메뉴 건너뛰기




Volumn 3, Issue C, 1997, Pages 107-171

Chapter 5 Three hundred years of bacterial motility

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0000721525     PISSN: 18745660     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5660(97)80007-X     Document Type: Review
Times cited : (7)

References (160)
  • 1
    • 0013839358 scopus 로고
    • Chemotaxis in E. coli
    • Adler J. Chemotaxis in E. coli. Cold Spring Harbor Symp 30 (1965) 289-293
    • (1965) Cold Spring Harbor Symp , vol.30 , pp. 289-293
    • Adler, J.1
  • 2
    • 0014013196 scopus 로고
    • Chemotaxis in bacteria
    • Adler J. Chemotaxis in bacteria. Science 153 (1966) 708-716
    • (1966) Science , vol.153 , pp. 708-716
    • Adler, J.1
  • 3
    • 0014692237 scopus 로고
    • Chemoreceptors in bacteria
    • Adler J. Chemoreceptors in bacteria. Science 166 (1969) 1588-1597
    • (1969) Science , vol.166 , pp. 1588-1597
    • Adler, J.1
  • 4
    • 0015540879 scopus 로고
    • A method for measuring chemotaxis and the use of the method to determine optimum conditions for chemotaxis by E. coli
    • Adler J. A method for measuring chemotaxis and the use of the method to determine optimum conditions for chemotaxis by E. coli. J. Gen. Microbiol. 74 (1973) 77-91
    • (1973) J. Gen. Microbiol. , vol.74 , pp. 77-91
    • Adler, J.1
  • 5
    • 0016943812 scopus 로고
    • The sensing of chemicals by bacteria
    • Adler J. The sensing of chemicals by bacteria. Sci. American 234 (1976) 40-47
    • (1976) Sci. American , vol.234 , pp. 40-47
    • Adler, J.1
  • 6
    • 0011512247 scopus 로고
    • Phosphotransferase-system enzymes as chemoreceptors for certain sugars in Escherichia coli chemotaxis
    • Adler J., and Epstein W. Phosphotransferase-system enzymes as chemoreceptors for certain sugars in Escherichia coli chemotaxis. Proc. Nat. Acad. Sci. USA 71 (1974) 2895-2899
    • (1974) Proc. Nat. Acad. Sci. USA , vol.71 , pp. 2895-2899
    • Adler, J.1    Epstein, W.2
  • 7
    • 0015797384 scopus 로고
    • Chemotaxis toward sugars in Escherichia coli
    • Adler J., Hazelbauer G.L., and Dahl M.M. Chemotaxis toward sugars in Escherichia coli. J. Bacteriol. 155 (1973) 824-847
    • (1973) J. Bacteriol. , vol.155 , pp. 824-847
    • Adler, J.1    Hazelbauer, G.L.2    Dahl, M.M.3
  • 8
    • 0021913736 scopus 로고
    • Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium
    • Aizawa S., Dean G.E., Jones C.J., Macnab R.M., and Yamaguchi S. Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium. J. Bacteriol. 161 (1985) 836-849
    • (1985) J. Bacteriol. , vol.161 , pp. 836-849
    • Aizawa, S.1    Dean, G.E.2    Jones, C.J.3    Macnab, R.M.4    Yamaguchi, S.5
  • 9
    • 0028282042 scopus 로고
    • Protein histidine kinases and signal transduction in prokaryotes and eukaryotes
    • Alex L.A., and Simon M.I. Protein histidine kinases and signal transduction in prokaryotes and eukaryotes. Trends Genet. 10 (1994) 133-138
    • (1994) Trends Genet. , vol.10 , pp. 133-138
    • Alex, L.A.1    Simon, M.I.2
  • 10
    • 0026009504 scopus 로고
    • Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus
    • Alley M.R.K., Gomes S.L., Alexander W., and Shapiro L. Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus. Genetics 129 (1991) 333-342
    • (1991) Genetics , vol.129 , pp. 333-342
    • Alley, M.R.K.1    Gomes, S.L.2    Alexander, W.3    Shapiro, L.4
  • 11
    • 0027010624 scopus 로고
    • Bacterial motility and chemotaxis
    • Armitage J.P. Bacterial motility and chemotaxis. Science Progress 76 (1992) 451-477
    • (1992) Science Progress , vol.76 , pp. 451-477
    • Armitage, J.P.1
  • 12
    • 0019424678 scopus 로고
    • The reaction centre in the phototactic and chemotactic responses of Rhodopseudomonas sphaeroides
    • Armitage J.P., and Evans M.C.W. The reaction centre in the phototactic and chemotactic responses of Rhodopseudomonas sphaeroides. FEMS Microbiol. Lett. 11 (1981) 89-92
    • (1981) FEMS Microbiol. Lett. , vol.11 , pp. 89-92
    • Armitage, J.P.1    Evans, M.C.W.2
  • 13
    • 0021950970 scopus 로고
    • Role of the proton motive force in phototactic and aerotactic responses of Rhodopseudomonas sphaeroides
    • Armitage J.P., Ingham C., and Evans M.C.W. Role of the proton motive force in phototactic and aerotactic responses of Rhodopseudomonas sphaeroides. J. Bacteriol. 163 (1985) 967-972
    • (1985) J. Bacteriol. , vol.163 , pp. 967-972
    • Armitage, J.P.1    Ingham, C.2    Evans, M.C.W.3
  • 14
    • 0015426504 scopus 로고
    • An S-adenosyl methionine requirement for chemotaxis in Escherichia coli
    • Armstrong J.B. An S-adenosyl methionine requirement for chemotaxis in Escherichia coli. Canad. J. Microbiol. 18 (1972) 1695-1701
    • (1972) Canad. J. Microbiol. , vol.18 , pp. 1695-1701
    • Armstrong, J.B.1
  • 15
    • 0014443922 scopus 로고
    • Location of genes for motility and chemotaxis on the Escherichia coli genetic map
    • Armstrong J.B., and Adler J. Location of genes for motility and chemotaxis on the Escherichia coli genetic map. J. Bacteriol. 97 (1969) 156-161
    • (1969) J. Bacteriol. , vol.97 , pp. 156-161
    • Armstrong, J.B.1    Adler, J.2
  • 16
    • 0014455603 scopus 로고
    • Complementation of nonchemotactic mutants of Escherichia coli
    • Armstrong J.B., and Adler J. Complementation of nonchemotactic mutants of Escherichia coli. Genetics 61 (1969) 61-66
    • (1969) Genetics , vol.61 , pp. 61-66
    • Armstrong, J.B.1    Adler, J.2
  • 17
    • 0014045581 scopus 로고
    • Non-chemotactic mutants of Escherichia coli
    • Armstrong J.B., Adler J., and Dahl M.M. Non-chemotactic mutants of Escherichia coli. J. Bacteriol. 93 (1967) 390-398
    • (1967) J. Bacteriol. , vol.93 , pp. 390-398
    • Armstrong, J.B.1    Adler, J.2    Dahl, M.M.3
  • 18
    • 0346660000 scopus 로고
    • Secondary sigma factor controls transcription of flagellar and chemotaxis genes in Escherichia coli
    • Arnosti D.N., and Chamberlin M.J. Secondary sigma factor controls transcription of flagellar and chemotaxis genes in Escherichia coli. Proc. Nat. Acad. Sci. USA 86 (1989) 830-834
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 830-834
    • Arnosti, D.N.1    Chamberlin, M.J.2
  • 19
    • 0344963541 scopus 로고
    • X-ray diffraction study of the structure of bacterial flagella
    • Ashbury W.T., and Weibull C. X-ray diffraction study of the structure of bacterial flagella. Nature (London) 163 (1949) 280-282
    • (1949) Nature (London) , vol.163 , pp. 280-282
    • Ashbury, W.T.1    Weibull, C.2
  • 20
    • 0016773863 scopus 로고
    • Evidence for an S-adenosyl methionine requirement in the chemotactic behavior of Salmonella typhimurium
    • Aswad D.W., and Koshland D.E.J. Evidence for an S-adenosyl methionine requirement in the chemotactic behavior of Salmonella typhimurium. J. Mol. Biol. 97 (1975) 207-223
    • (1975) J. Mol. Biol. , vol.97 , pp. 207-223
    • Aswad, D.W.1    Koshland, D.E.J.2
  • 21
    • 0016345574 scopus 로고
    • Dynamic properties of bacterial flagellar motors
    • Berg H.C. Dynamic properties of bacterial flagellar motors. Nature (London) 249 (1974) 77-79
    • (1974) Nature (London) , vol.249 , pp. 77-79
    • Berg, H.C.1
  • 23
    • 0015897650 scopus 로고
    • Bacteria swim by rotating their flagellar filaments
    • Berg H.C., and Anderson R.A. Bacteria swim by rotating their flagellar filaments. Nature (London) 245 (1973) 380-382
    • (1973) Nature (London) , vol.245 , pp. 380-382
    • Berg, H.C.1    Anderson, R.A.2
  • 24
    • 0021723473 scopus 로고
    • A miniature flow cell designed for rapid exchange of media under high-powered objectives
    • Berg H.C., and Block S.M. A miniature flow cell designed for rapid exchange of media under high-powered objectives. J. Gen. Microbiol. 130 (1984) 2915-2920
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2915-2920
    • Berg, H.C.1    Block, S.M.2
  • 25
    • 0015526205 scopus 로고
    • Chemotaxis in Escherichia coli analysed by three-dimensional tracking
    • Berg H.C., and Brown D.A. Chemotaxis in Escherichia coli analysed by three-dimensional tracking. Nature (London) 239 (1972) 500-504
    • (1972) Nature (London) , vol.239 , pp. 500-504
    • Berg, H.C.1    Brown, D.A.2
  • 27
    • 0001180444 scopus 로고
    • Transient responses to chemotactic stimuli in Escherichia coli
    • Berg H.C., and Tedesco P.M. Transient responses to chemotactic stimuli in Escherichia coli. Proc. Nat. Acad. Sci. USA 72 (1975) 3235-3239
    • (1975) Proc. Nat. Acad. Sci. USA , vol.72 , pp. 3235-3239
    • Berg, H.C.1    Tedesco, P.M.2
  • 28
    • 0022617933 scopus 로고
    • Analysis of the Products of the Myxococcus xanthus frz Genes
    • Blackhart B.D., and Zusman D.R. Analysis of the Products of the Myxococcus xanthus frz Genes. J. Bacteriol. 166 (1986) 673-678
    • (1986) J. Bacteriol. , vol.166 , pp. 673-678
    • Blackhart, B.D.1    Zusman, D.R.2
  • 29
    • 0024295536 scopus 로고
    • Restoration of torque in defective flagellar motors
    • Blair D.F., and Berg H.C. Restoration of torque in defective flagellar motors. Science 242 (1988) 1678-1681
    • (1988) Science , vol.242 , pp. 1678-1681
    • Blair, D.F.1    Berg, H.C.2
  • 30
    • 0025058346 scopus 로고
    • The MotA protein of E. coli is a proton-conducting component of the flagellar motor
    • Blair D.F., and Berg H.C. The MotA protein of E. coli is a proton-conducting component of the flagellar motor. Cell 60 (1990) 439-449
    • (1990) Cell , vol.60 , pp. 439-449
    • Blair, D.F.1    Berg, H.C.2
  • 31
    • 0026068420 scopus 로고
    • Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction
    • Blair D.F., and Berg H.C. Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction. J. Mol. Biol. 221 (1991) 1433-1442
    • (1991) J. Mol. Biol. , vol.221 , pp. 1433-1442
    • Blair, D.F.1    Berg, H.C.2
  • 32
    • 0021280816 scopus 로고
    • Successive incorporation of force generating units in the bacterial rotary motor
    • Block S.M., and Berg H.C. Successive incorporation of force generating units in the bacterial rotary motor. Nature (London) 309 (1984) 470-472
    • (1984) Nature (London) , vol.309 , pp. 470-472
    • Block, S.M.1    Berg, H.C.2
  • 33
    • 0020398978 scopus 로고
    • Impulse responses in bacterial chemotaxis
    • Block S.M., Segall J.E., and Berg H.C. Impulse responses in bacterial chemotaxis. Cell 31 (1982) 215-226
    • (1982) Cell , vol.31 , pp. 215-226
    • Block, S.M.1    Segall, J.E.2    Berg, H.C.3
  • 34
    • 0006611890 scopus 로고
    • Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer
    • Borkovich K.A., Kaplan N., Hess J.F., and Simon M.I. Transmembrane signal transduction in bacterial chemotaxis involves ligand-dependent activation of phosphate group transfer. Proc. Nat. Acad. Sci. USA 86 (1989) 1208-1212
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 1208-1212
    • Borkovich, K.A.1    Kaplan, N.2    Hess, J.F.3    Simon, M.I.4
  • 35
    • 0025647599 scopus 로고
    • The dynamics of protein phosphorylation in bacterial chemotaxis
    • Borkovich K.A., and Simon M.I. The dynamics of protein phosphorylation in bacterial chemotaxis. Cell 63 (1990) 1339-1348
    • (1990) Cell , vol.63 , pp. 1339-1348
    • Borkovich, K.A.1    Simon, M.I.2
  • 36
    • 0020693765 scopus 로고
    • Structure of the serine chemoreceptor of Escherichia coli
    • Boyd A., Kendall K., and Simon M. Structure of the serine chemoreceptor of Escherichia coli. Nature (London) 301 (1983) 623-626
    • (1983) Nature (London) , vol.301 , pp. 623-626
    • Boyd, A.1    Kendall, K.2    Simon, M.3
  • 37
    • 0020451748 scopus 로고
    • Purification and characterization of Bacillus subtilis methyl-accepting chemotaxis protein methyltransferase II
    • Burgess-Cassler A., Ullah A.H., and Ordal G.W. Purification and characterization of Bacillus subtilis methyl-accepting chemotaxis protein methyltransferase II. J. Biol. Chem. 257 (1982) 8412-8417
    • (1982) J. Biol. Chem. , vol.257 , pp. 8412-8417
    • Burgess-Cassler, A.1    Ullah, A.H.2    Ordal, G.W.3
  • 38
    • 0017841508 scopus 로고
    • Change of waveform in bacterial flagella: the role of mechanics at the molecular level
    • Calladine C.R. Change of waveform in bacterial flagella: the role of mechanics at the molecular level. J. Mol. Biol. 118 (1978) 457-479
    • (1978) J. Mol. Biol. , vol.118 , pp. 457-479
    • Calladine, C.R.1
  • 39
    • 0020437458 scopus 로고
    • Construction of bacterial flagellar filaments, and aspects of their conversion to different helical forms
    • Amos W.B., and Duckett J.G. (Eds), Cambridge University Press, Berlin
    • Calladine C.R. Construction of bacterial flagellar filaments, and aspects of their conversion to different helical forms. In: Amos W.B., and Duckett J.G. (Eds). Prokaryotic and Eukaryotic Flagella (1982), Cambridge University Press, Berlin 33-51
    • (1982) Prokaryotic and Eukaryotic Flagella , pp. 33-51
    • Calladine, C.R.1
  • 40
    • 0018852004 scopus 로고
    • Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: evidence for multiple methylation sites
    • Chelsky D., and Dahlquist F.W. Structural studies of methyl-accepting chemotaxis proteins of Escherichia coli: evidence for multiple methylation sites. Proc. Nat. Acad. Sci. USA 77 (1980) 2434-2438
    • (1980) Proc. Nat. Acad. Sci. USA , vol.77 , pp. 2434-2438
    • Chelsky, D.1    Dahlquist, F.W.2
  • 41
    • 0004262994 scopus 로고
    • Studies in the phototaxis of Rhodospirillum rubrum. II. The relation between phototaxis and photosynthesis
    • Clayton R.K. Studies in the phototaxis of Rhodospirillum rubrum. II. The relation between phototaxis and photosynthesis. Archiv fur Mikrobiologie 19 (1953) 125-140
    • (1953) Archiv fur Mikrobiologie , vol.19 , pp. 125-140
    • Clayton, R.K.1
  • 42
    • 34250960348 scopus 로고
    • Studies in the phototaxis of Rhodospirillum rubrum. I. Action spectrum, growth in green light and Weber-law adherence
    • Clayton R.K. Studies in the phototaxis of Rhodospirillum rubrum. I. Action spectrum, growth in green light and Weber-law adherence. Archiv fur Mikrobiologie 19 (1953) 107-124
    • (1953) Archiv fur Mikrobiologie , vol.19 , pp. 107-124
    • Clayton, R.K.1
  • 43
    • 34250950869 scopus 로고
    • Studies in the phototaxis of Rhodospirillum rubrum. III. Quantitative relationship between stimulus and response
    • Clayton R.K. Studies in the phototaxis of Rhodospirillum rubrum. III. Quantitative relationship between stimulus and response. Archiv fur Mikrobiologie 19 (1953) 141-165
    • (1953) Archiv fur Mikrobiologie , vol.19 , pp. 141-165
    • Clayton, R.K.1
  • 44
    • 0006875828 scopus 로고
    • Patterns of accumulation resulting from taxes and changes in motility of microorganisms
    • Clayton R.K. Patterns of accumulation resulting from taxes and changes in motility of microorganisms. Archiv fur Mikrobiologie 27 (1957) 311-319
    • (1957) Archiv fur Mikrobiologie , vol.27 , pp. 311-319
    • Clayton, R.K.1
  • 45
    • 0000078640 scopus 로고
    • On the interplay of environmental factors affecting taxis and mobility in Rhodospirillum rubrum
    • Clayton R.K. On the interplay of environmental factors affecting taxis and mobility in Rhodospirillum rubrum. Archiv fur Mikrobiologie 29 (1958) 189-212
    • (1958) Archiv fur Mikrobiologie , vol.29 , pp. 189-212
    • Clayton, R.K.1
  • 46
    • 0014115722 scopus 로고
    • Basal organelles of bacterial flagella
    • Cohen-Bazire G., and London J. Basal organelles of bacterial flagella. J. Bacteriol. 94 (1967) 458-465
    • (1967) J. Bacteriol. , vol.94 , pp. 458-465
    • Cohen-Bazire, G.1    London, J.2
  • 47
    • 0018131454 scopus 로고
    • Cell envelope associations of Aquaspirillum serpens flagella
    • Coulton J.W., and Murray R.G.E. Cell envelope associations of Aquaspirillum serpens flagella. J. Bacteriol. 136 (1978) 1037-1049
    • (1978) J. Bacteriol. , vol.136 , pp. 1037-1049
    • Coulton, J.W.1    Murray, R.G.E.2
  • 48
    • 0014974951 scopus 로고
    • Attachment of flagellar basal bodies to the cell envelope: specific attachment to the outer, lipopolysaccharide membrane and the cytoplasmic membrane
    • DePamphilis M.L., and Adler J. Attachment of flagellar basal bodies to the cell envelope: specific attachment to the outer, lipopolysaccharide membrane and the cytoplasmic membrane. J. Bacteriol. 105 (1971) 376-407
    • (1971) J. Bacteriol. , vol.105 , pp. 376-407
    • DePamphilis, M.L.1    Adler, J.2
  • 49
    • 0014979468 scopus 로고
    • Purification of intact flagella from Escherichia coli and Bacillus subtilis
    • DePamphilis M.L., and Adler J. Purification of intact flagella from Escherichia coli and Bacillus subtilis. J. Bacteriol. 105 (1971) 376-383
    • (1971) J. Bacteriol. , vol.105 , pp. 376-383
    • DePamphilis, M.L.1    Adler, J.2
  • 50
    • 0014976040 scopus 로고
    • Fine structure and isolation of the hook-basal body complex from flagella of Escherichia coli and Bacillus subtilis
    • DePamphilis M.L., and Adler J. Fine structure and isolation of the hook-basal body complex from flagella of Escherichia coli and Bacillus subtilis. J. Bacteriol. 105 (1971) 384-395
    • (1971) J. Bacteriol. , vol.105 , pp. 384-395
    • DePamphilis, M.L.1    Adler, J.2
  • 54
    • 0019785232 scopus 로고
    • Bacterial cell envelopes with functional flagella
    • Eisenbach M., and Adler J. Bacterial cell envelopes with functional flagella. J. Biol. Chem. 256 (1981) 8807-8814
    • (1981) J. Biol. Chem. , vol.256 , pp. 8807-8814
    • Eisenbach, M.1    Adler, J.2
  • 56
    • 0000426061 scopus 로고
    • Bacterium photometricum: Ein beitrag zur vergleichenden physiologie des licht und fabensinnes
    • Engelmann T.W. Bacterium photometricum: Ein beitrag zur vergleichenden physiologie des licht und fabensinnes. Pfug. Arch. Gesamte Physiol. Menschen Tiere 42 (1883) 183-186
    • (1883) Pfug. Arch. Gesamte Physiol. Menschen Tiere , vol.42 , pp. 183-186
    • Engelmann, T.W.1
  • 57
    • 76549205541 scopus 로고
    • Further observations on the motility of Proteus vulgaris grown on penicillin agar
    • Fleming A. Further observations on the motility of Proteus vulgaris grown on penicillin agar. J. Gen. Microbiol. 4 (1950) 457-463
    • (1950) J. Gen. Microbiol. , vol.4 , pp. 457-463
    • Fleming, A.1
  • 59
    • 0019357617 scopus 로고
    • A simple method for the isolation of flagellar shape mutants in Salmonella
    • Fujita H., Yamaguchi S., Taira T., and Iino T. A simple method for the isolation of flagellar shape mutants in Salmonella. J. Gen. Microbiol. 125 (1981) 213-216
    • (1981) J. Gen. Microbiol. , vol.125 , pp. 213-216
    • Fujita, H.1    Yamaguchi, S.2    Taira, T.3    Iino, T.4
  • 60
    • 0017835741 scopus 로고
    • The proton pump is a molecular engine of motile bacteria
    • Glagolev A.N., and Skulachev V.P. The proton pump is a molecular engine of motile bacteria. Nature (London) 272 (1978) 280-282
    • (1978) Nature (London) , vol.272 , pp. 280-282
    • Glagolev, A.N.1    Skulachev, V.P.2
  • 61
    • 0021770880 scopus 로고
    • Differential expression and positioning of chemotaxis methylation proteins in Caulobacter
    • Gomes S.L., and Shapiro L. Differential expression and positioning of chemotaxis methylation proteins in Caulobacter. J. Mol. Biol. 178 (1984) 551-568
    • (1984) J. Mol. Biol. , vol.178 , pp. 551-568
    • Gomes, S.L.1    Shapiro, L.2
  • 62
    • 0019950355 scopus 로고
    • Motility and chemotaxis in two strains of Rhizobium with complex flagella
    • Gotz R., Limmer N., Ober K., and Schmitt R. Motility and chemotaxis in two strains of Rhizobium with complex flagella. J. Gen. Microbiol. 128 (1982) 789-798
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 789-798
    • Gotz, R.1    Limmer, N.2    Ober, K.3    Schmitt, R.4
  • 63
    • 0018240590 scopus 로고
    • Failure of sensory adaptation in bacterial mutants that are defective in a protein methylation reaction
    • Goy M.F., Springer M.S., and Adler J. Failure of sensory adaptation in bacterial mutants that are defective in a protein methylation reaction. Cell 15 (1978) 1231-1240
    • (1978) Cell , vol.15 , pp. 1231-1240
    • Goy, M.F.1    Springer, M.S.2    Adler, J.3
  • 64
    • 0017378045 scopus 로고
    • Phototaxis and membrane potential in the photosynthetic bacterium Rhodospirillum rubrum
    • Harayama S. Phototaxis and membrane potential in the photosynthetic bacterium Rhodospirillum rubrum. J. Bacteriol. 131 (1977) 34-41
    • (1977) J. Bacteriol. , vol.131 , pp. 34-41
    • Harayama, S.1
  • 65
    • 0015238086 scopus 로고
    • Role of the galactose binding protein in chemotaxis of Escherichia coli towards galactose
    • Hazelbauer G.L., and Adler J. Role of the galactose binding protein in chemotaxis of Escherichia coli towards galactose. Nature (London) 230 (1971) 101-104
    • (1971) Nature (London) , vol.230 , pp. 101-104
    • Hazelbauer, G.L.1    Adler, J.2
  • 66
    • 0019519886 scopus 로고
    • Multiple forms of methyl-accepting chemotaxis proteins distinguished by a factor in addition to multiple methylation
    • Hazelbauer G.L., and Engstrom P. Multiple forms of methyl-accepting chemotaxis proteins distinguished by a factor in addition to multiple methylation. J. Bacteriol. 145 (1981) 35-42
    • (1981) J. Bacteriol. , vol.145 , pp. 35-42
    • Hazelbauer, G.L.1    Engstrom, P.2
  • 68
    • 0023723766 scopus 로고
    • Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis
    • Hess J.F., Bourret R.B., and Simon M.I. Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis. Nature (London) 336 (1988) 139-143
    • (1988) Nature (London) , vol.336 , pp. 139-143
    • Hess, J.F.1    Bourret, R.B.2    Simon, M.I.3
  • 69
    • 0014515268 scopus 로고
    • Polarity of flagellar growth in Salmonella
    • Iino T. Polarity of flagellar growth in Salmonella. J. Gen. Microbiol. 56 (1969) 227-239
    • (1969) J. Gen. Microbiol. , vol.56 , pp. 227-239
    • Iino, T.1
  • 70
    • 0041483888 scopus 로고
    • Genetic control of flagellar morphogenesis in Salmonella
    • Eisenbach M., and Balaban M. (Eds), Elsevier, Bristol and London
    • Iino T. Genetic control of flagellar morphogenesis in Salmonella. In: Eisenbach M., and Balaban M. (Eds). Sensing and Response in Microorganisms (1985), Elsevier, Bristol and London 83-92
    • (1985) Sensing and Response in Microorganisms , pp. 83-92
    • Iino, T.1
  • 71
    • 0024273804 scopus 로고
    • New unified nomenclature for the flagellar genes of Escherichia coli and Salmonella typhimurium
    • Iino T., Komeda Y., Kutsukake K., et al. New unified nomenclature for the flagellar genes of Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 52 (1988) 533-535
    • (1988) Microbiol. Rev. , vol.52 , pp. 533-535
    • Iino, T.1    Komeda, Y.2    Kutsukake, K.3
  • 72
    • 0020535125 scopus 로고
    • Coordination of flagella on filamentous cells of Escherichia coli
    • Ishihara A., Segall J.E., Block S.M., and Berg H.C. Coordination of flagella on filamentous cells of Escherichia coli. J. Bacteriol. 155 (1983) 228-237
    • (1983) J. Bacteriol. , vol.155 , pp. 228-237
    • Ishihara, A.1    Segall, J.E.2    Block, S.M.3    Berg, H.C.4
  • 73
    • 0020351895 scopus 로고
    • Polymorphic transition in bacterial flagella
    • Amos W.B., and Duckett J.G. (Eds), Cambridge University Press, Amsterdam
    • Kamiya R., Hotani H., and Asakura S. Polymorphic transition in bacterial flagella. In: Amos W.B., and Duckett J.G. (Eds). Prokaryotic and Eukaryotic Flagella (1982), Cambridge University Press, Amsterdam 53-76
    • (1982) Prokaryotic and Eukaryotic Flagella , pp. 53-76
    • Kamiya, R.1    Hotani, H.2    Asakura, S.3
  • 74
    • 0020770030 scopus 로고
    • Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product
    • Kehry M.R., Bond M.W., Hunkapiller M.W., and Dahlquist F.W. Enzymatic deamidation of methyl-accepting chemotaxis proteins in Escherichia coli catalyzed by the cheB gene product. Proc. Nat. Acad. Sci. USA 80 (1983) 3599-3603
    • (1983) Proc. Nat. Acad. Sci. USA , vol.80 , pp. 3599-3603
    • Kehry, M.R.1    Bond, M.W.2    Hunkapiller, M.W.3    Dahlquist, F.W.4
  • 75
    • 0020162182 scopus 로고
    • Adaptation in bacterial chemotaxis: cheB-dependent modification permits additional methylations of sensory transducing proteins
    • Kehry M.R., and Dahlquist F.W. Adaptation in bacterial chemotaxis: cheB-dependent modification permits additional methylations of sensory transducing proteins. Cell 29 (1982) 761-772
    • (1982) Cell , vol.29 , pp. 761-772
    • Kehry, M.R.1    Dahlquist, F.W.2
  • 76
    • 0021162295 scopus 로고
    • Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli
    • Kehry M.R., Doak T.G., and Dahlquist F.W. Stimulus-induced changes in methylesterase activity during chemotaxis in Escherichia coli. J. Biol. Chem. 259 (1984) 11828-11835
    • (1984) J. Biol. Chem. , vol.259 , pp. 11828-11835
    • Kehry, M.R.1    Doak, T.G.2    Dahlquist, F.W.3
  • 77
    • 0026720647 scopus 로고
    • The cytoplasmic component of the bacterial flagellar motor
    • Khan I.H., Reese T.S., and Khan S. The cytoplasmic component of the bacterial flagellar motor. Proc. Nat. Acad. Sci. USA 89 (1992) 5956-5960
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , pp. 5956-5960
    • Khan, I.H.1    Reese, T.S.2    Khan, S.3
  • 78
    • 0020728661 scopus 로고
    • Isotope and thermal effects in chemiosmotic coupling to the flagellar motor of Streptococcus
    • Khan S., and Berg H.C. Isotope and thermal effects in chemiosmotic coupling to the flagellar motor of Streptococcus. Cell 32 (1983) 913-919
    • (1983) Cell , vol.32 , pp. 913-919
    • Khan, S.1    Berg, H.C.2
  • 79
    • 0023750050 scopus 로고
    • Effects of mot gene expression on the structure of the flagellar motor
    • Khan S., Dapice M., and Reese T.S. Effects of mot gene expression on the structure of the flagellar motor. J. Mol. Biol. 202 (1988) 575-584
    • (1988) J. Mol. Biol. , vol.202 , pp. 575-584
    • Khan, S.1    Dapice, M.2    Reese, T.S.3
  • 80
    • 0021882438 scopus 로고
    • Constraints on flagellar rotation
    • Khan S., Meister M., and Berg H.C. Constraints on flagellar rotation. J. Mol. Biol. 184 (1985) 645-656
    • (1985) J. Mol. Biol. , vol.184 , pp. 645-656
    • Khan, S.1    Meister, M.2    Berg, H.C.3
  • 81
    • 0017392255 scopus 로고
    • Isolation of a glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis
    • Kleene S.J., Toews M.L., and Adler J. Isolation of a glutamic acid methyl ester from an Escherichia coli membrane protein involved in chemotaxis. J. Biol. Chem. 252 (1977) 3214-3218
    • (1977) J. Biol. Chem. , vol.252 , pp. 3214-3218
    • Kleene, S.J.1    Toews, M.L.2    Adler, J.3
  • 82
    • 0025284633 scopus 로고
    • Coupling of proton flow and rotation in the bacterial flagellar motor: stochastic simulation of a microscopic model
    • Kleutsch B., and Lauger P. Coupling of proton flow and rotation in the bacterial flagellar motor: stochastic simulation of a microscopic model. Eur. Biophys. J. 18 (1990) 175-191
    • (1990) Eur. Biophys. J. , vol.18 , pp. 175-191
    • Kleutsch, B.1    Lauger, P.2
  • 83
    • 0004258020 scopus 로고
    • Methylation of a membrane protein involved in bacterial chemotaxis
    • Kort E.N., Goy M.F., Larsen S.H., and Adler J. Methylation of a membrane protein involved in bacterial chemotaxis. Proc. Nat. Acad. Sci. USA 72 (1972) 3939-3943
    • (1972) Proc. Nat. Acad. Sci. USA , vol.72 , pp. 3939-3943
    • Kort, E.N.1    Goy, M.F.2    Larsen, S.H.3    Adler, J.4
  • 84
    • 0023116688 scopus 로고
    • Roles of cheY and cheZ gene products in controlling flagellar rotation in bacterial chemotaxis in Escherichia coli
    • Kuo S.C., and Koshland D.E.J. Roles of cheY and cheZ gene products in controlling flagellar rotation in bacterial chemotaxis in Escherichia coli. J. Bacteriol. 169 (1987) 1307-1314
    • (1987) J. Bacteriol. , vol.169 , pp. 1307-1314
    • Kuo, S.C.1    Koshland, D.E.J.2
  • 86
    • 0016219080 scopus 로고
    • Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria
    • Larsen S.H., Adler J., Gargus J.J., and Hogg R.W. Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria. Proc. Nat. Acad. Sci. USA 71 (1974) 1239-1243
    • (1974) Proc. Nat. Acad. Sci. USA , vol.71 , pp. 1239-1243
    • Larsen, S.H.1    Adler, J.2    Gargus, J.J.3    Hogg, R.W.4
  • 87
    • 0016345728 scopus 로고
    • Change in direction of flagellar rotation is the basis of the chemotactic response in Escherichia coli
    • Larsen S.H., Reader R.W., Kort E.N., Tso W., and Adler J. Change in direction of flagellar rotation is the basis of the chemotactic response in Escherichia coli. Nature (London) 249 (1974) 74-77
    • (1974) Nature (London) , vol.249 , pp. 74-77
    • Larsen, S.H.1    Reader, R.W.2    Kort, E.N.3    Tso, W.4    Adler, J.5
  • 88
    • 0017384266 scopus 로고
    • Ion transport and the rotation of bacterial flagella
    • Lauger P. Ion transport and the rotation of bacterial flagella. Nature (London) 268 (1977) 360-361
    • (1977) Nature (London) , vol.268 , pp. 360-361
    • Lauger, P.1
  • 89
    • 0026317733 scopus 로고
    • Genetic evidence for interaction between the CheW and Tsr proteins during chemoreceptor signalling by Escherichia coli
    • Liu J., and Parkinson J.S. Genetic evidence for interaction between the CheW and Tsr proteins during chemoreceptor signalling by Escherichia coli. J. Bacteriol. 173 (1991) 4941-4951
    • (1991) J. Bacteriol. , vol.173 , pp. 4941-4951
    • Liu, J.1    Parkinson, J.S.2
  • 90
    • 0024316868 scopus 로고
    • Role of CheW protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis
    • Lui J., and Parkinson J.S. Role of CheW protein in coupling membrane receptors to the intracellular signaling system of bacterial chemotaxis. Proc. Nat. Acad. Sci. USA 86 (1989) 8703-8707
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 8703-8707
    • Lui, J.1    Parkinson, J.S.2
  • 91
    • 0023128224 scopus 로고
    • Rapid rotation of flagellar bundles in swimming bacteria
    • Lowe G., Meister M., and Berg H.C. Rapid rotation of flagellar bundles in swimming bacteria. Nature (London) 325 (1987) 637-640
    • (1987) Nature (London) , vol.325 , pp. 637-640
    • Lowe, G.1    Meister, M.2    Berg, H.C.3
  • 92
    • 0017132660 scopus 로고
    • Examination of bacterial flagellation by dark-field microscopy
    • Macnab R.M. Examination of bacterial flagellation by dark-field microscopy. J. Clin. Microbiol. 4 (1976) 258-265
    • (1976) J. Clin. Microbiol. , vol.4 , pp. 258-265
    • Macnab, R.M.1
  • 93
    • 0009481832 scopus 로고
    • Bacterial flagella rotating in bundles: a study in helical geometry
    • Macnab R.M. Bacterial flagella rotating in bundles: a study in helical geometry. Proc. Nat. Acad. Sci. USA 74 (1977) 221-225
    • (1977) Proc. Nat. Acad. Sci. USA , vol.74 , pp. 221-225
    • Macnab, R.M.1
  • 94
    • 0000558342 scopus 로고
    • Biology of the chemotactic reponse
    • Neidhardt F.C. (Ed), Amer. Soc. Microbiol., Cambridge, U.K.
    • Macnab R.M. Biology of the chemotactic reponse. In: Neidhardt F.C. (Ed). E. coli and Salmonella typhimurium (1987), Amer. Soc. Microbiol., Cambridge, U.K. 732-759
    • (1987) E. coli and Salmonella typhimurium , pp. 732-759
    • Macnab, R.M.1
  • 95
    • 0005817694 scopus 로고
    • Genetics, structure, and assembly of the bacterial flagellum
    • Armitage J.P., and Lackie J.M. (Eds), CUP, Washington, DC
    • Macnab R.M. Genetics, structure, and assembly of the bacterial flagellum. In: Armitage J.P., and Lackie J.M. (Eds). Biology of the Chemotactic Response (1990), CUP, Washington, DC 77-107
    • (1990) Biology of the Chemotactic Response , pp. 77-107
    • Macnab, R.M.1
  • 96
    • 0020671884 scopus 로고
    • Asynchronous switching of flagellar motors on a single cell
    • Macnab R.M., and Han D.P. Asynchronous switching of flagellar motors on a single cell. Cell 32 (1983) 109-117
    • (1983) Cell , vol.32 , pp. 109-117
    • Macnab, R.M.1    Han, D.P.2
  • 97
    • 0018426004 scopus 로고
    • Thermosensory transduction in Escherichia coli: inhibition of the thermosensory response by L-serine
    • Maeda K., and Imae Y. Thermosensory transduction in Escherichia coli: inhibition of the thermosensory response by L-serine. Proc. Nat. Acad. Sci. USA 76 (1979) 91-95
    • (1979) Proc. Nat. Acad. Sci. USA , vol.76 , pp. 91-95
    • Maeda, K.1    Imae, Y.2
  • 99
    • 0002586889 scopus 로고
    • Phototaxis in the purple bacterium Rhodospirillum rubrum and the relationship between phototaxis and photosynthesis
    • Manten A. Phototaxis in the purple bacterium Rhodospirillum rubrum and the relationship between phototaxis and photosynthesis. Ant. van Leeuw. 14 (1948) 65-86
    • (1948) Ant. van Leeuw. , vol.14 , pp. 65-86
    • Manten, A.1
  • 100
    • 0004867816 scopus 로고
    • "Frizzy" aggregation genes of the gliding bacterium Myxococcus xanthus show sequence similarities to the chemotaxis genes of enteric bacteria
    • McBride M.J., Weinberg R.A., and Zusman D.R. "Frizzy" aggregation genes of the gliding bacterium Myxococcus xanthus show sequence similarities to the chemotaxis genes of enteric bacteria. Proc. Nat. Acad. Sci. USA 86 (1989) 424-428
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 424-428
    • McBride, M.J.1    Weinberg, R.A.2    Zusman, D.R.3
  • 101
    • 0023405067 scopus 로고
    • The stall torque of the bacterial flagellar motor
    • Meister M., and Berg H.C. The stall torque of the bacterial flagellar motor. Biophysical J 52 (1987) 413-419
    • (1987) Biophysical J , vol.52 , pp. 413-419
    • Meister, M.1    Berg, H.C.2
  • 102
    • 0024670659 scopus 로고
    • Dynamics of a tightly coupled mechanism for flagellar rotation
    • Meister M., Caplan S.R., and Berg H.C. Dynamics of a tightly coupled mechanism for flagellar rotation. Biophysical J 55 (1989) 905-914
    • (1989) Biophysical J , vol.55 , pp. 905-914
    • Meister, M.1    Caplan, S.R.2    Berg, H.C.3
  • 103
    • 0023644878 scopus 로고
    • The proton flux through the bacterial flagellar motor
    • Meister M., Lowe G., and Berg H.C. The proton flux through the bacterial flagellar motor. Cell 49 (1987) 643-650
    • (1987) Cell , vol.49 , pp. 643-650
    • Meister, M.1    Lowe, G.2    Berg, H.C.3
  • 104
    • 0015413647 scopus 로고
    • Chemotaxis towards amino acids in Escherichia coli
    • Mesibov R., and Adler J. Chemotaxis towards amino acids in Escherichia coli. J. Bacteriol. 112 (1972) 315-326
    • (1972) J. Bacteriol. , vol.112 , pp. 315-326
    • Mesibov, R.1    Adler, J.2
  • 105
    • 0023917333 scopus 로고
    • Site-directed cross-linking: Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis
    • Milligan D.L., and Koshland D.E.J. Site-directed cross-linking: Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. J. Biol. Chem. 263 (1988) 6268-6275
    • (1988) J. Biol. Chem. , vol.263 , pp. 6268-6275
    • Milligan, D.L.1    Koshland, D.E.J.2
  • 106
    • 0013647655 scopus 로고
    • Hypothetical thermokinetic and electrokinetic mechanisms of locomotion in microorganisms
    • Mitchell P. Hypothetical thermokinetic and electrokinetic mechanisms of locomotion in microorganisms. Proc. Roys. Phys. Soc. (Edinburgh) 25 (1956) 32-34
    • (1956) Proc. Roys. Phys. Soc. (Edinburgh) , vol.25 , pp. 32-34
    • Mitchell, P.1
  • 107
    • 0000266432 scopus 로고
    • Bacterial flagellar motors and osmoelectric molecular motion by an axially transmembrane well and turnstile mechanism
    • Mitchell P. Bacterial flagellar motors and osmoelectric molecular motion by an axially transmembrane well and turnstile mechanism. FEBS Lett 176 (1984) 287-294
    • (1984) FEBS Lett , vol.176 , pp. 287-294
    • Mitchell, P.1
  • 108
    • 0022179404 scopus 로고
    • Proteolytic fragments identified with domains of the aspartate chemoreceptor
    • Mowbray S.L., Foster D.L., and Koshland D.E.J. Proteolytic fragments identified with domains of the aspartate chemoreceptor. J. Biol. Chem. 260 (1985) 11711-11718
    • (1985) J. Biol. Chem. , vol.260 , pp. 11711-11718
    • Mowbray, S.L.1    Foster, D.L.2    Koshland, D.E.J.3
  • 109
    • 0026060881 scopus 로고
    • Thermosensing ability of Trg and Tap chemoreceptors in Escherichia coli
    • Nara T., Lee L., and Imae Y. Thermosensing ability of Trg and Tap chemoreceptors in Escherichia coli. J. Bacteriol. 173 (1991) 1120-1124
    • (1991) J. Bacteriol. , vol.173 , pp. 1120-1124
    • Nara, T.1    Lee, L.2    Imae, Y.3
  • 110
    • 0024568384 scopus 로고
    • Functional homology of chemotactic methylesterases from Bacillus subtilis and Escherichia coli
    • Nettleton D.O., and Ordal G.W. Functional homology of chemotactic methylesterases from Bacillus subtilis and Escherichia coli. J. Bacteriol. 171 (1989) 120-123
    • (1989) J. Bacteriol. , vol.171 , pp. 120-123
    • Nettleton, D.O.1    Ordal, G.W.2
  • 111
    • 0021846091 scopus 로고
    • Chemotactic transducer proteins of Escherichia coli exhibit homology with methyl-accepting proteins from distantly related bacteria
    • Nowlin D.W., Nettleton D.O., Ordal G.W., and Hazelbauer G.L. Chemotactic transducer proteins of Escherichia coli exhibit homology with methyl-accepting proteins from distantly related bacteria. J. Bacteriol. 163 (1985) 262-266
    • (1985) J. Bacteriol. , vol.163 , pp. 262-266
    • Nowlin, D.W.1    Nettleton, D.O.2    Ordal, G.W.3    Hazelbauer, G.L.4
  • 112
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt D., and Stoeckenius W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature (London) 233 (1971) 149-152
    • (1971) Nature (London) , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 113
    • 0015973775 scopus 로고
    • Isolation and complementation of mutants in galactose taxis and transport
    • Ordal G.W., and Adler J. Isolation and complementation of mutants in galactose taxis and transport. J. Bacteriol. 117 (1974) 509-516
    • (1974) J. Bacteriol. , vol.117 , pp. 509-516
    • Ordal, G.W.1    Adler, J.2
  • 114
    • 0019123531 scopus 로고
    • Novel mutations affecting a signalling component for chemotaxis of Escherichia coli
    • Parkinson J.S. Novel mutations affecting a signalling component for chemotaxis of Escherichia coli. J. Bacteriol. 142 (1980) 953-961
    • (1980) J. Bacteriol. , vol.142 , pp. 953-961
    • Parkinson, J.S.1
  • 115
    • 0020504891 scopus 로고
    • Interaction between chemotaxis genes and flagellar genes in Escherichia coli
    • Parkinson J.S., Parker S.R., Talbert P.B., and Houts S.E. Interaction between chemotaxis genes and flagellar genes in Escherichia coli. J. Bacteriol. 155 (1983) 265-274
    • (1983) J. Bacteriol. , vol.155 , pp. 265-274
    • Parkinson, J.S.1    Parker, S.R.2    Talbert, P.B.3    Houts, S.E.4
  • 116
    • 0024281416 scopus 로고
    • Protein phosphorylation in bacterial chemotaxis
    • Parkinson J.S. Protein phosphorylation in bacterial chemotaxis. Cell 53 (1988) 1-2
    • (1988) Cell , vol.53 , pp. 1-2
    • Parkinson, J.S.1
  • 117
    • 84909654149 scopus 로고
    • Bacterial chemotaxis: molecular genetics of sensory transduction and chemotactic gene expression
    • Cold Spring Harbor, NY. Beckwith J., Davies J.E., and Gallant J.A. (Eds)
    • Cold Spring Harbor, NY. Parkinson J.S., and Hazelbauer G.L. Bacterial chemotaxis: molecular genetics of sensory transduction and chemotactic gene expression. In: Beckwith J., Davies J.E., and Gallant J.A. (Eds). Gene Function in Prokaryotes (1983) 293-318
    • (1983) Gene Function in Prokaryotes , pp. 293-318
    • Parkinson, J.S.1    Hazelbauer, G.L.2
  • 118
    • 0018221367 scopus 로고
    • Sensory adaptation mutants of E. coli
    • Parkinson J.S., and Revello P.T. Sensory adaptation mutants of E. coli. Cell 15 (1978) 1221-1230
    • (1978) Cell , vol.15 , pp. 1221-1230
    • Parkinson, J.S.1    Revello, P.T.2
  • 120
    • 0004263020 scopus 로고
    • Bacterial flagella and motility
    • Pijper A. Bacterial flagella and motility. Nature (London) 161 (1948) 200-201
    • (1948) Nature (London) , vol.161 , pp. 200-201
    • Pijper, A.1
  • 121
    • 33750129784 scopus 로고
    • Bacterial flagella
    • Pijper A. Bacterial flagella. Nature (London) 168 (1951) 749-750
    • (1951) Nature (London) , vol.168 , pp. 749-750
    • Pijper, A.1
  • 122
    • 0343247695 scopus 로고
    • Shape of bacterial flagella
    • Pijper A. Shape of bacterial flagella. Nature (London) 175 (1955) 214-215
    • (1955) Nature (London) , vol.175 , pp. 214-215
    • Pijper, A.1
  • 123
    • 0017035296 scopus 로고
    • Survival value of chemotaxis in mixed cultures
    • Pilgram W.K., and Williams F.D. Survival value of chemotaxis in mixed cultures. Canad. J. Microbiol. 22 (1976) 1771-1773
    • (1976) Canad. J. Microbiol. , vol.22 , pp. 1771-1773
    • Pilgram, W.K.1    Williams, F.D.2
  • 124
    • 0024222177 scopus 로고
    • Motility response of Rhodobacter sphaeroides to chemotactic stimulation
    • Poole P.S., and Armitage J.P. Motility response of Rhodobacter sphaeroides to chemotactic stimulation. J. Bacteriol. 170 (1988) 5673-5679
    • (1988) J. Bacteriol. , vol.170 , pp. 5673-5679
    • Poole, P.S.1    Armitage, J.P.2
  • 125
    • 0024671717 scopus 로고
    • Role of metabolism in the chemotactic response of Rhodobacter sphaeroides to ammonia
    • Poole P.S., and Armitage J.P. Role of metabolism in the chemotactic response of Rhodobacter sphaeroides to ammonia. J. Bacteriol. 171 (1989) 2900-2902
    • (1989) J. Bacteriol. , vol.171 , pp. 2900-2902
    • Poole, P.S.1    Armitage, J.P.2
  • 126
    • 0021136238 scopus 로고
    • Direction of flagellar rotation in bacterial cell envelopes
    • Ravid S., and Eisenbach M. Direction of flagellar rotation in bacterial cell envelopes. J. Bacteriol. 158 (1984) 222-230
    • (1984) J. Bacteriol. , vol.158 , pp. 222-230
    • Ravid, S.1    Eisenbach, M.2
  • 127
    • 0039515450 scopus 로고
    • Restoration of flagellar clockwise rotation in bacterial envelopes by insertion of the chemotaxis protein CheY
    • Ravid S., Matsumura P., and Eisenbach M. Restoration of flagellar clockwise rotation in bacterial envelopes by insertion of the chemotaxis protein CheY. Proc. Nat. Acad. Sci. USA 83 (1986) 7157-7161
    • (1986) Proc. Nat. Acad. Sci. USA , vol.83 , pp. 7157-7161
    • Ravid, S.1    Matsumura, P.2    Eisenbach, M.3
  • 128
    • 0019136731 scopus 로고
    • Methylation of chemotaxis-specific proteins in Escherichia coli cells permeable to S-adenosyl methionine
    • Rollins C.M., and Dahlquist F.W. Methylation of chemotaxis-specific proteins in Escherichia coli cells permeable to S-adenosyl methionine. Biochemistry 19 (1980) 4627-4632
    • (1980) Biochemistry , vol.19 , pp. 4627-4632
    • Rollins, C.M.1    Dahlquist, F.W.2
  • 129
    • 0021919409 scopus 로고
    • Chemotactic signalling in filamentous cells of Escherichia coli
    • Segall J.E., Ishihara A., and Berg H.C. Chemotactic signalling in filamentous cells of Escherichia coli. J. Bacteriol. 161 (1985) 51-59
    • (1985) J. Bacteriol. , vol.161 , pp. 51-59
    • Segall, J.E.1    Ishihara, A.2    Berg, H.C.3
  • 130
    • 0024365923 scopus 로고
    • The molecular genetics of differentiation
    • Shapiro E., Shapiro B., and Shapiro L. The molecular genetics of differentiation. Genetics 123 (1989) 427-429
    • (1989) Genetics , vol.123 , pp. 427-429
    • Shapiro, E.1    Shapiro, B.2    Shapiro, L.3
  • 131
    • 0017222316 scopus 로고
    • Differentiation in the Caulobacter cell cycle
    • Shapiro L. Differentiation in the Caulobacter cell cycle. Annu. Rev. Microbiol. 30 (1976) 377-407
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 377-407
    • Shapiro, L.1
  • 132
    • 0019810611 scopus 로고
    • Posttranslational processing of methyl-accepting chemotaxis proteins in Escherichia coli
    • Sherris D., and Parkinson J.S. Posttranslational processing of methyl-accepting chemotaxis proteins in Escherichia coli. Proc. Nat. Acad. Sci. USA 78 (1981) 6051-6055
    • (1981) Proc. Nat. Acad. Sci. USA , vol.78 , pp. 6051-6055
    • Sherris, D.1    Parkinson, J.S.2
  • 133
    • 0016351193 scopus 로고
    • Flagellar rotation and the mechanism of bacterial motility
    • Silverman M., and Simon M. Flagellar rotation and the mechanism of bacterial motility. Nature (London) 249 (1974) 73-74
    • (1974) Nature (London) , vol.249 , pp. 73-74
    • Silverman, M.1    Simon, M.2
  • 134
    • 0017722425 scopus 로고
    • Identification of polypeptides necessary for chemotaxis in Escherichia coli
    • Silverman M., and Simon M. Identification of polypeptides necessary for chemotaxis in Escherichia coli. J. Bacteriol. 130 (1977) 1317-1325
    • (1977) J. Bacteriol. , vol.130 , pp. 1317-1325
    • Silverman, M.1    Simon, M.2
  • 135
    • 0017718458 scopus 로고
    • Chemotaxis in Escherichia coli: methylation of the che gene products
    • Silverman M., and Simon M. Chemotaxis in Escherichia coli: methylation of the che gene products. Proc. Nat. Acad. Sci. USA 74 (1977) 3317-3321
    • (1977) Proc. Nat. Acad. Sci. USA , vol.74 , pp. 3317-3321
    • Silverman, M.1    Simon, M.2
  • 136
    • 0023517745 scopus 로고
    • Methylation-independent and methylation-dependent chemotaxis in Rhodobacter sphaeroides and Rhodospirillum rubrum
    • Sockett R.E., Armitage J.P., and Evans M.C.W. Methylation-independent and methylation-dependent chemotaxis in Rhodobacter sphaeroides and Rhodospirillum rubrum. J. Bacteriol. 169 (1987) 5808-5814
    • (1987) J. Bacteriol. , vol.169 , pp. 5808-5814
    • Sockett, R.E.1    Armitage, J.P.2    Evans, M.C.W.3
  • 137
    • 0024741720 scopus 로고
    • Sensory rhodopsin I and II modulate a methylation/demethylation system in Halobacterium halobium
    • Spudich E.N., Takahashi T., and Spudich J.L. Sensory rhodopsin I and II modulate a methylation/demethylation system in Halobacterium halobium. Proc. Nat. Acad. Sci. USA 86 (1989) 7746-7750
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 7746-7750
    • Spudich, E.N.1    Takahashi, T.2    Spudich, J.L.3
  • 138
    • 0021756564 scopus 로고
    • Mechanism of colour discrimination by a bacterial sensory rhodopsin
    • Spudich J.L., and Bogomolni R.A. Mechanism of colour discrimination by a bacterial sensory rhodopsin. Nature (London) 312 (1984) 509-513
    • (1984) Nature (London) , vol.312 , pp. 509-513
    • Spudich, J.L.1    Bogomolni, R.A.2
  • 139
    • 0022531430 scopus 로고
    • Nucleotide sequence of the Escherichia coli motB gene and site limited incorporation of its product into the cytoplasmic membrane
    • Stader J., Matsumura P., Vacante D., Dean G.E., and Macnab R.M. Nucleotide sequence of the Escherichia coli motB gene and site limited incorporation of its product into the cytoplasmic membrane. J. Bacteriol. 166 (1986) 244-252
    • (1986) J. Bacteriol. , vol.166 , pp. 244-252
    • Stader, J.1    Matsumura, P.2    Vacante, D.3    Dean, G.E.4    Macnab, R.M.5
  • 141
    • 0024562159 scopus 로고
    • Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis
    • Stock A.M., Mottonen J.M., Stock J.B., and Schutt C.E. Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis. Nature (London) 337 (1989) 745-749
    • (1989) Nature (London) , vol.337 , pp. 745-749
    • Stock, A.M.1    Mottonen, J.M.2    Stock, J.B.3    Schutt, C.E.4
  • 142
    • 0023203997 scopus 로고
    • Purification and characterization of the CheZ protein of bacterial chemotaxis
    • Stock A.M., and Stock J.B. Purification and characterization of the CheZ protein of bacterial chemotaxis. J. Bacteriol. 169 (1987) 3301-3311
    • (1987) J. Bacteriol. , vol.169 , pp. 3301-3311
    • Stock, A.M.1    Stock, J.B.2
  • 143
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock J.B., Ninfa A.J., and Stock A.M. Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol. Rev. 53 (1989) 450-490
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 144
    • 0007526113 scopus 로고    scopus 로고
    • Strick J. Isis 87 (1996) 274-305
    • (1996) Isis , vol.87 , pp. 274-305
    • Strick, J.1
  • 145
    • 0017808121 scopus 로고
    • Incomplete flagellar structures in non-flagellate mutants of Salmonella typhimurium
    • Suzuki T., Iino T., Horiguchi T., and Yamaguchi S. Incomplete flagellar structures in non-flagellate mutants of Salmonella typhimurium. J. Bacteriol. 133 (1978) 904-915
    • (1978) J. Bacteriol. , vol.133 , pp. 904-915
    • Suzuki, T.1    Iino, T.2    Horiguchi, T.3    Yamaguchi, S.4
  • 146
    • 0025024705 scopus 로고
    • Color regulation in the archaebacterial phototaxis receptor phoborhodopsin (sensory rhodopsin II)
    • Takahashi T., Yan B., Mazur P., Derguini F., Nakanishi K., and Spudich J.L. Color regulation in the archaebacterial phototaxis receptor phoborhodopsin (sensory rhodopsin II). Biochemistry 29 (1990) 8467-8474
    • (1990) Biochemistry , vol.29 , pp. 8467-8474
    • Takahashi, T.1    Yan, B.2    Mazur, P.3    Derguini, F.4    Nakanishi, K.5    Spudich, J.L.6
  • 147
    • 0000767299 scopus 로고
    • Attractants and repellents control demethylation of methylated chemotaxis proteins in Escherichia coli
    • Toews M.L., Goy M.F., Springer M.S., and Adler J. Attractants and repellents control demethylation of methylated chemotaxis proteins in Escherichia coli. Proc. Nat. Acad. Sci. USA 76 (1979) 5544-5548
    • (1979) Proc. Nat. Acad. Sci. USA , vol.76 , pp. 5544-5548
    • Toews, M.L.1    Goy, M.F.2    Springer, M.S.3    Adler, J.4
  • 148
    • 0018800404 scopus 로고
    • Methanol formation in vivo from methylated chemotaxis proteins in Escherichia coli
    • Toews M.L., and Adler J. Methanol formation in vivo from methylated chemotaxis proteins in Escherichia coli. J. Biol. Chem. 254 (1979) 1761-1764
    • (1979) J. Biol. Chem. , vol.254 , pp. 1761-1764
    • Toews, M.L.1    Adler, J.2
  • 149
    • 0023644892 scopus 로고
    • Three-dimensional structure of the frozen-hydrated flagellar filament: The left-handed filament of Salmonella typhimurium
    • Trachtenberg S., and DeRosier D.J. Three-dimensional structure of the frozen-hydrated flagellar filament: The left-handed filament of Salmonella typhimurium. J. Mol. Biol. 195 (1987) 581-601
    • (1987) J. Mol. Biol. , vol.195 , pp. 581-601
    • Trachtenberg, S.1    DeRosier, D.J.2
  • 150
    • 0015888205 scopus 로고
    • Common mechanism for repellents and attractants in bacterial chemotaxis
    • Tsang N., Macnab R.M., and Koshland D.E.J. Common mechanism for repellents and attractants in bacterial chemotaxis. Science 181 (1973) 60-63
    • (1973) Science , vol.181 , pp. 60-63
    • Tsang, N.1    Macnab, R.M.2    Koshland, D.E.J.3
  • 151
    • 0026792838 scopus 로고
    • M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF
    • Ueno T., Oosawa K., and Aizawa S.-I. M ring, S ring and proximal rod of the flagellar basal body of Salmonella typhimurium are composed of subunits of a single protein, FliF. J. Mol. Biol. 227 (1992) 672-677
    • (1992) J. Mol. Biol. , vol.227 , pp. 672-677
    • Ueno, T.1    Oosawa, K.2    Aizawa, S.-I.3
  • 152
    • 0019422223 scopus 로고
    • In vivo and in vitro chemotactic methylation in Bacillus subtilis
    • Ullah A.H.J., and Ordal G.W. In vivo and in vitro chemotactic methylation in Bacillus subtilis. J. Bacteriol. 145 (1981) 958-965
    • (1981) J. Bacteriol. , vol.145 , pp. 958-965
    • Ullah, A.H.J.1    Ordal, G.W.2
  • 153
    • 0022550998 scopus 로고
    • A plausible mechanism for flagellar rotation
    • Wagenknecht T. A plausible mechanism for flagellar rotation. FEBS Lett. 196 (1986) 193-197
    • (1986) FEBS Lett. , vol.196 , pp. 193-197
    • Wagenknecht, T.1
  • 154
    • 33750130334 scopus 로고
    • Movement of bacterial flagella
    • Weibull C. Movement of bacterial flagella. Nature (London) 167 (1951) 511-512
    • (1951) Nature (London) , vol.167 , pp. 511-512
    • Weibull, C.1
  • 155
    • 0000527523 scopus 로고
    • Movement
    • Gunsalus I.C., and Stanier R.Y. (Eds), Academic Press, London
    • Weibull C. Movement. In: Gunsalus I.C., and Stanier R.Y. (Eds). The Bacteria: A Treatise on Structure and Function (1960), Academic Press, London 153-205
    • (1960) The Bacteria: A Treatise on Structure and Function , pp. 153-205
    • Weibull, C.1
  • 156
    • 0023213791 scopus 로고
    • Reconstitution of signalling in bacterial chemotaxis
    • Wolfe A.J., Conley M.P., Kramer T.J., and Berg H.C. Reconstitution of signalling in bacterial chemotaxis. J. Bacteriol. 169 (1987) 1878-1885
    • (1987) J. Bacteriol. , vol.169 , pp. 1878-1885
    • Wolfe, A.J.1    Conley, M.P.2    Kramer, T.J.3    Berg, H.C.4
  • 157
    • 0007809063 scopus 로고
    • Migration of Bacteria in Semisolid Agar
    • Wolfe A.J., and Berg H.C. Migration of Bacteria in Semisolid Agar. Proc. Nat. Acad. Sci. USA 86 (1989) 6973-6977
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 6973-6977
    • Wolfe, A.J.1    Berg, H.C.2
  • 158
    • 0022790908 scopus 로고
    • Color discrimination in halobacteria: spectroscopic characterisation of a second sensory receptor covering the blue-green region of the spectrum
    • Wolfe E., Bogomolni R., Scherrer P., Hess B., and Stoeckenius W. Color discrimination in halobacteria: spectroscopic characterisation of a second sensory receptor covering the blue-green region of the spectrum. Proc. Nat. Acad. Sci. USA 83 (1986) 7272-7276
    • (1986) Proc. Nat. Acad. Sci. USA , vol.83 , pp. 7272-7276
    • Wolfe, E.1    Bogomolni, R.2    Scherrer, P.3    Hess, B.4    Stoeckenius, W.5
  • 159
    • 0022454124 scopus 로고
    • Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching
    • Yamaguchi S., Fujita H., Ishihara A., Aizawa S.-I., and Macnab R.M. Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching. J. Bacteriol. 166 (1986) 187-193
    • (1986) J. Bacteriol. , vol.166 , pp. 187-193
    • Yamaguchi, S.1    Fujita, H.2    Ishihara, A.3    Aizawa, S.-I.4    Macnab, R.M.5
  • 160
    • 0021083453 scopus 로고
    • Requirement of the cheB function for sensory adaptation in Escherichia coli
    • Yonekawa H., Hayashi H., and Parkinson J.S. Requirement of the cheB function for sensory adaptation in Escherichia coli. J. Bacteriol. 156 (1983) 1228-1235
    • (1983) J. Bacteriol. , vol.156 , pp. 1228-1235
    • Yonekawa, H.1    Hayashi, H.2    Parkinson, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.