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Volumn 423, Issue 4, 2012, Pages 528-539

Quantifying interactions of β-synuclein and γ-synuclein with model membranes

Author keywords

aggregation; amphipathic; dementia with Lewy bodies; intrinsically disordered proteins; Parkinson's disease

Indexed keywords

ALPHA SYNUCLEIN; ANIONIC LIPID; BETA SYNUCLEIN; GAMMA SYNUCLEIN; LIPID BINDING PROTEIN; LIPOSOME; UNCLASSIFIED DRUG;

EID: 84867252794     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.08.008     Document Type: Article
Times cited : (26)

References (85)
  • 2
    • 0031763264 scopus 로고    scopus 로고
    • The synuclein family
    • C. Lavedan The synuclein family Genome Res. 8 1998 871 880
    • (1998) Genome Res. , vol.8 , pp. 871-880
    • Lavedan, C.1
  • 3
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • M.H. Polymeropoulos, C. Lavedan, E. Leroy, S.E. Ide, A. Dehejia, and A. Dutra Mutation in the α-synuclein gene identified in families with Parkinson's disease Science 276 1997 2045 2047
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5    Dutra, A.6
  • 5
    • 78650066331 scopus 로고    scopus 로고
    • A β-synuclein mutation linked to dementia produces neurodegeneration when expressed in mouse brain
    • M. Fujita, S. Sugama, K. Sekiyama, A. Sekigawa, T. Tsukui, and M. Nakai A β-synuclein mutation linked to dementia produces neurodegeneration when expressed in mouse brain Nat. Commun. 1 2010 110
    • (2010) Nat. Commun. , vol.1 , pp. 110
    • Fujita, M.1    Sugama, S.2    Sekiyama, K.3    Sekigawa, A.4    Tsukui, T.5    Nakai, M.6
  • 7
    • 0035950270 scopus 로고    scopus 로고
    • β-Synuclein inhibits α-synuclein aggregation: A possible role as an anti-Parkinsonian factor
    • M. Hashimoto, E. Rockenstein, M. Mante, M. Mallory, and E. Masliah β-Synuclein inhibits α-synuclein aggregation: a possible role as an anti-Parkinsonian factor Neuron 32 2001 213 223
    • (2001) Neuron , vol.32 , pp. 213-223
    • Hashimoto, M.1    Rockenstein, E.2    Mante, M.3    Mallory, M.4    Masliah, E.5
  • 8
    • 0037144401 scopus 로고    scopus 로고
    • γ-Synuclein promotes cancer cell survival and inhibits stress- and chemotherapy drug-induced apoptosis by modulating MAPK pathways
    • Z.-Z. Pan, W. Bruening, B.I. Giasson, V.M.Y. Lee, and A.K. Godwin γ-Synuclein promotes cancer cell survival and inhibits stress- and chemotherapy drug-induced apoptosis by modulating MAPK pathways J. Biol. Chem. 277 2002 35050 35060
    • (2002) J. Biol. Chem. , vol.277 , pp. 35050-35060
    • Pan, Z.-Z.1    Bruening, W.2    Giasson, B.I.3    Lee, V.M.Y.4    Godwin, A.K.5
  • 10
    • 33846650691 scopus 로고    scopus 로고
    • Synuclein-γ targeting peptide inhibitor that enhances sensitivity of breast cancer cells to antimicrotubule drugs
    • V.K. Singh, Y. Zhou, J.A. Marsh, V.N. Uversky, J.D. Forman-Kay, J. Liu, and Z. Jia Synuclein-γ targeting peptide inhibitor that enhances sensitivity of breast cancer cells to antimicrotubule drugs Cancer Res. 67 2007 626 633
    • (2007) Cancer Res. , vol.67 , pp. 626-633
    • Singh, V.K.1    Zhou, Y.2    Marsh, J.A.3    Uversky, V.N.4    Forman-Kay, J.D.5    Liu, J.6    Jia, Z.7
  • 12
    • 80052398365 scopus 로고    scopus 로고
    • α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • T. Bartels, J.G. Choi, and D.J. Selkoe α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation Nature 477 2011 107 110
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 13
    • 84860172516 scopus 로고    scopus 로고
    • N-terminal acetylation is critical for forming α-helical oligomer of α-synuclein
    • A.J. Trexler, and E. Rhoades N-terminal acetylation is critical for forming α-helical oligomer of α-synuclein Protein Sci. 21 2012 601 605
    • (2012) Protein Sci. , vol.21 , pp. 601-605
    • Trexler, A.J.1    Rhoades, E.2
  • 14
    • 34548189188 scopus 로고    scopus 로고
    • Structural characterization of the intrinsically unfolded protein β-synuclein, a natural negative regulator of α-synuclein aggregation
    • C.W. Bertoncini, R.M. Rasia, G.R. Lamberto, A. Binolfi, M. Zweckstetter, C. Griesinger, and C.O. Fernandez Structural characterization of the intrinsically unfolded protein β-synuclein, a natural negative regulator of α-synuclein aggregation J. Mol. Biol. 372 2007 708 722
    • (2007) J. Mol. Biol. , vol.372 , pp. 708-722
    • Bertoncini, C.W.1    Rasia, R.M.2    Lamberto, G.R.3    Binolfi, A.4    Zweckstetter, M.5    Griesinger, C.6    Fernandez, C.O.7
  • 16
    • 77951896130 scopus 로고    scopus 로고
    • Amphipathic helices and membrane curvature
    • G. Drin, and B. Antonny Amphipathic helices and membrane curvature FEBS Lett. 584 2010 1840 1847
    • (2010) FEBS Lett. , vol.584 , pp. 1840-1847
    • Drin, G.1    Antonny, B.2
  • 18
    • 0037023699 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate
    • V.N. Uversky, J. Li, P. Souillac, I.S. Millett, S. Doniach, and R. Jakes Biophysical properties of the synucleins and their propensities to fibrillate J. Biol. Chem. 277 2002 11970 11978
    • (2002) J. Biol. Chem. , vol.277 , pp. 11970-11978
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Millett, I.S.4    Doniach, S.5    Jakes, R.6
  • 19
    • 33646156188 scopus 로고    scopus 로고
    • Secondary structure and dynamics of micelle bound β- And γ-synuclein
    • Y.-H. Sung, and D. Eliezer Secondary structure and dynamics of micelle bound β- and γ-synuclein Protein Sci. 15 2006 1162 1174
    • (2006) Protein Sci. , vol.15 , pp. 1162-1174
    • Sung, Y.-H.1    Eliezer, D.2
  • 22
    • 0030159894 scopus 로고    scopus 로고
    • Electric fields at the plasma membrane level: A neglected element in the mechanisms of cell signalling
    • M. Olivotto, A. Arcangeli, M. Carla, and E. Wanke Electric fields at the plasma membrane level: a neglected element in the mechanisms of cell signalling BioEssays 18 1996 495 504
    • (1996) BioEssays , vol.18 , pp. 495-504
    • Olivotto, M.1    Arcangeli, A.2    Carla, M.3    Wanke, E.4
  • 23
    • 34548550595 scopus 로고    scopus 로고
    • Lipid signaling and the modulation of surface charge during phagocytosis
    • T. Yeung, and S. Grinstein Lipid signaling and the modulation of surface charge during phagocytosis Immunol. Rev. 219 2007 17 36
    • (2007) Immunol. Rev. , vol.219 , pp. 17-36
    • Yeung, T.1    Grinstein, S.2
  • 24
    • 33744788870 scopus 로고    scopus 로고
    • Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy
    • E. Rhoades, T.F. Ramlall, W.W. Webb, and D. Eliezer Quantification of α-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy Biophys. J. 90 2006 4692 4700
    • (2006) Biophys. J. , vol.90 , pp. 4692-4700
    • Rhoades, E.1    Ramlall, T.F.2    Webb, W.W.3    Eliezer, D.4
  • 25
    • 4143120995 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles
    • L. Rusu, A. Gambhir, S. McLaughlin, and J. Rädler Fluorescence correlation spectroscopy studies of peptide and protein binding to phospholipid vesicles Biophys. J. 87 2004 1044 1053
    • (2004) Biophys. J. , vol.87 , pp. 1044-1053
    • Rusu, L.1    Gambhir, A.2    McLaughlin, S.3    Rädler, J.4
  • 26
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
    • W.S. Davidson, A. Jonas, D.F. Clayton, and J.M. George Stabilization of α-synuclein secondary structure upon binding to synthetic membranes J. Biol. Chem. 273 1998 9443 9449
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 27
    • 77958455514 scopus 로고    scopus 로고
    • Effects of curvature and composition on α-synuclein binding to lipid vesicles
    • E.R. Middleton, and E. Rhoades Effects of curvature and composition on α-synuclein binding to lipid vesicles Biophys. J. 99 2010 2279 2288
    • (2010) Biophys. J. , vol.99 , pp. 2279-2288
    • Middleton, E.R.1    Rhoades, E.2
  • 28
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • D. Eliezer, E. Kutluay, R. Bussell Jr., and G. Browne Conformational properties of α-synuclein in its free and lipid-associated states J. Mol. Biol. 307 2001 1061 1073
    • (2001) J. Mol. Biol. , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell, Jr.R.3    Browne, G.4
  • 29
    • 2942555022 scopus 로고    scopus 로고
    • Structure of membrane-bound α-synuclein studied by site-directed spin labeling
    • C.C. Jao, A. Der-Sarkissian, J. Chen, and R. Langen Structure of membrane-bound α-synuclein studied by site-directed spin labeling Proc. Natl Acad. Sci. USA 101 2004 8331 8336
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8331-8336
    • Jao, C.C.1    Der-Sarkissian, A.2    Chen, J.3    Langen, R.4
  • 30
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human α-synuclein
    • T.S. Ulmer, A. Bax, N.B. Cole, and R.L. Nussbaum Structure and dynamics of micelle-bound human α-synuclein J. Biol. Chem. 280 2005 9595 9603
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 31
    • 0035827137 scopus 로고    scopus 로고
    • Protein chemistry at membrane interfaces: Non-additivity of electrostatic and hydrophobic interactions
    • A.S. Ladokhin, and S.H. White Protein chemistry at membrane interfaces: non-additivity of electrostatic and hydrophobic interactions J. Mol. Biol. 309 2001 543 552
    • (2001) J. Mol. Biol. , vol.309 , pp. 543-552
    • Ladokhin, A.S.1    White, S.H.2
  • 32
    • 0025061113 scopus 로고
    • Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes
    • G. Beschiaschvili, and J. Seelig Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes Biochemistry 29 1990 52 58
    • (1990) Biochemistry , vol.29 , pp. 52-58
    • Beschiaschvili, G.1    Seelig, J.2
  • 34
    • 0038054286 scopus 로고    scopus 로고
    • A structural and functional role for 11-mer repeats in α-synuclein and other exchangeable lipid binding proteins
    • R. Bussell Jr., and D. Eliezer A structural and functional role for 11-mer repeats in α-synuclein and other exchangeable lipid binding proteins J. Mol. Biol. 329 2003 763 778
    • (2003) J. Mol. Biol. , vol.329 , pp. 763-778
    • Bussell, Jr.R.1    Eliezer, D.2
  • 35
    • 79960279832 scopus 로고    scopus 로고
    • α-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding
    • I.M. Pranke, V. Morello, J. Bigay, K. Gibson, J.M. Verbavatz, B. Antonny, and C.L. Jackson α-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding J. Cell Biol. 194 2011 89 103
    • (2011) J. Cell Biol. , vol.194 , pp. 89-103
    • Pranke, I.M.1    Morello, V.2    Bigay, J.3    Gibson, K.4    Verbavatz, J.M.5    Antonny, B.6    Jackson, C.L.7
  • 36
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • H.T. McMahon, and J.L. Gallop Membrane curvature and mechanisms of dynamic cell membrane remodelling Nature 438 2005 590 596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 38
    • 79953850289 scopus 로고    scopus 로고
    • Specificity and kinetics of α-synuclein binding to model membranes determined with fluorescent excited state intramolecular proton transfer (ESIPT) probe
    • V.V. Shvadchak, L.J. Falomir-Lockhart, D.A. Yushchenko, and T.M. Jovin Specificity and kinetics of α-synuclein binding to model membranes determined with fluorescent excited state intramolecular proton transfer (ESIPT) probe J. Biol. Chem. 286 2011 13023 13032
    • (2011) J. Biol. Chem. , vol.286 , pp. 13023-13032
    • Shvadchak, V.V.1    Falomir-Lockhart, L.J.2    Yushchenko, D.A.3    Jovin, T.M.4
  • 39
    • 33646912812 scopus 로고    scopus 로고
    • Binding of α-synuclein affects the lipid packing in bilayers of small vesicles
    • F. Kamp, and K. Beyer Binding of α-synuclein affects the lipid packing in bilayers of small vesicles J. Biol. Chem. 281 2006 9251 9259
    • (2006) J. Biol. Chem. , vol.281 , pp. 9251-9259
    • Kamp, F.1    Beyer, K.2
  • 41
    • 79953862815 scopus 로고    scopus 로고
    • Mechanism of membrane curvature sensing by amphipathic helix containing proteins
    • H. Cui, E. Lyman, and G.A. Voth Mechanism of membrane curvature sensing by amphipathic helix containing proteins Biophys. J. 100 2011 1271 1279
    • (2011) Biophys. J. , vol.100 , pp. 1271-1279
    • Cui, H.1    Lyman, E.2    Voth, G.A.3
  • 42
    • 0033613815 scopus 로고    scopus 로고
    • Folding of amphipathic α-helices on membranes: Energetics of helix formation by melittin
    • A.S. Ladokhin, and S.H. White Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin J. Mol. Biol. 285 1999 1363 1369
    • (1999) J. Mol. Biol. , vol.285 , pp. 1363-1369
    • Ladokhin, A.S.1    White, S.H.2
  • 43
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • S.H. White, and W.C. Wimley Membrane protein folding and stability: physical principles Annu. Rev. Biophys. Biomol. Struct. 28 1999 319 365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 44
    • 79959928058 scopus 로고    scopus 로고
    • Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers
    • C.P. Moon, and K.G. Fleming Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers Proc. Natl Acad. Sci. USA 108 2011 10174 10177
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 10174-10177
    • Moon, C.P.1    Fleming, K.G.2
  • 45
    • 0031808074 scopus 로고    scopus 로고
    • A helix propensity scale based on experimental studies of peptides and proteins
    • C.N. Pace, and J.M. Scholtz A helix propensity scale based on experimental studies of peptides and proteins Biophys. J. 75 1998 422 427
    • (1998) Biophys. J. , vol.75 , pp. 422-427
    • Pace, C.N.1    Scholtz, J.M.2
  • 46
    • 34547618240 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in positioning of peripheral proteins in membranes
    • A. Lomize, I. Pogozheva, M. Lomize, and H. Mosberg The role of hydrophobic interactions in positioning of peripheral proteins in membranes BMC Struct. Biol. 7(2007 44
    • (2007) BMC Struct. Biol. , vol.7 , pp. 44
    • Lomize, A.1    Pogozheva, I.2    Lomize, M.3    Mosberg, H.4
  • 47
    • 0025996974 scopus 로고
    • Nonclassical hydrophobic effect in membrane binding equilibria
    • J. Seelig, and P. Ganz Nonclassical hydrophobic effect in membrane binding equilibria Biochemistry 30 1991 9354 9359
    • (1991) Biochemistry , vol.30 , pp. 9354-9359
    • Seelig, J.1    Ganz, P.2
  • 48
    • 0031567121 scopus 로고    scopus 로고
    • Titration calorimetry of lipid-peptide interactions
    • J. Seelig Titration calorimetry of lipid-peptide interactions Biochim. Biophys. Acta, Rev. Biomembr. 1331 1997 103 116
    • (1997) Biochim. Biophys. Acta, Rev. Biomembr. , vol.1331 , pp. 103-116
    • Seelig, J.1
  • 49
    • 79955685287 scopus 로고    scopus 로고
    • Allostery in a disordered protein: Oxidative modifications to α-synuclein act distally to regulate membrane binding
    • E. Sevcsik, A.J. Trexler, J.M. Dunn, and E. Rhoades Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding J. Am. Chem. Soc. 133 2011 7152 7158
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7152-7158
    • Sevcsik, E.1    Trexler, A.J.2    Dunn, J.M.3    Rhoades, E.4
  • 50
    • 35348957237 scopus 로고    scopus 로고
    • Enhanced lysosomal pathology caused by β-synuclein mutants linked to dementia with Lewy bodies
    • J. Wei, M. Fujita, M. Nakai, M. Waragai, K. Watabe, and H. Akatsu Enhanced lysosomal pathology caused by β-synuclein mutants linked to dementia with Lewy bodies J. Biol. Chem. 282 2007 28904 28914
    • (2007) J. Biol. Chem. , vol.282 , pp. 28904-28914
    • Wei, J.1    Fujita, M.2    Nakai, M.3    Waragai, M.4    Watabe, K.5    Akatsu, H.6
  • 51
    • 69549116416 scopus 로고    scopus 로고
    • Neurotoxic conversion of β-synuclein: A novel approach to generate a transgenic mouse model of synucleinopathies?
    • M. Fujita, A. Sekigawa, K. Sekiyama, S. Sugama, and M. Hashimoto Neurotoxic conversion of β-synuclein: a novel approach to generate a transgenic mouse model of synucleinopathies? J. Neurol. 256 2009 286 292
    • (2009) J. Neurol. , vol.256 , pp. 286-292
    • Fujita, M.1    Sekigawa, A.2    Sekiyama, K.3    Sugama, S.4    Hashimoto, M.5
  • 52
    • 0029962468 scopus 로고    scopus 로고
    • Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains
    • M. Vey, S. Pilkuhn, H. Wille, R. Nixon, S.J. DeArmond, and E.J. Smart Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains Proc. Natl Acad. Sci. USA 93 1996 14945 14949
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14945-14949
    • Vey, M.1    Pilkuhn, S.2    Wille, H.3    Nixon, R.4    Dearmond, S.J.5    Smart, E.J.6
  • 53
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • R. Ehehalt, P. Keller, C. Haass, C. Thiele, and K. Simons Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts J. Cell Biol. 160 2003 113 123
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 55
    • 33747119677 scopus 로고    scopus 로고
    • Conserved and cooperative assembly of membrane-bound α-helical states of islet amyloid polypeptide
    • J.D. Knight, J.A. Hebda, and A.D. Miranker Conserved and cooperative assembly of membrane-bound α-helical states of islet amyloid polypeptide Biochemistry 45 2006 9496 9508
    • (2006) Biochemistry , vol.45 , pp. 9496-9508
    • Knight, J.D.1    Hebda, J.A.2    Miranker, A.D.3
  • 56
    • 0032321726 scopus 로고    scopus 로고
    • Protein folding in membranes: Determining energetics of peptide-bilayer interactions
    • S.H. White, W.C. Wimley, A.S. Ladokhin, and K. Hristova Protein folding in membranes: determining energetics of peptide-bilayer interactions Methods Enzymol. 295 1998 62 87
    • (1998) Methods Enzymol. , vol.295 , pp. 62-87
    • White, S.H.1    Wimley, W.C.2    Ladokhin, A.S.3    Hristova, K.4
  • 57
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • A.S. Ladokhin, S. Jayasinghe, and S.H. White How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? Anal. Biochem. 285 2000 235 245
    • (2000) Anal. Biochem. , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 58
    • 77957775523 scopus 로고    scopus 로고
    • Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins
    • J. Varkey, J.M. Isas, N. Mizuno, M.B. Jensen, V.K. Bhatia, and C.C. Jao Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins J. Biol. Chem. 285 2010 32486 32493
    • (2010) J. Biol. Chem. , vol.285 , pp. 32486-32493
    • Varkey, J.1    Isas, J.M.2    Mizuno, N.3    Jensen, M.B.4    Bhatia, V.K.5    Jao, C.C.6
  • 60
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • R.M. Epand Lipid polymorphism and protein-lipid interactions Biochim. Biophys. Acta, Rev. Biomembr. 1376 1998 353 368
    • (1998) Biochim. Biophys. Acta, Rev. Biomembr. , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 61
    • 0030831998 scopus 로고    scopus 로고
    • Role of lipid polymorphism in G protein-membrane interactions: Nonlamellar-prone phospholipids and peripheral protein binding to membranes
    • P.V. Escribá, A. Ozaita, C. Ribas, A. Miralles, E. Fodor, T. Farkas, and J.A. García-Sevilla Role of lipid polymorphism in G protein-membrane interactions: nonlamellar-prone phospholipids and peripheral protein binding to membranes Proc. Natl Acad. Sci. USA 94 1997 11375 11380
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11375-11380
    • Escribá, P.V.1    Ozaita, A.2    Ribas, C.3    Miralles, A.4    Fodor, E.5    Farkas, T.6    García-Sevilla, J.A.7
  • 62
    • 0035979795 scopus 로고    scopus 로고
    • Imaging domains in model membranes with atomic force microscopy
    • H.A. Rinia, and B. de Kruijff Imaging domains in model membranes with atomic force microscopy FEBS Lett. 504 2001 194 199
    • (2001) FEBS Lett. , vol.504 , pp. 194-199
    • Rinia, H.A.1    De Kruijff, B.2
  • 63
    • 0029048818 scopus 로고
    • Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: A surface plasmon resonance spectroscopy study
    • J.L. Soulages, Z. Salamon, M.A. Wells, and G. Tollin Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: a surface plasmon resonance spectroscopy study Proc. Natl Acad. Sci. USA 92 1995 5650 5654
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5650-5654
    • Soulages, J.L.1    Salamon, Z.2    Wells, M.A.3    Tollin, G.4
  • 64
    • 0029074355 scopus 로고
    • Hydration and order in lipid bilayers
    • C. Ho, S.J. Slater, and C.D. Stubbs Hydration and order in lipid bilayers Biochemistry 34 1995 6188 6195
    • (1995) Biochemistry , vol.34 , pp. 6188-6195
    • Ho, C.1    Slater, S.J.2    Stubbs, C.D.3
  • 65
    • 72149093512 scopus 로고    scopus 로고
    • Cholesterol involvement in the pathogenesis of neurodegenerative diseases
    • J.-P. Liu, Y. Tang, S. Zhou, B.H. Toh, C. McLean, and H. Li Cholesterol involvement in the pathogenesis of neurodegenerative diseases Mol. Cell. Neurosci. 43 2010 33 42
    • (2010) Mol. Cell. Neurosci. , vol.43 , pp. 33-42
    • Liu, J.-P.1    Tang, Y.2    Zhou, S.3    Toh, B.H.4    McLean, C.5    Li, H.6
  • 66
    • 81855211988 scopus 로고    scopus 로고
    • Early steps in steroidogenesis: Intracellular cholesterol trafficking
    • W.L. Miller, and H.S. Bose Early steps in steroidogenesis: intracellular cholesterol trafficking J. Lipid Res. 52 2011 2111 2135
    • (2011) J. Lipid Res. , vol.52 , pp. 2111-2135
    • Miller, W.L.1    Bose, H.S.2
  • 67
    • 0017862842 scopus 로고
    • 31P NMR. Evidence that cholesterol may destabilize bilayer structure in membrane systems containing phosphatidylethanolamine
    • 31P NMR. Evidence that cholesterol may destabilize bilayer structure in membrane systems containing phosphatidylethanolamine Biochim. Biophys. Acta, Biomembr. 507 1978 207 218
    • (1978) Biochim. Biophys. Acta, Biomembr. , vol.507 , pp. 207-218
    • Cullis, P.R.1    De Kruijff, B.2
  • 68
    • 0024452439 scopus 로고
    • Role of the stereochemistry of the hydroxyl group of cholesterol and the formation of nonbilayer structures in phosphatidylethanolamines
    • J.J. Cheetham, E. Wachtel, D. Bach, and R.M. Epand Role of the stereochemistry of the hydroxyl group of cholesterol and the formation of nonbilayer structures in phosphatidylethanolamines Biochemistry 28 1989 8928 8934
    • (1989) Biochemistry , vol.28 , pp. 8928-8934
    • Cheetham, J.J.1    Wachtel, E.2    Bach, D.3    Epand, R.M.4
  • 69
    • 2342586664 scopus 로고    scopus 로고
    • Measurement of the affinity and cooperativity of annexin V-membrane binding under conditions of low membrane occupancy
    • J.F. Tait, D.F. Gibson, and C. Smith Measurement of the affinity and cooperativity of annexin V-membrane binding under conditions of low membrane occupancy Anal. Biochem. 329 2004 112 119
    • (2004) Anal. Biochem. , vol.329 , pp. 112-119
    • Tait, J.F.1    Gibson, D.F.2    Smith, C.3
  • 70
    • 42949116926 scopus 로고    scopus 로고
    • Membrane insertion pathway of annexin B12: Thermodynamic and kinetic characterization by fluorescence correlation spectroscopy and fluorescence quenching
    • Y.O. Posokhov, M.V. Rodnin, L. Lu, and A.S. Ladokhin Membrane insertion pathway of annexin B12: thermodynamic and kinetic characterization by fluorescence correlation spectroscopy and fluorescence quenching Biochemistry 47 2008 5078 5087
    • (2008) Biochemistry , vol.47 , pp. 5078-5087
    • Posokhov, Y.O.1    Rodnin, M.V.2    Lu, L.3    Ladokhin, A.S.4
  • 71
    • 33244475771 scopus 로고    scopus 로고
    • The biotin-capture lipid affinity assay: A rapid method for determining lipid binding parameters for apolipoproteins
    • W.S. Davidson, A.B. Ghering, L. Beish, M.R. Tubb, D.Y. Hui, and K. Pearson The biotin-capture lipid affinity assay: a rapid method for determining lipid binding parameters for apolipoproteins J. Lipid Res. 47 2006 440 449
    • (2006) J. Lipid Res. , vol.47 , pp. 440-449
    • Davidson, W.S.1    Ghering, A.B.2    Beish, L.3    Tubb, M.R.4    Hui, D.Y.5    Pearson, K.6
  • 72
    • 0028053759 scopus 로고
    • Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids
    • C.T. Sigal, W. Zhou, C.A. Buser, S. McLaughlin, and M.D. Resh Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids Proc. Natl Acad. Sci. USA 91 1994 12253 12257
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12253-12257
    • Sigal, C.T.1    Zhou, W.2    Buser, C.A.3    McLaughlin, S.4    Resh, M.D.5
  • 74
    • 57149084065 scopus 로고    scopus 로고
    • Molecular and cellular biology of synucleins
    • A. Surguchov Molecular and cellular biology of synucleins Int. Rev. Cell Mol. Biol. 270 2008 225 317
    • (2008) Int. Rev. Cell Mol. Biol. , vol.270 , pp. 225-317
    • Surguchov, A.1
  • 75
    • 79953236488 scopus 로고    scopus 로고
    • Synuclein modulation of monoamine transporters
    • A.W. Oaks, and A. Sidhu Synuclein modulation of monoamine transporters FEBS Lett. 585 2011 1001 1006
    • (2011) FEBS Lett. , vol.585 , pp. 1001-1006
    • Oaks, A.W.1    Sidhu, A.2
  • 76
    • 0032492689 scopus 로고    scopus 로고
    • Regulation of phospholipase D2: Selective inhibition of mammalian phospholipase D isoenzymes by α- And β-synucleins
    • J.M. Jenco, A. Rawlingson, B. Daniels, and A.J. Morris Regulation of phospholipase D2: selective inhibition of mammalian phospholipase D isoenzymes by α- and β-synucleins Biochemistry 37 1998 4901 4909
    • (1998) Biochemistry , vol.37 , pp. 4901-4909
    • Jenco, J.M.1    Rawlingson, A.2    Daniels, B.3    Morris, A.J.4
  • 77
    • 34948870171 scopus 로고    scopus 로고
    • Involvement of RHO GTPases and ERK in synuclein-γ enhanced cancer cell motility
    • Z.-Z. Pan, and A.K. Godwin Involvement of RHO GTPases and ERK in synuclein-γ enhanced cancer cell motility Int. J. Oncol. 29 2006 1201 1205
    • (2006) Int. J. Oncol. , vol.29 , pp. 1201-1205
    • Pan, Z.-Z.1    Godwin, A.K.2
  • 78
    • 77957608019 scopus 로고    scopus 로고
    • α-Synuclein expression in rat substantia nigra suppresses phospholipase D2 toxicity and nigral neurodegeneration
    • O.S. Gorbatyuk, S. Li, F. Nha Nguyen, F.P. Manfredsson, G. Kondrikova, and L.F. Sullivan α-Synuclein expression in rat substantia nigra suppresses phospholipase D2 toxicity and nigral neurodegeneration Mol. Ther. 18 2010 1758 1768
    • (2010) Mol. Ther. , vol.18 , pp. 1758-1768
    • Gorbatyuk, O.S.1    Li, S.2    Nha Nguyen, F.3    Manfredsson, F.P.4    Kondrikova, G.5    Sullivan, L.F.6
  • 80
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • C.H. Fiske, and Y. Subbarow The colorimetric determination of phosphorus J. Biol. Chem. 66 1925 375 400
    • (1925) J. Biol. Chem. , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 81
  • 82
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and low-background-analysis of translational diffusion
    • R. Rigler, U. Mets, J. Widegren, and P. Kask Fluorescence correlation spectroscopy with high count rate and low-background-analysis of translational diffusion Eur. Biophys. J. Biophys. Lett. 22 1993 169 175
    • (1993) Eur. Biophys. J. Biophys. Lett. , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, U.2    Widegren, J.3    Kask, P.4
  • 83
    • 0001579306 scopus 로고
    • Fluorescence correlation spectroscopy
    • J. Lakowicz, Plenum Press New York, NY
    • N.L. Thompson Fluorescence correlation spectroscopy J. Lakowicz, Topics in Fluorescence Microscopy 1991 Plenum Press New York, NY 337 378
    • (1991) Topics in Fluorescence Microscopy , pp. 337-378
    • Thompson, N.L.1
  • 84
    • 80051786035 scopus 로고    scopus 로고
    • The effect of variable liposome brightness on quantifying lipid-protein interactions using fluorescence correlation spectroscopy
    • A.M. Melo, M. Prieto, and A. Coutinho The effect of variable liposome brightness on quantifying lipid-protein interactions using fluorescence correlation spectroscopy Biochim. Biophys. Acta, Biomembr. 1808 2011 2559 2568
    • (2011) Biochim. Biophys. Acta, Biomembr. , vol.1808 , pp. 2559-2568
    • Melo, A.M.1    Prieto, M.2    Coutinho, A.3
  • 85
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • N. Kučerka, S. Tristram-Nagle, and J. Nagle Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains J. Membr. Biol. 208 2006 193 202
    • (2006) J. Membr. Biol. , vol.208 , pp. 193-202
    • Kučerka, N.1    Tristram-Nagle, S.2    Nagle, J.3


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