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Volumn 404, Issue 5, 2010, Pages 773-777

Fluidizing the Membrane by a Local Anesthetic: Phenylethanol Affects Membrane Protein Oligomerization

Author keywords

Anesthetic; Glycophorin A; Helix helix interaction; Membrane; TOXCAT

Indexed keywords

1,2 DIEICOSENOYLGLYCERO 3 PHOSPHOCHOLINE; CHOLINE DERIVATIVE; DIMER; DIMYRISTOYLPHOSPHATIDYLCHOLINE; GLYCOPHORIN A; LAURDAN; PHENETHYL ALCOHOL; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG;

EID: 78649529371     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.10.026     Document Type: Article
Times cited : (34)

References (17)
  • 1
    • 30444459043 scopus 로고    scopus 로고
    • Molecular targets underlying general anaesthesia
    • Franks N.P. Molecular targets underlying general anaesthesia. Br. J. Pharmacol. 2006, 147:S72-S81.
    • (2006) Br. J. Pharmacol. , vol.147
    • Franks, N.P.1
  • 2
    • 0001098317 scopus 로고    scopus 로고
    • Lateral pressures in cell membranes: a mechanism for modulation of protein function
    • Cantor R.S. Lateral pressures in cell membranes: a mechanism for modulation of protein function. J. Phys. Chem. B 1997, 101:1723-1725.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 1723-1725
    • Cantor, R.S.1
  • 3
    • 34247574730 scopus 로고    scopus 로고
    • The thermodynamics of general anesthesia
    • Heimburg T., Jackson A.D. The thermodynamics of general anesthesia. Biophys. J. 2007, 92:3159-3165.
    • (2007) Biophys. J. , vol.92 , pp. 3159-3165
    • Heimburg, T.1    Jackson, A.D.2
  • 4
    • 33646902110 scopus 로고    scopus 로고
    • Folding and stability of alpha-helical integral membrane proteins
    • Mackenzie K.R. Folding and stability of alpha-helical integral membrane proteins. Chem. Rev. 2006, 106:1931-1977.
    • (2006) Chem. Rev. , vol.106 , pp. 1931-1977
    • Mackenzie, K.R.1
  • 5
    • 77953594623 scopus 로고    scopus 로고
    • Transmembrane helix-helix interactions involved in ErbB receptor signaling
    • Cymer F., Schneider D. Transmembrane helix-helix interactions involved in ErbB receptor signaling. Cell Adhes. Migr. 2010, 4:299-312.
    • (2010) Cell Adhes. Migr. , vol.4 , pp. 299-312
    • Cymer, F.1    Schneider, D.2
  • 6
    • 77953603192 scopus 로고    scopus 로고
    • Receptor tyrosine kinase transmembrane domains: function, dimer structure and dimerization energetics
    • Li E., Hristova K. Receptor tyrosine kinase transmembrane domains: function, dimer structure and dimerization energetics. Cell Adhes. Migr. 2010, 4:249-254.
    • (2010) Cell Adhes. Migr. , vol.4 , pp. 249-254
    • Li, E.1    Hristova, K.2
  • 7
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: structure and implications
    • MacKenzie K.R., Prestegard J.H., Engelman D.M. A transmembrane helix dimer: structure and implications. Science 1997, 276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 8
    • 77049106259 scopus 로고    scopus 로고
    • Unfolding a transmembrane helix dimer: a FRET study in mixed micelles
    • Anbazhagan V., Cymer F., Schneider D. Unfolding a transmembrane helix dimer: a FRET study in mixed micelles. Arch. Biochem. Biophys. 2010, 495:159-164.
    • (2010) Arch. Biochem. Biophys. , vol.495 , pp. 159-164
    • Anbazhagan, V.1    Cymer, F.2    Schneider, D.3
  • 9
    • 15544385324 scopus 로고    scopus 로고
    • Forster resonance energy transfer in liposomes: measurements of transmembrane helix dimerization in the native bilayer environment
    • You M., Li E., Wimley W.C., Hristova K. Forster resonance energy transfer in liposomes: measurements of transmembrane helix dimerization in the native bilayer environment. Anal. Biochem. 2005, 340:154-164.
    • (2005) Anal. Biochem. , vol.340 , pp. 154-164
    • You, M.1    Li, E.2    Wimley, W.C.3    Hristova, K.4
  • 10
    • 77955656071 scopus 로고    scopus 로고
    • The membrane environment modulates self-association of the human GpA TM domain-implications for membrane protein folding and transmembrane signaling
    • Anbazhagan V., Schneider D. The membrane environment modulates self-association of the human GpA TM domain-implications for membrane protein folding and transmembrane signaling. Biochim. Biophys. Acta 2010, 1798:1899-1907.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1899-1907
    • Anbazhagan, V.1    Schneider, D.2
  • 11
    • 0025295884 scopus 로고
    • Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence
    • Parasassi T., De Stasio G., d'Ubaldo A., Gratton E. Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence. Biophys. J. 1990, 57:1179-1186.
    • (1990) Biophys. J. , vol.57 , pp. 1179-1186
    • Parasassi, T.1    De Stasio, G.2    d'Ubaldo, A.3    Gratton, E.4
  • 12
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: a measure of transmembrane helix association in a biological membrane
    • Russ W.P., Engelman D.M. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl Acad. Sci. USA 1999, 96:863-868.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 13
    • 73349087177 scopus 로고    scopus 로고
    • The single transmembrane domains of human receptor tyrosine kinases encode self-interactions
    • Finger C., Escher C., Schneider D. The single transmembrane domains of human receptor tyrosine kinases encode self-interactions. Sci. Signaling 2009, 2:ra56.
    • (2009) Sci. Signaling , vol.2
    • Finger, C.1    Escher, C.2    Schneider, D.3
  • 14
    • 33847696075 scopus 로고    scopus 로고
    • Receptor tyrosine kinases: mechanisms of activation and signaling
    • Hubbard S.R., Miller W.T. Receptor tyrosine kinases: mechanisms of activation and signaling. Curr. Opin. Cell. Biol. 2007, 19:117-123.
    • (2007) Curr. Opin. Cell. Biol. , vol.19 , pp. 117-123
    • Hubbard, S.R.1    Miller, W.T.2
  • 15
    • 33748062987 scopus 로고    scopus 로고
    • GIRK channel activation involves a local rearrangement of a preformed G protein channel complex
    • Riven I., Iwanir S., Reuveny E. GIRK channel activation involves a local rearrangement of a preformed G protein channel complex. Neuron 2006, 51:561-573.
    • (2006) Neuron , vol.51 , pp. 561-573
    • Riven, I.1    Iwanir, S.2    Reuveny, E.3
  • 16
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum D.M., Rasmussen S.G., Kobilka B.K. The structure and function of G-protein-coupled receptors. Nature 2009, 459:356-363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 17
    • 77953297286 scopus 로고    scopus 로고
    • Membrane-mediated effect on ion channels induced by the anesthetic drug ketamine
    • Jerabek H., Pabst G., Rappolt M., Stockner T. Membrane-mediated effect on ion channels induced by the anesthetic drug ketamine. J. Am. Chem. Soc. 2010, 132:7990-7997.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7990-7997
    • Jerabek, H.1    Pabst, G.2    Rappolt, M.3    Stockner, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.