniae
    • Hahn T.-W., M.J. Willby & D.C. Krause. HMW1 is required for cytadhesin P1 trafficking to the attachment organelle in Mycoplasma pneumoniae. J Bacteriol 180, 1270-1276 (1998)
    • (1998) J Bacteriol , vol.180 , pp. 1270-1276
    • Hahn, T.-W.1    Willby, M.J.2    Krause, D.C.3
  • 111
    • 4944232464 scopus 로고    scopus 로고
    • Use of fluorescent-protein tagging to determine the subcellular localization of Mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus
    • Kenri T., S. Seto, A. Horino, Y. Sasaki, T. Sasaki & M. Miyata. Use of fluorescent-protein tagging to determine the subcellular localization of Mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus. J Bacteriol 186, 6944-6955 (2004)
    • (2004) J Bacteriol , vol.186 , pp. 6944-6955
    • Kenri, T.1    Seto, S.2    Horino, A.3    Sasaki, Y.4    Sasaki, T.5    Miyata, M.6
  • 112
    • 0029025535 scopus 로고
    • The proline-rich P65 protein of Mycoplasma pneumoniae is a component of the Triton X-100-insoluble fraction and exhibits size polymorphism in the strains M129 and FH
    • Proft T., H. Hilbert, G. Layh-Schmitt & R. Herrmann. The proline-rich P65 protein of Mycoplasma pneumoniae is a component of the Triton X-100-insoluble fraction and exhibits size polymorphism in the strains M129 and FH. J Bacteriol 177, 3370-3378 (1995)
    • (1995) J Bacteriol , vol.177 , pp. 3370-3378
    • Proft, T.1    Hilbert, H.2    Layh-Schmitt, G.3    Herrmann, R.4
  • 114
    • 0015119585 scopus 로고
    • The effect of hypotonic solutions on the morphology of cells of Mycoplasma gallisepticum
    • Bernstein-Ziv R. The effect of hypotonic solutions on the morphology of cells of Mycoplasma gallisepticum. Can J Microbiol 17, 1203-1205 (1971)
    • (1971) Can J Microbiol , vol.17 , pp. 1203-1205
    • Bernstein-Ziv, R.1
  • 115
    • 0014975206 scopus 로고
    • Analysis of the helical ribosome structures of Mycoplasma gallisepticum
    • Maniloff J. Analysis of the helical ribosome structures of Mycoplasma gallisepticum. Proc Natl Acad Sci USA 68, 43-47 (1971)
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 43-47
    • Maniloff, J.1
  • 117
    • 0016730780 scopus 로고
    • Striated fibers of the rho form of Mycoplasma: In vitro reassembly, composition, and structure
    • Rodwell A.W., J.E. Peterson & E.S. Rodwell. Striated fibers of the rho form of Mycoplasma: in vitro reassembly, composition, and structure. J Bacteriol 122, 1216-1229 (1975)
    • (1975) J Bacteriol , vol.122 , pp. 1216-1229
    • Rodwell, A.W.1    Peterson, J.E.2    Rodwell, E.S.3
  • 118
    • 0141701190 scopus 로고    scopus 로고
    • Spiroplasma citri, a plant pathogenic mollicute: Relationships with its two hosts, the plant and the leafhopper vector
    • Bove J.M., J. Renaudin, C. Saillard, X. Foissac & M. Garnier. Spiroplasma citri, a plant pathogenic mollicute: relationships with its two hosts, the plant and the leafhopper vector. Annu Rev Phytopathol 41, 483-500 (2003)
    • (2003) Annu Rev Phytopathol , vol.41 , pp. 483-500
    • Bove, J.M.1    Renaudin, J.2    Saillard, C.3    Foissac, X.4    Garnier, M.5
  • 119
    • 12344274281 scopus 로고    scopus 로고
    • Cryo-electron tomography reveals the cytoskeletal structure of Spiroplasma melliferum
    • Kurner J., A.S. Frangakis & W. Baumeister. Cryo-electron tomography reveals the cytoskeletal structure of Spiroplasma melliferum. Science 307, 436-438 (2005)
    • (2005) Science , vol.307 , pp. 436-438
    • Kurner, J.1    Frangakis, A.S.2    Baumeister, W.3
  • 120
    • 0035724921 scopus 로고    scopus 로고
    • A bacterial linear motor: Cellular and molecular organization of the contractile cytoskeleton of the helical bacterium Spiroplasma melliferum BC3
    • Trachtenberg S. & R. Gilad. A bacterial linear motor: cellular and molecular organization of the contractile cytoskeleton of the helical bacterium Spiroplasma melliferum BC3. Mol Microbiol 41, 827-848 (2001)
    • (2001) Mol Microbiol , vol.41 , pp. 827-848
    • Trachtenberg, S.1    Gilad, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.