메뉴 건너뛰기




Volumn 79, Issue 10, 1996, Pages 1728-1733

Interactions of Amphiphilic Peptides Derived from αs2-Casein with Calmodulin

Author keywords

Casein; Complex model; Peptide calmodulin interaction

Indexed keywords

3',5' CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; CALMODULIN; CASEIN; ENZYME INHIBITOR; PEPTIDE;

EID: 0030253959     PISSN: 00220302     EISSN: None     Source Type: Journal    
DOI: 10.3168/jds.S0022-0302(96)76539-6     Document Type: Article
Times cited : (15)

References (24)
  • 1
    • 0028124954 scopus 로고
    • Investigating the high affinity and low sequence specificity of calmodulin binding to its targets
    • Afshar, M., L.S.D. Caves, L. Guimard, R. E. Hubbard, B. Calas, G. Grassy, and J. Haiech 1994. Investigating the high affinity and low sequence specificity of calmodulin binding to its targets. J. Mol. Biol. 244:554.
    • (1994) J. Mol. Biol. , vol.244 , pp. 554
    • Afshar, M.1    Caves, L.S.D.2    Guimard, L.3    Hubbard, R.E.4    Calas, B.5    Grassy, G.6    Haiech, J.7
  • 2
    • 0020635354 scopus 로고
    • Inhibition of calmodulin activity by insect venom peptide
    • Barnette, M. S., and B. Weiss. 1983. Inhibition of calmodulin activity by insect venom peptide. Biochem. Pharmacol. 32:2929.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 2929
    • Barnette, M.S.1    Weiss, B.2
  • 3
    • 0022391166 scopus 로고
    • Inhibition of calmodulin-stimulated phosphodiesterase activity by vasoactive intestinal peptide
    • Barnette, M. S., and B. Weiss. 1985. Inhibition of calmodulin-stimulated phosphodiesterase activity by vasoactive intestinal peptide. J. Neurochem. 45:640.
    • (1985) J. Neurochem. , vol.45 , pp. 640
    • Barnette, M.S.1    Weiss, B.2
  • 5
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou, P. Y., and G. D. Fasman. 1978. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47:251.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251
    • Chou, P.Y.1    Fasman, G.D.2
  • 7
    • 0020647518 scopus 로고
    • 2+-dependent high-affinity complex formation between calmodulin and melittin
    • 2+-dependent high-affinity complex formation between calmodulin and melittin. Biochem. J. 209:269.
    • (1983) Biochem. J. , vol.209 , pp. 269
    • Comte, M.1    Maulet, Y.2    Cox, J.A.3
  • 8
    • 0021943841 scopus 로고
    • The interaction of calmodulin with amphiphilic peptides
    • Cox, J. A., M. Comte, J. E. Fitton, and W. F. DeGrado. 1985. The interaction of calmodulin with amphiphilic peptides. J. Biol. Chem. 260:2527.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2527
    • Cox, J.A.1    Comte, M.2    Fitton, J.E.3    Degrado, W.F.4
  • 9
    • 0023195547 scopus 로고
    • Functional analysis of a complementary DNA for the 50-kilodalton subunit of calmodulin kinase II
    • Hanley, R. M., A. R. Means, T. Ono, B. E. Kemp, K. E. Burgin, N. Waxham, and P. T. Kelly. 1987. Functional analysis of a complementary DNA for the 50-kilodalton subunit of calmodulin kinase II. Science 237:293.
    • (1987) Science , vol.237 , pp. 293
    • Hanley, R.M.1    Means, A.R.2    Ono, T.3    Kemp, B.E.4    Burgin, K.E.5    Waxham, N.6    Kelly, P.T.7
  • 10
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M., G. M. Clore, A. M. Gronenborn, G. Zhu, C. B. Klee, and A. Bax. 1992. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256:632.
    • (1992) Science , vol.256 , pp. 632
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 11
    • 0019065883 scopus 로고
    • Interaction of basic polypeptides and proteins with calmodulin
    • Itano, T., R. Itano, and J. T. Penniston. 1980. Interaction of basic polypeptides and proteins with calmodulin. Biochem. J. 189:455.
    • (1980) Biochem. J. , vol.189 , pp. 455
    • Itano, T.1    Itano, R.2    Penniston, J.T.3
  • 12
    • 0029395013 scopus 로고
    • Calmodulin binding peptides isolated from α-casein peptone
    • Kizawa, K. K. Naganuma, and U. Murakami. 1995. Calmodulin binding peptides isolated from α-casein peptone. J. Dairy Res. 62:587.
    • (1995) J. Dairy Res. , vol.62 , pp. 587
    • Kizawa, K.1    Naganuma, K.2    Murakami, U.3
  • 13
    • 0014932616 scopus 로고
    • Insulin methyl ester specific cleavage of a peptide chain resulting from a nitrogen to oxygen acyl shift at a threonine residue
    • Levy, D., and F. H. Carpenter. 1970. Insulin methyl ester specific cleavage of a peptide chain resulting from a nitrogen to oxygen acyl shift at a threonine residue. Biochemistry 9:3215.
    • (1970) Biochemistry , vol.9 , pp. 3215
    • Levy, D.1    Carpenter, F.H.2
  • 14
    • 0015930702 scopus 로고
    • Conversion of exposed aspartyl and glutamyl residues in proteins to asparaginyl and glutaminyl residues
    • Lewis, S. D., and J. A. Shaffer. 1973. Conversion of exposed aspartyl and glutamyl residues in proteins to asparaginyl and glutaminyl residues. Biochim. Biophys. Acta 303:284.
    • (1973) Biochim. Biophys. Acta , vol.303 , pp. 284
    • Lewis, S.D.1    Shaffer, J.A.2
  • 15
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4Å structure of calmodulin-peptide complex
    • Meador, W. E., A. R. Means, and F. A. Quiocho. 1992. Target enzyme recognition by calmodulin: 2.4Å structure of calmodulin-peptide complex. Science 257:1251.
    • (1992) Science , vol.257 , pp. 1251
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 16
    • 0027759276 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Meador, W. E., A. R. Means, and F. A. Quiocho. 1993. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 262:1718.
    • (1993) Science , vol.262 , pp. 1718
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 17
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic αhelices
    • O'Neill, K. T., and W. F. DeGrado. 1990. How calmodulin binds its targets: sequence independent recognition of amphiphilic αhelices. Trends Biochem. Sci. 15:59.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59
    • O'Neill, K.T.1    Degrado, W.F.2
  • 18
    • 0009704509 scopus 로고
    • Evidence for nonidentical chain in the β-galactosidase of Escherichia coli K12
    • Steers, E., Jr., G. R. Craven, C. B. Anfinsen, and J. L. Bethune. 1965. Evidence for nonidentical chain in the β-galactosidase of Escherichia coli K12. J. Biol. Chem. 240:2478.
    • (1965) J. Biol. Chem. , vol.240 , pp. 2478
    • Steers Jr., E.1    Craven, G.R.2    Anfinsen, C.B.3    Bethune, J.L.4
  • 19
    • 0011562310 scopus 로고
    • Histidine in solid phase peptide synthesis: Tyrotropin releasing hormone and the angiotensins
    • ed. Gordon and Beach Sci. Publ., New York, NY
    • Stewart, J. M., M. Knight, A.C.M. Paiva, and T. Paiva. 1972. Histidine in solid phase peptide synthesis: Tyrotropin releasing hormone and the angiotensins. Page 59 in Progress in Peptide Research: Vol. U. S. Lande, ed. Gordon and Beach Sci. Publ., New York, NY.
    • (1972) Progress in Peptide Research: Vol. U. S. Lande , pp. 59
    • Stewart, J.M.1    Knight, M.2    Paiva, A.C.M.3    Paiva, T.4
  • 20
    • 13344276445 scopus 로고
    • N2 deprotection of synthetic peptides with a low concentration of HF in dimethyl sulfide: Evidence and application in peptide synthesis
    • N2 deprotection of synthetic peptides with a low concentration of HF in dimethyl sulfide: evidence and application in peptide synthesis. J. Am. Chem. Soc. 105:6442.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 6442
    • Tam, J.P.1    Heath, W.F.2    Merrifield, R.B.3
  • 22
    • 0028340559 scopus 로고
    • Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein
    • Verghese, G. M., J. D. Johnson, C. Vasulka, D. M. Haupt, D. J. Stumpo, and P. J. Blackshear. 1994. Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein. J. Biol. Chem. 269:9361.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9361
    • Verghese, G.M.1    Johnson, J.D.2    Vasulka, C.3    Haupt, D.M.4    Stumpo, D.J.5    Blackshear, P.J.6
  • 23
    • 0015254094 scopus 로고
    • Rapid microassay of adenosine 3′, 5′-monophosphate phosphodiesterase activity
    • Weiss, B., R. Lehne, and S. Strada. 1972. Rapid microassay of adenosine 3′, 5′-monophosphate phosphodiesterase activity. Anal. Biochem. 45:222.
    • (1972) Anal. Biochem. , vol.45 , pp. 222
    • Weiss, B.1    Lehne, R.2    Strada, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.