메뉴 건너뛰기




Volumn 1385, Issue 1, 1998, Pages 157-164

Conformational stability studies of the pleckstrin DEP domain: Definition of the domain boundaries

Author keywords

Domain boundary; Modular protein; Pleckstrin; Thermal stability

Indexed keywords

PLECKSTRIN; PROTEIN KINASE C;

EID: 0031863027     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00041-7     Document Type: Article
Times cited : (29)

References (24)
  • 1
    • 0017393127 scopus 로고    scopus 로고
    • Relationship between phosphorylation of blood platelet proteins and secretion of platelet granule constituents: I. Effects of different aggregating agents
    • Haslam R.J., Lynhan J.A. Relationship between phosphorylation of blood platelet proteins and secretion of platelet granule constituents: I. Effects of different aggregating agents. Biochem. Biophys. Res. Commun. 779:1997;714-722.
    • (1997) Biochem. Biophys. Res. Commun. , vol.779 , pp. 714-722
    • Haslam, R.J.1    Lynhan, J.A.2
  • 3
    • 0025162104 scopus 로고
    • P47 phosphoprotein of blood platelets (pleckstrin) is a major target for phorbol ester-induced protein phosphorylation in intact platelets, granulocytes, lymphocytes, monocytes and cultured leukaemic cells: Absence of P47 in non-haematopoietic cells
    • Gailani D., Fisher T.C., Mills D.C., Macfarlane D.E. P47 phosphoprotein of blood platelets (pleckstrin) is a major target for phorbol ester-induced protein phosphorylation in intact platelets, granulocytes, lymphocytes, monocytes and cultured leukaemic cells: absence of P47 in non-haematopoietic cells. Br. J. Haematol. 74(2):1990;192-202.
    • (1990) Br. J. Haematol. , vol.74 , Issue.2 , pp. 192-202
    • Gailani, D.1    Fisher, T.C.2    Mills, D.C.3    Macfarlane, D.E.4
  • 4
    • 0020614164 scopus 로고
    • A role of calcium-activated phospholipid-dependent protein kinase in human platelet activation. Comparison of thrombin and collagen actions
    • Sano K., Takai Y., Yamanishi J., Nishizuka Y. A role of calcium-activated phospholipid-dependent protein kinase in human platelet activation. Comparison of thrombin and collagen actions. J. Biol. Chem. 258(14):1983;2010-2013.
    • (1983) J. Biol. Chem. , vol.258 , Issue.14 , pp. 2010-2013
    • Sano, K.1    Takai, Y.2    Yamanishi, J.3    Nishizuka, Y.4
  • 5
    • 0018741860 scopus 로고
    • Effects of collagen, ionophore A23187 and prostaglandin E1 on the phosphorylation of specific proteins in blood platelets
    • Haslam R.J., Lynhan J.A., Fox J.E.B. Effects of collagen, ionophore A23187 and prostaglandin E1 on the phosphorylation of specific proteins in blood platelets. Biochem. J. 178:1979;397-406.
    • (1979) Biochem. J. , vol.178 , pp. 397-406
    • Haslam, R.J.1    Lynhan, J.A.2    Fox, J.E.B.3
  • 6
    • 0024336014 scopus 로고
    • Molecular analysis of pleckstrin: The major protein kinase C substrate of platelets
    • Tyers M., Haslam R.J., Rachubinski R.A., Harley C.B. Molecular analysis of pleckstrin: the major protein kinase C substrate of platelets. J. Cell Biochem. 40(2):1989;133-145.
    • (1989) J. Cell Biochem. , vol.40 , Issue.2 , pp. 133-145
    • Tyers, M.1    Haslam, R.J.2    Rachubinski, R.A.3    Harley, C.B.4
  • 7
    • 0029157058 scopus 로고
    • Pleckstrin homology domains: A fact file
    • Saraste M., Hyvvnen M. Pleckstrin homology domains: a fact file. Curr. Opin. Struct. Biol. 5(3):1995;403-408.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , Issue.3 , pp. 403-408
    • Saraste, M.1    Hyvvnen, M.2
  • 9
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan J.E., Hajduk P.J., Yoon H., Fesik S.W. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature. 371(6493):1994;168-170.
    • (1994) Nature , vol.371 , Issue.6493 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.3    Fesik, S.W.4
  • 10
    • 0028246440 scopus 로고
    • Binding of G protein beta gamma-subunits to pleckstrin homology domains
    • Touhara K., Inglese J., Pitcher J.A., Shaw G., Lefkowitz R.J. Binding of G protein beta gamma-subunits to pleckstrin homology domains. J. Biol. Chem. 269(14):1994;10217-10220.
    • (1994) J. Biol. Chem. , vol.269 , Issue.14 , pp. 10217-10220
    • Touhara, K.1    Inglese, J.2    Pitcher, J.A.3    Shaw, G.4    Lefkowitz, R.J.5
  • 12
    • 0028891875 scopus 로고
    • Mutational analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase. Differential effects on G beta gamma and phosphatidylinositol 4,5-bisphosphate binding
    • Touhara K., Koch W.J., Hawes B.E., Lefkowitz R.J. Mutational analysis of the pleckstrin homology domain of the beta-adrenergic receptor kinase. Differential effects on G beta gamma and phosphatidylinositol 4,5-bisphosphate binding. J. Biol. Chem. 270(28):1995;17000-17015.
    • (1995) J. Biol. Chem. , vol.270 , Issue.28 , pp. 17000-17015
    • Touhara, K.1    Koch, W.J.2    Hawes, B.E.3    Lefkowitz, R.J.4
  • 13
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon M.A., Ferguson K.M., O'Brien R., Sigler P.B., Schlessinger J. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc. Natl. Acad. Sci. U.S.A. 92(23):1995;10472-10476.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , Issue.23 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 14
    • 0030040967 scopus 로고    scopus 로고
    • The pleckstrin homology domain: An intriguing multifunctional protein module
    • Shaw G. The pleckstrin homology domain: an intriguing multifunctional protein module. Bioessays. 18(1):1996;35-46.
    • (1996) Bioessays , vol.18 , Issue.1 , pp. 35-46
    • Shaw, G.1
  • 15
    • 0030200001 scopus 로고    scopus 로고
    • Pleckstrin's repeat performance: A novel domain in G-protein signaling?
    • Ponting C.P., Bork P. Pleckstrin's repeat performance: a novel domain in G-protein signaling? Trends Biochem. Sci. 21(7):1996;245-246.
    • (1996) Trends Biochem. Sci. , vol.21 , Issue.7 , pp. 245-246
    • Ponting, C.P.1    Bork, P.2
  • 16
    • 0028865255 scopus 로고
    • Protein kinase C regulates pleckstrin by phosphorylation of sites adjacent to the N-terminal pleckstrin homology domain
    • Abrams C.S., Zhao W., Belmonte E., Brass L.F. Protein kinase C regulates pleckstrin by phosphorylation of sites adjacent to the N-terminal pleckstrin homology domain. J. Biol. Chem. 270(40):1995;23317-23321.
    • (1995) J. Biol. Chem. , vol.270 , Issue.40 , pp. 23317-23321
    • Abrams, C.S.1    Zhao, W.2    Belmonte, E.3    Brass, L.F.4
  • 17
    • 0028347588 scopus 로고
    • Immunoglobulin-type domains of titin: Same folding, different stability?
    • Politou A., Gautel M., Pfuhl M., Labeit S., Pastore A. Immunoglobulin-type domains of titin: same folding, different stability? Biochemistry. 33:1994;4730-4737.
    • (1994) Biochemistry , vol.33 , pp. 4730-4737
    • Politou, A.1    Gautel, M.2    Pfuhl, M.3    Labeit, S.4    Pastore, A.5
  • 19
    • 0029988528 scopus 로고    scopus 로고
    • Three-dimensional structure and stability of the KH domain: Molecular insights into the fragile X syndrome
    • Musco G., Stier G., Joseph C., Castiglione Morelli M.A., Nilges M., Gibson T.J., Pastore A. Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell. 85:1996;237-245.
    • (1996) Cell , vol.85 , pp. 237-245
    • Musco, G.1    Stier, G.2    Joseph, C.3    Castiglione Morelli, M.A.4    Nilges, M.5    Gibson, T.J.6    Pastore, A.7
  • 20
    • 0031575331 scopus 로고    scopus 로고
    • When a module is also a domain: The role of the N terminus in the stability and the dynamics of immunoglobulin domains from titin
    • Pfuhl M., Improta S., Politou A.S., Pastore A. When a module is also a domain: the role of the N terminus in the stability and the dynamics of immunoglobulin domains from titin. J. Mol. Biol. 265:1997;242-256.
    • (1997) J. Mol. Biol. , vol.265 , pp. 242-256
    • Pfuhl, M.1    Improta, S.2    Politou, A.S.3    Pastore, A.4
  • 21
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • Macias M.J., Hyvonen M., Baraldi E., Schultz J., Sudol M., Saraste M., Oschkinat H. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature. 382(6592):1996;646-649.
    • (1996) Nature , vol.382 , Issue.6592 , pp. 646-649
    • Macias, M.J.1    Hyvonen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5    Saraste, M.6    Oschkinat, H.7
  • 22
    • 0030000052 scopus 로고    scopus 로고
    • Chemical cross-linking of pleckstrin in human platelets: Evidence for oligomerization of the protein and its dissociation by protein kinase
    • McDermott A.M., Haslam R.J. Chemical cross-linking of pleckstrin in human platelets: evidence for oligomerization of the protein and its dissociation by protein kinase. Can. Biochem J. 317:1996;119-124.
    • (1996) Can. Biochem J. , vol.317 , pp. 119-124
    • McDermott, A.M.1    Haslam, R.J.2
  • 23
    • 0029983371 scopus 로고    scopus 로고
    • T7 vectors with a modified T7lac promoter for expression of proteins in Escherichia coli
    • Peranen J., Rikkonen M., Hyvonen M., Kaariainen L. T7 vectors with a modified T7lac promoter for expression of proteins in Escherichia coli. Anal. Biochem. 236:1996;371-373.
    • (1996) Anal. Biochem. , vol.236 , pp. 371-373
    • Peranen, J.1    Rikkonen, M.2    Hyvonen, M.3    Kaariainen, L.4
  • 24
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney E., Kumar S., Krainer A.R. Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res. 21:1993;5803-5816.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.