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Volumn 78, Issue 1-2, 1996, Pages 171-183

Regulation of Ca2+/calmodulin-dependent protein kinase from

Author keywords

cam dependent protein kinase; Ca2+; Regulation; Trypanosoma cruzi

Indexed keywords

MAMMALIA; TRYPANOSOMA; TRYPANOSOMA CRUZI;

EID: 0030155244     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0166-6851(96)02622-9     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 0027586519 scopus 로고
    • 2+/calmodulin-dependent protein kinases
    • 2+/calmodulin-dependent protein kinases. Curr. Opin. Cell Biol. 5, 247-253.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 247-253
    • Schulman, H.1
  • 3
    • 0025994387 scopus 로고
    • Protein phosphorylation and neuronal function
    • Walaas, S.I. and Greengard, P. (1991) Protein phosphorylation and neuronal function. Pharmacol. Rev. 43, 299-349.
    • (1991) Pharmacol. Rev. , vol.43 , pp. 299-349
    • Walaas, S.I.1    Greengard, P.2
  • 4
    • 0021928975 scopus 로고
    • 2+/calmodulin-dependent protein kinase produces an autonomous enzyme in Aplysia neurons
    • 2+/calmodulin-dependent protein kinase produces an autonomous enzyme in Aplysia neurons. J. Cell Biol. 100, 835-842.
    • (1985) J. Cell Biol. , vol.100 , pp. 835-842
    • Saitoh, T.1    Schwartz, J.H.2
  • 5
    • 0007643129 scopus 로고
    • Calcium-dependent regulatory pathways in Trypanosoma brucei: Characterization of 22000-dalton calcium-binding protein, calcimedins, and calmodulin
    • (O'Day, D.H., ed.), American Society for Microbiology, Washington, D.C.
    • Ruben, L. and Haghighat, N. (1990) Calcium-dependent regulatory pathways in Trypanosoma brucei: characterization of 22000-dalton calcium-binding protein, calcimedins, and calmodulin. In: Calcium as an Intracellular Messenger in Eucaryotic Microbes. (O'Day, D.H., ed.), pp. 317-342. American Society for Microbiology, Washington, D.C.
    • (1990) Calcium as an Intracellular Messenger in Eucaryotic Microbes , pp. 317-342
    • Ruben, L.1    Haghighat, N.2
  • 6
    • 0016988839 scopus 로고
    • 2+ on flagellar movement in the T Crithidia oncolpeti
    • 2+ on flagellar movement in the T Crithidia oncolpeti. J. Exp. Biol. 65, 229-242.
    • (1976) J. Exp. Biol. , vol.65 , pp. 229-242
    • Holwill, M.E.J.1    McGregor, J.L.2
  • 7
    • 0023446787 scopus 로고
    • Identification of a developmentally regulated calcium-binding protein in Trypanosoma brucei
    • Ruben, L. (1987) Identification of a developmentally regulated calcium-binding protein in Trypanosoma brucei. J. Protozool. 34, 367-370.
    • (1987) J. Protozool. , vol.34 , pp. 367-370
    • Ruben, L.1
  • 8
    • 0022661190 scopus 로고
    • Calcium ions initiate the selective depolymerization of the pellicular microtubules in bloodstream forms of Trypanosoma brucei
    • Dolan, M.T., Reid, C.G. and Voorheis, H.P. (1986) Calcium ions initiate the selective depolymerization of the pellicular microtubules in bloodstream forms of Trypanosoma brucei. J. Cell Sci. 80, 123-140.
    • (1986) J. Cell Sci. , vol.80 , pp. 123-140
    • Dolan, M.T.1    Reid, C.G.2    Voorheis, H.P.3
  • 9
    • 0019863142 scopus 로고
    • Characteristics of the calcium-mediated mechanisms activating adenylate cyclase in Trypanosoma brucei
    • Voorheis, H.P. and Martin, B.P. (1981) Characteristics of the calcium-mediated mechanisms activating adenylate cyclase in Trypanosoma brucei. Eur. J. Biochem. 116, 471-477.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 471-477
    • Voorheis, H.P.1    Martin, B.P.2
  • 10
    • 0025865088 scopus 로고
    • The inositol phosphate/diacylglycerol signalling pathway in Trypanosoma cruzi
    • Docampo, R. and Pignataro, O.P. (1991) The inositol phosphate/diacylglycerol signalling pathway in Trypanosoma cruzi. Biochem. J. 275, 407-411.
    • (1991) Biochem. J. , vol.275 , pp. 407-411
    • Docampo, R.1    Pignataro, O.P.2
  • 11
    • 0028170370 scopus 로고
    • Changes in Trypanosoma cruzi infectivity by treatments that affect calcium ion levels
    • Yakubu, M.A., Majumder, S. and Kierszenbaum, F. (1994) Changes in Trypanosoma cruzi infectivity by treatments that affect calcium ion levels. Mol. Biochem. Parasitol. 66, 119-125.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 119-125
    • Yakubu, M.A.1    Majumder, S.2    Kierszenbaum, F.3
  • 12
    • 0027941410 scopus 로고
    • Cytosolic free calcium elevation in Trypanosoma cruzi is required for cell invasion
    • Moreno, S.N.J., Silva, J., Vercesi, A.E. and Docampo, R. (1994) Cytosolic free calcium elevation in Trypanosoma cruzi is required for cell invasion. J. Exp. Med. 180, 1535-1540.
    • (1994) J. Exp. Med. , vol.180 , pp. 1535-1540
    • Moreno, S.N.J.1    Silva, J.2    Vercesi, A.E.3    Docampo, R.4
  • 16
    • 0023652677 scopus 로고
    • 2+/ calmodulin-dependent protein kinase in Saccharomyces cerevisiae
    • 2+/ calmodulin-dependent protein kinase in Saccharomyces cerevisiae. FEBS Lett. 219, 249-253.
    • (1987) FEBS Lett. , vol.219 , pp. 249-253
    • Londesborough, J.1    Nuutinen, M.2
  • 19
    • 0026554801 scopus 로고
    • Cloning and sequence determination of a cDNA encoding Aspergillus nidulans calmodulin-dependent multifunctional protein kinase
    • Kornstein, L.B., Gaiso, M.L., Hammell, R.L. and Bartelt, D.C. (1992) Cloning and sequence determination of a cDNA encoding Aspergillus nidulans calmodulin-dependent multifunctional protein kinase. Gene 113, 75-82.
    • (1992) Gene , vol.113 , pp. 75-82
    • Kornstein, L.B.1    Gaiso, M.L.2    Hammell, R.L.3    Bartelt, D.C.4
  • 21
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behavior of enzymes: Application to protein mixtures
    • Martin, R.G. and Ames, B.N. (1961) A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J. Biol. Chem. 236, 1372-1379.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 25
    • 0025181418 scopus 로고
    • Okadaic acid: A new probe for the study of cellular regulation
    • Cohen, P., Holmes, C.F.B. and Tsukitani, Y. (1990) Okadaic acid: a new probe for the study of cellular regulation. Trends Biochem. Sci. 15, 98-102.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 98-102
    • Cohen, P.1    Holmes, C.F.B.2    Tsukitani, Y.3
  • 26
    • 0023077830 scopus 로고
    • Role of autophosphorylation in regulating calmodulin-dependent protein kinases
    • Kelly, P.T. and Shenolikar, S. (1987) Role of autophosphorylation in regulating calmodulin-dependent protein kinases. Methods Enzymol. 139, 690-714.
    • (1987) Methods Enzymol. , vol.139 , pp. 690-714
    • Kelly, P.T.1    Shenolikar, S.2
  • 27
    • 0021089951 scopus 로고
    • Purification and characterization of a calmodulin-dependent kinase from rat brain cytosol able to phosphorylate tubulin and microtubule-associated proteins
    • Goldenring, J.R., Gonzalez, B., McGuire, J.S. Jr. and DeLorenzo, R. (1983) Purification and characterization of a calmodulin-dependent kinase from rat brain cytosol able to phosphorylate tubulin and microtubule-associated proteins. J. Biol. Chem. 258, 12632-12640.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12632-12640
    • Goldenring, J.R.1    Gonzalez, B.2    McGuire J.S., Jr.3    DeLorenzo, R.4
  • 28
    • 0023164984 scopus 로고
    • Calcium.calmodulin-dependent protein kinase II and calcium.Phospholipid-dependent protein kinase activities in rat tissues assayed with a synthetic peptide
    • Hashimoto, Y. and Soderling, T.R. (1987) Calcium.calmodulin-dependent protein kinase II and calcium.phospholipid-dependent protein kinase activities in rat tissues assayed with a synthetic peptide. Arch. Biochem. Biophys. 252, 418-425.
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 418-425
    • Hashimoto, Y.1    Soderling, T.R.2
  • 29
    • 0343374101 scopus 로고
    • N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide hydrochloride a calmodulin antagonist, inhibits cell proliferation
    • Hidaka, H., Sasaki, Y., Tanaka, T., Endo, T., Ohno, S., Fujii, Y. and Nagata, T. (1981) N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide hydrochloride a calmodulin antagonist, inhibits cell proliferation. Proc. Natl. Acad. Sci. USA 78, 4354-4357.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4354-4357
    • Hidaka, H.1    Sasaki, Y.2    Tanaka, T.3    Endo, T.4    Ohno, S.5    Fujii, Y.6    Nagata, T.7
  • 30
    • 0022373739 scopus 로고
    • Substrate specificity of a multifunctional calmodulin-dependent protein kinase
    • Pearson, R.B., Woodgett, J.R., Cohen, P. and Kemp, B.E. (1985) Substrate specificity of a multifunctional calmodulin-dependent protein kinase. J. Biol. Chem. 260, 14471-14476.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14471-14476
    • Pearson, R.B.1    Woodgett, J.R.2    Cohen, P.3    Kemp, B.E.4
  • 31
    • 0021362939 scopus 로고
    • 2+-independent phosphorylation of protamine catalyzed by a new protein kinase from brain
    • 2+-independent phosphorylation of protamine catalyzed by a new protein kinase from brain. J. Neurochem. 42, 458-465.
    • (1984) J. Neurochem. , vol.42 , pp. 458-465
    • Qi, D.-F.1    Turner, R.S.2    Kuo, J.F.3
  • 32
    • 0018471288 scopus 로고
    • 2+ and cyclic AMP regulate phosphorylation of same two membrane-associated proteins specific to nerve tissue
    • 2+ and cyclic AMP regulate phosphorylation of same two membrane-associated proteins specific to nerve tissue. Proc. Natl. Acad. Sci. USA 76, 2475-2481.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2475-2481
    • Sieghart, W.1    Forn, J.2    Greengard, P.3
  • 33
    • 0022519298 scopus 로고
    • 2+-triggered molecular switch
    • 2+-triggered molecular switch. Cell 44, 861-870.
    • (1986) Cell , vol.44 , pp. 861-870
    • Miller, S.G.1    Kennedy, M.B.2
  • 34
    • 0021807380 scopus 로고
    • 2+/calmodulin-dependent protein kinase
    • 2+/calmodulin-dependent protein kinase. J. Biol. Chem. 260, 6427-6433.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6427-6433
    • Kuret, J.1    Schulman, H.2
  • 36
    • 0026010586 scopus 로고
    • Characterization of trypanosome protein phosphatase 1 and 2A catalytic subunits
    • Erondu, N.E. and Donelson, J.E. (1991) Characterization of trypanosome protein phosphatase 1 and 2A catalytic subunits. Mol. Biochem. Parasitol. 49, 303-314.
    • (1991) Mol. Biochem. Parasitol. , vol.49 , pp. 303-314
    • Erondu, N.E.1    Donelson, J.E.2
  • 38
    • 0028142819 scopus 로고
    • Effect of protein kinase inhibitors on the invasion process of macrophages by Trypanosoma cruzi
    • Vieira, M.C.F., de Carvalho, T.U. and de Souza, W. (1994) Effect of protein kinase inhibitors on the invasion process of macrophages by Trypanosoma cruzi. Biochem. Biophys. Res. Commun. 203, 967-971.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 967-971
    • Vieira, M.C.F.1    De Carvalho, T.U.2    De Souza, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.