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Volumn 91, Issue 12, 2006, Pages 4589-4597

Coarse-grained molecular dynamics simulations of a rotating bacterial flagellum

Author keywords

[No Author keywords available]

Indexed keywords

MONOMER; SOLVENT;

EID: 33845381177     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.093443     Document Type: Article
Times cited : (88)

References (33)
  • 1
    • 0014979468 scopus 로고
    • Purification of intact flagella from Escherichia coli and Bacillus subtilis
    • DePamphilis, M. L., and J. Adler. 1971. Purification of intact flagella from Escherichia coli and Bacillus subtilis. J. Bacteriol. 105:376-383.
    • (1971) J. Bacteriol. , vol.105 , pp. 376-383
    • DePamphilis, M.L.1    Adler, J.2
  • 2
    • 0016345728 scopus 로고
    • Change in direction of flagellar rotation is the basis of the chemotactic response in Escherichia coli
    • Larsen, S. H., R. W. Reader, E. N. Kort, W.-W. Tso, and J. Adler. 1974. Change in direction of flagellar rotation is the basis of the chemotactic response in Escherichia coli. Nature. 249:74-77.
    • (1974) Nature , vol.249 , pp. 74-77
    • Larsen, S.H.1    Reader, R.W.2    Kort, E.N.3    Tso, W.-W.4    Adler, J.5
  • 3
    • 0017704180 scopus 로고
    • Normal-to-curly flagellar transitions and their role in bacterial tumbling. Stabilization of an alternative quaternary structure by mechanical force
    • Macnab, R. M., and M. K. Ornston. 1977. Normal-to-curly flagellar transitions and their role in bacterial tumbling. Stabilization of an alternative quaternary structure by mechanical force. J. Mol. Biol. 112:1-30.
    • (1977) J. Mol. Biol. , vol.112 , pp. 1-30
    • Macnab, R.M.1    Ornston, M.K.2
  • 4
    • 0018791734 scopus 로고
    • Transition of bacterial flagella from helical to straight forms with different subunit arrangements
    • Kamiya, R., S. Asakura, K. Wakabayashi, and K. Namba. 1979. Transition of bacterial flagella from helical to straight forms with different subunit arrangements. J. Mol. Biol. 131:725-742.
    • (1979) J. Mol. Biol. , vol.131 , pp. 725-742
    • Kamiya, R.1    Asakura, S.2    Wakabayashi, K.3    Namba, K.4
  • 5
    • 0029039662 scopus 로고
    • The structure of the R-type straight flagellar filament of Salmonella at 9 Å resolution by electron cryomicroscopy
    • Mimori, Y., I. Yamashita, K. Murata, Y. Fujiyoshi, K. Yonekura, C. Toyoshima, and K. Namba. 1995. The structure of the R-type straight flagellar filament of Salmonella at 9 Å resolution by electron cryomicroscopy. J. Mol. Biol. 249:69-87.
    • (1995) J. Mol. Biol. , vol.249 , pp. 69-87
    • Mimori, Y.1    Yamashita, I.2    Murata, K.3    Fujiyoshi, Y.4    Yonekura, K.5    Toyoshima, C.6    Namba, K.7
  • 6
    • 0029042213 scopus 로고
    • Structure of bacterial flagellar filaments at 11 Å resolution: Packing of the α-helices
    • Morgan, D. G., C. Owen, L. A. Melanson, and D. J. DeRosier. 1995. Structure of bacterial flagellar filaments at 11 Å resolution: packing of the α-helices. J. Mol. Biol. 249:88-110.
    • (1995) J. Mol. Biol. , vol.249 , pp. 88-110
    • Morgan, D.G.1    Owen, C.2    Melanson, L.A.3    DeRosier, D.J.4
  • 7
    • 0035868953 scopus 로고    scopus 로고
    • Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling
    • Samatey, F. A., K. Imada, S. Nagashima, F. Vonderviszt, T. Kumasaka, M. Yamamoto, and K. Namba. 2001. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature. 410:331-337.
    • (2001) Nature , vol.410 , pp. 331-337
    • Samatey, F.A.1    Imada, K.2    Nagashima, S.3    Vonderviszt, F.4    Kumasaka, T.5    Yamamoto, M.6    Namba, K.7
  • 8
    • 0014889416 scopus 로고
    • Polymerization of flagellin and polymorphism of flagella
    • Asakura, S. 1970. Polymerization of flagellin and polymorphism of flagella. Adv. Biophys. 1:99-155.
    • (1970) Adv. Biophys. , vol.1 , pp. 99-155
    • Asakura, S.1
  • 9
    • 0017841508 scopus 로고
    • Change of waveform in bacterial flagella: The role of mechanics at the molecular level
    • Calladine, C. R. 1978. Change of waveform in bacterial flagella: the role of mechanics at the molecular level. J. Mol. Biol. 118:457-479.
    • (1978) J. Mol. Biol. , vol.118 , pp. 457-479
    • Calladine, C.R.1
  • 11
    • 0031982793 scopus 로고    scopus 로고
    • Quasi- and non-equivalence in the structure of bacterial flagellar filament
    • Hasegawa, K., I. Yamashita, and K. Namba. 1998. Quasi- and non-equivalence in the structure of bacterial flagellar filament. Biophys. J. 74:569-575.
    • (1998) Biophys. J. , vol.74 , pp. 569-575
    • Hasegawa, K.1    Yamashita, I.2    Namba, K.3
  • 13
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura, K., S. Maki-Yonekura, and K. Namba. 2003. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature. 424:643-650.
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 14
    • 4344685227 scopus 로고    scopus 로고
    • Global ribosome motions revealed with elastic network model
    • Wang, Y., A. J. Rader, I. Bahar, and R. L. Jernigan. 2004. Global ribosome motions revealed with elastic network model. J. Struct. Biol. 147:302-314.
    • (2004) J. Struct. Biol. , vol.147 , pp. 302-314
    • Wang, Y.1    Rader, A.J.2    Bahar, I.3    Jernigan, R.L.4
  • 15
    • 24144478280 scopus 로고    scopus 로고
    • Exploring global motions and correlations in the ribosome
    • Trylska, J., V. Tozzini, and J. A. McCammon. 2005. Exploring global motions and correlations in the ribosome. Biophys. J. 89:1455-1463.
    • (2005) Biophys. J. , vol.89 , pp. 1455-1463
    • Trylska, J.1    Tozzini, V.2    McCammon, J.A.3
  • 16
    • 9644266693 scopus 로고    scopus 로고
    • Diversity and identity of mechanical properties of icosahedral viral capsids studied with elastic network normal mode analysis
    • Tama, F., and C. L. Brooks III. 2005. Diversity and identity of mechanical properties of icosahedral viral capsids studied with elastic network normal mode analysis. J. Mol. Biol. 345:299-314.
    • (2005) J. Mol. Biol. , vol.345 , pp. 299-314
    • Tama, F.1    Brooks III, C.L.2
  • 17
    • 24344438610 scopus 로고    scopus 로고
    • A coarse grained model for the dynamics of flap opening in HIV-1 protease
    • Tozzini, V., and A. McCammon. 2005. A coarse grained model for the dynamics of flap opening in HIV-1 protease. Chem. Phys. Lett. 413:123-128.
    • (2005) Chem. Phys. Lett. , vol.413 , pp. 123-128
    • Tozzini, V.1    McCammon, A.2
  • 18
    • 24944541377 scopus 로고    scopus 로고
    • Allostery of actin filaments: Molecular dynamics simulations and coarse-grained analysis
    • Chu, J.-W., and G. A. Voth. 2005. Allostery of actin filaments: molecular dynamics simulations and coarse-grained analysis. Proc. Natl. Acad. Sci. USA. 102:13111-13116.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13111-13116
    • Chu, J.-W.1    Voth, G.A.2
  • 19
    • 1642485164 scopus 로고    scopus 로고
    • Coarse-grained model for semiquantitative lipid simulations
    • Marrink, S. J., A. H. de Vries, and A. E. Mark. 2004. Coarse-grained model for semiquantitative lipid simulations. J. Phys. Chem. B. 108:750-760.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 750-760
    • Marrink, S.J.1    De Vries, A.H.2    Mark, A.E.3
  • 20
    • 19744367689 scopus 로고    scopus 로고
    • Simulation of gel phase formation and melting in lipid bilayers using a coarse-grained model
    • Marrink, S. J., J. Risselada, and A. E. Mark. 2005. Simulation of gel phase formation and melting in lipid bilayers using a coarse-grained model. Chem. Phys. Lipids. 135:223-244.
    • (2005) Chem. Phys. Lipids. , vol.135 , pp. 223-244
    • Marrink, S.J.1    Risselada, J.2    Mark, A.E.3
  • 22
    • 0036681718 scopus 로고    scopus 로고
    • Computer simulation studies of biomembranes using a coarse-grain model
    • Lopez, C., P. Moore, J. Shelley, M. Shelley, and M. Klein. 2002. Computer simulation studies of biomembranes using a coarse-grain model. Comput. Phys. Commun. 147:1-6.
    • (2002) Comput. Phys. Commun. , vol.147 , pp. 1-6
    • Lopez, C.1    Moore, P.2    Shelley, J.3    Shelley, M.4    Klein, M.5
  • 23
    • 33644893631 scopus 로고    scopus 로고
    • Coarse-grained protein-lipid model with application to lipoprotein particles
    • Shih, A. Y., A. Arkhipov, P. L. Freddolino, and K. Schulten. 2006. Coarse-grained protein-lipid model with application to lipoprotein particles. J. Phys. Chem. B. 110:3674-3684.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3674-3684
    • Shih, A.Y.1    Arkhipov, A.2    Freddolino, P.L.3    Schulten, K.4
  • 24
    • 33847193915 scopus 로고    scopus 로고
    • Assembly of lipoprotein particles revealed by molecular dynamics simulations
    • In press
    • Shih, A. Y., P. L. Freddolino, A. Arkhipov, and K. Schulten. 2006. Assembly of lipoprotein particles revealed by molecular dynamics simulations. J. Struct. Biol. In press.
    • (2006) J. Struct. Biol.
    • Shih, A.Y.1    Freddolino, P.L.2    Arkhipov, A.3    Schulten, K.4
  • 26
    • 0000742931 scopus 로고
    • A "neural gas" network learns topologies
    • T. Kohonen, K. Mäkisara, O. Simula, and J. Kangas, editors. Elsevier, Amsterdam
    • Martinetz, T., and K. Schulten. 1991. A "neural gas" network learns topologies. In Artificial Neural Networks. T. Kohonen, K. Mäkisara, O. Simula, and J. Kangas, editors. Elsevier, Amsterdam.
    • (1991) Artificial Neural Networks
    • Martinetz, T.1    Schulten, K.2
  • 27
    • 0028204732 scopus 로고
    • Topology-representing networks
    • Martinetz, T., and K. Schulten. 1994. Topology-representing networks. Neural Networks. 7:507-522.
    • (1994) Neural Networks , vol.7 , pp. 507-522
    • Martinetz, T.1    Schulten, K.2
  • 29
    • 0030832809 scopus 로고    scopus 로고
    • Short-range conformational energies, secondary structure propensities, and recognition of correct sequence-structure matches
    • Bahar, I., M. Kaplan, and R. L. Jernigan. 1997. Short-range conformational energies, secondary structure propensities, and recognition of correct sequence-structure matches. Protein Struct. Funct. Gen. 29:292-308.
    • (1997) Protein Struct. Funct. Gen. , vol.29 , pp. 292-308
    • Bahar, I.1    Kaplan, M.2    Jernigan, R.L.3
  • 32
    • 0025148428 scopus 로고
    • Abrupt changes in flagellar rotation observed by laser dark-field microscopy
    • Kudo, S., Y. Magariyama, and S.-I. Aizawa. 1990. Abrupt changes in flagellar rotation observed by laser dark-field microscopy. Nature. 346:677-680.
    • (1990) Nature , vol.346 , pp. 677-680
    • Kudo, S.1    Magariyama, Y.2    Aizawa, S.-I.3
  • 33
    • 0034015656 scopus 로고    scopus 로고
    • Real-time imaging of fluorescent flagellar filaments
    • Turner, L., W. S. Ryu, and H. C. Berg. 2000. Real-time imaging of fluorescent flagellar filaments. J. Bacteriol. 182:2793-2801.
    • (2000) J. Bacteriol. , vol.182 , pp. 2793-2801
    • Turner, L.1    Ryu, W.S.2    Berg, H.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.