메뉴 건너뛰기




Volumn 1818, Issue 2, 2012, Pages 172-177

Lipid-protein interactions in biological membranes: A dynamic perspective

Author keywords

Fluorescence cross correlation spectroscopy; Lipid protein dynamics; Two dimensional infrared spectroscopy

Indexed keywords

BETA 2 ADRENERGIC RECEPTOR; CARDIOLIPIN; RHODOPSIN; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 82955185523     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.06.015     Document Type: Review
Times cited : (76)

References (75)
  • 1
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • DOI 10.1016/S0005-2736(03)00056-7
    • A.G. Lee Lipid-protein interactions in biological membranes: a structural perspective Biochim. Biophys. Acta (BBA) Biomembr. 1612 2003 1 40 (Pubitemid 36555684)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1612 , Issue.1 , pp. 1-40
    • Lee, A.G.1
  • 2
    • 0021837375 scopus 로고
    • Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosinetriphosphatase
    • DOI 10.1021/bi00332a005
    • J.M. East, D. Melville, and A.G. Lee Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosine triphosphatase Biochemistry 24 1985 2615 2623 (Pubitemid 15015993)
    • (1985) Biochemistry , vol.24 , Issue.11 , pp. 2615-2623
    • East, J.M.1    Melville, D.2    Lee, A.G.3
  • 4
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • DOI 10.1038/nature05416, PII NATURE05416
    • D. Schmidt, Q.-X. Jiang, and R. MacKinnon Phospholipids and the origin of cationic gating charges in voltage sensors Nature 444 2006 775 779 (Pubitemid 44949608)
    • (2006) Nature , vol.444 , Issue.7120 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.-X.2    MacKinnon, R.3
  • 5
    • 33747062707 scopus 로고    scopus 로고
    • Enzymatic activation of voltage-gated potassium channels
    • DOI 10.1038/nature04880, PII NATURE04880
    • Y. Ramu, Y. Xu, and Z. Lu Enzymatic activation of voltage-gated potassium channels Nature 442 2006 696 699 (Pubitemid 44215325)
    • (2006) Nature , vol.442 , Issue.7103 , pp. 696-699
    • Ramu, Y.1    Xu, Y.2    Lu, Z.3
  • 6
    • 0032546013 scopus 로고    scopus 로고
    • 2 and its stabilization by Gβγ
    • DOI 10.1038/35882
    • C.-L. Huang, S. Feng, and D.W. Hilgemann Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by G[beta][gamma] Nature 391 1998 803 806 (Pubitemid 28099680)
    • (1998) Nature , vol.391 , Issue.6669 , pp. 803-806
    • Huang, C.-L.1    Feng, S.2    Hilgemann, D.W.3
  • 8
    • 0343152628 scopus 로고    scopus 로고
    • Movement of voltage sensor S4 in domain 4 is tightly coupled to sodium channel fast inactivation and gating charge immobilization
    • F.J.P. Kahn, and N.G. Greeff Movement of voltage sensor S4 in domain 4 is tightly coupled to sodium channel fast inactivation and gating charge immobilization J. Gen. Physiol. 114 1999 167 184
    • (1999) J. Gen. Physiol. , vol.114 , pp. 167-184
    • Kahn, F.J.P.1    Greeff, N.G.2
  • 9
    • 77956906517 scopus 로고    scopus 로고
    • Mechanosensitivity of ion channels based on protein-lipid interactions
    • K. Yoshimura, and M. Sokabe Mechanosensitivity of ion channels based on protein-lipid interactions J. R. Soc. Interface 7 2010 S307 S320
    • (2010) J. R. Soc. Interface , vol.7
    • Yoshimura, K.1    Sokabe, M.2
  • 10
    • 41849136544 scopus 로고    scopus 로고
    • Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL
    • DOI 10.1021/bi702409t
    • A.M. Powl, J.M. East, and A.G. Lee Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL Biochemistry 47 2008 4317 4328 (Pubitemid 351499887)
    • (2008) Biochemistry , vol.47 , Issue.14 , pp. 4317-4328
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 11
    • 56249140425 scopus 로고    scopus 로고
    • Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL
    • A.M. Powl, J.M. East, and A.G. Lee Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL Biochemistry 47 2008 12175 12184
    • (2008) Biochemistry , vol.47 , pp. 12175-12184
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 12
    • 51049102167 scopus 로고    scopus 로고
    • Regulation of membrane proteins by dietary lipids: Effects of cholesterol and docosahexaenoic acid acyl chain-containing phospholipids on rhodopsin stability and function
    • M.P. Bennett, and D.C. Mitchell Regulation of membrane proteins by dietary lipids: effects of cholesterol and docosahexaenoic acid acyl chain-containing phospholipids on rhodopsin stability and function Biophys. J. 95 2008 1206 1216
    • (2008) Biophys. J. , vol.95 , pp. 1206-1216
    • Bennett, M.P.1    Mitchell, D.C.2
  • 14
    • 23044445764 scopus 로고    scopus 로고
    • 2 adrenoceptor in detergent micelles
    • DOI 10.1016/j.ab.2005.05.002, PII S0003269705003635
    • Z. Yao, and B. Kobilka Using synthetic lipids to stabilize purified [beta]2 adrenoceptor in detergent micelles Anal. Biochem. 343 2005 344 346 (Pubitemid 41074051)
    • (2005) Analytical Biochemistry , vol.343 , Issue.2 , pp. 344-346
    • Yao, Z.1    Kobilka, B.2
  • 15
    • 2442509293 scopus 로고    scopus 로고
    • 1A receptors from bovine hippocampus
    • DOI 10.1016/j.bbamem.2004.03.010, PII S0005273604000896
    • T.J. Pucadyil, and A. Chattopadhyay Cholesterol modulates ligand binding and G-protein coupling to serotonin1A receptors from bovine hippocampus Biochim. Biophys. Acta (BBA) Biomembr. 1663 2004 188 200 (Pubitemid 38625593)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1663 , Issue.1-2 , pp. 188-200
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 16
    • 59249094898 scopus 로고    scopus 로고
    • Are specific nonannular cholesterol binding sites present in G-protein coupled receptors?
    • Y.D. Paila, S. Tiwari, and A. Chattopadhyay Are specific nonannular cholesterol binding sites present in G-protein coupled receptors? Biochim. Biophys. Acta (BBA) Biomembr. 1788 2009 295 302
    • (2009) Biochim. Biophys. Acta (BBA) Biomembr. , vol.1788 , pp. 295-302
    • Paila, Y.D.1    Tiwari, S.2    Chattopadhyay, A.3
  • 17
    • 5044235587 scopus 로고    scopus 로고
    • Electron crystallography reveals the structure of metarhodopsin I
    • DOI 10.1038/sj.emboj.7600374
    • J.J. Ruprecht, T. Mielke, R. Vogel, C. Villa, and G.F.X. Schertler Electron crystallography reveals the structure of metarhodopsin I EMBO J. 23 2004 3609 3620 (Pubitemid 39336283)
    • (2004) EMBO Journal , vol.23 , Issue.18 , pp. 3609-3620
    • Ruprecht, J.J.1    Mielke, T.2    Vogel, R.3    Villa, C.4    Schertler, G.F.X.5
  • 19
    • 0035970108 scopus 로고    scopus 로고
    • Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide
    • DOI 10.1073/pnas.031461598
    • H. Li, Z.-x. Yao, B. Degenhardt, G. Teper, and V. Papadopoulos Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide Proc. Natl. Acad. Sci. U. S. A. 98 2001 1267 1272 (Pubitemid 32121221)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.3 , pp. 1267-1272
    • Li, H.1    Yao, Z.-X.2    Degenhardt, B.3    Teper, G.4    Papadopoulos, V.5
  • 20
    • 58749087365 scopus 로고    scopus 로고
    • Behavioral differences between phosphatidic acid and phosphatidylcholine in the presence of the nicotinic acetylcholine receptor
    • A.N. Dickey, and R. Faller Behavioral differences between phosphatidic acid and phosphatidylcholine in the presence of the nicotinic acetylcholine receptor Biophys. J. 95 2008 5637 5647
    • (2008) Biophys. J. , vol.95 , pp. 5637-5647
    • Dickey, A.N.1    Faller, R.2
  • 21
    • 0022552318 scopus 로고
    • Correlation between acetylcholine receptor function and structural properties of membranes
    • T.M. Fong, and M.G. McNamee Correlation between acetylcholine receptor function and structural properties of membranes Biochemistry 25 1986 830 840 (Pubitemid 16028268)
    • (1986) Biochemistry , vol.25 , Issue.4 , pp. 830-840
    • Tung Ming Fong1    McNamee, M.G.2
  • 22
    • 0024278441 scopus 로고
    • Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor
    • O.T. Jones, and M.G. McNamee Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor Biochemistry 27 1988 2364 2374
    • (1988) Biochemistry , vol.27 , pp. 2364-2374
    • Jones, O.T.1    McNamee, M.G.2
  • 23
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • DOI 10.1038/nrm2328, PII NRM2328
    • M.A. Lemmon Membrane recognition by phospholipid-binding domains Nat. Rev. Mol. Cell Biol. 9 2008 99 111 (Pubitemid 351158910)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.2 , pp. 99-111
    • Lemmon, M.A.1
  • 24
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • DOI 10.1038/nchembio834, PII NCHEMBIO834
    • M.D. Resh Trafficking and signaling by fatty-acylated and prenylated proteins Nat. Chem. Biol. 2 2006 584 590 (Pubitemid 44610342)
    • (2006) Nature Chemical Biology , vol.2 , Issue.11 , pp. 584-590
    • Resh, M.D.1
  • 25
    • 0031019429 scopus 로고    scopus 로고
    • Understanding covalent modifications of proteins by lipids: Where cell biology and biophysics mingle
    • DOI 10.1016/S0962-8924(97)10044-7, PII S0962892497100441
    • R.S. Bhatnagar, and J.I. Gordon Understanding covalent modifications of proteins by lipids: where cell biology and biophysics mingle Trends Cell Biol. 7 1997 14 20 (Pubitemid 27056378)
    • (1997) Trends in Cell Biology , vol.7 , Issue.1 , pp. 14-20
    • Bhatnagar, R.S.1    Gordon, J.I.2
  • 27
    • 78649821287 scopus 로고    scopus 로고
    • Segregation of negatively charged phospholipids by the polycationic and farnesylated membrane anchor of Kras
    • L. Janosi, and A.A. Gorfe Segregation of negatively charged phospholipids by the polycationic and farnesylated membrane anchor of Kras Biophys. J. 99 2010 3666 3674
    • (2010) Biophys. J. , vol.99 , pp. 3666-3674
    • Janosi, L.1    Gorfe, A.A.2
  • 28
    • 11244252192 scopus 로고    scopus 로고
    • Differential insertion of GPI-anchored GFPs into lipid rafts of live cells
    • DOI 10.1096/fj.03-1338fje
    • D.F. Legler, M.-A.s. Doucey, P. Schneider, L. Chapatte, F.C. Bender, and C. Bron Differential insertion of GPI-anchored GFPs into lipid rafts of live cells FASEB J. 19 2005 73 75 (Pubitemid 40069922)
    • (2005) FASEB Journal , vol.19 , Issue.1 , pp. 73-75
    • Legler, D.F.1    Doucey, M.-A.2    Schneider, P.3    Chapatte, L.4    Bender, F.C.5    Bron, C.6
  • 29
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl- phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction
    • W. Rodgers, B. Crise, and J.K. Rose Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction Mol. Cell. Biol. 14 1994 5384 5391
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5384-5391
    • Rodgers, W.1    Crise, B.2    Rose, J.K.3
  • 30
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes
    • DOI 10.1093/emboj/16.16.4983
    • P.S. Kabouridis, A.I. Magee, and S.C. Ley S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes EMBO J. 16 1997 4983 4998 (Pubitemid 27348407)
    • (1997) EMBO Journal , vol.16 , Issue.16 , pp. 4983-4998
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 31
    • 77951669557 scopus 로고    scopus 로고
    • Chemistry of Hofmeister anions and osmolytes
    • Y. Zhang, and P.S. Cremer Chemistry of Hofmeister anions and osmolytes Annu. Rev. Phys. Chem. 61 2010 63 83
    • (2010) Annu. Rev. Phys. Chem. , vol.61 , pp. 63-83
    • Zhang, Y.1    Cremer, P.S.2
  • 32
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator-binding domain of protein kinase C[delta] in complex with phorbol ester
    • G. Zhang, M.G. Kazanietz, P.M. Blumberg, and J.H. Hurley Crystal structure of the Cys2 activator-binding domain of protein kinase C[delta] in complex with phorbol ester Cell 81 1995 917 924
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 33
    • 0022424027 scopus 로고
    • Specificity of lipid-protein interactions as determined by spectroscopic techniques
    • P.F. Devaux, and M. Seigneuret Specificity of lipid-protein interactions as determined by spectroscopic techniques Biochim. Biophys. Acta (BBA) Rev. Biomembr. 822 1985 63 125
    • (1985) Biochim. Biophys. Acta (BBA) Rev. Biomembr. , vol.822 , pp. 63-125
    • Devaux, P.F.1    Seigneuret, M.2
  • 34
    • 33845930555 scopus 로고    scopus 로고
    • Evidence for specificity in lipid-rhodopsin interactions
    • DOI 10.1074/jbc.M603059200
    • O. Soubias, W.E. Teague, and K. Gawrisch Evidence for specificity in lipid-rhodopsin interactions J. Biol. Chem. 281 2006 33233 33241 (Pubitemid 46036705)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.44 , pp. 33233-33241
    • Soubias, O.1    Teague, W.E.2    Gawrisch, K.3
  • 35
    • 0020490463 scopus 로고
    • Evidence for protein-associated lipids from deuterium nuclear magnetic resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants
    • A. Bienvenue, M. Bloom, J.H. Davis, and P.F. Devaux Evidence for protein-associated lipids from deuterium nuclear magnetic resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants J. Biol. Chem. 257 1982 3032 3038
    • (1982) J. Biol. Chem. , vol.257 , pp. 3032-3038
    • Bienvenue, A.1    Bloom, M.2    Davis, J.H.3    Devaux, P.F.4
  • 36
    • 0035846923 scopus 로고    scopus 로고
    • Electron spin resonance in studies of membranes and proteins
    • DOI 10.1126/science.291.5502.266
    • P.P. Borbat, A.J. Costa-Filho, K.A. Earle, J.K. Moscicki, and J.H. Freed Electron spin resonance in studies of membranes and proteins Science 291 2001 266 269 (Pubitemid 32096305)
    • (2001) Science , vol.291 , Issue.5502 , pp. 266-269
    • Borbat, P.P.1    Costa-Filho, A.J.2    Earle, K.A.3    Moscicki, J.K.4    Freed, J.H.5
  • 37
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • DOI 10.1016/S0304-4157(98)00009-4, PII S0304415798000094
    • D. Marsh, and L.I. Horváth Structure, dynamics and composition of the lipid-protein interface, perspectives from spin-labelling Biochim. Biophys. Acta (BBA) Rev. Biomembr. 1376 1998 267 296 (Pubitemid 28517881)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 267-296
    • Marsh, D.1    Horvath, L.I.2
  • 40
    • 33845360042 scopus 로고    scopus 로고
    • Ultra-high resolution imaging by fluorescence photoactivation localization microscopy
    • DOI 10.1529/biophysj.106.091116
    • S.T. Hess, T.P.K. Girirajan, and M.D. Mason Ultra-high resolution imaging by fluorescence photoactivation localization microscopy Biophys. J. 91 2006 4258 4272 (Pubitemid 44887284)
    • (2006) Biophysical Journal , vol.91 , Issue.11 , pp. 4258-4272
    • Hess, S.T.1    Girirajan, T.P.K.2    Mason, M.D.3
  • 41
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • M.J. Rust, M. Bates, and X. Zhuang Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM) Nat. Methods 3 2006 793 796
    • (2006) Nat. Methods , vol.3 , pp. 793-796
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 42
    • 58849094579 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of a PH domain: New insights into the membrane docking reaction
    • J.D. Knight, and J.J. Falke Single-molecule fluorescence studies of a PH domain: new insights into the membrane docking reaction Biophys. J. 96 2009 566 582
    • (2009) Biophys. J. , vol.96 , pp. 566-582
    • Knight, J.D.1    Falke, J.J.2
  • 43
    • 77956789005 scopus 로고    scopus 로고
    • Membrane docking geometry and target lipid stoichiometry of membrane-bound PKC[alpha] C2 domain: A combined molecular dynamics and experimental study
    • C.-L. Lai, K.E. Landgraf, G.A. Voth, and J.J. Falke Membrane docking geometry and target lipid stoichiometry of membrane-bound PKC[alpha] C2 domain: a combined molecular dynamics and experimental study J. Mol. Biol. 402 2010 301 310
    • (2010) J. Mol. Biol. , vol.402 , pp. 301-310
    • Lai, C.-L.1    Landgraf, K.E.2    Voth, G.A.3    Falke, J.J.4
  • 44
    • 78249261241 scopus 로고    scopus 로고
    • Single molecule diffusion of membrane-bound proteins: Window into lipid contacts and bilayer dynamics
    • J.D. Knight, M.G. Lerner, J.G. Marcano-Velázquez, R.W. Pastor, and Joseph J. Falke Single molecule diffusion of membrane-bound proteins: window into lipid contacts and bilayer dynamics Biophys. J. 99 2010 2879 2887
    • (2010) Biophys. J. , vol.99 , pp. 2879-2887
    • Knight, J.D.1    Lerner, M.G.2    Marcano-Velázquez, J.G.3    Pastor, R.W.4    Falke, J.J.5
  • 45
    • 0036175642 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: The technique and its applications
    • O. Krichevsky, and G. Bonnet Fluorescence correlation spectroscopy: the technique and its applications Rep. Prog. Phys. 65 2002 251
    • (2002) Rep. Prog. Phys. , vol.65 , pp. 251
    • Krichevsky, O.1    Bonnet, G.2
  • 46
    • 55849133025 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy for the study of membrane dynamics and protein/lipid interactions
    • A.J. García-Sáez, and P. Schwille Fluorescence correlation spectroscopy for the study of membrane dynamics and protein/lipid interactions Methods 46 2008 116 122
    • (2008) Methods , vol.46 , pp. 116-122
    • García-Sáez, A.J.1    Schwille, P.2
  • 47
    • 0038699021 scopus 로고    scopus 로고
    • How to determine diffusion coefficients in planar phospholipid systems by confocal fluorescence correlation spectroscopy
    • A. Benda, M. Benes, V. Marecek, A. Lhotsky, W.T. Hermens, and M. Hof How to determine diffusion coefficients in planar phospholipid systems by confocal fluorescence correlation spectroscopy Langmuir 19 2003 4120 4126
    • (2003) Langmuir , vol.19 , pp. 4120-4126
    • Benda, A.1    Benes, M.2    Marecek, V.3    Lhotsky, A.4    Hermens, W.T.5    Hof, M.6
  • 48
    • 38949147878 scopus 로고    scopus 로고
    • Precise measurement of diffusion coefficients using scanning fluorescence correlation spectroscopy
    • Z. Petrasek, and P. Schwille Precise measurement of diffusion coefficients using scanning fluorescence correlation spectroscopy Biophys. J. 94 2008 1437 1448
    • (2008) Biophys. J. , vol.94 , pp. 1437-1448
    • Petrasek, Z.1    Schwille, P.2
  • 49
    • 28444443820 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization
    • DOI 10.1529/biophysj.105.067959
    • L. Wawrezinieck, H. Rigneault, D. Marguet, and P.-F. Lenne Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization Biophys. J. 89 2005 4029 4042 (Pubitemid 41725623)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 4029-4042
    • Wawrezinieck, L.1    Rigneault, H.2    Marguet, D.3    Lenne, P.-F.4
  • 50
    • 31744436399 scopus 로고    scopus 로고
    • Fluorescence cross-correlation spectroscopy in living cells
    • DOI 10.1038/nmeth822, PII N822
    • K. Bacia, S.A. Kim, and P. Schwille Fluorescence cross-correlation spectroscopy in living cells Nat. Methods 3 2006 83 89 (Pubitemid 43173305)
    • (2006) Nature Methods , vol.3 , Issue.2 , pp. 83-89
    • Bacia, K.1    Kim, S.A.2    Schwille, P.3
  • 51
    • 74049157769 scopus 로고    scopus 로고
    • TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation
    • B.F. Lillemeier, M.A. Mortelmaier, M.B. Forstner, J.B. Huppa, J.T. Groves, and M.M. Davis TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation Nat. Immunol. 11 2010 90 96
    • (2010) Nat. Immunol. , vol.11 , pp. 90-96
    • Lillemeier, B.F.1    Mortelmaier, M.A.2    Forstner, M.B.3    Huppa, J.B.4    Groves, J.T.5    Davis, M.M.6
  • 53
    • 84855445145 scopus 로고    scopus 로고
    • Optical characterization of the spatial distribution of lipid-anchored membrane proteins
    • A.W. Smith, S.B. Triffo, H.H. Huang, and J.T. Groves Optical characterization of the spatial distribution of lipid-anchored membrane proteins Am. Chem. Soc. 2011 PHYS-107
    • (2011) Am. Chem. Soc. , pp. 107
    • Smith, A.W.1    Triffo, S.B.2    Huang, H.H.3    Groves, J.T.4
  • 54
    • 4444293957 scopus 로고    scopus 로고
    • SNAREs prefer liquid-disordered over "raft" (liquid-ordered) domains when reconstituted into giant unilamellar vesicles
    • DOI 10.1074/jbc.M407020200
    • K. Bacia, C.G. Schuette, N. Kahya, R. Jahn, and P. Schwille SNAREs prefer liquid-disordered over "raft" (liquid-ordered) domains when reconstituted into giant unilamellar vesicles J. Biol. Chem. 279 2004 37951 37955 (Pubitemid 39195510)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37951-37955
    • Bacia, K.1    Schuette, C.G.2    Kahya, N.3    Jahn, R.4    Schwille, P.5
  • 55
    • 21244447355 scopus 로고    scopus 로고
    • Distribution, lateral mobility and function of membrane proteins incorporated into giant unilamellar vesicles
    • DOI 10.1529/biophysj.104.053413
    • M.K. Doeven, J.H.A. Folgering, V. Krasnikov, E.R. Geertsma, G. van den Bogaart, and B. Poolman Distribution, lateral mobility and function of membrane proteins incorporated into giant unilamellar vesicles Biophys. J. 88 2005 1134 1142 (Pubitemid 40975944)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1134-1142
    • Doeven, M.K.1    Folgering, J.H.A.2    Krasnikov, V.3    Geertsma, E.R.4    Van Den Bogaart, G.5    Poolman, B.6
  • 56
    • 0037131368 scopus 로고    scopus 로고
    • Spatial organization of bacteriorhodopsin in model membranes
    • N. Kahya, D.A. Wiersma, B. Poolman, and D. Hoekstra Spatial organization of bacteriorhodopsin in model membranes J. Biol. Chem. 277 2002 39304 39311
    • (2002) J. Biol. Chem. , vol.277 , pp. 39304-39311
    • Kahya, N.1    Wiersma, D.A.2    Poolman, B.3    Hoekstra, D.4
  • 59
    • 2942637980 scopus 로고    scopus 로고
    • Site-specific vibrational dynamics of the CD3 zeta membrane peptide using heterodyned two-dimensional infrared photon echo spectroscopy
    • P. Mukherjee, A.T. Krummel, E.C. Fulmer, I. Kass, I.T. Arkin, and M.T. Zanni Site-specific vibrational dynamics of the CD3 zeta membrane peptide using heterodyned two-dimensional infrared photon echo spectroscopy J. Chem. Phys. 120 2004 10215 10224
    • (2004) J. Chem. Phys. , vol.120 , pp. 10215-10224
    • Mukherjee, P.1    Krummel, A.T.2    Fulmer, E.C.3    Kass, I.4    Arkin, I.T.5    Zanni, M.T.6
  • 62
    • 23944499045 scopus 로고    scopus 로고
    • Physics: Ultrafast dynamics of solute-solvent complexation observed at thermal equilibrium in real time
    • DOI 10.1126/science.1116213
    • J. Zheng, K. Kwak, J. Asbury, X. Chen, I.R. Piletic, and M.D. Fayer Ultrafast dynamics of solute-solvent complexation observed at thermal equilibrium in real time Science 309 2005 1338 1343 (Pubitemid 41209356)
    • (2005) Science , vol.309 , Issue.5739 , pp. 1338-1343
    • Zheng, J.1    Kwak, K.2    Asbury, J.3    Chen, X.4    Piletic, I.R.5    Fayer, M.D.6
  • 63
    • 0141432008 scopus 로고    scopus 로고
    • Ultrafast hydrogen-bond dynamics in the infrared spectroscopy of water
    • DOI 10.1126/science.1087251
    • C.J. Fecko, J.D. Eaves, J.J. Loparo, A. Tokmakoff, and P.L. Geissler Ultrafast hydrogen-bond dynamics in the infrared spectroscopy of water Science 301 2003 1698 1702 (Pubitemid 37174358)
    • (2003) Science , vol.301 , Issue.5640 , pp. 1698-1702
    • Fecko, C.J.1    Eaves, J.D.2    Loparo, J.J.3    Tokmakoff, A.4    Geissler, P.L.5
  • 64
    • 67149138048 scopus 로고    scopus 로고
    • Applications of 2D IR spectroscopy to peptides, proteins, and hydrogen-bond dynamics
    • Y.S. Kim, and R.M. Hochstrasser Applications of 2D IR spectroscopy to peptides, proteins, and hydrogen-bond dynamics J. Phys. Chem. B 113 2009 8231 8251
    • (2009) J. Phys. Chem. B , vol.113 , pp. 8231-8251
    • Kim, Y.S.1    Hochstrasser, R.M.2
  • 66
    • 79958224038 scopus 로고    scopus 로고
    • Structural properties of a membrane associated anchor dipeptide
    • V.V. Volkov, R. Chelli, F. Muniz-Miranda, and R. Righini Structural properties of a membrane associated anchor dipeptide J. Phys. Chem. B 115 2011 5294 5303
    • (2011) J. Phys. Chem. B , vol.115 , pp. 5294-5303
    • Volkov, V.V.1    Chelli, R.2    Muniz-Miranda, F.3    Righini, R.4
  • 71
    • 65249173508 scopus 로고    scopus 로고
    • Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid
    • Y.L. Ling, D.B. Strasfeld, S.-H. Shim, D.P. Raleigh, and M.T. Zanni Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid J. Phys. Chem. B 113 2009 2498 2505
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2498-2505
    • Ling, Y.L.1    Strasfeld, D.B.2    Shim, S.-H.3    Raleigh, D.P.4    Zanni, M.T.5
  • 72
    • 33748715411 scopus 로고    scopus 로고
    • Isotope-edited IR spectroscopy for the study of membrane proteins
    • DOI 10.1016/j.cbpa.2006.08.013, PII S1367593106001207, Analytical Techniques/Mechanisms
    • I.T. Arkin Isotope-edited IR spectroscopy for the study of membrane proteins Curr. Opin. Chem. Biol. 10 2006 394 401 (Pubitemid 44389917)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 394-401
    • Arkin, I.T.1
  • 74
    • 33750239249 scopus 로고    scopus 로고
    • The physical chemistry of biological membranes
    • DOI 10.1038/nchembio1106-564, PII NCHEMBIO1106564
    • J. Zimmerberg, and K. Gawrisch The physical chemistry of biological membranes Nat. Chem. Biol. 2 2006 564 567 (Pubitemid 44610336)
    • (2006) Nature Chemical Biology , vol.2 , Issue.11 , pp. 564-567
    • Zimmerberg, J.1    Gawrisch, K.2
  • 75
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, and K. Simons Lipid rafts as a membrane-organizing principle Science 327 2010 46 50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.