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Volumn 1761, Issue 8, 2006, Pages 913-926

Phosphatidic acid- and phosphatidylserine-binding proteins

Author keywords

Lipid recognition; Lipid signaling; Phosphatidic acid; Phosphatidylserine; Phospholipase D

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ANNEXIN; BINDING PROTEIN; DISCOIDIN; FK 506 BINDING PROTEIN; GROWTH ARREST SPECIFIC PROTEIN 6; KINESIN; LIPOCORTIN 5; MAMMALIAN TARGET OF RAPAMYCIN; MARCKS PROTEIN; NITRIC OXIDE SYNTHASE; PHOSPHATIDIC ACID; PHOSPHATIDYLSERINE; PHOSPHODIESTERASE IV; PHOSPHOENOLPYRUVATE CARBOXYLASE; PHOSPHOLIPASE D; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN C; PROTEIN KINASE C EPSILON; PROTEIN KINASE C GAMMA; PROTEIN P47; PROTEIN S; PROTEIN TYROSINE PHOSPHATASE SHP 1; RAF PROTEIN; SCAVENGER RECEPTOR; SNARE PROTEIN; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOSINE KINASE 1; SYNAPTOTAGMIN; VINCULIN;

EID: 33748300590     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2006.03.006     Document Type: Review
Times cited : (322)

References (128)
  • 1
    • 0025746264 scopus 로고
    • Organelle biogenesis and intracellular lipid transport in eukaryotes
    • Voelker D.R. Organelle biogenesis and intracellular lipid transport in eukaryotes. Microbiol. Rev. 55 (1991) 543
    • (1991) Microbiol. Rev. , vol.55 , pp. 543
    • Voelker, D.R.1
  • 2
    • 0033571069 scopus 로고    scopus 로고
    • Phosphatidic acid, a key intermediate in lipid metabolism
    • Athenstaedt K., and Daum G. Phosphatidic acid, a key intermediate in lipid metabolism. Eur. J. Biochem. 266 (1999) 1
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1
    • Athenstaedt, K.1    Daum, G.2
  • 3
    • 0032775007 scopus 로고    scopus 로고
    • Regulation of phospholipase D
    • Exton J. Regulation of phospholipase D. Biochim. Biophys. Acta 1439 (1999) 121
    • (1999) Biochim. Biophys. Acta , vol.1439 , pp. 121
    • Exton, J.1
  • 4
    • 23644455714 scopus 로고    scopus 로고
    • Phospholipase D: a lipid centric review
    • Jenkins G.M., and Frohman M.A. Phospholipase D: a lipid centric review. Cell. Mol. Life Sci. 62 (2005) 2305
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2305
    • Jenkins, G.M.1    Frohman, M.A.2
  • 6
    • 21044440329 scopus 로고    scopus 로고
    • Isolation of a Drosophila gene coding for a protein containing a novel phosphatidylserine-binding motif
    • Nakai Y., Nomura Y., Sato T., Shiratsuchi A., and Nakanishi Y. Isolation of a Drosophila gene coding for a protein containing a novel phosphatidylserine-binding motif. J. Biochem. (Tokyo) 137 (2005) 593
    • (2005) J. Biochem. (Tokyo) , vol.137 , pp. 593
    • Nakai, Y.1    Nomura, Y.2    Sato, T.3    Shiratsuchi, A.4    Nakanishi, Y.5
  • 7
    • 25844442435 scopus 로고    scopus 로고
    • A membrane binding domain in the ste5 scaffold synergizes with gbetagamma binding to control localization and signaling in pheromone response
    • Winters M.J., Lamson R.E., Nakanishi H., Neiman A.M., and Pryciak P.M. A membrane binding domain in the ste5 scaffold synergizes with gbetagamma binding to control localization and signaling in pheromone response. Mol. Cell 20 (2005) 21
    • (2005) Mol. Cell , vol.20 , pp. 21
    • Winters, M.J.1    Lamson, R.E.2    Nakanishi, H.3    Neiman, A.M.4    Pryciak, P.M.5
  • 8
  • 9
    • 0031972511 scopus 로고    scopus 로고
    • Replacements of single basic amino acids in the pleckstrin homology domain of phospholipase C-delta1 alter the ligand binding, phospholipase activity, and interaction with the plasma membrane
    • Yagisawa H., Sakuma K., Paterson H.F., Cheung R., Allen V., Hirata H., Watanabe Y., Hirata M., Williams R.L., and Katan M. Replacements of single basic amino acids in the pleckstrin homology domain of phospholipase C-delta1 alter the ligand binding, phospholipase activity, and interaction with the plasma membrane. J. Biol. Chem. 273 (1998) 417
    • (1998) J. Biol. Chem. , vol.273 , pp. 417
    • Yagisawa, H.1    Sakuma, K.2    Paterson, H.F.3    Cheung, R.4    Allen, V.5    Hirata, H.6    Watanabe, Y.7    Hirata, M.8    Williams, R.L.9    Katan, M.10
  • 10
    • 0032555778 scopus 로고    scopus 로고
    • Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules
    • Newton A.C., and Johnson J.E. Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules. Biochim. Biophys. Acta 1376 (1998) 155
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 155
    • Newton, A.C.1    Johnson, J.E.2
  • 11
    • 0036791737 scopus 로고    scopus 로고
    • Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction
    • Karathanassis D., Stahelin R.V., Bravo J., Perisic O., Pacold C.M., Cho W., and Williams R.L. Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. EMBO J. 21 (2002) 5057
    • (2002) EMBO J. , vol.21 , pp. 5057
    • Karathanassis, D.1    Stahelin, R.V.2    Bravo, J.3    Perisic, O.4    Pacold, C.M.5    Cho, W.6    Williams, R.L.7
  • 12
    • 0032007533 scopus 로고    scopus 로고
    • Interaction of phosphatidic acid and phosphatidylserine with the Ca2+-ATPase of sarcoplasmic reticulum and the mechanism of inhibition
    • Dalton K.A., East J.M., Mall S., Oliver S., Starling A.P., and Lee A.G. Interaction of phosphatidic acid and phosphatidylserine with the Ca2+-ATPase of sarcoplasmic reticulum and the mechanism of inhibition. Biochem. J. 329 Pt 3 (1998) 637
    • (1998) Biochem. J. , vol.329 , Issue.PART 3 , pp. 637
    • Dalton, K.A.1    East, J.M.2    Mall, S.3    Oliver, S.4    Starling, A.P.5    Lee, A.G.6
  • 13
    • 0037213576 scopus 로고    scopus 로고
    • Phosphatidic acid stimulates cardiac KATP channels like phosphatidylinositols, but with novel gating kinetics
    • Fan Z., Gao L., and Wang W. Phosphatidic acid stimulates cardiac KATP channels like phosphatidylinositols, but with novel gating kinetics. Am. J. Physiol.: Cell Physiol. 284 (2003) C94
    • (2003) Am. J. Physiol.: Cell Physiol. , vol.284
    • Fan, Z.1    Gao, L.2    Wang, W.3
  • 15
    • 0026744154 scopus 로고
    • Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase.
    • Moritz A., De P., Graan N., Gispen W.H., and Wirtz K.W. Phosphatidic acid is a specific activator of phosphatidylinositol-4-phosphate kinase. J. Biol. Chem. 267 (1992) 7207
    • (1992) J. Biol. Chem. , vol.267 , pp. 7207
    • Moritz, A.1    De, P.2    Graan, N.3    Gispen, W.H.4    Wirtz, K.W.5
  • 18
    • 0028346383 scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid.
    • Jenkins G., Fisette P., and Anderson R. Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid. J. Biol. Chem. 269 (1994) 11547
    • (1994) J. Biol. Chem. , vol.269 , pp. 11547
    • Jenkins, G.1    Fisette, P.2    Anderson, R.3
  • 19
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: the PITP/phosphoinositide connection
    • Liscovitch M., and Cantley L.C. Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell 81 (1995) 659
    • (1995) Cell , vol.81 , pp. 659
    • Liscovitch, M.1    Cantley, L.C.2
  • 20
    • 0029964454 scopus 로고    scopus 로고
    • Effect of acidic phospholipids on sphingosine kinase
    • Olivera A., Rosenthal J., and Spiegel S. Effect of acidic phospholipids on sphingosine kinase. J. Cell. Biochem. 60 (1996) 529
    • (1996) J. Cell. Biochem. , vol.60 , pp. 529
    • Olivera, A.1    Rosenthal, J.2    Spiegel, S.3
  • 21
    • 0036196957 scopus 로고    scopus 로고
    • Phospholipase D and immune receptor signalling
    • Melendez A., and Allen J. Phospholipase D and immune receptor signalling. Semin. Immunol. 14 (2002) 49
    • (2002) Semin. Immunol. , vol.14 , pp. 49
    • Melendez, A.1    Allen, J.2
  • 24
    • 3042694078 scopus 로고    scopus 로고
    • Phospholipase D alpha 1-derived phosphatidic acid interacts with ABI1 phosphatase 2C and regulates abscisic acid signaling
    • Zhang W., Qin C., Zhao J., and Wang X. Phospholipase D alpha 1-derived phosphatidic acid interacts with ABI1 phosphatase 2C and regulates abscisic acid signaling. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 9508
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9508
    • Zhang, W.1    Qin, C.2    Zhao, J.3    Wang, X.4
  • 25
    • 23044460008 scopus 로고    scopus 로고
    • Phosphatidic acid: a multifunctional stress signaling lipid in plants
    • Testerink C., and Munnik T. Phosphatidic acid: a multifunctional stress signaling lipid in plants. Trends Plant Sci. 10 (2005) 368
    • (2005) Trends Plant Sci. , vol.10 , pp. 368
    • Testerink, C.1    Munnik, T.2
  • 26
    • 31844454590 scopus 로고    scopus 로고
    • Regulatory functions of phospholipase D and phosphatidic acid in plant growth, development, and stress responses
    • Wang X. Regulatory functions of phospholipase D and phosphatidic acid in plant growth, development, and stress responses. Plant Physiol. 139 (2005) 566
    • (2005) Plant Physiol. , vol.139 , pp. 566
    • Wang, X.1
  • 27
    • 0029935339 scopus 로고    scopus 로고
    • Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells
    • Ghosh S., Strum J.C., Sciorra V.A., Daniel L., and Bell R.M. Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells. J. Biol. Chem. 271 (1996) 8472
    • (1996) J. Biol. Chem. , vol.271 , pp. 8472
    • Ghosh, S.1    Strum, J.C.2    Sciorra, V.A.3    Daniel, L.4    Bell, R.M.5
  • 28
    • 0034604717 scopus 로고    scopus 로고
    • The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras
    • Rizzo M.A., Shome K., Watkins S.C., and Romero G. The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras. J. Biol. Chem. 275 (2000) 23911
    • (2000) J. Biol. Chem. , vol.275 , pp. 23911
    • Rizzo, M.A.1    Shome, K.2    Watkins, S.C.3    Romero, G.4
  • 29
    • 0037201947 scopus 로고    scopus 로고
    • The role of phosphatidic acid in the regulation of the Ras/MEK/Erk signaling cascade
    • Andresen B.T., Rizzo M.A., Shome K., and Romero G. The role of phosphatidic acid in the regulation of the Ras/MEK/Erk signaling cascade. FEBS Lett. 531 (2002) 65
    • (2002) FEBS Lett. , vol.531 , pp. 65
    • Andresen, B.T.1    Rizzo, M.A.2    Shome, K.3    Romero, G.4
  • 30
    • 0242664746 scopus 로고    scopus 로고
    • Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos
    • Ghosh S., Moore S., Bell R.M., and Dush M. Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos. J. Biol. Chem. 278 (2003) 45690
    • (2003) J. Biol. Chem. , vol.278 , pp. 45690
    • Ghosh, S.1    Moore, S.2    Bell, R.M.3    Dush, M.4
  • 31
    • 0344443675 scopus 로고    scopus 로고
    • The simultaneous production of phosphatidic acid and diacylglycerol is essential for the translocation of protein kinase Cepsilon to the plasma membrane in RBL-2H3 cells
    • Jose Lopez-Andreo M., Corbalan-Garcia J.C.G.-F., and S. The simultaneous production of phosphatidic acid and diacylglycerol is essential for the translocation of protein kinase Cepsilon to the plasma membrane in RBL-2H3 cells. Mol. Biol. Cell 14 (2003) 4885
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4885
    • Jose Lopez-Andreo, M.1    Corbalan-Garcia J.C.G.-F.,, S.2
  • 33
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N., and Sonenberg N. Upstream and downstream of mTOR. Genes Dev. 18 (2004) 1926
    • (2004) Genes Dev. , vol.18 , pp. 1926
    • Hay, N.1    Sonenberg, N.2
  • 34
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation of mTOR signaling
    • Fang Y., Vilella-Bach M., Bachmann R., Flanigan A., and Chen J. Phosphatidic acid-mediated mitogenic activation of mTOR signaling. Science 294 (2001) 1942
    • (2001) Science , vol.294 , pp. 1942
    • Fang, Y.1    Vilella-Bach, M.2    Bachmann, R.3    Flanigan, A.4    Chen, J.5
  • 36
    • 15444378732 scopus 로고    scopus 로고
    • Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid
    • Avila-Flores A., Santos T., Rincon E., and Merida I. Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid. J. Biol. Chem. 280 (2005) 10091
    • (2005) J. Biol. Chem. , vol.280 , pp. 10091
    • Avila-Flores, A.1    Santos, T.2    Rincon, E.3    Merida, I.4
  • 37
    • 1642546271 scopus 로고    scopus 로고
    • Positive and negative regulation of a SNARE protein by control of intracellular localization
    • Nakanishi H., de los Santos P., and Neiman A.M. Positive and negative regulation of a SNARE protein by control of intracellular localization. Mol. Biol. Cell 15 (2004) 1802
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1802
    • Nakanishi, H.1    de los Santos, P.2    Neiman, A.M.3
  • 38
    • 26944463126 scopus 로고    scopus 로고
    • Phosphatidylserine-dependent engulfment by macrophages of nuclei from erythroid precursor cells
    • Yoshida H., Kawane K., Koike M., Mori Y., Uchiyama Y., and Nagata S. Phosphatidylserine-dependent engulfment by macrophages of nuclei from erythroid precursor cells. Nature 437 (2005) 754
    • (2005) Nature , vol.437 , pp. 754
    • Yoshida, H.1    Kawane, K.2    Koike, M.3    Mori, Y.4    Uchiyama, Y.5    Nagata, S.6
  • 39
    • 0026635971 scopus 로고
    • Interaction of protein kinase C with phosphatidylserine. 2. Specificity and regulation
    • Orr J.W., and Newton A.C. Interaction of protein kinase C with phosphatidylserine. 2. Specificity and regulation. Biochemistry 31 (1992) 4667
    • (1992) Biochemistry , vol.31 , pp. 4667
    • Orr, J.W.1    Newton, A.C.2
  • 41
    • 0035830872 scopus 로고    scopus 로고
    • Roles of ionic residues of the C1 domain in protein kinase C-alpha activation and the origin of phosphatidylserine specificity
    • Bittova L., Stahelin R.V., and Cho W. Roles of ionic residues of the C1 domain in protein kinase C-alpha activation and the origin of phosphatidylserine specificity. J. Biol. Chem. 276 (2001) 4218
    • (2001) J. Biol. Chem. , vol.276 , pp. 4218
    • Bittova, L.1    Stahelin, R.V.2    Cho, W.3
  • 42
    • 0032533457 scopus 로고    scopus 로고
    • Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+
    • Sutton R.B., and Sprang S.R. Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+. Structure 6 (1998) 1395
    • (1998) Structure , vol.6 , pp. 1395
    • Sutton, R.B.1    Sprang, S.R.2
  • 43
    • 0033571223 scopus 로고    scopus 로고
    • Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine
    • Verdaguer N., Corbalan-Garcia S., Ochoa W.F., Fita I., and Gomez-Fernandez J.C. Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine. EMBO J. 18 (1999) 6329
    • (1999) EMBO J. , vol.18 , pp. 6329
    • Verdaguer, N.1    Corbalan-Garcia, S.2    Ochoa, W.F.3    Fita, I.4    Gomez-Fernandez, J.C.5
  • 44
    • 0036297772 scopus 로고    scopus 로고
    • Additional binding sites for anionic phospholipids and calcium ions in the crystal structures of complexes of the C2 domain of protein kinase calpha
    • Ochoa W.F., Corbalan-Garcia S., Eritja R., Rodriguez-Alfaro J.A., Gomez-Fernandez J.C., Fita I., and Verdaguer N. Additional binding sites for anionic phospholipids and calcium ions in the crystal structures of complexes of the C2 domain of protein kinase calpha. J. Mol. Biol. 320 (2002) 277
    • (2002) J. Mol. Biol. , vol.320 , pp. 277
    • Ochoa, W.F.1    Corbalan-Garcia, S.2    Eritja, R.3    Rodriguez-Alfaro, J.A.4    Gomez-Fernandez, J.C.5    Fita, I.6    Verdaguer, N.7
  • 45
    • 0035923393 scopus 로고    scopus 로고
    • Identification of the phosphatidylserine binding site in the C2 domain that is important for PKC alpha activation and in vivo cell localization
    • Conesa-Zamora P., Lopez-Andreo M.J., Gomez-Fernandez J.C., and Corbalan-Garcia S. Identification of the phosphatidylserine binding site in the C2 domain that is important for PKC alpha activation and in vivo cell localization. Biochemistry 40 (2001) 13898
    • (2001) Biochemistry , vol.40 , pp. 13898
    • Conesa-Zamora, P.1    Lopez-Andreo, M.J.2    Gomez-Fernandez, J.C.3    Corbalan-Garcia, S.4
  • 46
    • 0031915943 scopus 로고    scopus 로고
    • Independent folding and ligand specificity of the C2 calcium-dependent lipid binding domain of cytosolic phospholipase A2
    • Nalefski E.A., McDonagh T., Somers W., Seehra J., Falke J.J., and Clark J.D. Independent folding and ligand specificity of the C2 calcium-dependent lipid binding domain of cytosolic phospholipase A2. J. Biol. Chem. 273 (1998) 1365
    • (1998) J. Biol. Chem. , vol.273 , pp. 1365
    • Nalefski, E.A.1    McDonagh, T.2    Somers, W.3    Seehra, J.4    Falke, J.J.5    Clark, J.D.6
  • 47
    • 0027332736 scopus 로고
    • A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding
    • Davletov B.A., and Sudhof T.C. A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding. J. Biol. Chem. 268 (1993) 26386
    • (1993) J. Biol. Chem. , vol.268 , pp. 26386
    • Davletov, B.A.1    Sudhof, T.C.2
  • 48
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold
    • Sutton R.B., Davletov B.A., Berghuis A.M., Sudhof T.C., and Sprang S.R. Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell 80 (1995) 929
    • (1995) Cell , vol.80 , pp. 929
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Sudhof, T.C.4    Sprang, S.R.5
  • 49
    • 0031019191 scopus 로고    scopus 로고
    • Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch
    • Shao X., Li C., Fernandez I., Zhang X., Sudhof T.C., and Rizo J. Synaptotagmin-syntaxin interaction: the C2 domain as a Ca2+-dependent electrostatic switch. Neuron 18 (1997) 133
    • (1997) Neuron , vol.18 , pp. 133
    • Shao, X.1    Li, C.2    Fernandez, I.3    Zhang, X.4    Sudhof, T.C.5    Rizo, J.6
  • 50
    • 0035943587 scopus 로고    scopus 로고
    • The top loops of the C(2) domains from synaptotagmin and phospholipase A(2) control functional specificity
    • Gerber S.H., Rizo J., and Sudhof T.C. The top loops of the C(2) domains from synaptotagmin and phospholipase A(2) control functional specificity. J. Biol. Chem. 276 (2001) 32288
    • (2001) J. Biol. Chem. , vol.276 , pp. 32288
    • Gerber, S.H.1    Rizo, J.2    Sudhof, T.C.3
  • 51
    • 0030933176 scopus 로고    scopus 로고
    • A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-delta1
    • Essen L.O., Perisic O., Lynch D.E., Katan M., and Williams R.L. A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-delta1. Biochemistry 36 (1997) 2753
    • (1997) Biochemistry , vol.36 , pp. 2753
    • Essen, L.O.1    Perisic, O.2    Lynch, D.E.3    Katan, M.4    Williams, R.L.5
  • 52
  • 53
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen L.O., Perisic O., Cheung R., Katan M., and Williams R.L. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature 380 (1996) 595
    • (1996) Nature , vol.380 , pp. 595
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 56
    • 0030967015 scopus 로고    scopus 로고
    • Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site
    • McDonald J.F., Shah A.M., Schwalbe R.A., Kisiel W., Dahlback B., and Nelsestuen G.L. Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site. Biochemistry 36 (1997) 5120
    • (1997) Biochemistry , vol.36 , pp. 5120
    • McDonald, J.F.1    Shah, A.M.2    Schwalbe, R.A.3    Kisiel, W.4    Dahlback, B.5    Nelsestuen, G.L.6
  • 57
    • 0026610682 scopus 로고
    • The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1
    • Soriano-Garcia M., Padmanabhan K., de Vos A.M., and Tulinsky A. The Ca2+ ion and membrane binding structure of the Gla domain of Ca-prothrombin fragment 1. Biochemistry 31 (1992) 2554
    • (1992) Biochemistry , vol.31 , pp. 2554
    • Soriano-Garcia, M.1    Padmanabhan, K.2    de Vos, A.M.3    Tulinsky, A.4
  • 58
    • 0025042434 scopus 로고
    • Prothrombin activation on membranes with anionic lipids containing phosphate, sulfate, and/or carboxyl groups
    • Gerads I., Govers-Riemslag J.W., Tans G., Zwaal R.F., and Rosing J. Prothrombin activation on membranes with anionic lipids containing phosphate, sulfate, and/or carboxyl groups. Biochemistry 29 (1990) 7967
    • (1990) Biochemistry , vol.29 , pp. 7967
    • Gerads, I.1    Govers-Riemslag, J.W.2    Tans, G.3    Zwaal, R.F.4    Rosing, J.5
  • 61
    • 12144254763 scopus 로고    scopus 로고
    • The phosphatidylserine binding site of the factor Va C2 domain accounts for membrane binding but does not contribute to the assembly or activity of a human factor Xa-factor Va complex
    • Majumder R., Quinn-Allen M.A., Kane W.H., and Lentz B.R. The phosphatidylserine binding site of the factor Va C2 domain accounts for membrane binding but does not contribute to the assembly or activity of a human factor Xa-factor Va complex. Biochemistry 44 (2005) 711
    • (2005) Biochemistry , vol.44 , pp. 711
    • Majumder, R.1    Quinn-Allen, M.A.2    Kane, W.H.3    Lentz, B.R.4
  • 63
    • 0028783371 scopus 로고
    • Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V
    • Swairjo M.A., Concha N.O., Kaetzel M.A., Dedman J.R., and Seaton B.A. Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V. Nat. Struct. Biol. 2 (1995) 968
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 968
    • Swairjo, M.A.1    Concha, N.O.2    Kaetzel, M.A.3    Dedman, J.R.4    Seaton, B.A.5
  • 64
    • 0028245914 scopus 로고
    • Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study
    • Voges D., Berendes R., Burger A., Demange P., Baumeister W., and Huber R. Three-dimensional structure of membrane-bound annexin V. A correlative electron microscopy-X-ray crystallography study. J. Mol. Biol. 238 (1994) 199
    • (1994) J. Mol. Biol. , vol.238 , pp. 199
    • Voges, D.1    Berendes, R.2    Burger, A.3    Demange, P.4    Baumeister, W.5    Huber, R.6
  • 66
    • 0033521695 scopus 로고    scopus 로고
    • Receptors for oxidized low density lipoprotein
    • Steinbrecher U.P. Receptors for oxidized low density lipoprotein. Biochim. Biophys. Acta 1436 (1999) 279
    • (1999) Biochim. Biophys. Acta , vol.1436 , pp. 279
    • Steinbrecher, U.P.1
  • 67
    • 0028173897 scopus 로고
    • Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP)
    • Krieger M., and Herz J. Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP). Annu. Rev. Biochem. 63 (1994) 601
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 601
    • Krieger, M.1    Herz, J.2
  • 69
    • 0029855586 scopus 로고    scopus 로고
    • Role of divalency in the high-affinity binding of anticardiolipin antibody-beta 2-glycoprotein I complexes to lipid membranes
    • Willems G.M., Janssen M.P., Pelsers M.M., Comfurius P., Galli M., Zwaal R.F., and Bevers E.M. Role of divalency in the high-affinity binding of anticardiolipin antibody-beta 2-glycoprotein I complexes to lipid membranes. Biochemistry 35 (1996) 13833
    • (1996) Biochemistry , vol.35 , pp. 13833
    • Willems, G.M.1    Janssen, M.P.2    Pelsers, M.M.3    Comfurius, P.4    Galli, M.5    Zwaal, R.F.6    Bevers, E.M.7
  • 70
    • 0037821876 scopus 로고    scopus 로고
    • Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer
    • Zhang W., Crocker E., McLaughlin S., and Smith S.O. Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer. J. Biol. Chem. 278 (2003) 21459
    • (2003) J. Biol. Chem. , vol.278 , pp. 21459
    • Zhang, W.1    Crocker, E.2    McLaughlin, S.3    Smith, S.O.4
  • 71
    • 0029075019 scopus 로고
    • Characterization of the phosphatidylserine-binding region of rat MARCKS (myristoylated, alanine-rich protein kinase C substrate). Its regulation through phosphorylation of serine 152
    • Nakaoka T., Kojima N., Ogita T., and Tsuji S. Characterization of the phosphatidylserine-binding region of rat MARCKS (myristoylated, alanine-rich protein kinase C substrate). Its regulation through phosphorylation of serine 152. J. Biol. Chem. 270 (1995) 12147
    • (1995) J. Biol. Chem. , vol.270 , pp. 12147
    • Nakaoka, T.1    Kojima, N.2    Ogita, T.3    Tsuji, S.4
  • 72
    • 0035895882 scopus 로고    scopus 로고
    • The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate
    • Wang J., Arbuzova A., Hangyas-Mihalyne G., and McLaughlin S. The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 276 (2001) 5012
    • (2001) J. Biol. Chem. , vol.276 , pp. 5012
    • Wang, J.1    Arbuzova, A.2    Hangyas-Mihalyne, G.3    McLaughlin, S.4
  • 73
    • 0033554368 scopus 로고    scopus 로고
    • Binding of phosphatidic acid to protein-tyrosine phosphatase SHP-1 as a basis for activity modulation.
    • Frank C., Keilhack H., Opitz F., Zschoring O., and Bohmer F. Binding of phosphatidic acid to protein-tyrosine phosphatase SHP-1 as a basis for activity modulation. Biochemistry 38 (1999) 11993
    • (1999) Biochemistry , vol.38 , pp. 11993
    • Frank, C.1    Keilhack, H.2    Opitz, F.3    Zschoring, O.4    Bohmer, F.5
  • 74
    • 0037013237 scopus 로고    scopus 로고
    • Tight binding inhibition of protein phosphatase-1 by phosphatidic acid. Specificity of inhibition by the phospholipid
    • Jones J.A., and Hannun Y.A. Tight binding inhibition of protein phosphatase-1 by phosphatidic acid. Specificity of inhibition by the phospholipid. J. Biol. Chem. 277 (2002) 15530
    • (2002) J. Biol. Chem. , vol.277 , pp. 15530
    • Jones, J.A.1    Hannun, Y.A.2
  • 75
    • 26444524348 scopus 로고    scopus 로고
    • Identification of a novel phosphatidic acid binding domain in protein phosphatase-1
    • Jones J.A., Rawles R., and Hannun Y.A. Identification of a novel phosphatidic acid binding domain in protein phosphatase-1. Biochemistry 44 (2005) 13235
    • (2005) Biochemistry , vol.44 , pp. 13235
    • Jones, J.A.1    Rawles, R.2    Hannun, Y.A.3
  • 76
    • 0034721870 scopus 로고    scopus 로고
    • The cAMP-specific phosphodiesterase PDE4D3 is regulated by phosphatidic acid binding. Consequences for cAMP signaling pathway and characterization of a phosphatidic acid binding site
    • Grange M., Sette C., Cuomo M., Conti M., Lagarde M., Prigent A.F., and Nemoz G. The cAMP-specific phosphodiesterase PDE4D3 is regulated by phosphatidic acid binding. Consequences for cAMP signaling pathway and characterization of a phosphatidic acid binding site. J. Biol. Chem. 275 (2000) 33379
    • (2000) J. Biol. Chem. , vol.275 , pp. 33379
    • Grange, M.1    Sette, C.2    Cuomo, M.3    Conti, M.4    Lagarde, M.5    Prigent, A.F.6    Nemoz, G.7
  • 78
    • 0037073704 scopus 로고    scopus 로고
    • AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton
    • Nie Z., Stanley K.T., Stauffer S., Jacques K.M., Hirsch D.S., Takei J., and Randazzo P.A. AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton. J. Biol. Chem. 277 (2002) 48965
    • (2002) J. Biol. Chem. , vol.277 , pp. 48965
    • Nie, Z.1    Stanley, K.T.2    Stauffer, S.3    Jacques, K.M.4    Hirsch, D.S.5    Takei, J.6    Randazzo, P.A.7
  • 79
    • 0038514242 scopus 로고    scopus 로고
    • Regulators of G-protein signaling (RGS) 4, insertion into model membranes and inhibition of activity by phosphatidic acid
    • Ouyang Y.S., Tu Y., Barker S.A., and Yang F. Regulators of G-protein signaling (RGS) 4, insertion into model membranes and inhibition of activity by phosphatidic acid. J. Biol. Chem. 278 (2003) 11115
    • (2003) J. Biol. Chem. , vol.278 , pp. 11115
    • Ouyang, Y.S.1    Tu, Y.2    Barker, S.A.3    Yang, F.4
  • 80
    • 4344600505 scopus 로고    scopus 로고
    • Allosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling
    • Tu Y., and Wilkie T.M. Allosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling. Methods Enzymol. 389 (2004) 89
    • (2004) Methods Enzymol. , vol.389 , pp. 89
    • Tu, Y.1    Wilkie, T.M.2
  • 81
    • 0035937773 scopus 로고    scopus 로고
    • Differential binding of traffic-related proteins to phosphatidic acid- or phosphatidylinositol (4,5)-bisphosphate-coupled affinity reagents
    • Manifava M., Thuring J.W., Lim Z.Y., Packman L., Holmes A.B., and Ktistakis N.T. Differential binding of traffic-related proteins to phosphatidic acid- or phosphatidylinositol (4,5)-bisphosphate-coupled affinity reagents. J. Biol. Chem. 276 (2001) 8987
    • (2001) J. Biol. Chem. , vol.276 , pp. 8987
    • Manifava, M.1    Thuring, J.W.2    Lim, Z.Y.3    Packman, L.4    Holmes, A.B.5    Ktistakis, N.T.6
  • 84
    • 0025195030 scopus 로고
    • Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins
    • Blackwood R.A., and Ernst J.D. Characterization of Ca2(+)-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins. Biochem. J. 266 (1990) 195
    • (1990) Biochem. J. , vol.266 , pp. 195
    • Blackwood, R.A.1    Ernst, J.D.2
  • 85
    • 0000049034 scopus 로고    scopus 로고
    • Lipid binding ridge on loops 2 and 3 of the C2A domain of synaptotagmin I as revealed by NMR spectroscopy
    • Chae Y.K., Abildgaard F., Chapman E.R., and Markley J.L. Lipid binding ridge on loops 2 and 3 of the C2A domain of synaptotagmin I as revealed by NMR spectroscopy. J. Biol. Chem. 273 (1998) 25659
    • (1998) J. Biol. Chem. , vol.273 , pp. 25659
    • Chae, Y.K.1    Abildgaard, F.2    Chapman, E.R.3    Markley, J.L.4
  • 86
    • 0032577067 scopus 로고    scopus 로고
    • Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers
    • Chapman E.R., and Davis A.F. Direct interaction of a Ca2+-binding loop of synaptotagmin with lipid bilayers. J. Biol. Chem. 273 (1998) 13995
    • (1998) J. Biol. Chem. , vol.273 , pp. 13995
    • Chapman, E.R.1    Davis, A.F.2
  • 87
    • 0032497406 scopus 로고    scopus 로고
    • Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I
    • Zhang X., Rizo J., and Sudhof T.C. Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I. Biochemistry 37 (1998) 12395
    • (1998) Biochemistry , vol.37 , pp. 12395
    • Zhang, X.1    Rizo, J.2    Sudhof, T.C.3
  • 89
    • 0032496273 scopus 로고    scopus 로고
    • Catalytic domain of phosphoinositide-specific phospholipase C (PLC). Mutational analysis of residues within the active site and hydrophobic ridge of plcdelta1
    • Ellis M.V., James S.R., Perisic O., Downes C.P., Williams R.L., and Katan M. Catalytic domain of phosphoinositide-specific phospholipase C (PLC). Mutational analysis of residues within the active site and hydrophobic ridge of plcdelta1. J. Biol. Chem. 273 (1998) 11650
    • (1998) J. Biol. Chem. , vol.273 , pp. 11650
    • Ellis, M.V.1    James, S.R.2    Perisic, O.3    Downes, C.P.4    Williams, R.L.5    Katan, M.6
  • 90
    • 0033618352 scopus 로고    scopus 로고
    • Activation of phospholipase C delta1 through C2 domain by a Ca(2+)-enzyme-phosphatidylserine ternary complex
    • Lomasney J.W., Cheng H.F., Roffler S.R., and King K. Activation of phospholipase C delta1 through C2 domain by a Ca(2+)-enzyme-phosphatidylserine ternary complex. J. Biol. Chem. 274 (1999) 21995
    • (1999) J. Biol. Chem. , vol.274 , pp. 21995
    • Lomasney, J.W.1    Cheng, H.F.2    Roffler, S.R.3    King, K.4
  • 92
    • 0032562636 scopus 로고    scopus 로고
    • The C2 domains of Rabphilin3A specifically bind phosphatidylinositol 4,5-bisphosphate containing vesicles in a Ca2+-dependent manner. In vitro characteristics and possible significance
    • Chung S.H., Song W.J., Kim K., Bednarski J.J., Chen J., Prestwich G.D., and Holz R.W. The C2 domains of Rabphilin3A specifically bind phosphatidylinositol 4,5-bisphosphate containing vesicles in a Ca2+-dependent manner. In vitro characteristics and possible significance. J. Biol. Chem. 273 (1998) 10240
    • (1998) J. Biol. Chem. , vol.273 , pp. 10240
    • Chung, S.H.1    Song, W.J.2    Kim, K.3    Bednarski, J.J.4    Chen, J.5    Prestwich, G.D.6    Holz, R.W.7
  • 93
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A
    • Ostermeier C., and Brunger A.T. Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. Cell 96 (1999) 363
    • (1999) Cell , vol.96 , pp. 363
    • Ostermeier, C.1    Brunger, A.T.2
  • 94
    • 0031939689 scopus 로고    scopus 로고
    • The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans
    • Creutz C.E., Tomsig J.L., Snyder S.L., Gautier M.C., Skouri F., Beisson J., and Cohen J. The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans. J. Biol. Chem. 273 (1998) 1393
    • (1998) J. Biol. Chem. , vol.273 , pp. 1393
    • Creutz, C.E.1    Tomsig, J.L.2    Snyder, S.L.3    Gautier, M.C.4    Skouri, F.5    Beisson, J.6    Cohen, J.7
  • 95
    • 0034719141 scopus 로고    scopus 로고
    • Biochemical characterization of copine: a ubiquitous Ca2+-dependent, phospholipid-binding protein
    • Tomsig J.L., and Creutz C.E. Biochemical characterization of copine: a ubiquitous Ca2+-dependent, phospholipid-binding protein. Biochemistry 39 (2000) 16163
    • (2000) Biochemistry , vol.39 , pp. 16163
    • Tomsig, J.L.1    Creutz, C.E.2
  • 96
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: structural and functional diversity
    • Nalefski E.A., and Falke J.J. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5 (1996) 2375
    • (1996) Protein Sci. , vol.5 , pp. 2375
    • Nalefski, E.A.1    Falke, J.J.2
  • 97
    • 0029921472 scopus 로고    scopus 로고
    • Membrane structure of protein kinase C and calmodulin binding domain of myristoylated alanine rich C kinase substrate determined by site-directed spin labeling
    • Qin Z., and Cafiso D.S. Membrane structure of protein kinase C and calmodulin binding domain of myristoylated alanine rich C kinase substrate determined by site-directed spin labeling. Biochemistry 35 (1996) 2917
    • (1996) Biochemistry , vol.35 , pp. 2917
    • Qin, Z.1    Cafiso, D.S.2
  • 98
    • 0027241408 scopus 로고
    • Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids
    • Taniguchi H., and Manenti S. Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids. J. Biol. Chem. 268 (1993) 9960
    • (1993) J. Biol. Chem. , vol.268 , pp. 9960
    • Taniguchi, H.1    Manenti, S.2
  • 99
    • 0028181082 scopus 로고
    • Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells
    • Hyatt S.L., Liao L., Chapline C., and Jaken S. Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells. Biochemistry 33 (1994) 1223
    • (1994) Biochemistry , vol.33 , pp. 1223
    • Hyatt, S.L.1    Liao, L.2    Chapline, C.3    Jaken, S.4
  • 100
    • 0032516467 scopus 로고    scopus 로고
    • A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers
    • Johnson R.P., Niggli V., Durrer P., and Craig S.W. A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers. Biochemistry 37 (1998) 10211
    • (1998) Biochemistry , vol.37 , pp. 10211
    • Johnson, R.P.1    Niggli, V.2    Durrer, P.3    Craig, S.W.4
  • 101
    • 0001252591 scopus 로고    scopus 로고
    • Identification of functionally important amino acid residues within the C2-domain of human factor V using alanine-scanning mutagenesis
    • Kim S.W., Quinn-Allen M.A., Camp J.T., Macedo-Ribeiro S., Fuentes-Prior P., Bode W., and Kane W.H. Identification of functionally important amino acid residues within the C2-domain of human factor V using alanine-scanning mutagenesis. Biochemistry 39 (2000) 1951
    • (2000) Biochemistry , vol.39 , pp. 1951
    • Kim, S.W.1    Quinn-Allen, M.A.2    Camp, J.T.3    Macedo-Ribeiro, S.4    Fuentes-Prior, P.5    Bode, W.6    Kane, W.H.7
  • 102
    • 0028928203 scopus 로고
    • Membrane-binding peptide from the C2 domain of factor VIII forms an amphipathic structure as determined by NMR spectroscopy
    • Gilbert G.E., and Baleja J.D. Membrane-binding peptide from the C2 domain of factor VIII forms an amphipathic structure as determined by NMR spectroscopy. Biochemistry 34 (1995) 3022
    • (1995) Biochemistry , vol.34 , pp. 3022
    • Gilbert, G.E.1    Baleja, J.D.2
  • 104
    • 7744225985 scopus 로고    scopus 로고
    • Lactadherin binds selectively to membranes containing phosphatidyl-l-serine and increased curvature
    • Shi J., Heegaard C.W., Rasmussen J.T., and Gilbert G.E. Lactadherin binds selectively to membranes containing phosphatidyl-l-serine and increased curvature. Biochim. Biophys. Acta 1667 (2004) 82
    • (2004) Biochim. Biophys. Acta , vol.1667 , pp. 82
    • Shi, J.1    Heegaard, C.W.2    Rasmussen, J.T.3    Gilbert, G.E.4
  • 105
    • 0030993710 scopus 로고    scopus 로고
    • Bovine PAS-6/7 binds alpha v beta 5 integrins and anionic phospholipids through two domains
    • Andersen M.H., Berglund L., Rasmussen J.T., and Petersen T.E. Bovine PAS-6/7 binds alpha v beta 5 integrins and anionic phospholipids through two domains. Biochemistry 36 (1997) 5441
    • (1997) Biochemistry , vol.36 , pp. 5441
    • Andersen, M.H.1    Berglund, L.2    Rasmussen, J.T.3    Petersen, T.E.4
  • 106
    • 0036263042 scopus 로고    scopus 로고
    • New insights into binding interfaces of coagulation factors V and VIII and their homologues lessons from high resolution crystal structures
    • Fuentes-Prior P., Fujikawa K., and Pratt K.P. New insights into binding interfaces of coagulation factors V and VIII and their homologues lessons from high resolution crystal structures. Curr. Protein Pept. Sci. 3 (2002) 313
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 313
    • Fuentes-Prior, P.1    Fujikawa, K.2    Pratt, K.P.3
  • 107
    • 0037108445 scopus 로고    scopus 로고
    • Protein S Gla-domain mutations causing impaired Ca(2+)-induced phospholipid binding and severe functional protein S deficiency
    • Rezende S.M., Lane D.A., Mille-Baker B., Samama M.M., Conard J., and Simmonds R.E. Protein S Gla-domain mutations causing impaired Ca(2+)-induced phospholipid binding and severe functional protein S deficiency. Blood 100 (2002) 2812
    • (2002) Blood , vol.100 , pp. 2812
    • Rezende, S.M.1    Lane, D.A.2    Mille-Baker, B.3    Samama, M.M.4    Conard, J.5    Simmonds, R.E.6
  • 108
    • 0029148317 scopus 로고
    • Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid Vesicles
    • Christiansen W.T., Jalbert L.R., Robertson R.M., Jhingan A., Prorok M., and Castellino F.J. Hydrophobic amino acid residues of human anticoagulation protein C that contribute to its functional binding to phospholipid Vesicles. Biochemistry 34 (1995) 10376
    • (1995) Biochemistry , vol.34 , pp. 10376
    • Christiansen, W.T.1    Jalbert, L.R.2    Robertson, R.M.3    Jhingan, A.4    Prorok, M.5    Castellino, F.J.6
  • 110
    • 0037178865 scopus 로고    scopus 로고
    • Phosphatidylserine binding of class B scavenger receptor type I, a phagocytosis receptor of testicular Sertoli cells
    • Kawasaki Y., Nakagawa A., Nagaosa K., Shiratsuchi A., and Nakanishi Y. Phosphatidylserine binding of class B scavenger receptor type I, a phagocytosis receptor of testicular Sertoli cells. J. Biol. Chem. 277 (2002) 27559
    • (2002) J. Biol. Chem. , vol.277 , pp. 27559
    • Kawasaki, Y.1    Nakagawa, A.2    Nagaosa, K.3    Shiratsuchi, A.4    Nakanishi, Y.5
  • 111
    • 0028083893 scopus 로고
    • The cysteine-rich region of raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras
    • Ghosh S., Xie W.Q., Quest A.F., Mabrouk G.M., Strum J.C., and Bell R.M. The cysteine-rich region of raf-1 kinase contains zinc, translocates to liposomes, and is adjacent to a segment that binds GTP-ras. J. Biol. Chem. 269 (1994) 10000
    • (1994) J. Biol. Chem. , vol.269 , pp. 10000
    • Ghosh, S.1    Xie, W.Q.2    Quest, A.F.3    Mabrouk, G.M.4    Strum, J.C.5    Bell, R.M.6
  • 112
    • 0032828849 scopus 로고    scopus 로고
    • Mutational analysis of Raf-1 cysteine rich domain: requirement for a cluster of basic aminoacids for interaction with phosphatidylserine
    • Improta-Brears T., Ghosh S., and Bell R.M. Mutational analysis of Raf-1 cysteine rich domain: requirement for a cluster of basic aminoacids for interaction with phosphatidylserine. Mol. Cell. Biochem. 198 (1999) 171
    • (1999) Mol. Cell. Biochem. , vol.198 , pp. 171
    • Improta-Brears, T.1    Ghosh, S.2    Bell, R.M.3
  • 113
    • 0035929586 scopus 로고    scopus 로고
    • Structural and functional characterization of protein 4.1R-phosphatidylserine interaction: potential role in 4.1R sorting within cells
    • An X.L., Takakuwa Y., Manno S., Han B.G., Gascard P., and Mohandas N. Structural and functional characterization of protein 4.1R-phosphatidylserine interaction: potential role in 4.1R sorting within cells. J. Biol. Chem. 276 (2001) 35778
    • (2001) J. Biol. Chem. , vol.276 , pp. 35778
    • An, X.L.1    Takakuwa, Y.2    Manno, S.3    Han, B.G.4    Gascard, P.5    Mohandas, N.6
  • 114
    • 0030476301 scopus 로고    scopus 로고
    • Interaction of calmodulin-binding domain peptides of nitric oxide synthase with membrane phospholipids: regulation by protein phosphorylation and Ca(2+)-calmodulin
    • Matsubara M., Titani K., and Taniguchi H. Interaction of calmodulin-binding domain peptides of nitric oxide synthase with membrane phospholipids: regulation by protein phosphorylation and Ca(2+)-calmodulin. Biochemistry 35 (1996) 14651
    • (1996) Biochemistry , vol.35 , pp. 14651
    • Matsubara, M.1    Titani, K.2    Taniguchi, H.3
  • 116
    • 0033574154 scopus 로고    scopus 로고
    • Multiple factors influence the binding of a soluble, Ca2+-independent, diacylglycerol kinase to unilamellar phosphoglyceride vesicles
    • Thomas W.E., and Glomset J.A. Multiple factors influence the binding of a soluble, Ca2+-independent, diacylglycerol kinase to unilamellar phosphoglyceride vesicles. Biochemistry 38 (1999) 3310
    • (1999) Biochemistry , vol.38 , pp. 3310
    • Thomas, W.E.1    Glomset, J.A.2
  • 117
    • 0025873916 scopus 로고
    • Porcine 80-kDa diacylglycerol kinase is a calcium-binding and calcium/phospholipid-dependent enzyme and undergoes calcium-dependent translocation
    • Sakane F., Yamada K., Imai S., and Kanoh H. Porcine 80-kDa diacylglycerol kinase is a calcium-binding and calcium/phospholipid-dependent enzyme and undergoes calcium-dependent translocation. J. Biol. Chem. 266 (1991) 7096
    • (1991) J. Biol. Chem. , vol.266 , pp. 7096
    • Sakane, F.1    Yamada, K.2    Imai, S.3    Kanoh, H.4
  • 118
    • 0027217188 scopus 로고
    • Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles
    • Tuma P.L., Stachniak M.C., and Collins C.A. Activation of dynamin GTPase by acidic phospholipids and endogenous rat brain vesicles. J. Biol. Chem. 268 (1993) 17240
    • (1993) J. Biol. Chem. , vol.268 , pp. 17240
    • Tuma, P.L.1    Stachniak, M.C.2    Collins, C.A.3
  • 119
    • 0029978885 scopus 로고    scopus 로고
    • Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity
    • Zheng J., Cahill S.M., Lemmon M.A., Fushman D., Schlessinger J., and Cowburn D. Identification of the binding site for acidic phospholipids on the pH domain of dynamin: implications for stimulation of GTPase activity. J. Mol. Biol. 255 (1996) 14
    • (1996) J. Mol. Biol. , vol.255 , pp. 14
    • Zheng, J.1    Cahill, S.M.2    Lemmon, M.A.3    Fushman, D.4    Schlessinger, J.5    Cowburn, D.6
  • 120
    • 0028800457 scopus 로고
    • The cysteine residue responsible for the release of fibroblast growth factor-1 residues in a domain independent of the domain for phosphatidylserine binding
    • Tarantini F., Gamble S., Jackson A., and Maciag T. The cysteine residue responsible for the release of fibroblast growth factor-1 residues in a domain independent of the domain for phosphatidylserine binding. J. Biol. Chem. 270 (1995) 29039
    • (1995) J. Biol. Chem. , vol.270 , pp. 29039
    • Tarantini, F.1    Gamble, S.2    Jackson, A.3    Maciag, T.4
  • 121
    • 0029125354 scopus 로고
    • Interaction of partially structured states of acidic fibroblast growth factor with phospholipid membranes
    • Mach H., and Middaugh C.R. Interaction of partially structured states of acidic fibroblast growth factor with phospholipid membranes. Biochemistry 34 (1995) 9913
    • (1995) Biochemistry , vol.34 , pp. 9913
    • Mach, H.1    Middaugh, C.R.2
  • 122
    • 0032574953 scopus 로고    scopus 로고
    • Selectivity of lipid-protein interactions with trypsinized Na, K-ATPase studied by spin-label EPR
    • Arora A., Esmann M., and Marsh D. Selectivity of lipid-protein interactions with trypsinized Na, K-ATPase studied by spin-label EPR. Biochim. Biophys. Acta 1371 (1998) 163
    • (1998) Biochim. Biophys. Acta , vol.1371 , pp. 163
    • Arora, A.1    Esmann, M.2    Marsh, D.3
  • 123
    • 0022417663 scopus 로고
    • Spin-label studies on the origin of the specificity of lipid-protein interactions in Na+,K+-ATPase membranes from Squalus acanthias
    • Esmann M., and Marsh D. Spin-label studies on the origin of the specificity of lipid-protein interactions in Na+,K+-ATPase membranes from Squalus acanthias. Biochemistry 24 (1985) 3572
    • (1985) Biochemistry , vol.24 , pp. 3572
    • Esmann, M.1    Marsh, D.2
  • 124
    • 0032545461 scopus 로고    scopus 로고
    • Purification and characterization of a membrane bound neutral pH optimum magnesium-dependent and phosphatidylserine-stimulated sphingomyelinase from rat brain
    • Liu B., Hassler D.F., Smith G.K., Weaver K., and Hannun Y.A. Purification and characterization of a membrane bound neutral pH optimum magnesium-dependent and phosphatidylserine-stimulated sphingomyelinase from rat brain. J. Biol. Chem. 273 (1998) 34472
    • (1998) J. Biol. Chem. , vol.273 , pp. 34472
    • Liu, B.1    Hassler, D.F.2    Smith, G.K.3    Weaver, K.4    Hannun, Y.A.5
  • 125
    • 0037195915 scopus 로고    scopus 로고
    • Structural requirements for selective binding of ISC1 to anionic phospholipids
    • Okamoto Y., Vaena De Avalos S., and Hannun Y.A. Structural requirements for selective binding of ISC1 to anionic phospholipids. J. Biol. Chem. 277 (2002) 46470
    • (2002) J. Biol. Chem. , vol.277 , pp. 46470
    • Okamoto, Y.1    Vaena De Avalos, S.2    Hannun, Y.A.3
  • 127
    • 0034949428 scopus 로고    scopus 로고
    • If phosphatidylserine is the death knell, a new phosphatidylserine-specific receptor is the bellringer
    • Fadok V.A., Xue D., and Henson P. If phosphatidylserine is the death knell, a new phosphatidylserine-specific receptor is the bellringer. Cell Death Differ. 8 (2001) 582
    • (2001) Cell Death Differ. , vol.8 , pp. 582
    • Fadok, V.A.1    Xue, D.2    Henson, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.