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2 hydrolysis and regulation of phospholipase C isozymes. Curr Opin Cell Biol. 7:1995;183-189.
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Lee, S.B.1
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0030987070
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Regulation of protein kinase C
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of special interest. Lipid regulation of protein kinase C is put into context with its other regulatory mechanisms - protein phosphorylation and subcellular localization.
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Newton AC. Regulation of protein kinase C. of special interest Curr Opin Cell Biol. 9:1997;161-167 Lipid regulation of protein kinase C is put into context with its other regulatory mechanisms - protein phosphorylation and subcellular localization.
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Curr Opin Cell Biol
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Nishizuka Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9:1995;484-496.
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Nishizuka, Y.1
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Pleckstrin homology domains: A fact file
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Saraste M, Hyvonen M. Pleckstrin homology domains: a fact file. Curr Opin Struct Biol. 5:1995;403-408.
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Curr Opin Struct Biol
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Saraste, M.1
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6
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0029939448
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PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surfaces
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of special interest. The functions of different surfaces of PH and PTB domains in binding different ligands are discussed.
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Lemmon MA, Ferguson KM, Schlessinger J. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surfaces. of special interest Cell. 85:1996;621-624 The functions of different surfaces of PH and PTB domains in binding different ligands are discussed.
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Lemmon, M.A.1
Ferguson, K.M.2
Schlessinger, J.3
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0027310309
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Proteolytic fragments of phosphoinositide-specific phospholipase C-δ1. Catalytic and membrane binding properties
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Cifuentes ME, Honkanen L, Rebecchi MJ. Proteolytic fragments of phosphoinositide-specific phospholipase C-δ1. Catalytic and membrane binding properties. J Biol Chem. 268:1993;11586-11593.
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Cifuentes, M.E.1
Honkanen, L.2
Rebecchi, M.J.3
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8
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0028787055
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The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes
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Garcia P, Gupta R, Shah S, Morris AJ, Rudge SA, Scarlata S, Petrova V, McLaughlin S, Rebecchi MJ. The pleckstrin homology domain of phospholipase C-δ1 binds with high affinity to phosphatidylinositol 4,5-bisphosphate in bilayer membranes. Biochemistry. 34:1995;16228-16234.
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Biochemistry
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Garcia, P.1
Gupta, R.2
Shah, S.3
Morris, A.J.4
Rudge, S.A.5
Scarlata, S.6
Petrova, V.7
McLaughlin, S.8
Rebecchi, M.J.9
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9
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0028132554
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Expression and characterization of an inositol 1,4,5-trisphosphate binding domain of phosphatidylinositol-specific phospholipase C-δ1
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Yagisawa H, Hirata M, Takashi K, Watanabe Y, Ozaki S, Sakuma K, Tanaka H, Yabuta Y, Kamata H, Hirata H, Nojima H. Expression and characterization of an inositol 1,4,5-trisphosphate binding domain of phosphatidylinositol-specific phospholipase C-δ1. J Biol Chem. 269:1994;20179-20188.
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Yagisawa, H.1
Hirata, M.2
Takashi, K.3
Watanabe, Y.4
Ozaki, S.5
Sakuma, K.6
Tanaka, H.7
Yabuta, Y.8
Kamata, H.9
Hirata, H.10
Nojima, H.11
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10
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0028874438
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Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
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Lemmon MA, Ferguson KM, O'Brien R, Sigler PB, Schlessinger J. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc Natl Acad Sci USA. 92:1995;10472-10476.
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Proc Natl Acad Sci USA
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Lemmon, M.A.1
Ferguson, K.M.2
O'Brien, R.3
Sigler, P.B.4
Schlessinger, J.5
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11
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0029617615
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Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
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Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell. 83:1995;1037-1046.
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Ferguson, K.M.1
Lemmon, M.A.2
Schlessinger, J.3
Sigler, P.B.4
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12
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0031050299
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Taxonomy and function of C1 protein kinase C homology domains
-
of special interest. The C1 domain (formerly known as the 'cys1 and cys2', 'zinc butterfly', 'zinc finger' or 'cysteine-rich domain' among other terms) nomenclature is standardized. The domains are considered as a structural family with diverse functions, enumerated and subdivided into those that bind phorbol ester (typical) and those that do not (atypical).
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Hurley JH, Newton AC, Parker PJ, Blumberg PM, Nishizuka Y. Taxonomy and function of C1 protein kinase C homology domains. of special interest Protein Sci. 6:1997;477-480 The C1 domain (formerly known as the 'cys1 and cys2', 'zinc butterfly', 'zinc finger' or 'cysteine-rich domain' among other terms) nomenclature is standardized. The domains are considered as a structural family with diverse functions, enumerated and subdivided into those that bind phorbol ester (typical) and those that do not (atypical).
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Protein Sci
, vol.6
, pp. 477-480
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Hurley, J.H.1
Newton, A.C.2
Parker, P.J.3
Blumberg, P.M.4
Nishizuka, Y.5
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13
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0028979464
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Crystal structure of the Cys2 activator-binding domain of protein kinase C δ in complex with phorbol ester
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Zhang G, Kazanietz MG, Blumberg PM, Hurley JH. Crystal structure of the Cys2 activator-binding domain of protein kinase C δ in complex with phorbol ester. Cell. 81:1995;917-924.
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Zhang, G.1
Kazanietz, M.G.2
Blumberg, P.M.3
Hurley, J.H.4
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14
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0028310840
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Zinc finger domains and phorbol ester pharmacophore: Analysis of binding to mutated form of protein kinase Cζ and the vav and c-raf proto-oncogene products
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Kazanietz MG, Bustelo XR, Barbacid M, Kolch W, Mischak H, Wong G, Pettit GR, Bruns JD, Blumberg PM. Zinc finger domains and phorbol ester pharmacophore: analysis of binding to mutated form of protein kinase Cζ and the vav and c-raf proto-oncogene products. J Biol Chem. 269:1994;11590-11594.
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Kazanietz, M.G.1
Bustelo, X.R.2
Barbacid, M.3
Kolch, W.4
Mischak, H.5
Wong, G.6
Pettit, G.R.7
Bruns, J.D.8
Blumberg, P.M.9
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15
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-
0029102822
-
Residues in the second cysteine-rich region of protein kinase C δ relevant to phorbol ester binding as revealed by site-directed mutagenesis
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Kazanietz MG, Wang S, Milne GWA, Lewin NE, Lui HL, Blumberg PM. Residues in the second cysteine-rich region of protein kinase C δ relevant to phorbol ester binding as revealed by site-directed mutagenesis. J Biol Chem. 270:1995;21852-21859.
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J Biol Chem
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Kazanietz, M.G.1
Wang, S.2
Milne, G.W.A.3
Lewin, N.E.4
Lui, H.L.5
Blumberg, P.M.6
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16
-
-
0029757119
-
The solution structure of the Raf-1 cysteine-rich domain: A novel Ras and phospholipid binding site
-
of special interest. The first structure of an atypical C1 domain explains why the atypical C1 domains do not bind phorbol ester or diacylglycerol. One wall of the binding groove is torn away as compared with a typical C1 domain.
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Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM, Campbell SL. The solution structure of the Raf-1 cysteine-rich domain: a novel Ras and phospholipid binding site. of special interest Proc Natl Acad Sci USA. 93:1996;8312-8317 The first structure of an atypical C1 domain explains why the atypical C1 domains do not bind phorbol ester or diacylglycerol. One wall of the binding groove is torn away as compared with a typical C1 domain.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 8312-8317
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-
Mott, H.R.1
Carpenter, J.W.2
Zhong, S.3
Ghosh, S.4
Bell, R.M.5
Campbell, S.L.6
-
17
-
-
0030467967
-
The C2 domain calcium-binding motif: Structural and functional diversity
-
of special interest. An invaluable compilation of the vast amount of information available on the full range of C2 domains and C2 domain containing proteins.
-
Nalefski EA, Falke JJ. The C2 domain calcium-binding motif: structural and functional diversity. of special interest Protein Sci. 5:1996;2375-2390 An invaluable compilation of the vast amount of information available on the full range of C2 domains and C2 domain containing proteins.
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(1996)
Protein Sci
, vol.5
, pp. 2375-2390
-
-
Nalefski, E.A.1
Falke, J.J.2
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19
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0029924329
-
Crystal structure of a mammalian phosphoinositide-specific phospholipase C δ
-
of outstanding interest. The structure of rat phosphoinositide-specific phospholipase C δ1, containing the EF-hand, catalytic, and C2 domains but with the PH domain removed, is reported. The catalytic domain resembles that of bacterial phosphatidylinositol-specific phospholipase C, and the C2 domain is a topologically permuted cousin of the synaptotagmin I C2 domain. All three domains interact via extensive contact surfaces.
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Essen LO, Perisic O, Cheung R, Katan M, Williams RL. Crystal structure of a mammalian phosphoinositide-specific phospholipase C δ of outstanding interest Nature. 380:1996;595-602 The structure of rat phosphoinositide-specific phospholipase C δ1, containing the EF-hand, catalytic, and C2 domains but with the PH domain removed, is reported. The catalytic domain resembles that of bacterial phosphatidylinositol-specific phospholipase C, and the C2 domain is a topologically permuted cousin of the synaptotagmin I C2 domain. All three domains interact via extensive contact surfaces.
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(1996)
Nature
, vol.380
, pp. 595-602
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Essen, L.O.1
Perisic, O.2
Cheung, R.3
Katan, M.4
Williams, R.L.5
-
20
-
-
0030967642
-
Similarity between C2 domain jaws and immunoglobulin CDRs
-
of special interest. The immunoglobulin fold has cropped up almost everywhere else in cell biology, and now we know that C2 domains are Ig folds. The occurrence of this fold in intracellular signal transduction is rationalized in terms of its unique suitability as a scaffold for generating diverse molecular recognition surfaces.
-
Grobler JA, Hurley JH. Similarity between C2 domain jaws and immunoglobulin CDRs. of special interest Nat Struct Biol. 4:1997;261-262 The immunoglobulin fold has cropped up almost everywhere else in cell biology, and now we know that C2 domains are Ig folds. The occurrence of this fold in intracellular signal transduction is rationalized in terms of its unique suitability as a scaffold for generating diverse molecular recognition surfaces.
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(1997)
Nat Struct Biol
, vol.4
, pp. 261-262
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Grobler, J.A.1
Hurley, J.H.2
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21
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0029772577
-
C2 domain conformational changes in phospholipase C δ
-
2+ activation of protein kinase C and other C2 domain containing proteins. The C2 domain jaws are implicated in function by this conformational change and by the docking of phospholipase C δ1 to a bilayer model.
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2+ activation of protein kinase C and other C2 domain containing proteins. The C2 domain jaws are implicated in function by this conformational change and by the docking of phospholipase C δ1 to a bilayer model.
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(1996)
Nat Struct Biol
, vol.3
, pp. 788-795
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Grobler, J.A.1
Essen, L.O.2
Williams, R.L.3
Hurley, J.H.4
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22
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-
0029666292
-
2+-binding motif in C2 domains of synaptotagmin and protein kinase C
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2+ ions to the C2 domains of protein kinase C βII and synaptotagmin I. Some resonances disappear in the aposynaptotagmin I spectrum, indicating changes in dynamics or average conformation, or both.
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2+ ions to the C2 domains of protein kinase C βII and synaptotagmin I. Some resonances disappear in the aposynaptotagmin I spectrum, indicating changes in dynamics or average conformation, or both.
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(1996)
Science
, vol.273
, pp. 248-251
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Shao, X.1
Davletov, B.A.2
Sutton, R.B.3
Sudhof, T.C.4
Rizo, J.5
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23
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0028356989
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Characterization of the calcium-binding site that regulates association of protein kinase C with phospholipid bilayers
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Mosior M, Epand RM. Characterization of the calcium-binding site that regulates association of protein kinase C with phospholipid bilayers. J Biol Chem. 269:1994;13798-13805.
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(1994)
J Biol Chem
, vol.269
, pp. 13798-13805
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Mosior, M.1
Epand, R.M.2
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24
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0028172171
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2+-dependent conformational change in synaptotagmin I
-
2+-dependent conformational change in synaptotagmin I. J Biol Chem. 269:1994;28547-28550.
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J Biol Chem
, vol.269
, pp. 28547-28550
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Davletov, B.A.1
Sudhof, T.C.2
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25
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0031016185
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Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C
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Essen L-O, Perisic O, Katan M, Wu Y, Roberts MF, Williams RL. Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C. Biochemistry. 36:1997;1704-1718.
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(1997)
Biochemistry
, vol.36
, pp. 1704-1718
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Essen, L.-O.1
Perisic, O.2
Katan, M.3
Wu, Y.4
Roberts, M.F.5
Williams, R.L.6
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26
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0029121937
-
Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol
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Heinz DW, Ryan M, Bullock TL, Griffith OH. Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol. EMBO J. 14:1995;3855-3863.
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EMBO J
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, pp. 3855-3863
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Heinz, D.W.1
Ryan, M.2
Bullock, T.L.3
Griffith, O.H.4
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27
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0027232834
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Interaction of proteins with lipid headgroups: Lessons from protein kinase C
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Newton AC. Interaction of proteins with lipid headgroups: lessons from protein kinase C. Annu Rev Biophys Biomol Struct. 22:1993;1-25.
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Annu Rev Biophys Biomol Struct
, vol.22
, pp. 1-25
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Newton, A.C.1
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28
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0030586160
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The effects of non-lamellar forming lipids on membrane protein - lipid interactions
-
of special interest. This paper presents a thoughtful argument that curvature stress is an important factor in protein - bilayer interactions.
-
Stubbs CD, Slater SJ. The effects of non-lamellar forming lipids on membrane protein - lipid interactions. of special interest Chem Phys Lipids. 81:1996;185-195 This paper presents a thoughtful argument that curvature stress is an important factor in protein - bilayer interactions.
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(1996)
Chem Phys Lipids
, vol.81
, pp. 185-195
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Stubbs, C.D.1
Slater, S.J.2
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29
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0027092982
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Phosphoinositide-specific phospholipase C-δ1: Effect of monolayer surface pressure and electrostatic surface potentials on activity
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Rebecchi M, Boguslavsky V, Boguslavsky L, McLaughlin S. Phosphoinositide-specific phospholipase C-δ1: effect of monolayer surface pressure and electrostatic surface potentials on activity. Biochemistry. 31:1992;12748-12753.
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(1992)
Biochemistry
, vol.31
, pp. 12748-12753
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Rebecchi, M.1
Boguslavsky, V.2
Boguslavsky, L.3
McLaughlin, S.4
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31
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0029130345
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Lipid signaling enzymes and surface dilution kinetics
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Carman GM, Deems RA, Dennis EA. Lipid signaling enzymes and surface dilution kinetics. J Biol Chem. 270:1995;18711-18714.
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(1995)
J Biol Chem
, vol.270
, pp. 18711-18714
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Carman, G.M.1
Deems, R.A.2
Dennis, E.A.3
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32
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0030062076
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Calcium-independent binding to interfacial phorbol esters causes protein kinase C to associate with membranes in the absence of acidic lipids
-
of outstanding interest. This ambitious attempt to formulate the membrane binding of protein kinase C in terms of a rigorous model of linked equilibria puts the classical activation scheme into a new perspective. Binding experiments and mathematical modeling show that the requirement of protein kinase C for one type of activator can be bypassed in the presence of a large excess of another activator.
-
Mosior M, Newton AC. Calcium-independent binding to interfacial phorbol esters causes protein kinase C to associate with membranes in the absence of acidic lipids. of outstanding interest Biochemistry. 35:1996;1612-1623 This ambitious attempt to formulate the membrane binding of protein kinase C in terms of a rigorous model of linked equilibria puts the classical activation scheme into a new perspective. Binding experiments and mathematical modeling show that the requirement of protein kinase C for one type of activator can be bypassed in the presence of a large excess of another activator.
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(1996)
Biochemistry
, vol.35
, pp. 1612-1623
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Mosior, M.1
Newton, A.C.2
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33
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0028203902
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Effect of monolayer surface pressure on the activities of phosphoinositide-specific phospholipase C-β1, γ1, and δ1
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Boguslavsky V, Rebecchi M, Morris AJ, Jhon DY, Rhee SG, McLaughlin S. Effect of monolayer surface pressure on the activities of phosphoinositide-specific phospholipase C-β1, γ1, and δ1. Biochemistry. 33:1994;3032-3037.
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(1994)
Biochemistry
, vol.33
, pp. 3032-3037
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Boguslavsky, V.1
Rebecchi, M.2
Morris, A.J.3
Jhon, D.Y.4
Rhee, S.G.5
McLaughlin, S.6
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34
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0031050619
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Dependence of the activity of phospholipase Cβ on surface pressure and surface composition in phospholipid monolayers and its implications for their regulation
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James SR, Paterson A, Harden TK, Demel RA, Downes CP. Dependence of the activity of phospholipase Cβ on surface pressure and surface composition in phospholipid monolayers and its implications for their regulation. Biochemistry. 36:1997;848-855.
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Biochemistry
, vol.36
, pp. 848-855
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James, S.R.1
Paterson, A.2
Harden, T.K.3
Demel, R.A.4
Downes, C.P.5
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35
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0023747140
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Association of protein kinase C with phospholipid monolayers: Two-stage irreversible binding
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Bazzi MD, Nelsestuen GL. Association of protein kinase C with phospholipid monolayers: two-stage irreversible binding. Biochemistry. 27:1988;6776-6783.
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(1988)
Biochemistry
, vol.27
, pp. 6776-6783
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Bazzi, M.D.1
Nelsestuen, G.L.2
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36
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0026074358
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Activation of protein kinase C in lipid monolayers
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Souvignet C, Pelosin J-M, Daniel S, Chambaz E, Ransac S, Verger R. Activation of protein kinase C in lipid monolayers. J Biol Chem. 266:1991;40-44.
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J Biol Chem
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Souvignet, C.1
Pelosin, J.-M.2
Daniel, S.3
Chambaz, E.4
Ransac, S.5
Verger, R.6
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37
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0026729365
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Effect of phospholipid unsaturation on protein kinase C activation
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Bolen EJ, Sando JJ. Effect of phospholipid unsaturation on protein kinase C activation. Biochemistry. 31:1992;5945-5951.
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Biochemistry
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Bolen, E.J.1
Sando, J.J.2
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0028840703
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Role of phospholipids containing docosahexaenoyl chains in modulating the activity of protein kinase C
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Giorgione J, Epand RM, Buda C, Farkas T. Role of phospholipids containing docosahexaenoyl chains in modulating the activity of protein kinase C. Proc Natl Acad Sci USA. 92:1995;9767-9770.
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Proc Natl Acad Sci USA
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, pp. 9767-9770
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Giorgione, J.1
Epand, R.M.2
Buda, C.3
Farkas, T.4
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39
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0028075333
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The modulation of protein kinase C activity by membrane lipid bilayer structure
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Slater SJ, Kelly MB, Taddeo FJ, Ho C, Rugin E, Stubbs CD. The modulation of protein kinase C activity by membrane lipid bilayer structure. J Biol Chem. 269:1994;4866-4871.
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(1994)
J Biol Chem
, vol.269
, pp. 4866-4871
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Slater, S.J.1
Kelly, M.B.2
Taddeo, F.J.3
Ho, C.4
Rugin, E.5
Stubbs, C.D.6
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40
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0029966229
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Transbilayer inhibition of protein kinase C by the lipophosphoglycan from Leishmania donovani
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Giorgione JR, Turco SJ, Epand RM. Transbilayer inhibition of protein kinase C by the lipophosphoglycan from Leishmania donovani. Proc Natl Acad Sci USA. 93:1996;11634-11639.
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Proc Natl Acad Sci USA
, vol.93
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Giorgione, J.R.1
Turco, S.J.2
Epand, R.M.3
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41
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10244224044
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Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol-4,5 bisphosphate in lateral domains
-
of outstanding interest. Microdomain formation induced by the MARCKS protein inhibits phospholipase C and is reversible by protein kinase C phosphorylation.
-
Glaser M, Wanaski S, Buser CA, Boguslavsky V, Rashidzada W, Morris A, Rebecchi M, Scarlata SF, Runnels LW, Prestwich GD, et al. Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol-4,5 bisphosphate in lateral domains. of outstanding interest J Biol Chem. 271:1996;26187-26193 Microdomain formation induced by the MARCKS protein inhibits phospholipase C and is reversible by protein kinase C phosphorylation.
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(1996)
J Biol Chem
, vol.271
, pp. 26187-26193
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-
Glaser, M.1
Wanaski, S.2
Buser, C.A.3
Boguslavsky, V.4
Rashidzada, W.5
Morris, A.6
Rebecchi, M.7
Scarlata, S.F.8
Runnels, L.W.9
Prestwich, G.D.10
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42
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0028952293
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Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C
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Yang L, Glaser M. Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C. Biochemistry. 34:1995;1500-1506.
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(1995)
Biochemistry
, vol.34
, pp. 1500-1506
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Yang, L.1
Glaser, M.2
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43
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0029904712
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Formation of membrane domains during the activation of protein kinase C
-
of outstanding interest. Fluorescence microscopy is used to directly observe protein kinase C colocalizing with membrane domains under activating conditions.
-
Yang L, Glaser M. Formation of membrane domains during the activation of protein kinase C. of outstanding interest Biochemistry. 35:1996;13966-13974 Fluorescence microscopy is used to directly observe protein kinase C colocalizing with membrane domains under activating conditions.
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(1996)
Biochemistry
, vol.35
, pp. 13966-13974
-
-
Yang, L.1
Glaser, M.2
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44
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0029792683
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Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation
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of special interest. Microdomains and microdomain boundary formation monitored thermodynamically and correlated with protein kinase C activation.
-
Dibble ARG, Hinderliter AK, Sando JJ, Biltonen RL. Lipid lateral heterogeneity in phosphatidylcholine/phosphatidylserine/diacylglycerol vesicles and its influence on protein kinase C activation. of special interest Biophys J. 71:1996;1877-1890 Microdomains and microdomain boundary formation monitored thermodynamically and correlated with protein kinase C activation.
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(1996)
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