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Journal of Bacteriology
Volumn 196, Issue 21, 2014, Pages 3675-3682
Mycoplasma pneumoniae, an underutilized model for bacterial cell biology
Author keywords

[No Author keywords available]
Indexed keywords

ADHESIN; CYTOSKELETON PROTEIN; BACTERIAL PROTEIN;
EID: 84907831143     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01865-14     Document Type: Short Survey
Times cited : (40)
References (97)
  • 1
    • 0031770391 scopus 로고    scopus 로고
    • Molecular biology and pathogenicity of mycoplasmas
    • Razin S, Yogev D, Naot Y. 1998. Molecular biology and pathogenicity of mycoplasmas. Microbiol. Mol. Biol. Rev. 62:1094-1156.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1094-1156
    • Razin, S.1    Yogev, D.2    Naot, Y.3
  • 2
    • 84879824469 scopus 로고    scopus 로고
    • Genomes of the class Erysipelotrichia clarity the firmicute origin of the class Mollicutes
    • Davis JJ, Xia F, Overbeek RA, Olsen GH. 2013. Genomes of the class Erysipelotrichia clarity the firmicute origin of the class Mollicutes. Int. J. Syst. Evol. Microbiol. 63:2727-2741. http://dx.doi.org/10.1099/ijs.0.048983-0.
    • (2013) Int. J. Syst. Evol. Microbiol. , vol.63 , pp. 2727-2741
    • Davis, J.J.1    Xia, F.2    Overbeek, R.A.3    Olsen, G.H.4
  • 3
    • 35348825853 scopus 로고    scopus 로고
    • Mycoplasma genomics: tailoring the genome for minimal life requirements through reductive evolution
    • Fadiel A, Eichenbaum KD, El Semary N, Epperson B. 2007. Mycoplasma genomics: tailoring the genome for minimal life requirements through reductive evolution. Front. Biosci. 12:2020-2028. http://dx.doi.org/10.2741/2207.
    • (2007) Front. Biosci. , vol.12 , pp. 2020-2028
    • Fadiel, A.1    Eichenbaum, K.D.2    El Semary, N.3    Epperson, B.4
  • 5
    • 53749101273 scopus 로고    scopus 로고
    • Epidemiology, clinical manifestations, pathogenesis and laboratory detection of Mycoplasma pneumoniae infections
    • Atkinson TP, Balish MF, Waites KB. 2008. Epidemiology, clinical manifestations, pathogenesis and laboratory detection of Mycoplasma pneumoniae infections. FEMS Microbiol. Rev. 32:956-973. http://dx.doi.org/10.1111/j.1574-6976.2008.00129.x.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 956-973
    • Atkinson, T.P.1    Balish, M.F.2    Waites, K.B.3
  • 6
    • 33744739470 scopus 로고    scopus 로고
    • Subcellular structures of mycoplasmas
    • Balish MF. 2006. Subcellular structures of mycoplasmas. Front. Biosci. 11:2017-2027. http://dx.doi.org/10.2741/1943.
    • (2006) Front. Biosci. , vol.11 , pp. 2017-2027
    • Balish, M.F.1
  • 7
    • 84866748474 scopus 로고    scopus 로고
    • Mycoplasma genitalium, an emerging sexually transmitted pathogen
    • Cazanave C, Manhart LE, Bébéar C. 2012. Mycoplasma genitalium, an emerging sexually transmitted pathogen. Med. Mal. Infect. 42:381-392. http://dx.doi.org/10.1016/j.medmal.2012.05.006.
    • (2012) Med. Mal. Infect. , vol.42 , pp. 381-392
    • Cazanave, C.1    Manhart, L.E.2    Bébéar, C.3
  • 8
    • 10544255079 scopus 로고    scopus 로고
    • Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae
    • Himmelreich R, Hilbert H, Plagens H, Pirkl E, Li BC, Herrmann R. 1996. Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae. Nucleic Acids Res. 24:4420-4449. http://dx.doi.org/10.1093/nar/24.22.4420.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4420-4449
    • Himmelreich, R.1    Hilbert, H.2    Plagens, H.3    Pirkl, E.4    Li, B.C.5    Herrmann, R.6
  • 9
    • 30544445654 scopus 로고    scopus 로고
    • Spatial control of bacterial division-site placement
    • Rothfield L, Taghbalout A, Shih YL. 2005. Spatial control of bacterial division-site placement. Nat. Rev. Microbiol. 3:959-968. http://dx.doi.org/10.1038/nrmicro1290.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 959-968
    • Rothfield, L.1    Taghbalout, A.2    Shih, Y.L.3
  • 10
    • 84872272882 scopus 로고    scopus 로고
    • Polarity and cell fate asymmetry in Caulobacter crescentus
    • Tsokos CG, Laub MT. 2012. Polarity and cell fate asymmetry in Caulobacter crescentus. Curr. Opin. Microbiol. 15:744-750. http://dx.doi.org/10.1016/j.mib.2012.10.011.
    • (2012) Curr. Opin. Microbiol. , vol.15 , pp. 744-750
    • Tsokos, C.G.1    Laub, M.T.2
  • 12
    • 33644764886 scopus 로고    scopus 로고
    • Bacterial birth scar proteins mark future flagellum assembly site
    • Huitema E, Pritchard S, Matteson D, Radhakrishnan SK, Viollier PH. 2006. Bacterial birth scar proteins mark future flagellum assembly site. Cell 124:1025-1037. http://dx.doi.org/10.1016/j.cell.2006.01.019.
    • (2006) Cell , vol.124 , pp. 1025-1037
    • Huitema, E.1    Pritchard, S.2    Matteson, D.3    Radhakrishnan, S.K.4    Viollier, P.H.5
  • 13
    • 62149141206 scopus 로고    scopus 로고
    • Geometric cue for protein localization in a bacterium
    • Ramamurthi KS, Lecuyer S, Stone HA, Losick R. 2009. Geometric cue for protein localization in a bacterium. Science 323:1354-1357. http://dx.doi.org/10.1126/science.1169218.
    • (2009) Science , vol.323 , pp. 1354-1357
    • Ramamurthi, K.S.1    Lecuyer, S.2    Stone, H.A.3    Losick, R.4
  • 14
    • 0020466617 scopus 로고
    • Molecular basis for cytadsorption of Mycoplasma pneumoniae
    • Baseman JB, Cole RM, Krause DC, Leith DK. 1982. Molecular basis for cytadsorption of Mycoplasma pneumoniae. J. Bacteriol. 151:1514-1522.
    • (1982) J. Bacteriol. , vol.151 , pp. 1514-1522
    • Baseman, J.B.1    Cole, R.M.2    Krause, D.C.3    Leith, D.K.4
  • 15
    • 0020962645 scopus 로고
    • Location of an attachment moiety on Mycoplasma pneumoniae
    • Collier AM, Hu PC, Clyde WA, Jr. 1983. Location of an attachment moiety on Mycoplasma pneumoniae. Yale J. Biol. Med. 56:671-677.
    • (1983) Yale J. Biol. Med. , vol.56 , pp. 671-677
    • Collier, A.M.1    Hu, P.C.2    Clyde Jr., W.A.3
  • 17
    • 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, Miyata M. 2003. 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. http://dx.doi.org/10.1128/JB.185.3.1082-1091.2003.
    • (2003) J. Bacteriol. , vol.185 , pp. 1082-1091
    • Seto, S.1    Miyata, M.2
  • 18
    • 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. 2004. Cellular engineering in a minimal microbe: structure and assembly of the terminal organelle of Mycoplasma pneumoniae. Mol. Microbiol. 51:917-924. http://dx.doi.org/10.1046/j.1365-2958.2003.03899.x.
    • (2004) Mol. Microbiol. , vol.51 , pp. 917-924
    • Krause, D.C.1    Balish, M.F.2
  • 19
    • 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. 2006. Three-dimensional structure of Mycoplasma pneumoniae's attachment organelle and a model for its role in gliding motility. Mol. Microbiol. 60:376-385. http://dx.doi.org/10.1111/j.1365-2958.2006.05113.x.
    • (2006) Mol. Microbiol. , vol.60 , pp. 376-385
    • Henderson, G.P.1    Jensen, G.J.2
  • 20
    • 33750512775 scopus 로고    scopus 로고
    • Structural analysis of Mycoplasma pneumoniae by cryo-electron tomography
    • Seybert A, Herrmann R, Frangakis AS. 2006. Structural analysis of Mycoplasma pneumoniae by cryo-electron tomography. J. Struct. Biol. 156:342-354. http://dx.doi.org/10.1016/j.jsb.2006.04.010.
    • (2006) J. Struct. Biol. , vol.156 , pp. 342-354
    • Seybert, A.1    Herrmann, R.2    Frangakis, A.S.3
  • 21
    • 33748770937 scopus 로고    scopus 로고
    • Mycoplasmas: a distinct cytoskeleton for wall-less bacteria
    • Balish MF, Krause DC. 2006. Mycoplasmas: a distinct cytoskeleton for wall-less bacteria. J. Mol. Microbiol. Biotechnol. 11:244-255. http://dx.doi.org/10.1159/000094058.
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 244-255
    • Balish, M.F.1    Krause, D.C.2
  • 22
    • 77957945597 scopus 로고    scopus 로고
    • Unique centipede motion of mycoplasma gliding
    • Miyata M. 2010. Unique centipede motion of mycoplasma gliding. Annu. Rev. Microbiol. 64:519-537. http://dx.doi.org/10.1146/annurev.micro.112408.134116.
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 519-537
    • Miyata, M.1
  • 23
    • 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, Kusumoto A, Miyata M. 2004. Identification of a 349-kilodalton protein (Gli349) responsible for cytadherence and glass binding during gliding of Mycoplasma mobile. J. Bacteriol. 186:1537-1545. http://dx.doi.org/10.1128/JB.186.5.1537-1545.2004.
    • (2004) J. Bacteriol. , vol.186 , pp. 1537-1545
    • Uenoyama, A.1    Kusumoto, A.2    Miyata, M.3
  • 24
    • 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. 2007. Cytoskeletal protein P41 is required to anchor the terminal organelle of the wall-less prokaryote Mycoplasma pneumoniae. Mol. Microbiol. 63:44-53. http://dx.doi.org/10.1111/j.1365-2958.2006.05507.x.
    • (2007) Mol. Microbiol. , vol.63 , pp. 44-53
    • Hasselbring, B.M.1    Krause, D.C.2
  • 25
    • 0019205331 scopus 로고
    • Intracellular structures of Mycoplasma pneumoniae revealed after member removal
    • Meng KE, Pfister RM. 1980. Intracellular structures of Mycoplasma pneumoniae revealed after member removal. J. Bacteriol. 144:390-399.
    • (1980) J. Bacteriol. , vol.144 , pp. 390-399
    • Meng, K.E.1    Pfister, R.M.2
  • 26
    • 0019816823 scopus 로고
    • Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents
    • Göbel U, Speth V, Bredt W. 1981. Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents. J. Cell Biol. 91:537-543. http://dx.doi.org/10.1083/jcb.91.2.537.
    • (1981) J. Cell Biol. , vol.91 , pp. 537-543
    • Göbel, U.1    Speth, V.2    Bredt, W.3
  • 27
    • 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. 2001. Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy. J. Bacteriol. 183:1621-1630. http://dx.doi.org/10.1128/JB.183.5.1621-1630.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 1621-1630
    • Seto, S.1    Layh-Schmitt, G.2    Kenri, T.3    Miyata, M.4
  • 28
    • 38849184101 scopus 로고    scopus 로고
    • Attachment organelle ultrastructure correlates with phylogeny, not gliding motility properties, in Mycoplasma pneumoniae relatives
    • Hatchel JM, Balish MF. 2008. Attachment organelle ultrastructure correlates with phylogeny, not gliding motility properties, in Mycoplasma pneumoniae relatives. Microbiology 154:286-295. http://dx.doi.org/10.1099/mic.0.2007/012765-0.
    • (2008) Microbiology , vol.154 , pp. 286-295
    • Hatchel, J.M.1    Balish, M.F.2
  • 29
    • 55549107183 scopus 로고    scopus 로고
    • Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence
    • Pich OQ, Burgos R, Ferrer-Navarro M, Querol E, Piñol J. 2008. Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence. Microbiology 154:3188-3198. http://dx.doi.org/10.1099/mic.0.2008/020636-0.
    • (2008) Microbiology , vol.154 , pp. 3188-3198
    • Pich, O.Q.1    Burgos, R.2    Ferrer-Navarro, M.3    Querol, E.4    Piñol, J.5
  • 30
    • 65549131482 scopus 로고    scopus 로고
    • Cytoskeletal asymmetrical dumbbell structure of a gliding mycoplasma, Mycoplasma gallisepticum, revealed by neg-ative-staining electron microscopy
    • Nakane D, Miyata M. 2009. Cytoskeletal asymmetrical dumbbell structure of a gliding mycoplasma, Mycoplasma gallisepticum, revealed by neg-ative-staining electron microscopy. J. Bacteriol. 191:3256-3264. http://dx.doi.org/10.1128/JB.01823-08.
    • (2009) J. Bacteriol. , vol.191 , pp. 3256-3264
    • Nakane, D.1    Miyata, M.2
  • 31
    • 75049083437 scopus 로고    scopus 로고
    • Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus
    • Kühn J, Briegel A, Mörschel E, Kahnt J, Leser K, Wick S, Jensen GJ, Thanbichler M. 2010. Bactofilins, a ubiquitous class of cytoskeletal proteins mediating polar localization of a cell wall synthase in Caulobacter crescentus. EMBO J. 29:327-339. http://dx.doi.org/10.1038/emboj.2009.358.
    • (2010) EMBO J , vol.29 , pp. 327-339
    • Kühn, J.1    Briegel, A.2    Mörschel, E.3    Kahnt, J.4    Leser, K.5    Wick, S.6    Jensen, G.J.7    Thanbichler, M.8
  • 32
    • 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. 1997. Transposon mutagenesis reinforces the correlation between Mycoplasma pneumoniae cytoskeletal protein HMW2 and cytadherence. J. Bacteriol. 179:2668-2677.
    • (1997) J. Bacteriol. , vol.179 , pp. 2668-2677
    • Krause, D.C.1    Proft, T.2    Hedreyda, C.T.3    Hilbert, H.4    Plagens, H.5    Herrmann, R.6
  • 34
    • 79955717294 scopus 로고    scopus 로고
    • BacM, an N-terminally processed bactofilin of Myxococcus xanthus, is crucial for proper cell shape
    • Koch MK, McHugh CA, Hoiczyk E. 2011. BacM, an N-terminally processed bactofilin of Myxococcus xanthus, is crucial for proper cell shape. Mol. Microbiol. 80:1031-1051. http://dx.doi.org/10.1111/j.1365-2958.2011.07629.x.
    • (2011) Mol. Microbiol. , vol.80 , pp. 1031-1051
    • Koch, M.K.1    McHugh, C.A.2    Hoiczyk, E.3
  • 35
    • 0029025535 scopus 로고
    • The prolinerich 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, Hilbert H, Layh-Schmitt G, Herrmann R. 1995. The prolinerich 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) J. Bacteriol. , vol.177 , pp. 3370-3378
    • Proft, T.1    Hilbert, H.2    Layh-Schmitt, G.3    Herrmann, R.4
  • 36
    • 34948904290 scopus 로고    scopus 로고
    • Functional analysis of the Mycoplasma genitalium MG312 protein reveals a specific requirement of the MG312 N-terminal domain for gliding motility
    • Burgos R, Pich OQ, Querol E, Piñol J. 2007. Functional analysis of the Mycoplasma genitalium MG312 protein reveals a specific requirement of the MG312 N-terminal domain for gliding motility. J. Bacteriol. 189: 7014-7023. http://dx.doi.org/10.1128/JB.00975-07.
    • (2007) J. Bacteriol. , vol.189 , pp. 7014-7023
    • Burgos, R.1    Pich, O.Q.2    Querol, E.3    Piñol, J.4
  • 37
    • 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. 2001. Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell. J. Bacteriol. 183:3680-3688. http://dx.doi.org/10.1128/JB.183.12.3680-3688.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 3680-3688
    • Balish, M.F.1    Hahn, T.W.2    Popham, P.L.3    Krause, D.C.4
  • 38
    • 84867439435 scopus 로고    scopus 로고
    • The EAGR box structure: a motif involved in mycoplasma motility
    • Calisto BM, Broto A, Martinelli L, Querol E, Piñol J, Fita I. 2012. The EAGR box structure: a motif involved in mycoplasma motility. Mol. Microbiol. 86:382-393. http://dx.doi.org/10.1111/j.1365-2958.2012.08200.x.
    • (2012) Mol. Microbiol. , vol.86 , pp. 382-393
    • Calisto, B.M.1    Broto, A.2    Martinelli, L.3    Querol, E.4    Piñol, J.5    Fita, I.6
  • 39
    • 55549109423 scopus 로고    scopus 로고
    • Polar secretion of proteins via the Xcp type II secretion system in Pseudomonas aeruginosa
    • Senf F, Tommassen J, Koster M. 2008. Polar secretion of proteins via the Xcp type II secretion system in Pseudomonas aeruginosa. Microbiology 154:3025-3032. http://dx.doi.org/10.1099/mic.0.2008/018069-0.
    • (2008) Microbiology , vol.154 , pp. 3025-3032
    • Senf, F.1    Tommassen, J.2    Koster, M.3
  • 40
    • 84155164758 scopus 로고    scopus 로고
    • Surface contact stimulates the just-in-time deployment of bacterial adhesins
    • Li G, Brown PJ, Tang JX, Xu J, Quardokus EM, Fuqua C, Brun YV. 2012. Surface contact stimulates the just-in-time deployment of bacterial adhesins. Mol. Microbiol. 83:41-51. http://dx.doi.org/10.1111/j.1365-2958.2011.07909.x.
    • (2012) Mol. Microbiol. , vol.83 , pp. 41-51
    • Li, G.1    Brown, P.J.2    Tang, J.X.3    Xu, J.4    Quardokus, E.M.5    Fuqua, C.6    Brun, Y.V.7
  • 41
    • 84867899841 scopus 로고    scopus 로고
    • Structure and regulation of the type VI secretion system
    • Silverman JM, Brunet YR, Cascales E, Mougous JD. 2012. Structure and regulation of the type VI secretion system. Annu. Rev. Microbiol. 66:453-472. http://dx.doi.org/10.1146/annurev-micro-121809-151619.
    • (2012) Annu. Rev. Microbiol. , vol.66 , pp. 453-472
    • Silverman, J.M.1    Brunet, Y.R.2    Cascales, E.3    Mougous, J.D.4
  • 42
    • 84877817732 scopus 로고    scopus 로고
    • Spatial and numerical regulation of flagellar biosynthesis in polarly flagellated bacteria
    • Kazmierczak BI, Hendrixson DR. 2013. Spatial and numerical regulation of flagellar biosynthesis in polarly flagellated bacteria. Mol. Microbiol. 88:655-663. http://dx.doi.org/10.1111/mmi.12221.
    • (2013) Mol. Microbiol. , vol.88 , pp. 655-663
    • Kazmierczak, B.I.1    Hendrixson, D.R.2
  • 43
    • 35048903258 scopus 로고    scopus 로고
    • Proteins P24 and P41 function in the regulation of terminal-organelle development and gliding motility in Mycoplasma pneumoniae
    • Hasselbring BM, Krause DC. 2007. Proteins P24 and P41 function in the regulation of terminal-organelle development and gliding motility in Mycoplasma pneumoniae. J. Bacteriol. 189:7442-7449. http://dx.doi.org/10.1128/JB.00867-07.
    • (2007) J. Bacteriol. , vol.189 , pp. 7442-7449
    • Hasselbring, B.M.1    Krause, D.C.2
  • 44
    • 79955532633 scopus 로고    scopus 로고
    • More than one way to control hair growth: regulatory mechanisms in enterobacteria that affect fimbriae assembled by the chaperone/usher pathway
    • Clegg S, Wilson J, Johnson J. 2011. More than one way to control hair growth: regulatory mechanisms in enterobacteria that affect fimbriae assembled by the chaperone/usher pathway. J. Bacteriol. 193:2081-2088. http://dx.doi.org/10.1128/JB.00071-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 2081-2088
    • Clegg, S.1    Wilson, J.2    Johnson, J.3
  • 45
    • 33751265748 scopus 로고    scopus 로고
    • The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones
    • Qiu XB, Shao YM, Miao S, Wang L. 2006. The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell. Mol. Life Sci. 63:2560-2570. http://dx.doi.org/10.1007/s00018-006-6192-6.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2560-2570
    • Qiu, X.B.1    Shao, Y.M.2    Miao, S.3    Wang, L.4
  • 46
    • 60649098854 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae J-domain protein required for terminal organelle function
    • Cloward JM, Krause DC. 2009. Mycoplasma pneumoniae J-domain protein required for terminal organelle function. Mol. Microbiol. 71:1296-1307. http://dx.doi.org/10.1111/j.1365-2958.2009.06602.x.
    • (2009) Mol. Microbiol. , vol.71 , pp. 1296-1307
    • Cloward, J.M.1    Krause, D.C.2
  • 47
    • 79960153393 scopus 로고    scopus 로고
    • Loss of co-chaperone TopJ impacts adhesin P1 presentation and terminal organelle maturation in Mycoplasma pneumoniae
    • Cloward JM, Krause DC. 2011. Loss of co-chaperone TopJ impacts adhesin P1 presentation and terminal organelle maturation in Mycoplasma pneumoniae. Mol. Microbiol. 81:528-539. http://dx.doi.org/10.1111/j.1365-2958.2011.07712.x.
    • (2011) Mol. Microbiol. , vol.81 , pp. 528-539
    • Cloward, J.M.1    Krause, D.C.2
  • 48
    • 77953997512 scopus 로고    scopus 로고
    • Functional domain analysis of the Mycoplasma pneumoniae co-chaperone TopJ
    • Cloward JM, Krause DC. 2010. Functional domain analysis of the Mycoplasma pneumoniae co-chaperone TopJ. Mol. Microbiol. 77:158-169. http://dx.doi.org/10.1111/j.1365-2958.2010.07196.x.
    • (2010) Mol. Microbiol. , vol.77 , pp. 158-169
    • Cloward, J.M.1    Krause, D.C.2
  • 49
    • 0026707466 scopus 로고
    • DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli
    • Shi W, Zhou Y, Wild J, Adler J, Gross CA. 1992. DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli. J. Bacteriol. 174: 6256-6263.
    • (1992) J. Bacteriol. , vol.174 , pp. 6256-6263
    • Shi, W.1    Zhou, Y.2    Wild, J.3    Adler, J.4    Gross, C.A.5
  • 50
    • 84873539977 scopus 로고    scopus 로고
    • A novel dnaJ family gene, sflA, encodes an inhibitor of flagellation in marine Vibrio species
    • Kitaoka M, Nishigaki T, Ihara K, Nishioka N, Kojima S, Homma M. 2013. A novel dnaJ family gene, sflA, encodes an inhibitor of flagellation in marine Vibrio species. J. Bacteriol. 195:816-822. http://dx.doi.org/10.1128/JB.01850-12.
    • (2013) J. Bacteriol. , vol.195 , pp. 816-822
    • Kitaoka, M.1    Nishigaki, T.2    Ihara, K.3    Nishioka, N.4    Kojima, S.5    Homma, M.6
  • 51
    • 55949133468 scopus 로고    scopus 로고
    • Two-component signaling systems and cell cycle control in Caulobacter crescentus
    • Purcell EB, Boutte CC, Crosson S. 2008. Two-component signaling systems and cell cycle control in Caulobacter crescentus. Adv. Exp. Med. Biol. 631:122-130. http://dx.doi.org/10.1007/978-0-387-78885-2_8.
    • (2008) Adv. Exp. Med. Biol. , vol.631 , pp. 122-130
    • Purcell, E.B.1    Boutte, C.C.2    Crosson, S.3
  • 52
    • 77349099314 scopus 로고    scopus 로고
    • Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way
    • Molle V, Kremer L. 2010. Division and cell envelope regulation by Ser/Thr phosphorylation: Mycobacterium shows the way. Mol. Microbiol. 75: 1064-1077. http://dx.doi.org/10.1111/j.1365-2958.2009.07041.x.
    • (2010) Mol. Microbiol. , vol.75 , pp. 1064-1077
    • Molle, V.1    Kremer, L.2
  • 53
    • 84856585868 scopus 로고    scopus 로고
    • Mutational dissection of the S/T-kinase StkP reveal crucial roles in cell division of Streptococcus pneumoniae
    • Fleurie A, Cluzel C, Guiral S, Freton C, Galisson F, Zanella-Cleon I, Di Guilmi AM, Grangeasse C. 2012. Mutational dissection of the S/T-kinase StkP reveal crucial roles in cell division of Streptococcus pneumoniae. Mol. Microbiol. 83:746-758. http://dx.doi.org/10.1111/j.1365-2958.2011.07962.x.
    • (2012) Mol. Microbiol. , vol.83 , pp. 746-758
    • Fleurie, A.1    Cluzel, C.2    Guiral, S.3    Freton, C.4    Galisson, F.5    Zanella-Cleon, I.6    Di Guilmi, A.M.7    Grangeasse, C.8
  • 54
    • 84905281353 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrkC
    • Ravikumar V, Shi L, Krug K, Derouiche A, Jers C, Cousin C, Kobir A, Mijakovic I, Macek B. 2014. Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrkC. Mol. Cell. Proteomics 13:1965-1978. http://dx.doi.org/10.1074/mcp. M113.035949.
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 1965-1978
    • Ravikumar, V.1    Shi, L.2    Krug, K.3    Derouiche, A.4    Jers, C.5    Cousin, C.6    Kobir, A.7    Mijakovic, I.8    Macek, B.9
  • 55
    • 73449134487 scopus 로고    scopus 로고
    • The stability of cytadherence proteins in Mycoplasma pneumoniae requires activity of the protein kinase PrkC
    • Schmidl SR, Gronau K, Hames C, Busse J, Becher D, Hecker M, Stülke J. 2010. The stability of cytadherence proteins in Mycoplasma pneumoniae requires activity of the protein kinase PrkC. Infect. Immun. 78:184-192. http://dx.doi.org/10.1128/IAI.00958-09.
    • (2010) Infect. Immun. , vol.78 , pp. 184-192
    • Schmidl, S.R.1    Gronau, K.2    Hames, C.3    Busse, J.4    Becher, D.5    Hecker, M.6    Stülke, J.7
  • 57
    • 84876091163 scopus 로고    scopus 로고
    • Protein kinase/phosphatase function correlates with gliding motility in Mycoplasma pneumoniae
    • Page CA, Krause DC. 2013. Protein kinase/phosphatase function correlates with gliding motility in Mycoplasma pneumoniae. J. Bacteriol. 195: 1750-1757. http://dx.doi.org/10.1128/JB.02277-12.
    • (2013) J. Bacteriol. , vol.195 , pp. 1750-1757
    • Page, C.A.1    Krause, D.C.2
  • 58
    • 77953160473 scopus 로고    scopus 로고
    • The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: analysis of the complete known Ser/Thr kinome suggests the existence of novel kinases
    • Schmidl SR, Gronau K, Pietack N, Hecker M, Becher D, Stülke J. 2010. The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: analysis of the complete known Ser/Thr kinome suggests the existence of novel kinases. Mol. Cell. Proteomics 9:1228-1242. http://dx.doi.org/10.1074/mcp. M900267-MCP200.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1228-1242
    • Schmidl, S.R.1    Gronau, K.2    Pietack, N.3    Hecker, M.4    Becher, D.5    Stülke, J.6
  • 59
    • 56749185690 scopus 로고    scopus 로고
    • A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD
    • Bramkamp M, Emmins R, Weston L, Donovan C, Daniel RA, Errington J. 2008. A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD. Mol. Microbiol. 70:1556-1569. http://dx.doi.org/10.1111/j.1365-2958.2008.06501.x.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1556-1569
    • Bramkamp, M.1    Emmins, R.2    Weston, L.3    Donovan, C.4    Daniel, R.A.5    Errington, J.6
  • 60
    • 55349109965 scopus 로고    scopus 로고
    • MinJ (YvjD) is a topological determinant of cell division in Bacillus subtilis
    • Patrick JE, Kearns DB. 2008. MinJ (YvjD) is a topological determinant of cell division in Bacillus subtilis. Mol. Microbiol. 70:1166-1179. http://dx.doi.org/10.1111/j.1365-2958.2008.06469.x.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1166-1179
    • Patrick, J.E.1    Kearns, D.B.2
  • 62
    • 65449137972 scopus 로고    scopus 로고
    • Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin
    • Charbon G, Cabeen MT, Jacobs-Wagner C. 2009. Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin. Genes Dev. 23:1131-1144. http://dx.doi.org/10.1101/gad.1795509.
    • (2009) Genes Dev , vol.23 , pp. 1131-1144
    • Charbon, G.1    Cabeen, M.T.2    Jacobs-Wagner, C.3
  • 63
    • 34547651288 scopus 로고    scopus 로고
    • The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli
    • Mohammadi T, Karczmarek A, Crouvoisier M, Bouhss A, Mengin-Lecreulx D, Den Blaauwen T. 2007. The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli. Mol. Microbiol. 65:1106-1121. http://dx.doi.org/10.1111/j.1365-2958.2007.05851.x.
    • (2007) Mol. Microbiol. , vol.65 , pp. 1106-1121
    • Mohammadi, T.1    Karczmarek, A.2    Crouvoisier, M.3    Bouhss, A.4    Mengin-Lecreulx, D.5    Den Blaauwen, T.6
  • 64
    • 77951608842 scopus 로고    scopus 로고
    • Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD
    • White CL, Kitich A, Gober JW. 2010. Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD. Mol. Microbiol. 76:616-633. http://dx.doi.org/10.1111/j.1365-2958.2010.07108.x.
    • (2010) Mol. Microbiol. , vol.76 , pp. 616-633
    • White, C.L.1    Kitich, A.2    Gober, J.W.3
  • 65
    • 80053616695 scopus 로고    scopus 로고
    • Functional analysis of the cytoskeleton protein MreB from Chlamydophila pneumoniae
    • Gaballah A, Kloeckner A, Otten C, Sahl HG, Henrichfreise B. 2011. Functional analysis of the cytoskeleton protein MreB from Chlamydophila pneumoniae. PLoS One 6:e25129. http://dx.doi.org/10.1371/journal.pone.0025129.
    • (2011) PLoS One , vol.6 , pp. e25129
    • Gaballah, A.1    Kloeckner, A.2    Otten, C.3    Sahl, H.G.4    Henrichfreise, B.5
  • 66
    • 0346887117 scopus 로고    scopus 로고
    • Deletion analysis identifies key functional domains of the cytadherence-associated protein HMW2 of Mycoplasma pneumoniae
    • Balish MF, Ross SM, Fisseha M, Krause DC. 2003. Deletion analysis identifies key functional domains of the cytadherence-associated protein HMW2 of Mycoplasma pneumoniae. Mol. Microbiol. 50:1507-1516. http://dx.doi.org/10.1046/j.1365-2958.2003.03807.x.
    • (2003) Mol. Microbiol. , vol.50 , pp. 1507-1516
    • Balish, M.F.1    Ross, S.M.2    Fisseha, M.3    Krause, D.C.4
  • 67
    • 0035212227 scopus 로고    scopus 로고
    • Stability and subcellular localization of cytadherence-associated protein P65 in Myco-plasma pneumoniae
    • Jordan JL, Berry KM, Balish MF, Krause DC. 2001. Stability and subcellular localization of cytadherence-associated protein P65 in Myco-plasma pneumoniae. J. Bacteriol. 183:7387-7391. http://dx.doi.org/10.1128/JB.183.24.7387-7891.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 7387-7391
    • Jordan, J.L.1    Berry, K.M.2    Balish, M.F.3    Krause, D.C.4
  • 68
    • 84864020161 scopus 로고    scopus 로고
    • P65 truncation impacts P30 dynamics during Mycoplasma pneumoniae gliding
    • Hasselbring BM, Sheppard ES, Krause DC. 2012. P65 truncation impacts P30 dynamics during Mycoplasma pneumoniae gliding. J. Bacteriol. 194:3000-3007. http://dx.doi.org/10.1128/JB.00091-12.
    • (2012) J. Bacteriol. , vol.194 , pp. 3000-3007
    • Hasselbring, B.M.1    Sheppard, E.S.2    Krause, D.C.3
  • 69
    • 0034769801 scopus 로고    scopus 로고
    • Bacterial gliding motility: multiple mechanisms for cell movement over surfaces
    • McBride MJ. 2001. Bacterial gliding motility: multiple mechanisms for cell movement over surfaces. Annu. Rev. Microbiol. 55:49-75. http://dx.doi.org/10.1146/annurev.micro.55.1.49.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 49-75
    • McBride, M.J.1
  • 71
    • 84895070481 scopus 로고    scopus 로고
    • Deletion of the Cytophaga hutchinsonii type IX secretion system gene sprP results in defects in gliding motility and cellulose utilization
    • Zhu Y, McBride MJ. 2014. Deletion of the Cytophaga hutchinsonii type IX secretion system gene sprP results in defects in gliding motility and cellulose utilization. Appl. Microbiol. Biotechnol. 98:763-775. http://dx.doi.org/10.1007/s00253-013-5355-2.
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 763-775
    • Zhu, Y.1    McBride, M.J.2
  • 72
    • 47749149566 scopus 로고    scopus 로고
    • Deletion of the Mycoplasma genitalium MG_217 gene modifies cell gliding behavior by altering terminal organelle curvature
    • Burgos R, Pich OQ, Querol E, Piñol J. 2008. Deletion of the Mycoplasma genitalium MG_217 gene modifies cell gliding behavior by altering terminal organelle curvature. Mol. Microbiol. 69:1029-1040. http://dx.doi.org/10.1111/j.1365-2958.2008.06343.x.
    • (2008) Mol. Microbiol. , vol.69 , pp. 1029-1040
    • Burgos, R.1    Pich, O.Q.2    Querol, E.3    Piñol, J.4
  • 73
    • 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. 2014. In vitro spatial and temporal analysis of Mycoplasma pneumoniae colonization of human airway epithelium. Infect. Immun. 82:579-586. http://dx.doi.org/10.1128/IAI.01036-13.
    • (2014) Infect. Immun. , vol.82 , pp. 579-586
    • Prince, O.A.1    Krunkosky, T.M.2    Krause, D.C.3
  • 74
    • 37648998892 scopus 로고    scopus 로고
    • Cytoskeletal "jellyfish" structure of Mycoplasma mobile
    • Nakane D, Miyata M. 2007. Cytoskeletal "jellyfish" structure of Mycoplasma mobile. Proc. Natl. Acad. Sci. U. S. A. 104:19518-19523. http://dx.doi.org/10.1073/pnas.0704280104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 19518-19523
    • Nakane, D.1    Miyata, M.2
  • 75
    • 84864012598 scopus 로고    scopus 로고
    • Conserved terminal organelle morphology and function in Mycoplasma penetrans and Mycoplasma iowae
    • Jurkovic DA, Newman JT, Balish MF. 2012. Conserved terminal organelle morphology and function in Mycoplasma penetrans and Mycoplasma iowae. J. Bacteriol. 194:2877-2883. http://dx.doi.org/10.1128/JB.00060-12.
    • (2012) J. Bacteriol. , vol.194 , pp. 2877-2883
    • Jurkovic, D.A.1    Newman, J.T.2    Balish, M.F.3
  • 76
    • 84870910791 scopus 로고    scopus 로고
    • Analysis of energy sources for Mycoplasma penetrans gliding motility
    • Jurkovic DA, Hughes MR, Balish MF. 2013. Analysis of energy sources for Mycoplasma penetrans gliding motility. FEMS Microbiol. Lett. 338:39. http://dx.doi.org/10.1111/1574-6968.12026.
    • (2013) FEMS Microbiol. Lett. , vol.338 , pp. 39
    • Jurkovic, D.A.1    Hughes, M.R.2    Balish, M.F.3
  • 77
    • 3042515670 scopus 로고    scopus 로고
    • Energetics of gliding motility in Mycoplasma mobile
    • Jaffe JD, Miyata M, Berg HC. 2004. Energetics of gliding motility in Mycoplasma mobile. J. Bacteriol. 186:4254-4261. http://dx.doi.org/10.1128/JB.186.13.4254-4261.2004.
    • (2004) J. Bacteriol. , vol.186 , pp. 4254-4261
    • Jaffe, J.D.1    Miyata, M.2    Berg, H.C.3
  • 78
    • 24944547468 scopus 로고    scopus 로고
    • Mutant analysis reveals a specific requirement for P30 in Mycoplasma pneumoniae gliding motility
    • Hasselbring BM, Jordan JL, Krause DC. 2005. Mutant analysis reveals a specific requirement for P30 in Mycoplasma pneumoniae gliding motility. J. Bacteriol. 187:6281-6289. http://dx.doi.org/10.1128/JB.187.18.6281-6289.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 6281-6289
    • Hasselbring, B.M.1    Jordan, J.L.2    Krause, D.C.3
  • 79
    • 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. 2005. Involvement of P1 adhesin in gliding motility of Mycoplasma pneumoniae as revealed by the inhibitory effects of antibody under optimized gliding conditions. J. Bacteriol. 187: 1875-1877. http://dx.doi.org/10.1128/JB.187.5.1875-1877.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 1875-1877
    • Seto, S.1    Kenri, T.2    Tomiyama, T.3    Miyata, M.4
  • 80
    • 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. 2011. Isolation and characterization of P1 adhesin, a leg protein of the gliding bacterium Mycoplasma pneumoniae. J. Bacteriol. 193:715-722. http://dx.doi.org/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
  • 81
    • 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 LL, Keeler CL, Jr, Tessmer LL, Czymmek K, Dohms JE. 1998. 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) Infect. Immun. , vol.66 , pp. 3436-3442
    • Hnatow, L.L.1    Keeler Jr., C.L.2    Tessmer, L.L.3    Czymmek, K.4    Dohms, J.E.5
  • 82
    • 0025610222 scopus 로고
    • Characterization of the gene for a 30-kilodalton adhesion-related protein of Mycoplasma pneumoniae
    • Dallo SF, Chavoya A, Baseman JB. 1990. Characterization of the gene for a 30-kilodalton adhesion-related protein of Mycoplasma pneumoniae. Infect. Immun. 58:4163-4165.
    • (1990) Infect. Immun. , vol.58 , pp. 4163-4165
    • Dallo, S.F.1    Chavoya, A.2    Baseman, J.B.3
  • 83
    • 0030833639 scopus 로고    scopus 로고
    • The adhesin related 30-kDa protein of Mycoplasma pneumoniae exhibits size and antigen variability
    • Layh-Schmitt G, Himmelreich R, Leibfried U. 1997. The adhesin related 30-kDa protein of Mycoplasma pneumoniae exhibits size and antigen variability. FEMS Microbiol. Lett. 152:101-108. http://dx.doi.org/10.1111/j.1574-6968.1997.tb10415.x.
    • (1997) FEMS Microbiol. Lett. , vol.152 , pp. 101-108
    • Layh-Schmitt, G.1    Himmelreich, R.2    Leibfried, U.3
  • 84
    • 79952797271 scopus 로고    scopus 로고
    • Domain analysis of protein P30 in Mycoplasma pneumoniae cytadherence and gliding motility
    • Chang HY, Jordan JL, Krause DC. 2011. Domain analysis of protein P30 in Mycoplasma pneumoniae cytadherence and gliding motility. J. Bacteriol. 193:1726-1733. http://dx.doi.org/10.1128/JB.01228-10.
    • (2011) J. Bacteriol. , vol.193 , pp. 1726-1733
    • Chang, H.Y.1    Jordan, J.L.2    Krause, D.C.3
  • 85
    • 80053440055 scopus 로고    scopus 로고
    • Insights into the function of Mycoplasma pneumoniae protein P30 from orthologous gene replacement
    • Relich RF, Balish MF. 2011. Insights into the function of Mycoplasma pneumoniae protein P30 from orthologous gene replacement. Microbiology 157:2862-2870. http://dx.doi.org/10.1099/mic.0.052464-0.
    • (2011) Microbiology , vol.157 , pp. 2862-2870
    • Relich, R.F.1    Balish, M.F.2
  • 86
    • 0028786874 scopus 로고
    • Molecular cloning and characterization of an adherence-related operon of Mycoplasma genitalium
    • Reddy SP, Rasmussen WG, Baseman JB. 1995. Molecular cloning and characterization of an adherence-related operon of Mycoplasma genitalium. J. Bacteriol. 177:5943-5951.
    • (1995) J. Bacteriol. , vol.177 , pp. 5943-5951
    • Reddy, S.P.1    Rasmussen, W.G.2    Baseman, J.B.3
  • 87
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li Z, Trimble MJ, Brun YV, Jensen GJ. 2007. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J. 26:4694-4708. http://dx.doi.org/10.1038/sj.emboj.7601895.
    • (2007) EMBO J , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 88
    • 84870573233 scopus 로고    scopus 로고
    • The plastiddividing machinery: formation, constriction and fission
    • Yoshida Y, Miyagishima SY, Kuroiwa H, Kuroiwa T. 2012. The plastiddividing machinery: formation, constriction and fission. Curr. Opin. Plant Biol. 15:714-721. http://dx.doi.org/10.1016/j.pbi.2012.07.002.
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 714-721
    • Yoshida, Y.1    Miyagishima, S.Y.2    Kuroiwa, H.3    Kuroiwa, T.4
  • 89
    • 84871802627 scopus 로고    scopus 로고
    • Recent advances into the understanding of mitochondrial fission
    • Elgass K, Pakay J, Ryan MT, Palmer CS. 2013. Recent advances into the understanding of mitochondrial fission. Biochim. Biophys. Acta 1833: 150-161. http://dx.doi.org/10.1016/j.bbamcr.2012.05.002.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 150-161
    • Elgass, K.1    Pakay, J.2    Ryan, M.T.3    Palmer, C.S.4
  • 90
    • 78649385769 scopus 로고    scopus 로고
    • Cell division in a minimal bacterium in the absence of FtsZ
    • Lluch-Senar M, Querol E, Piñol J. 2010. Cell division in a minimal bacterium in the absence of FtsZ. Mol. Microbiol. 78:278-289. http://dx.doi.org/10.1111/j.1365-2958.2010.07306.x.
    • (2010) Mol. Microbiol. , vol.78 , pp. 278-289
    • Lluch-Senar, M.1    Querol, E.2    Piñol, J.3
  • 91
    • 33750815099 scopus 로고    scopus 로고
    • Terminal organelle development in the cell wall-less bacterium Mycoplasma pneumoniae
    • Hasselbring BM, Jordan JL, Krause RW, Krause DC. 2006. Terminal organelle development in the cell wall-less bacterium Mycoplasma pneumoniae. Proc. Natl. Acad. Sci. U. S. A. 103:16478-16483. http://dx.doi.org/10.1073/pnas.0608051103.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 16478-16483
    • Hasselbring, B.M.1    Jordan, J.L.2    Krause, R.W.3    Krause, D.C.4
  • 92
    • 33144471122 scopus 로고    scopus 로고
    • Probing in vivo promoter activities in Mycoplasma pneumoniae: a system for generation of single-copy reporter constructs
    • Halbedel S, Stülke J. 2006. Probing in vivo promoter activities in Mycoplasma pneumoniae: a system for generation of single-copy reporter constructs. Appl. Environ. Microbiol. 72:1696-1699. http://dx.doi.org/10.1128/AEM.72.2.1696-1699.2006.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1696-1699
    • Halbedel, S.1    Stülke, J.2
  • 93
    • 22144457451 scopus 로고    scopus 로고
    • Multiple-mutation reaction: a method for simultaneous introduction of multiple mutations into the glpK gene of Mycoplasma pneumoniae
    • Hames C, Halbedel S, Schilling O, Stülke J. 2005. Multiple-mutation reaction: a method for simultaneous introduction of multiple mutations into the glpK gene of Mycoplasma pneumoniae. Appl. Environ. Microbiol. 71:4097-4100. http://dx.doi.org/10.1128/AEM.71.7.4097-4100.2005.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4097-4100
    • Hames, C.1    Halbedel, S.2    Schilling, O.3    Stülke, J.4
  • 94
    • 38449122258 scopus 로고    scopus 로고
    • Expression of Mycoplasma proteins carrying an affinity tag in M. pneumoniae allows rapid purification and circumvents problems related to the aberrant genetic code
    • Schmidl SR, Hames C, Stülke J. 2007. Expression of Mycoplasma proteins carrying an affinity tag in M. pneumoniae allows rapid purification and circumvents problems related to the aberrant genetic code. Appl. Environ. Microbiol. 73:7799-7801. http://dx.doi.org/10.1128/AEM.01861-07.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 7799-7801
    • Schmidl, S.R.1    Hames, C.2    Stülke, J.3
  • 96
    • 84874768439 scopus 로고    scopus 로고
    • Excess membrane synthesis drives a primitive mode of cell proliferation
    • Mercier R, Kawai Y, Errington J. 2013. Excess membrane synthesis drives a primitive mode of cell proliferation. Cell 152:997-1007. http://dx.doi.org/10.1016/j.cell.2013.01.043.
    • (2013) Cell , vol.152 , pp. 997-1007
    • Mercier, R.1    Kawai, Y.2    Errington, J.3
  • 97
    • 84907840161 scopus 로고    scopus 로고
    • In Browning GF, Citti C (ed), Mollicutes: molecular biology and pathogenesis. Caister Academic Press, Norfolk, United Kingdom
    • Balish MF. 2014. Organization of the cytoskeletons of diverse Mollicutes, p 215-236. In Browning GF, Citti C (ed), Mollicutes: molecular biology and pathogenesis. Caister Academic Press, Norfolk, United Kingdom.
    • (2014) Organization of the cytoskeletons of diverse Mollicutes , pp. 215-236
    • Balish, M.F.1

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.