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Volumn 178, Issue 13, 1996, Pages 3677-3682

Calcium signalling in bacteria

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIHYDRO 2,6 DIMETHYL 5 NITRO 4 [2 (TRIFLUOROMETHYL)PHENYL] 3 PYRIDINECARBOXYLIC ACID METHYL ESTER; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM CHANNEL; CALCIUM ION; CALMODULIN; DIHYDROPYRIDINE; LANTHANUM; PHENYLALKYLAMINE; PROTEIN KINASE (CALCIUM,CALMODULIN);

EID: 0029976581     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.13.3677-3682.1996     Document Type: Short Survey
Times cited : (199)

References (89)
  • 3
    • 0028230588 scopus 로고
    • Physiological concentration of magnesium ions induces a strong macroscopic curvature in GGGCCC-containing DNA
    • Bruckner, I., S. Susic, M. Dlakic, A. Savic, and S. Pongor. 1994. Physiological concentration of magnesium ions induces a strong macroscopic curvature in GGGCCC-containing DNA. J. Mol. Biol. 236:26-32.
    • (1994) J. Mol. Biol. , vol.236 , pp. 26-32
    • Bruckner, I.1    Susic, S.2    Dlakic, M.3    Savic, A.4    Pongor, S.5
  • 4
    • 0024421347 scopus 로고
    • △dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures
    • Bukau, B., and G. C. Walker. 1989. △dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures. J. Bacteriol. 171:6030-6038.
    • (1989) J. Bacteriol. , vol.171 , pp. 6030-6038
    • Bukau, B.1    Walker, G.C.2
  • 5
    • 0029073731 scopus 로고
    • Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes
    • Burland, V., G. Plunkett III, H. J. Sofia, D. L. Daniels, and F. R. Blattner. 1995. Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 23:2105-2119.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2105-2119
    • Burland, V.1    Plunkett III, G.2    Sofia, H.J.3    Daniels, D.L.4    Blattner, F.R.5
  • 6
    • 0026517218 scopus 로고
    • Prokaryotic calcium-binding protein of the calmodulin superfamily-calcium binding to a Saccharopolyspora erythraea 20 kDa protein
    • Bylsma, N., T. Drakenburg, I. Andersson, P. F. Leadlay, and S. Forcen. 1992. Prokaryotic calcium-binding protein of the calmodulin superfamily-calcium binding to a Saccharopolyspora erythraea 20 kDa protein. FEBS Lett. 299:44-47.
    • (1992) FEBS Lett. , vol.299 , pp. 44-47
    • Bylsma, N.1    Drakenburg, T.2    Andersson, I.3    Leadlay, P.F.4    Forcen, S.5
  • 8
    • 0023069451 scopus 로고
    • Intracellular calcium homeostasis
    • Carafoli, E. 1987. Intracellular calcium homeostasis. Annu. Rev. Biochem. 56:395-433.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 395-433
    • Carafoli, E.1
  • 10
    • 0029025311 scopus 로고
    • Inorganic polyphosphates in the acquisition of competence in Escherichia coli
    • Castuma, C. E., R. Huang, A. Kornberg, and R. N. Reusch. 1995. Inorganic polyphosphates in the acquisition of competence in Escherichia coli. J. Biol. Chem. 270:12980-12983.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12980-12983
    • Castuma, C.E.1    Huang, R.2    Kornberg, A.3    Reusch, R.N.4
  • 11
    • 0026697667 scopus 로고
    • Cell surface modifications induced by calcium ion in the myxobacterium Stigmatella aurantiaca
    • Chang, B.-Y., and D. White. 1992. Cell surface modifications induced by calcium ion in the myxobacterium Stigmatella aurantiaca. J. Bacteriol. 174:5780-5787.
    • (1992) J. Bacteriol. , vol.174 , pp. 5780-5787
    • Chang, B.-Y.1    White, D.2
  • 12
    • 0022548922 scopus 로고
    • Electron probe analysis. X-ray mapping, and electron energy-loss spectroscopy of calcium, magnesium, and monovalent ions in log-phase and in dividing Escherichia coli B cells
    • Chang, C.-F., H. Shuman, and A. P. Somlyo. 1986. Electron probe analysis. X-ray mapping, and electron energy-loss spectroscopy of calcium, magnesium, and monovalent ions in log-phase and in dividing Escherichia coli B cells. J. Bacteriol. 167:935-939.
    • (1986) J. Bacteriol. , vol.167 , pp. 935-939
    • Chang, C.-F.1    Shuman, H.2    Somlyo, A.P.3
  • 14
    • 0001906505 scopus 로고
    • Aequorin measurements of cytoplasmic free calcium
    • J. G. McCormack, and P. H. Cobbold (ed.), IRL Press, Oxford
    • Cobbold, P. H., and J. A. C. Lee. 1991. Aequorin measurements of cytoplasmic free calcium, p. 55-81. In J. G. McCormack, and P. H. Cobbold (ed.), Cellular calcium: a practical approach. IRL Press, Oxford.
    • (1991) Cellular Calcium: A Practical Approach , pp. 55-81
    • Cobbold, P.H.1    Lee, J.A.C.2
  • 16
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis, P. R., and B. de Kruijff. 1979. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta 559:399-420.
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    De Kruijff, B.2
  • 17
    • 0028865106 scopus 로고
    • Why sequence genomes - The Escherichia coli imbroglio
    • Danchin, A. 1995. Why sequence genomes - the Escherichia coli imbroglio. Mol. Microbiol. 18:371-376.
    • (1995) Mol. Microbiol. , vol.18 , pp. 371-376
    • Danchin, A.1
  • 19
    • 0026416875 scopus 로고
    • Sequence and inactivation of the pss gene of Escherichia coli - Phosphatidylethanolamine may not be essential for cell viability
    • DeChavigny, A., P. N. Heacock, and W. Dowhan. 1991. Sequence and inactivation of the pss gene of Escherichia coli - phosphatidylethanolamine may not be essential for cell viability. J. Biol. Chem. 266:5323-5332.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5323-5332
    • Dechavigny, A.1    Heacock, P.N.2    Dowhan, W.3
  • 20
    • 0025034686 scopus 로고
    • 2+ -binding protein that is exported without N-terminal cleavage and is homologous to hemolysin and related proteins
    • 2+ -binding protein that is exported without N-terminal cleavage and is homologous to hemolysin and related proteins. EMBO J. 9:349-354.
    • (1990) EMBO J. , vol.9 , pp. 349-354
    • Economou, A.1    Hamilton, W.D.O.2    Johnston, A.W.B.3    Downie, J.A.4
  • 21
    • 85035167121 scopus 로고    scopus 로고
    • Unpublished data
    • Freestone, P. Unpublished data.
    • Freestone, P.1
  • 23
    • 0025765499 scopus 로고
    • Purification and properties of an intracellular calmodulin-like protein from Bacillus subtilis cells
    • Fry, I. J., M. Becker-Hapak, and J. H. Hageman. 1991. Purification and properties of an intracellular calmodulin-like protein from Bacillus subtilis cells. J. Bacteriol. 173:2506-2513.
    • (1991) J. Bacteriol. , vol.173 , pp. 2506-2513
    • Fry, I.J.1    Becker-Hapak, M.2    Hageman, J.H.3
  • 25
    • 0023656068 scopus 로고
    • Maintenance of intracellular calcium in Escherichia coli
    • Gangola, P., and B. P. Rosen. 1987. Maintenance of intracellular calcium in Escherichia coli. J. Biol. Chem. 262:12570-12574.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12570-12574
    • Gangola, P.1    Rosen, B.P.2
  • 28
    • 0027459168 scopus 로고
    • Effect of protein kinase inhibitors on in vitro phosphorylation and cellular differentiation of Streptomyces griseus
    • Hong, S.-K., A. Matsumoto, S. Horinouchi, and T. Beppu. 1993. Effect of protein kinase inhibitors on in vitro phosphorylation and cellular differentiation of Streptomyces griseus. Mol. Gen. Genet. 236:347-354.
    • (1993) Mol. Gen. Genet. , vol.236 , pp. 347-354
    • Hong, S.-K.1    Matsumoto, A.2    Horinouchi, S.3    Beppu, T.4
  • 29
    • 0016842108 scopus 로고
    • Divalent cation ionophore A23187 forms lipid soluble complexes with leucine and other amino acids
    • Hovi, T., S. C. Williams, and A. C. Allison. 1975. Divalent cation ionophore A23187 forms lipid soluble complexes with leucine and other amino acids. Nature (London) 256:70-72.
    • (1975) Nature (London) , vol.256 , pp. 70-72
    • Hovi, T.1    Williams, S.C.2    Allison, A.C.3
  • 30
    • 0028854402 scopus 로고
    • Genetic competence in Escherichia coli requires poly-β-hydroxybutyrate/calcium polyphosphate membrane complexes and certain divalent cations
    • Huang, R.-P., and R. N. Reusch. 1995. Genetic competence in Escherichia coli requires poly-β-hydroxybutyrate/calcium polyphosphate membrane complexes and certain divalent cations. J. Bacteriol. 177:486-490.
    • (1995) J. Bacteriol. , vol.177 , pp. 486-490
    • Huang, R.-P.1    Reusch, R.N.2
  • 31
    • 0025904248 scopus 로고
    • Metal speciation and microbial growth - The hard (and soft) facts
    • Hughes, M. N., and R. Poole. 1991. Metal speciation and microbial growth - the hard (and soft) facts. J. Gen. Microbiol. 137:725-734.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 725-734
    • Hughes, M.N.1    Poole, R.2
  • 32
    • 0025010878 scopus 로고
    • Aggregated DnaA protein is dissociated and activated for DNA replication by phospholipase or DnaK protein
    • Hwang, D. S., E. Crooke, and A. Kornberg. 1990. Aggregated DnaA protein is dissociated and activated for DNA replication by phospholipase or DnaK protein. J. Biol. Chem. 265:19244-19248.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19244-19248
    • Hwang, D.S.1    Crooke, E.2    Kornberg, A.3
  • 33
    • 0020853773 scopus 로고
    • Structural similarities between the developmental-specific protein S from a Gram-negative bacterium, Myxococcus xanthus, and calmodulin
    • Inouye, S., T. Franceshini, and M. Inouye. 1983. Structural similarities between the developmental-specific protein S from a Gram-negative bacterium, Myxococcus xanthus, and calmodulin. Proc. Natl. Acad. Sci. USA 80:6828-6833.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6828-6833
    • Inouye, S.1    Franceshini, T.2    Inouye, M.3
  • 35
    • 0019881140 scopus 로고
    • A heat-stable inhibitor protein for bovine brain cyclic nucleotide phosphodiesterase from Escherichia coli
    • Iwasa, Y., K. Yonemitsu, K. Matsui, K. Fukunaga, and E. Miyamoto. 1981. A heat-stable inhibitor protein for bovine brain cyclic nucleotide phosphodiesterase from Escherichia coli. FEBS Lett. 128:311-314.
    • (1981) FEBS Lett , vol.128 , pp. 311-314
    • Iwasa, Y.1    Yonemitsu, K.2    Matsui, K.3    Fukunaga, K.4    Miyamoto, E.5
  • 36
    • 8944238490 scopus 로고
    • An approach to the control of the initiation of chromosome replication in Escherichia coli
    • Jimenez-Sanchez, A., E. C. Guzman, and E. Botello. 1993. An approach to the control of the initiation of chromosome replication in Escherichia coli. Curr. Top. Mol. Genet. (Life Sci. Adv.) 1:33-48.
    • (1993) Curr. Top. Mol. Genet. (Life Sci. Adv.) , vol.1 , pp. 33-48
    • Jimenez-Sanchez, A.1    Guzman, E.C.2    Botello, E.3
  • 37
    • 0027180525 scopus 로고
    • The cyanobacterium Synechococcus sp. PCC7942 possesses 2 distinct genes encoding cation-transporting P-type ATPases
    • Kanamaru, K., S. Kashiwagi, and T. Mizuno. 1993. The cyanobacterium Synechococcus sp. PCC7942 possesses 2 distinct genes encoding cation-transporting P-type ATPases. FEBS Lett. 330:99-104.
    • (1993) FEBS Lett , vol.330 , pp. 99-104
    • Kanamaru, K.1    Kashiwagi, S.2    Mizuno, T.3
  • 41
    • 0017121654 scopus 로고
    • Metal ion content of Escherichia coli versus cell age
    • Kung, F.-C., J. Raymond, and D. A. Glaser. 1976. Metal ion content of Escherichia coli versus cell age. J. Bacteriol. 126:1089-1095.
    • (1976) J. Bacteriol. , vol.126 , pp. 1089-1095
    • Kung, F.-C.1    Raymond, J.2    Glaser, D.A.3
  • 42
    • 0028075453 scopus 로고
    • EGTA induces the synthesis in Escherichia coli of 3 proteins that cross-react with calmodulin antibodies
    • Laoudj, D., C. L. Andersen, A. Bras, M. Goldberg, A. Jacq, and I. B. Holland. 1994. EGTA induces the synthesis in Escherichia coli of 3 proteins that cross-react with calmodulin antibodies. Mol. Microbiol. 13:445-457.
    • (1994) Mol. Microbiol. , vol.13 , pp. 445-457
    • Laoudj, D.1    Andersen, C.L.2    Bras, A.3    Goldberg, M.4    Jacq, A.5    Holland, I.B.6
  • 43
    • 0027205053 scopus 로고
    • Prokaryotic plant parasites
    • Long, S. R., and B. J. Staskawicz. 1993. Prokaryotic plant parasites. Cell 73:921-935.
    • (1993) Cell , vol.73 , pp. 921-935
    • Long, S.R.1    Staskawicz, B.J.2
  • 44
    • 0009573805 scopus 로고
    • Calcium transport in prokaryotes
    • B. P. Rosen and S. Silver (ed.), Academic Press, New York
    • Lynn, A. R., and B. P. Rosen. 1987. Calcium transport in prokaryotes, p. 181-201. In B. P. Rosen and S. Silver (ed.), Ion transport in prokaryotes. Academic Press, New York.
    • (1987) Ion Transport in Prokaryotes , pp. 181-201
    • Lynn, A.R.1    Rosen, B.P.2
  • 47
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • McCarthy, J. S., and G. C. Walker. 1991. DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc. Natl. Acad. Sci. USA 88:9513-9517.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9513-9517
    • McCarthy, J.S.1    Walker, G.C.2
  • 48
    • 0027411095 scopus 로고
    • Eukaryotic-like protein serine/threonine kinases in Myxococcus xanthus, a developmental bacterium exhibiting social behaviour
    • Munoz-Dorada, J., S. Inouye, and M. Inouye. 1993. Eukaryotic-like protein serine/threonine kinases in Myxococcus xanthus, a developmental bacterium exhibiting social behaviour. J. Cell. Biochem. 51:29-33.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 29-33
    • Munoz-Dorada, J.1    Inouye, S.2    Inouye, M.3
  • 49
    • 8944227058 scopus 로고
    • Premature division in Escherichia coli in the presence of Tris-EDTA
    • Walter de Gruyter, Berlin
    • Nanninga, N., T. den Blaauwen, P. M. Nederlof, and P. de Boer, 1983. Premature division in Escherichia coli in the presence of Tris-EDTA, p. 147-152. In The target of penicillin. Walter de Gruyter, Berlin.
    • (1983) The Target of Penicillin , pp. 147-152
    • Nanninga, N.1    Den Blaauwen, T.2    Nederlof, P.M.3    De Boer, P.4
  • 50
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka, Y. 1988. The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature (London) 334:661-665.
    • (1988) Nature (London) , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 51
    • 0024836087 scopus 로고
    • A calcium flux at the termination of replication triggers cell division in E. coli
    • Norris, V. 1989. A calcium flux at the termination of replication triggers cell division in E. coli. Cell Calcium 10:511-517.
    • (1989) Cell Calcium , vol.10 , pp. 511-517
    • Norris, V.1
  • 55
    • 0024280963 scopus 로고
    • A single calcium flux triggers chromosome replication, segregation and septation in bacteria: A model
    • Norris, V., S. J. Seror, S. Casaregola, and I. B. Holland. 1988. A single calcium flux triggers chromosome replication, segregation and septation in bacteria: a model. J. Theor. Biol. 134:341-350.
    • (1988) J. Theor. Biol. , vol.134 , pp. 341-350
    • Norris, V.1    Seror, S.J.2    Casaregola, S.3    Holland, I.B.4
  • 56
    • 0030047024 scopus 로고    scopus 로고
    • The Escherichia coli enzoskeleton
    • Norris, V., G. Turnock, and D. Sigee. 1996. The Escherichia coli enzoskeleton. Mol. Microbiol. 19:197-204.
    • (1996) Mol. Microbiol. , vol.19 , pp. 197-204
    • Norris, V.1    Turnock, G.2    Sigee, D.3
  • 57
    • 0025338544 scopus 로고
    • Energy and calcium ion dependence of proteolysis during sporulation of Bacillus subtilis cells
    • O'Hara, M. B., and J. H. Hageman. 1990. Energy and calcium ion dependence of proteolysis during sporulation of Bacillus subtilis cells. J. Bacteriol. 172:4161-4170.
    • (1990) J. Bacteriol. , vol.172 , pp. 4161-4170
    • O'Hara, M.B.1    Hageman, J.H.2
  • 58
    • 0028225939 scopus 로고
    • Physiological role of the chaA gene in sodium and calcium circulations at a high pH in Escherichia coli
    • Ohyama, T., K. Igarashi, and H. Kobayashi. 1994. Physiological role of the chaA gene in sodium and calcium circulations at a high pH in Escherichia coli. J. Bacteriol. 176:4311-4315.
    • (1994) J. Bacteriol. , vol.176 , pp. 4311-4315
    • Ohyama, T.1    Igarashi, K.2    Kobayashi, H.3
  • 59
    • 0028346040 scopus 로고
    • Isolation and characterization of a calmodulin-like protein from the cyanobacterium Nostoc sp. PCC 6720
    • Onek, L. A., P. J. Lea, and R. J. Smith. 1994. Isolation and characterization of a calmodulin-like protein from the cyanobacterium Nostoc sp. PCC 6720. Arch. Microbiol. 161:352-358.
    • (1994) Arch. Microbiol. , vol.161 , pp. 352-358
    • Onek, L.A.1    Lea, P.J.2    Smith, R.J.3
  • 60
    • 0026703903 scopus 로고
    • Calmodulin and calcium mediated regulation in prokaryotes
    • Onek, L. A., and R. J. Smith. 1992. Calmodulin and calcium mediated regulation in prokaryotes. J. Gen. Microbiol. 138:1039-1049.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1039-1049
    • Onek, L.A.1    Smith, R.J.2
  • 62
    • 0017761157 scopus 로고
    • Calcium ion regulates chemotactic behaviour in bacteria
    • Ordal, G. W. 1977. Calcium ion regulates chemotactic behaviour in bacteria. Nature (London) 270:66-67.
    • (1977) Nature (London) , vol.270 , pp. 66-67
    • Ordal, G.W.1
  • 63
  • 65
    • 0027354188 scopus 로고
    • A quantitative study of calcium binding and aggregation in selected oral bacteria
    • Rose, R. K., G. H. Dibdin, and R. P. Shellis. 1993. A quantitative study of calcium binding and aggregation in selected oral bacteria. J. Dent. Res. 72:78-84.
    • (1993) J. Dent. Res. , vol.72 , pp. 78-84
    • Rose, R.K.1    Dibdin, G.H.2    Shellis, R.P.3
  • 66
    • 0028961645 scopus 로고
    • Isolation and characterization of a calmodulin-like protein from Halobacterium salinarium
    • Rotharmel, T., and G. Wagner. 1995. Isolation and characterization of a calmodulin-like protein from Halobacterium salinarium. J. Bacteriol. 177:864-866.
    • (1995) J. Bacteriol. , vol.177 , pp. 864-866
    • Rotharmel, T.1    Wagner, G.2
  • 67
    • 0023901638 scopus 로고
    • Demonstration of two protein kinases in extracts of Legionella micdadei
    • Saha, A., J. N. Dowling, N. K. Mukhopadhyay, and R. H. Glew. 1988. Demonstration of two protein kinases in extracts of Legionella micdadei. J. Gen. Microbiol. 134:1275-1281.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 1275-1281
    • Saha, A.1    Dowling, J.N.2    Mukhopadhyay, N.K.3    Glew, R.H.4
  • 68
    • 0023956637 scopus 로고
    • The dnaK gene of Escherichia coli functions in initiation of chromosome replication
    • Sakakibara, Y. 1988. The dnaK gene of Escherichia coli functions in initiation of chromosome replication. J. Bacteriol. 170:972-979.
    • (1988) J. Bacteriol. , vol.170 , pp. 972-979
    • Sakakibara, Y.1
  • 69
    • 0027220168 scopus 로고
    • Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation
    • Sherman, M. Y., and A. L. Goldberg. 1993. Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation. Proc. Natl. Acad. Sci. USA 90:8648-8652.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8648-8652
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 70
    • 0028877134 scopus 로고
    • Calcium and bacteria
    • Smith, R. J. 1995. Calcium and bacteria. Adv. Microb. Physiol. 37:83-103.
    • (1995) Adv. Microb. Physiol. , vol.37 , pp. 83-103
    • Smith, R.J.1
  • 71
    • 0025058171 scopus 로고
    • Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain
    • Stevenson, M. A., and S. K. Calderwood. 1990. Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain. Mol. Cell. Biol. 10:1234-1238.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1234-1238
    • Stevenson, M.A.1    Calderwood, S.K.2
  • 73
    • 0027989818 scopus 로고
    • Calcium-dependent inactivation of RNA polymerase III transcription
    • Sturges, M. R., and L. J. Peck. 1994. Calcium-dependent inactivation of RNA polymerase III transcription. J. Biol. Chem. 269:5712-5719.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5712-5719
    • Sturges, M.R.1    Peck, L.J.2
  • 75
    • 0024415870 scopus 로고
    • Participation of Escherichia coli heat shock proteins DnaJ, DnaK, and GrpE in P1 plasmid replication
    • Tilly, K., and M. Yarmolinsky. 1989. Participation of Escherichia coli heat shock proteins DnaJ, DnaK, and GrpE in P1 plasmid replication. J. Bacteriol. 171:6025-6029.
    • (1989) J. Bacteriol. , vol.171 , pp. 6025-6029
    • Tilly, K.1    Yarmolinsky, M.2
  • 76
    • 0027052945 scopus 로고
    • Calcium ions are involved in Escherichia coli chemotaxis
    • Tisa, L. S., and J. Adler. 1992. Calcium ions are involved in Escherichia coli chemotaxis. Proc. Natl. Acad. Sci. USA 89:11804-11808.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11804-11808
    • Tisa, L.S.1    Adler, J.2
  • 78
    • 0028970741 scopus 로고
    • 2+ level rises with repellents and falls with attractants in Escherichia coli chemotaxis
    • 2+ level rises with repellents and falls with attractants in Escherichia coli chemotaxis. Proc. Natl. Acad. Sci. USA 92:10777-10781.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10777-10781
    • Tisa, L.S.1    Adler, J.2
  • 79
    • 0027467289 scopus 로고
    • Inhibition of Escherchia coli chemotaxis by ω-conotoxin, a calcium ion channel blocker
    • Tisa, L. S., B. M. Olivers, and J. Adler. 1993. Inhibition of Escherchia coli chemotaxis by ω-conotoxin, a calcium ion channel blocker. J. Bacteriol. 175:1235-1238.
    • (1993) J. Bacteriol. , vol.175 , pp. 1235-1238
    • Tisa, L.S.1    Olivers, B.M.2    Adler, J.3
  • 80
    • 0026620199 scopus 로고
    • Mutations conferring acid sensitivity in the acid-tolerant strains Rhizobium meliloti WSM419 and Rhizobium leguminosarum biovar viciae WSM710
    • Tiwari, R. P., W. G. Reeve, and A. R. Glenn. 1992. Mutations conferring acid sensitivity in the acid-tolerant strains Rhizobium meliloti WSM419 and Rhizobium leguminosarum biovar viciae WSM710. FEMS Microbiol. Lett. 100:107-112.
    • (1992) FEMS Microbiol. Lett. , vol.100 , pp. 107-112
    • Tiwari, R.P.1    Reeve, W.G.2    Glenn, A.R.3
  • 82
    • 0027538447 scopus 로고
    • Characterization of a calcium porter of Streptococcus pneumoniae involved in calcium regulation of growth and competence
    • Trombe, M.-C. 1993. Characterization of a calcium porter of Streptococcus pneumoniae involved in calcium regulation of growth and competence. J. Gen. Microbiol. 139:433-439.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 433-439
    • Trombe, M.-C.1
  • 83
    • 0028328305 scopus 로고
    • Mutations which alter the kinetics of calcium transport alter the regulation of competence in Streptococcus pneumoniae
    • Trombe, M.-C., V. Rieux, and F. Baille. 1994. Mutations which alter the kinetics of calcium transport alter the regulation of competence in Streptococcus pneumoniae. J. Bacteriol. 176:1992-1996.
    • (1994) J. Bacteriol. , vol.176 , pp. 1992-1996
    • Trombe, M.-C.1    Rieux, V.2    Baille, F.3
  • 84
    • 0025245420 scopus 로고
    • Calcium channels, stores, and oscillations
    • Tsien, R. W., and R. Y. Tsien. 1990. Calcium channels, stores, and oscillations. Annu. Rev. Cell Biol. 6:715-760.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 715-760
    • Tsien, R.W.1    Tsien, R.Y.2
  • 85
    • 0028298054 scopus 로고
    • Translocation of metal phosphate via the phosphate inorganic transport system of Escherichia coli
    • Van Veen, H. W., T. Abee, G. J. J. Kortstee, W. N. Konings, and A. J. B. Zehner. 1994. Translocation of metal phosphate via the phosphate inorganic transport system of Escherichia coli. Biochemistry 33:1766-1770.
    • (1994) Biochemistry , vol.33 , pp. 1766-1770
    • Van Veen, H.W.1    Abee, T.2    Kortstee, G.J.J.3    Konings, W.N.4    Zehner, A.J.B.5
  • 86
    • 0028913030 scopus 로고
    • Free calcium transients in chemotactic and non-chemotactic strains of Escherichia coli determined using recombinant aequorin
    • Watkins, N. J., M. R. Knight, A. J. Trewavas, and A. K. Campbell. 1995. Free calcium transients in chemotactic and non-chemotactic strains of Escherichia coli determined using recombinant aequorin. Biochem. J. 306:865-869.
    • (1995) Biochem. J. , vol.306 , pp. 865-869
    • Watkins, N.J.1    Knight, M.R.2    Trewavas, A.J.3    Campbell, A.K.4
  • 87
    • 0025266168 scopus 로고
    • Three Escherichia coli heat shock proteins are required for P1 plasmid DNA replication: Formation of an active complex between E. coli DnaJ protein and the P1 initiator protein
    • Wickner, S. H. 1990. Three Escherichia coli heat shock proteins are required for P1 plasmid DNA replication: formation of an active complex between E. coli DnaJ protein and the P1 initiator protein. Proc. Natl. Acad. Sci. USA 87:2690-2694.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2690-2694
    • Wickner, S.H.1
  • 88
    • 0027271997 scopus 로고
    • Calcium and micro-organisms
    • Youatt, J. 1993. Calcium and micro-organisms. Crit. Rev. Microbiol. 19:83-97.
    • (1993) Crit. Rev. Microbiol. , vol.19 , pp. 83-97
    • Youatt, J.1
  • 89
    • 21844498895 scopus 로고
    • The toxicity of metal chelate complexes of EGTA precludes the use of EGTA buffered media for the fungi Allomyces and Achlva
    • Youatt, J. 1994. The toxicity of metal chelate complexes of EGTA precludes the use of EGTA buffered media for the fungi Allomyces and Achlva. Microbios 79:171-185.
    • (1994) Microbios , vol.79 , pp. 171-185
    • Youatt, J.1


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