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Volumn 39, Issue 2, 1996, Pages

Prediction of affinities of peptides for calmodulin

Author keywords

Binding; Calmodulin; Peptide

Indexed keywords


EID: 5544226787     PISSN: 10069291     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (1)

References (27)
  • 2
    • 0022297841 scopus 로고
    • Interaction of calmodulin and a calmodulin binding peptide from myosin light chain kinase: Major spectral changes in both occur as the result of complexes formation
    • Klevit, R. E., Blumenthal, D. K., Wemmer, D. E. et al., Interaction of calmodulin and a calmodulin binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complexes formation, Biochemistry, 1985, 24: 8152.
    • (1985) Biochemistry , vol.24 , pp. 8152
    • Klevit, R.E.1    Blumenthal, D.K.2    Wemmer, D.E.3
  • 3
    • 0022549779 scopus 로고
    • Calmodulin-binding domains: Characterizaation of a phosphorylation and calmodulin binding site from myosin light chain kinase
    • Lukas, T. J., Burgess, W. H., Prendergast, F. G., Calmodulin-binding domains: characterizaation of a phosphorylation and calmodulin binding site from myosin light chain kinase, Biochemistry, 1986, 25: 1458.
    • (1986) Biochemistry , vol.25 , pp. 1458
    • Lukas, T.J.1    Burgess, W.H.2    Prendergast, F.G.3
  • 4
    • 0024341971 scopus 로고
    • The γ-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to binding calmodulin
    • Dasgupta, M., Honeycutt, T., Blumenthal, D. K., The γ-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to binding calmodulin, J. Biol. Chem., 1989, 264: 17156.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17156
    • Dasgupta, M.1    Honeycutt, T.2    Blumenthal, D.K.3
  • 5
    • 0023655530 scopus 로고
    • Characterization of the calmodulin-binding sites of muscle phosphofructo-kinase and comparison with known calmodulin-binding domains
    • Buschmeier, B., Meyer, H. E., Mayr, G. W., Characterization of the calmodulin-binding sites of muscle phosphofructo-kinase and comparison with known calmodulin-binding domains, J. Biol. Chem., 1987, 262: 9454.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9454
    • Buschmeier, B.1    Meyer, H.E.2    Mayr, G.W.3
  • 6
    • 0023195547 scopus 로고
    • Functional analysis of a complementary DNA for the 50-kilodalton subunit of calmodulin kinase II
    • Hanley, R. M., Means, A. R., One, T. et al., Functional analysis of a complementary DNA for the 50-kilodalton subunit of calmodulin kinase II, Science, 1987, 237: 293.
    • (1987) Science , vol.237 , pp. 293
    • Hanley, R.M.1    Means, A.R.2    One, T.3
  • 7
    • 0024361269 scopus 로고
    • 2+ pump interacts with both calmodulin and another part of the pump
    • 2+ pump interacts with both calmodulin and another part of the pump, J. Biol. Chem., 1989, 264: 12313.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12313
    • Enyedi, A.1    Vorherr, T.2    James, P.3
  • 8
    • 0021943841 scopus 로고
    • The interaction of calmodulin with amphiphilic peptide
    • Cox, J. A., Comte, M., Fitton, J. E. et al., The interaction of calmodulin with amphiphilic peptide, J. Biol. Chem., 1985, 260: 2527.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2527
    • Cox, J.A.1    Comte, M.2    Fitton, J.E.3
  • 9
    • 5544242425 scopus 로고
    • The effect of α-helical structure of peptide on its affinity for calmodulin
    • Yan, H., He, B., The effect of α-helical structure of peptide on its affinity for calmodulin, Chinese Biochem. J. (in Chinese), 1991, 7: 147.
    • (1991) Chinese Biochem. J. (in Chinese) , vol.7 , pp. 147
    • Yan, H.1    He, B.2
  • 10
    • 0020475449 scopus 로고
    • A simple method for displaying the hydrophobic character of a protein
    • Kyte, J., Dolittle, R. F., A simple method for displaying the hydrophobic character of a protein, J. Mol. Biol., 1982, 157: 105.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105
    • Kyte, J.1    Dolittle, R.F.2
  • 11
    • 0142167791 scopus 로고
    • The effect of the basicity and hydrophobicity of peptides on their affinities for calmodulin
    • Yan, H., He, B., The effect of the basicity and hydrophobicity of peptides on their affinities for calmodulin, Chinese J. Biochem. Biophys, 1992, 24: 295.
    • (1992) Chinese J. Biochem. Biophys , vol.24 , pp. 295
    • Yan, H.1    He, B.2
  • 12
    • 0022973943 scopus 로고
    • Affinity purification of seminalplasmin and characterization of its interaction with calmodolin
    • Comte, M., Malnoe, A., Cox, J. A., Affinity purification of seminalplasmin and characterization of its interaction with calmodolin, Biochem. J., 1986, 240: 567.
    • (1986) Biochem. J. , vol.240 , pp. 567
    • Comte, M.1    Malnoe, A.2    Cox, J.A.3
  • 13
    • 0022538061 scopus 로고
    • Demonstration of a fluorometrically distinguishable intermediate in calcium binding by calmodolin-mastoparan complexes
    • Malencik, D. A., Anderson, S. R., Demonstration of a fluorometrically distinguishable intermediate in calcium binding by calmodolin-mastoparan complexes, Biochem. Biophys. Res. Commun., 1986, 135: 1050.
    • (1986) Biochem. Biophys. Res. Commun. , vol.135 , pp. 1050
    • Malencik, D.A.1    Anderson, S.R.2
  • 14
    • 0024428060 scopus 로고
    • Interaction of troponin C and calmodolin
    • Lan, J., Albaugh, S., Steiner, R. F., Interaction of troponin C and calmodolin, Biochemistry, 1989, 28: 7380.
    • (1989) Biochemistry , vol.28 , pp. 7380
    • Lan, J.1    Albaugh, S.2    Steiner, R.F.3
  • 15
    • 0022462015 scopus 로고
    • Calmodolin-linked equilibria in smooth muscle myosin light chain kinase
    • Malencik, D. A., Anderson, S. R., Calmodolin-linked equilibria in smooth muscle myosin light chain kinase, Biochemistry, 1986, 25: 709.
    • (1986) Biochemistry , vol.25 , pp. 709
    • Malencik, D.A.1    Anderson, S.R.2
  • 16
    • 0020485292 scopus 로고
    • Binding of protein kinase substrates by fluoresentally labled calmodolin
    • Malencik, D. A., Huang, T. S., Anderson, S. R., Binding of protein kinase substrates by fluoresentally labled calmodolin, Biochem Biophys. Res. Commun., 1982, 108: 266.
    • (1982) Biochem Biophys. Res. Commun. , vol.108 , pp. 266
    • Malencik, D.A.1    Huang, T.S.2    Anderson, S.R.3
  • 17
    • 0022501262 scopus 로고
    • Association of calmodolin with peptide analogues of the inhibitory region of the heat-stable protein inhibitor of adenosine cyclic 3′, 5′-phosphate dependent protein kinase
    • Malencik, D. A., Scott, J. D., Fischer, E. H. et al., Association of calmodolin with peptide analogues of the inhibitory region of the heat-stable protein inhibitor of adenosine cyclic 3′, 5′-phosphate dependent protein kinase, Biochemistry, 1986, 25: 3502.
    • (1986) Biochemistry , vol.25 , pp. 3502
    • Malencik, D.A.1    Scott, J.D.2    Fischer, E.H.3
  • 18
    • 0020541529 scopus 로고
    • Binding of hormones and neuropeptides by calmodulin
    • Malencik, D. A., Anderson, S. R., Binding of hormones and neuropeptides by calmodulin, Biochemistry, 1983, 22: 1995.
    • (1983) Biochemistry , vol.22 , pp. 1995
    • Malencik, D.A.1    Anderson, S.R.2
  • 19
    • 0023645552 scopus 로고
    • Rabit skeletal muscle myosin light chain kinase
    • Kennelly, P. J., Edelman, A. M., Blumenthal, D. K. et al., Rabit skeletal muscle myosin light chain kinase, J. Biol. Chem., 1987, 262: 11958.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11958
    • Kennelly, P.J.1    Edelman, A.M.2    Blumenthal, D.K.3
  • 20
    • 0026755154 scopus 로고
    • 2+-dependent calmodulin-binding region of chromagranin A
    • 2+-dependent calmodulin-binding region of chromagranin A, Biochemistry, 1992, 31: 6134.
    • (1992) Biochemistry , vol.31 , pp. 6134
    • Yoo, S.H.1
  • 21
    • 0025807931 scopus 로고
    • Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain
    • Charbonneau, H. Kumar, S., Novack, J. P. et al., Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain, Biochemistry, 1991, 30: 7931.
    • (1991) Biochemistry , vol.30 , pp. 7931
    • Charbonneau, H.1    Kumar, S.2    Novack, J.P.3
  • 22
    • 0025837139 scopus 로고
    • A calmodulin-binding peptide of Caldesmon
    • Zhang, Q., Wong, S. S., Wang, C. L. A., A calmodulin-binding peptide of Caldesmon, J. Biol. Chem., 1991, 266: 21810.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21810
    • Zhang, Q.1    Wong, S.S.2    Wang, C.L.A.3
  • 23
    • 0024573939 scopus 로고
    • Characterization of the calmodulin-binding site of the nonerythoid β-spectrin
    • Leto, T. L., Pleasic, S., Forget, B. G. et al., Characterization of the calmodulin-binding site of the nonerythoid β-spectrin, J. Biol. Chem., 1989, 264: 5826.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5826
    • Leto, T.L.1    Pleasic, S.2    Forget, B.G.3
  • 24
    • 0024792279 scopus 로고
    • Phosphorylation-related calmodulin binding to a prominant cellular substrate for protein kinase C
    • Graff, J. M., Yong, T. N., Johnson, J. D. et al., Phosphorylation-related calmodulin binding to a prominant cellular substrate for protein kinase C, J. Biol. Chem., 1989, 264: 21818.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21818
    • Graff, J.M.1    Yong, T.N.2    Johnson, J.D.3
  • 25
    • 0026710613 scopus 로고
    • 2+ pump binds calmodulin, and the primary calmodulin-binding domain interacts with lipid
    • 2+ pump binds calmodulin, and the primary calmodulin-binding domain interacts with lipid, J. Biol. Chem., 1992, 267: 11800.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11800
    • Filoteo, A.G.1    Enyedi, A.2    Penniston, J.T.3
  • 26
    • 0025058171 scopus 로고
    • Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain
    • Stevenson, M. A., Calderwood, S. K., Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain, Mol. Cell. Biol., 1990, 10: 1234.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1234
    • Stevenson, M.A.1    Calderwood, S.K.2
  • 27


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.