메뉴 건너뛰기




Volumn 11, Issue 12, 2015, Pages

Systematic Structural Analyses of Attachment Organelle in Mycoplasma pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; YELLOW FLUORESCENT PROTEIN; BACTERIAL PROTEIN;

EID: 84953264252     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005299     Document Type: Article
Times cited : (42)

References (57)
  • 1
    • 0031770391 scopus 로고    scopus 로고
    • Molecular biology and pathogenicity of mycoplasmas
    • Razin S, Yogev D, Naot Y, Molecular biology and pathogenicity of mycoplasmas. Microbiol Mol Biol Rev. 1998;62(4):1094–156. 9841667.
    • (1998) Microbiol Mol Biol Rev , vol.62 , Issue.4 , pp. 1094-1156
    • Razin, S.1    Yogev, D.2    Naot, Y.3
  • 2
    • 84858796185 scopus 로고    scopus 로고
    • Rising rates of macrolide-resistant Mycoplasma pneumoniae in the central United States
    • Yamada M, Buller R, Bledsoe S, Storch GA, Rising rates of macrolide-resistant Mycoplasma pneumoniae in the central United States. Pediatr Infect Dis J. 2012;31(4):409–0. 22209916. doi: 10.1097/INF.0b013e318247f3e0
    • (2012) Pediatr Infect Dis J , vol.31 , Issue.4 , pp. 400-409
    • Yamada, M.1    Buller, R.2    Bledsoe, S.3    Storch, G.A.4
  • 3
    • 79955606245 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae: susceptibility and resistance to antibiotics
    • Bebear C, Pereyre S, Peuchant O, Mycoplasma pneumoniae: susceptibility and resistance to antibiotics. Future Microbiol. 2011;6(4):423–31. 21526943. doi: 10.2217/fmb.11.18
    • (2011) Future Microbiol , vol.6 , Issue.4 , pp. 423-431
    • Bebear, C.1    Pereyre, S.2    Peuchant, O.3
  • 4
    • 0034859086 scopus 로고    scopus 로고
    • Characteristics of macrolide-resistant Mycoplasma pneumoniae strains isolated from patients and induced with erythromycin in vitro
    • Okazaki N, Narita M, Yamada S, Izumikawa K, Umetsu M, Kenri T, et al. Characteristics of macrolide-resistant Mycoplasma pneumoniae strains isolated from patients and induced with erythromycin in vitro. Microbiol Immunol. 2001;45(8):617–20. 11592636.
    • (2001) Microbiol Immunol , vol.45 , Issue.8 , pp. 617-620
    • Okazaki, N.1    Narita, M.2    Yamada, S.3    Izumikawa, K.4    Umetsu, M.5    Kenri, T.6
  • 6
    • 65549131482 scopus 로고    scopus 로고
    • Cytoskeletal asymmetrical-dumbbell structure of a gliding mycoplasma, Mycoplasma gallisepticum, revealed by negative-staining electron microscopy
    • Nakane D, Miyata M, Cytoskeletal asymmetrical-dumbbell structure of a gliding mycoplasma, Mycoplasma gallisepticum, revealed by negative-staining electron microscopy. J Bacteriol. 2009;191(10):3256–64. 19286806. doi: 10.1128/JB.01823-08
    • (2009) J Bacteriol , vol.191 , Issue.10 , pp. 3256-3264
    • Nakane, D.1    Miyata, M.2
  • 7
    • 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, Seto S, Horino A, Sasaki Y, Sasaki T, Miyata M, Use of fluorescent-protein tagging to determine the subcellular localization of Mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus. J Bacteriol. 2004;186(20):6944–55. 15466048.
    • (2004) J Bacteriol , vol.186 , Issue.20 , pp. 6944-6955
    • Kenri, T.1    Seto, S.2    Horino, A.3    Sasaki, Y.4    Sasaki, T.5    Miyata, M.6
  • 8
    • 0017339823 scopus 로고
    • Motility of Mycoplasma pneumoniae
    • Radestock U, Bredt W, Motility of Mycoplasma pneumoniae. J Bacteriol. 1977;129(3):1495–501. 14925.
    • (1977) J Bacteriol , vol.129 , Issue.3 , pp. 1495-1501
    • Radestock, U.1    Bredt, W.2
  • 9
    • 84892963618 scopus 로고    scopus 로고
    • In vitro spatial and temporal analysis of Mycoplasma pneumoniae colonization of human airway epithelium
    • Prince OA, Krunkosky TM, Krause DC, In vitro spatial and temporal analysis of Mycoplasma pneumoniae colonization of human airway epithelium. Infect Immun. 2014;82(2):579–86. 24478073. doi: 10.1128/IAI.01036-13
    • (2014) Infect Immun , vol.82 , Issue.2 , pp. 579-586
    • Prince, O.A.1    Krunkosky, T.M.2    Krause, D.C.3
  • 10
    • 77957945597 scopus 로고    scopus 로고
    • Unique centipede mechanism of Mycoplasma gliding
    • Miyata M, Unique centipede mechanism of Mycoplasma gliding. Annu Rev Microbiol. 2010;64:519–37. 20533876. doi: 10.1146/annurev.micro.112408.134116
    • (2010) Annu Rev Microbiol , vol.64 , pp. 519-537
    • Miyata, M.1
  • 11
    • 37749037745 scopus 로고    scopus 로고
    • Centipede and inchworm models to explain Mycoplasma gliding
    • Miyata M, Centipede and inchworm models to explain Mycoplasma gliding. Trends Microbiol. 2008;16(1):6–12. 18083032.
    • (2008) Trends Microbiol , vol.16 , Issue.1 , pp. 6-12
    • Miyata, M.1
  • 12
    • 1442300837 scopus 로고    scopus 로고
    • Cellular engineering in a minimal microbe: structure and assembly of the terminal organelle of Mycoplasma pneumoniae
    • Krause DC, Balish MF, Cellular engineering in a minimal microbe: structure and assembly of the terminal organelle of Mycoplasma pneumoniae. Mol Microbiol. 2004;51:917–24. 14763969.
    • (2004) Mol Microbiol , vol.51 , pp. 917-924
    • Krause, D.C.1    Balish, M.F.2
  • 13
    • 0034284160 scopus 로고    scopus 로고
    • Re-annotating the Mycoplasma pneumoniae genome sequence: adding value, function and reading frames
    • Dandekar T, Huynen M, Regula JT, Ueberle B, Zimmermann CU, Andrade MA, et al. Re-annotating the Mycoplasma pneumoniae genome sequence: adding value, function and reading frames. Nucleic Acids Res. 2000;28(17):3278–88. 10954595.
    • (2000) Nucleic Acids Res , vol.28 , Issue.17 , pp. 3278-3288
    • Dandekar, T.1    Huynen, M.2    Regula, J.T.3    Ueberle, B.4    Zimmermann, C.U.5    Andrade, M.A.6
  • 14
    • 0029937832 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae cytadherence: unravelling the tie that binds
    • Krause DC, Mycoplasma pneumoniae cytadherence: unravelling the tie that binds. Mol Microbiol. 1996;20:247–53. 8733224.
    • (1996) Mol Microbiol , vol.20 , pp. 247-253
    • Krause, D.C.1
  • 15
    • 33750512775 scopus 로고    scopus 로고
    • Structural analysis of Mycoplasma pneumoniae by cryo-electron tomography
    • Seybert A, Herrmann R, Frangakis AS, Structural analysis of Mycoplasma pneumoniae by cryo-electron tomography. J Struct Biol. 2006;156(2):342–54. 16875842.
    • (2006) J Struct Biol , vol.156 , Issue.2 , pp. 342-354
    • Seybert, A.1    Herrmann, R.2    Frangakis, A.S.3
  • 16
    • 33645306591 scopus 로고    scopus 로고
    • Three-dimensional structure of Mycoplasma pneumoniae's attachment organelle and a model for its role in gliding motility
    • Henderson GP, Jensen GJ, Three-dimensional structure of Mycoplasma pneumoniae's attachment organelle and a model for its role in gliding motility. Mol Microbiol. 2006;60(2):376–85. 16573687.
    • (2006) Mol Microbiol , vol.60 , Issue.2 , pp. 376-385
    • Henderson, G.P.1    Jensen, G.J.2
  • 17
    • 84873037126 scopus 로고    scopus 로고
    • Role of binding in Mycoplasma mobile and Mycoplasma pneumoniae gliding analyzed through inhibition by synthesized sialylated compounds
    • Kasai T, Nakane D, Ishida H, Ando H, Kiso M, Miyata M, Role of binding in Mycoplasma mobile and Mycoplasma pneumoniae gliding analyzed through inhibition by synthesized sialylated compounds. J Bacteriol. 2012;195(3):429–35. 23123913. doi: 10.1128/JB.01141-12
    • (2012) J Bacteriol , vol.195 , Issue.3 , pp. 429-435
    • Kasai, T.1    Nakane, D.2    Ishida, H.3    Ando, H.4    Kiso, M.5    Miyata, M.6
  • 18
    • 78751536185 scopus 로고    scopus 로고
    • Isolation and characterization of P1 adhesin, a leg protein of the gliding bacterium Mycoplasma pneumoniae
    • Nakane D, Adan-Kubo J, Kenri T, Miyata M, Isolation and characterization of P1 adhesin, a leg protein of the gliding bacterium Mycoplasma pneumoniae. J Bacteriol. 2011;193:715–22. 21097617. doi: 10.1128/JB.00796-10
    • (2011) J Bacteriol , vol.193 , pp. 715-722
    • Nakane, D.1    Adan-Kubo, J.2    Kenri, T.3    Miyata, M.4
  • 19
    • 14244258697 scopus 로고    scopus 로고
    • Involvement of P1 adhesin in gliding motility of Mycoplasma pneumoniae as revealed by the inhibitory effects of antibody under optimized gliding conditions
    • Seto S, Kenri T, Tomiyama T, Miyata M, Involvement of P1 adhesin in gliding motility of Mycoplasma pneumoniae as revealed by the inhibitory effects of antibody under optimized gliding conditions. J Bacteriol. 2005;187(5):1875–7.
    • (2005) J Bacteriol , vol.187 , Issue.5 , pp. 1875-1877
    • Seto, S.1    Kenri, T.2    Tomiyama, T.3    Miyata, M.4
  • 20
    • 0019816823 scopus 로고
    • Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents
    • Gobel U, Speth V, Bredt W, Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents. J Cell Biol. 1981;91:537–43. 6796593.
    • (1981) J Cell Biol , vol.91 , pp. 537-543
    • Gobel, U.1    Speth, V.2    Bredt, W.3
  • 21
    • 0019205331 scopus 로고
    • Intracellular structures of Mycoplasma pneumoniae revealed after membrane removal
    • Meng KE, Pfister RM, Intracellular structures of Mycoplasma pneumoniae revealed after membrane removal. J Bacteriol. 1980;144:390–9. 6774963.
    • (1980) J Bacteriol , vol.144 , pp. 390-399
    • Meng, K.E.1    Pfister, R.M.2
  • 22
    • 0036809920 scopus 로고    scopus 로고
    • Cytoskeletal elements in the bacterium Mycoplasma pneumoniae
    • Hegermann J, Herrmann R, Mayer F, Cytoskeletal elements in the bacterium Mycoplasma pneumoniae. Naturwissenschaften. 2002;89(10):453–8. 12384719.
    • (2002) Naturwissenschaften , vol.89 , Issue.10 , pp. 453-458
    • Hegermann, J.1    Herrmann, R.2    Mayer, F.3
  • 23
    • 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 JT, Boguth G, Gorg A, Hegermann J, Mayer F, Frank R, et al. 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. 2001;147(Pt 4):1045–57. 11283300.
    • (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
  • 24
    • 84907831143 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae, an underutilized model for bacterial cell biology
    • Balish MF, Mycoplasma pneumoniae, an underutilized model for bacterial cell biology. J Bacteriol. 2014;196(21):3675–82. 25157081. doi: 10.1128/JB.01865-14
    • (2014) J Bacteriol , vol.196 , Issue.21 , pp. 3675-3682
    • Balish, M.F.1
  • 25
    • 0016531385 scopus 로고
    • Quantitation of submicrogram amounts of protein using coomassie brilliant blue R on sodium dodecyl sulfate-polyacrylamide slab-gels
    • Kahn R, Rubin RW, Quantitation of submicrogram amounts of protein using coomassie brilliant blue R on sodium dodecyl sulfate-polyacrylamide slab-gels. Anal Biochem. 1975;67(1):347–52. 50023.
    • (1975) Anal Biochem , vol.67 , Issue.1 , pp. 347-352
    • Kahn, R.1    Rubin, R.W.2
  • 27
    • 70849132924 scopus 로고    scopus 로고
    • Proteome organization in a genome-reduced bacterium
    • Kuhner S, van Noort V, Betts MJ, Leo-Macias A, Batisse C, Rode M, et al. Proteome organization in a genome-reduced bacterium. Science. 2009;326(5957):1235–40. 19965468. doi: 10.1126/science.1176343
    • (2009) Science , vol.326 , Issue.5957 , pp. 1235-1240
    • Kuhner, S.1    van Noort, V.2    Betts, M.J.3    Leo-Macias, A.4    Batisse, C.5    Rode, M.6
  • 28
    • 84898913940 scopus 로고    scopus 로고
    • Localization of P42 and F1-ATPase alpha-subunit homolog of the gliding machinery in Mycoplasma mobile revealed by newly developed gene manipulation and fluorescent protein tagging
    • Tulum I, Yabe M, Uenoyama A, Miyata M, Localization of P42 and F1-ATPase alpha-subunit homolog of the gliding machinery in Mycoplasma mobile revealed by newly developed gene manipulation and fluorescent protein tagging. J Bacteriol. 2014;196(10):1815–24. 24509320. doi: 10.1128/JB.01418-13
    • (2014) J Bacteriol , vol.196 , Issue.10 , pp. 1815-1824
    • Tulum, I.1    Yabe, M.2    Uenoyama, A.3    Miyata, M.4
  • 29
    • 0027878081 scopus 로고
    • Construction of Tn4001lac derivatives to be used as promoter probe vectors in mycoplasmas
    • Knudtson KL, Minion FC, Construction of Tn4001lac derivatives to be used as promoter probe vectors in mycoplasmas. Gene. 1993;137(2):217–22. 8299950.
    • (1993) Gene , vol.137 , Issue.2 , pp. 217-222
    • Knudtson, K.L.1    Minion, F.C.2
  • 30
    • 33750815099 scopus 로고    scopus 로고
    • Terminal organelle development in the cell wall-less bacterium Mycoplasma pneumoniae
    • Hasselbring BM, Jordan JL, Krause RW, Krause DC, Terminal organelle development in the cell wall-less bacterium Mycoplasma pneumoniae. Proc Natl Acad Sci USA. 2006;103(44):16478–83. 17062751.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.44 , pp. 16478-16483
    • Hasselbring, B.M.1    Jordan, J.L.2    Krause, R.W.3    Krause, D.C.4
  • 31
    • 0037307792 scopus 로고    scopus 로고
    • Attachment organelle formation represented by localization of cytadherence protein and formation of electron-dense core in the wild-type and mutant strains of Mycoplasma pneumoniae
    • Seto S, Miyata M, Attachment organelle formation represented by localization of cytadherence protein and formation of electron-dense core in the wild-type and mutant strains of Mycoplasma pneumoniae. J Bacteriol. 2003;185:1082–91. 12533484.
    • (2003) J Bacteriol , vol.185 , pp. 1082-1091
    • Seto, S.1    Miyata, M.2
  • 32
    • 0035113906 scopus 로고    scopus 로고
    • Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy
    • Seto S, Layh-Schmitt G, Kenri T, Miyata M, Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy. J Bacteriol. 2001;183:1621–30. 11160093.
    • (2001) J Bacteriol , vol.183 , pp. 1621-1630
    • Seto, S.1    Layh-Schmitt, G.2    Kenri, T.3    Miyata, M.4
  • 33
    • 84864020161 scopus 로고    scopus 로고
    • P65 truncation impacts P30 dynamics during Mycoplasma pneumoniae gliding
    • Hasselbring BM, Sheppard ES, Krause DC, P65 truncation impacts P30 dynamics during Mycoplasma pneumoniae gliding. J Bacteriol. 2012;194(11):3000–7. 22544269. doi: 10.1128/JB.00091-12
    • (2012) J Bacteriol , vol.194 , Issue.11 , pp. 3000-3007
    • Hasselbring, B.M.1    Sheppard, E.S.2    Krause, D.C.3
  • 35
    • 0026636512 scopus 로고
    • Localization and biochemical characterization of the ORF6 gene product of the Mycoplasma pneumoniae P1 operon
    • Layh-Schmitt G, Herrmann R, Localization and biochemical characterization of the ORF6 gene product of the Mycoplasma pneumoniae P1 operon. Infect Immun. 1992;60(7):2906–13. 1612757.
    • (1992) Infect Immun , vol.60 , Issue.7 , pp. 2906-2913
    • Layh-Schmitt, G.1    Herrmann, R.2
  • 36
    • 0033057626 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development
    • Romero-Arroyo CE, Jordan J, Peacock SJ, Willby MJ, Farmer MA, Krause DC, Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development. J Bacteriol. 1999;181(4):1079–87. 9973332.
    • (1999) J Bacteriol , vol.181 , Issue.4 , 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
  • 37
    • 0030899710 scopus 로고    scopus 로고
    • Transposon mutagenesis reinforces the correlation between Mycoplasma pneumoniae cytoskeletal protein HMW2 and cytadherence
    • Krause DC, Proft T, Hedreyda CT, Hilbert H, Plagens H, Herrmann R, Transposon mutagenesis reinforces the correlation between Mycoplasma pneumoniae cytoskeletal protein HMW2 and cytadherence. J Bacteriol. 1997;179(8):2668–77. 9098066.
    • (1997) J Bacteriol , vol.179 , Issue.8 , pp. 2668-2677
    • Krause, D.C.1    Proft, T.2    Hedreyda, C.T.3    Hilbert, H.4    Plagens, H.5    Herrmann, R.6
  • 38
    • 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 MF, Santurri RT, Ricci AM, Lee KK, Krause DC, Localization of Mycoplasma pneumoniae cytadherence-associated protein HMW2 by fusion with green fluorescent protein: implications for attachment organelle structure. Mol Microbiol. 2003;47:49–60. 12492853.
    • (2003) Mol Microbiol , vol.47 , pp. 49-60
    • Balish, M.F.1    Santurri, R.T.2    Ricci, A.M.3    Lee, K.K.4    Krause, D.C.5
  • 39
    • 70350462587 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae cytoskeletal protein HMW2 and the architecture of the terminal organelle
    • Bose SR, Balish MF, Krause DC, Mycoplasma pneumoniae cytoskeletal protein HMW2 and the architecture of the terminal organelle. J Bacteriol. 2009;191(21):6741–8. 19717588. doi: 10.1128/JB.01486-08
    • (2009) J Bacteriol , vol.191 , Issue.21 , pp. 6741-6748
    • Bose, S.R.1    Balish, M.F.2    Krause, D.C.3
  • 40
    • 57449119872 scopus 로고    scopus 로고
    • The gene mpn310 (hmw2) from Mycoplasma pneumoniae encodes two proteins, HMW2 and HMW2-s, which differ in size but use the same reading frame
    • Boonmee A, Ruppert T, Herrmann R, The gene mpn310 (hmw2) from Mycoplasma pneumoniae encodes two proteins, HMW2 and HMW2-s, which differ in size but use the same reading frame. FEMS Microbiol Lett. 2009;290(2):174–81. 19025563. doi: 10.1111/j.1574-6968.2008.01422.x
    • (2009) FEMS Microbiol Lett , vol.290 , Issue.2 , pp. 174-181
    • Boonmee, A.1    Ruppert, T.2    Herrmann, R.3
  • 41
    • 0344731371 scopus 로고    scopus 로고
    • Identification and complementation of frameshift mutations associated with loss of cytadherence in Mycoplasma pneumoniae
    • Fisseha M, Gohlmann HW, Herrmann R, Krause DC, Identification and complementation of frameshift mutations associated with loss of cytadherence in Mycoplasma pneumoniae. J Bacteriol. 1999;181(14):4404–10. 10400600.
    • (1999) J Bacteriol , vol.181 , Issue.14 , pp. 4404-4410
    • Fisseha, M.1    Gohlmann, H.W.2    Herrmann, R.3    Krause, D.C.4
  • 42
    • 10744222077 scopus 로고    scopus 로고
    • The complete genome sequence of the avian pathogen Mycoplasma gallisepticum strain R(low)
    • Papazisi L, Gorton TS, Kutish G, Markham PF, Browning GF, Nguyen DK, et al. The complete genome sequence of the avian pathogen Mycoplasma gallisepticum strain R(low). Microbiology. 2003;149(Pt 9):2307–16. 12949158.
    • (2003) Microbiology , vol.149 , pp. 2307-2316
    • Papazisi, L.1    Gorton, T.S.2    Kutish, G.3    Markham, P.F.4    Browning, G.F.5    Nguyen, D.K.6
  • 44
    • 33748989006 scopus 로고    scopus 로고
    • Transposon mutagenesis identifies genes associated with Mycoplasma pneumoniae gliding motility
    • Hasselbring BM, Page CA, Sheppard ES, Krause DC, Transposon mutagenesis identifies genes associated with Mycoplasma pneumoniae gliding motility. J Bacteriol. 2006;188(17):6335–45. 16923901.
    • (2006) J Bacteriol , vol.188 , Issue.17 , pp. 6335-6345
    • Hasselbring, B.M.1    Page, C.A.2    Sheppard, E.S.3    Krause, D.C.4
  • 45
    • 33845980239 scopus 로고    scopus 로고
    • Protein P200 is dispensable for Mycoplasma pneumoniae hemadsorption but not gliding motility or colonization of differentiated bronchial epithelium
    • Jordan JL, Chang HY, Balish MF, Holt LS, Bose SR, Hasselbring BM, et al. Protein P200 is dispensable for Mycoplasma pneumoniae hemadsorption but not gliding motility or colonization of differentiated bronchial epithelium. Infect Immun. 2007;75:518–22. 17043103.
    • (2007) Infect Immun , vol.75 , pp. 518-522
    • Jordan, J.L.1    Chang, H.Y.2    Balish, M.F.3    Holt, L.S.4    Bose, S.R.5    Hasselbring, B.M.6
  • 46
    • 0025793719 scopus 로고
    • The cps gene cluster of Salmonella strain LT2 includes a second mannose pathway: sequence of two genes and relationship to genes in the rfb gene cluster
    • Stevenson G, Lee SJ, Romana LK, Reeves PR, The cps gene cluster of Salmonella strain LT2 includes a second mannose pathway: sequence of two genes and relationship to genes in the rfb gene cluster. Mol Gen Genet. 1991;227(2):173–80. 1712067.
    • (1991) Mol Gen Genet , vol.227 , Issue.2 , pp. 173-180
    • Stevenson, G.1    Lee, S.J.2    Romana, L.K.3    Reeves, P.R.4
  • 47
    • 71749085978 scopus 로고    scopus 로고
    • The role of proteolysis in the Caulobacter crescentus cell cycle and development
    • Jenal U, The role of proteolysis in the Caulobacter crescentus cell cycle and development. Res Microbiol. 2009;160(9):687–95. 19781638. doi: 10.1016/j.resmic.2009.09.006
    • (2009) Res Microbiol , vol.160 , Issue.9 , pp. 687-695
    • Jenal, U.1
  • 48
    • 33748703166 scopus 로고    scopus 로고
    • Biological roles of the Lon ATP-dependent protease
    • Tsilibaris V, Maenhaut-Michel G, Van Melderen L, Biological roles of the Lon ATP-dependent protease. Res Microbiol. 2006;157(8):701–13. 16854568.
    • (2006) Res Microbiol , vol.157 , Issue.8 , pp. 701-713
    • Tsilibaris, V.1    Maenhaut-Michel, G.2    Van Melderen, L.3
  • 49
    • 0034986997 scopus 로고    scopus 로고
    • Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell
    • Balish MF, Hahn TW, Popham PL, Krause DC, Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell. J Bacteriol. 2001;183(12):3680–8. 11371532.
    • (2001) J Bacteriol , vol.183 , Issue.12 , pp. 3680-3688
    • Balish, M.F.1    Hahn, T.W.2    Popham, P.L.3    Krause, D.C.4
  • 50
    • 60649098854 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae J-domain protein required for terminal organelle function
    • Cloward JM, Krause DC, Mycoplasma pneumoniae J-domain protein required for terminal organelle function. Mol Microbiol. 2009;71(5):1296–307. 19183275. doi: 10.1111/j.1365-2958.2009.06602.x
    • (2009) Mol Microbiol , vol.71 , Issue.5 , pp. 1296-1307
    • Cloward, J.M.1    Krause, D.C.2
  • 51
    • 33845692808 scopus 로고    scopus 로고
    • Cytoskeletal protein P41 is required to anchor the terminal organelle of the wall-less prokaryote Mycoplasma pneumoniae
    • Hasselbring BM, Krause DC, Cytoskeletal protein P41 is required to anchor the terminal organelle of the wall-less prokaryote Mycoplasma pneumoniae. Mol Microbiol. 2007;63(1):44–53. 17163973.
    • (2007) Mol Microbiol , vol.63 , Issue.1 , pp. 44-53
    • Hasselbring, B.M.1    Krause, D.C.2
  • 52
    • 0020034447 scopus 로고
    • Mycoplasma pneumoniae infection: role of a surface protein in the attachment organelle
    • Hu PC, Cole RM, Huang YS, Graham JA, Gardner DE, Collier AM, et al. Mycoplasma pneumoniae infection: role of a surface protein in the attachment organelle. Science. 1982;216:313–5. 6801766.
    • (1982) Science , vol.216 , pp. 313-315
    • Hu, P.C.1    Cole, R.M.2    Huang, Y.S.3    Graham, J.A.4    Gardner, D.E.5    Collier, A.M.6
  • 53
    • 0019954368 scopus 로고
    • Mycoplasma pneumoniae adhesin localized to tip structure by monoclonal antibody
    • Feldner J, Gobel U, Bredt W, Mycoplasma pneumoniae adhesin localized to tip structure by monoclonal antibody. Nature. 1982;298:765–7. 7110314.
    • (1982) Nature , vol.298 , pp. 765-767
    • Feldner, J.1    Gobel, U.2    Bredt, W.3
  • 54
    • 0020466617 scopus 로고
    • Molecular basis for cytadsorption of Mycoplasma pneumoniae
    • Baseman JB, Cole RM, Krause DC, Leith DK, Molecular basis for cytadsorption of Mycoplasma pneumoniae. J Bacteriol. 1982;151:1514–22. 6809731.
    • (1982) J Bacteriol , vol.151 , pp. 1514-1522
    • Baseman, J.B.1    Cole, R.M.2    Krause, D.C.3    Leith, D.K.4
  • 55
    • 0014596997 scopus 로고
    • Characteristics of virulent, attenuated, and avirulent Mycoplasma pneumoniae strains
    • Lipman RP, Clyde WA, Jr.Denny FW, Characteristics of virulent, attenuated, and avirulent Mycoplasma pneumoniae strains. J Bacteriol. 1969;100(2):1037–43. 5359607.
    • (1969) J Bacteriol , vol.100 , Issue.2 , pp. 1037-1043
    • Lipman, R.P.1    Clyde, W.A.2    Denny, F.W.3
  • 56
    • 37648998892 scopus 로고    scopus 로고
    • Cytoskeletal “Jellyfish” structure of Mycoplasma mobile
    • Nakane D, Miyata M, Cytoskeletal “Jellyfish” structure of Mycoplasma mobile. Proc Natl Acad Sci USA. 2007;104:19518–23. 18042728.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19518-19523
    • Nakane, D.1    Miyata, M.2
  • 57
    • 84855904921 scopus 로고    scopus 로고
    • Mycoplasma mobile cells elongated by detergent and their pivoting movements in gliding
    • Nakane D, Miyata M, Mycoplasma mobile cells elongated by detergent and their pivoting movements in gliding. J Bacteriol. 2012;194(1):122–30. 22001513. doi: 10.1128/JB.05857-11
    • (2012) J Bacteriol , vol.194 , Issue.1 , pp. 122-130
    • Nakane, D.1    Miyata, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.