메뉴 건너뛰기




Volumn 137, Issue 1, 2011, Pages 93-110

Specificity of cholesterol and analogs to modulate BK channels points to direct sterol-channel protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; DRUG DERIVATIVE; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; STEROL;

EID: 78650905628     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201010519     Document Type: Article
Times cited : (72)

References (75)
  • 1
    • 0037474005 scopus 로고    scopus 로고
    • Low chemical specificity of the nicotinic acetylcholine receptor sterol activation site
    • doi:10.1016/S0005-2736(02)00685-5
    • Addona, G.H., H. Sandermann Jr., M.A. Kloczewiak, and K.W. Miller. 2003. Low chemical specificity of the nicotinic acetylcholine receptor sterol activation site. Biochim. Biophys. Acta. 1609:177-182. doi:10.1016/S0005- 2736(02)00685-5
    • (2003) Biochim. Biophys. Acta. , vol.1609 , pp. 177-182
    • Addona, G.H.1    Sandermann Jr., H.2    Kloczewiak, M.A.3    Miller., K.W.4
  • 2
    • 34548558868 scopus 로고    scopus 로고
    • Mechanisms of neurosteroid interactions with GABA(A) receptors
    • doi:10 .1016/j.pharmthera.2007.03.004
    • Akk, G., D.F. Covey, A.S. Evers, J.H. Steinbach, C.F. Zorumski, and S. Mennerick. 2007. Mechanisms of neurosteroid interactions with GABA(A) receptors. Pharmacol. Ther. 116:35-57. doi:10 .1016/j.pharmthera.2007.03.004
    • (2007) Pharmacol. Ther. , vol.116 , pp. 35-57
    • Akk, G.1    Covey, D.F.2    Evers, A.S.3    Steinbach, J.H.4    Zorumski, C.F.5    Mennerick, S.6
  • 3
    • 39449106286 scopus 로고    scopus 로고
    • Enantiospecific interactions between cholesterol and phospholipids
    • doi:10.1021/la702909q
    • Alakoskela, J.M., K. Sabatini, X. Jiang, V. Laitala, D.F. Covey, and P.K. Kinnunen. 2008. Enantiospecific interactions between cholesterol and phospholipids. Langmuir. 24:830-836. doi:10.1021/la702909q
    • (2008) Langmuir. , vol.24 , pp. 830-836
    • Alakoskela, J.M.1    Sabatini, K.2    Jiang, X.3    Laitala, V.4    Covey, D.F.5    Kinnunen., P.K.6
  • 4
    • 36549058256 scopus 로고    scopus 로고
    • Single-molecule methods for monitoring changes in bilayer elastic properties
    • doi:10.1007/ 978-1-59745-519-0-37
    • Andersen, O.S., M.J. Bruno, H. Sun, and R.E. Koeppe II. 2007. Single-molecule methods for monitoring changes in bilayer elastic properties. Methods Mol. Biol. 400:543-570. doi:10.1007/ 978-1-59745-519-0-37
    • (2007) Methods Mol. Biol. , vol.400 , pp. 543-570
    • Andersen, O.S.1    Bruno, M.J.2    Sun, H.3    Koeppe, I.I.R.E.4
  • 5
    • 0032564372 scopus 로고    scopus 로고
    • Disclosure of discrete sites for phospholipid and sterols at the protein-lipid interface in native acetylcholine receptor-rich membrane
    • doi:10.1021/bi9808215
    • Antollini, S.S., and F.J. Barrantes. 1998. Disclosure of discrete sites for phospholipid and sterols at the protein-lipid interface in native acetylcholine receptor-rich membrane. Biochemistry. 37:16653-16662. doi:10.1021/bi9808215
    • (1998) Biochemistry. , vol.37 , pp. 16653-16662
    • Antollini, S.S.1    Barrantes., F.J.2
  • 6
    • 0142027322 scopus 로고    scopus 로고
    • Modulation of nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains
    • Barrantes, F.J. 2003. Modulation of nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains. Curr. Opin. Drug Discov. Devel. 6:620-632.
    • (2003) Curr. Opin. Drug Discov. Devel. , vol.6 , pp. 620-632
    • Barrantes, F.J.1
  • 7
    • 9644294471 scopus 로고    scopus 로고
    • Structural basis for lipid modulation of nicotinic acetylcholine receptor function
    • doi:10.1016/j.brainresrev.2004.06.008
    • Barrantes, F.J. 2004. Structural basis for lipid modulation of nicotinic acetylcholine receptor function. Brain Res. Brain Res. Rev. 47:71-95. doi:10.1016/j.brainresrev.2004.06.008
    • (2004) Brain Res. Brain Res. Rev. , vol.47 , pp. 71-95
    • Barrantes, F.J.1
  • 8
    • 41649095760 scopus 로고    scopus 로고
    • A concise synthesis of ent- Cholesterol
    • doi:10.1021/jo702694g
    • Belani, J.D., and S.D. Rychnovsky. 2008. A concise synthesis of ent- Cholesterol. J. Org. Chem. 73:2768-2773. doi:10.1021/jo702694g
    • (2008) J. Org. Chem. , vol.73 , pp. 2768-2773
    • Belani, J.D.1    Rychnovsky., S.D.2
  • 9
    • 0033729495 scopus 로고    scopus 로고
    • Functional consequences of lipid packing stress
    • doi:10.1016/ S1359-0294(00)
    • Bezrukov, S. 2000. Functional consequences of lipid packing stress. Curr. Opin. Colloid Interface Sci. 5:237-243. doi:10.1016/ S1359-0294(00)00061-3
    • (2000) Curr. Opin. Colloid Interface Sci. , vol.5 , pp. 237-243
    • Bezrukov, S.1
  • 10
    • 0024430160 scopus 로고
    • Excess membrane cholesterol alters calcium channels in arterial smooth muscle
    • Bialecki, R.A., and T.N. Tulenko. 1989. Excess membrane cholesterol alters calcium channels in arterial smooth muscle. Am. J. Physiol. 257:C306-C314.
    • (1989) Am. J. Physiol. , vol.257
    • Bialecki, R.A.1    Tulenko., T.N.2
  • 11
    • 0030633451 scopus 로고    scopus 로고
    • Has nature designed the cholesterol side chain for optimal interaction with phospholipids?
    • R. Bittman, editor Plenum Press, New York
    • Bittman, R. 1997. Has nature designed the cholesterol side chain for optimal interaction with phospholipids? In Cholesterol: Its Functions and Metabolism in Biology and Medicine. R. Bittman, editor. Plenum Press, New York. 145-172.
    • (1997) Cholesterol: Its Functions and Metabolism in Biology and Medicine , pp. 145-172
    • Bittman, R.1
  • 12
    • 0024792686 scopus 로고
    • Variations of membrane cholesterol alter the kinetics of Ca2(+)-dependent K+ channels and membrane fluidity in vascular smooth muscle cells
    • doi:10.1007/BF00370875
    • Bolotina, V., V. Omelyanenko, B. Heyes, U. Ryan, and P. Bregestovski. 1989. Variations of membrane cholesterol alter the kinetics of Ca2(+)-dependent K+ channels and membrane fluidity in vascular smooth muscle cells. Pflugers Arch. 415:262-268. doi:10.1007/BF00370875
    • (1989) Pflugers Arch. , vol.415 , pp. 262-268
    • Bolotina, V.1    Omelyanenko, V.2    Heyes, B.3    Ryan, U.4    Bregestovski., P.5
  • 13
    • 34547191268 scopus 로고    scopus 로고
    • 2+-activated K+ channels and dilation in small, resistance-size arteries
    • doi:10 .1124/mol.107.034330
    • 2+-activated K+ channels and dilation in small, resistance-size arteries. Mol. Pharmacol. 72:359-369. doi:10 .1124/mol.107.034330
    • (2007) Mol. Pharmacol. , vol.72 , pp. 359-369
    • Bukiya, A.N.1    Liu, J.2    Toro, L.3    Dopico, A.M.4
  • 14
    • 58149474714 scopus 로고    scopus 로고
    • Structural determinants of monohydroxylated bile acids to activate beta 1 subunit-containing BK channels
    • doi:10.1194/jlr.M800286-JLR200
    • Bukiya, A.N., J. McMillan, A.L. Parrill, and A.M. Dopico. 2008a. Structural determinants of monohydroxylated bile acids to activate beta 1 subunit-containing BK channels. J. Lipid Res. 49:2441-2451. doi:10.1194/jlr. M800286-JLR200
    • (2008) J. Lipid Res. , vol.49 , pp. 2441-2451
    • Bukiya, A.N.1    McMillan, J.2    Parrill, A.L.3    Dopico., A.M.4
  • 15
    • 39649107151 scopus 로고    scopus 로고
    • The second transmembrane domain of the large conductance, voltage- and calcium-gated potassium channel beta(1) subunit is a lithocholate sensor
    • doi:10.1016/ j.febslet.2008.01.036
    • Bukiya, A.N., T. Vaithianathan, L. Toro, and A.M. Dopico. 2008b. The second transmembrane domain of the large conductance, voltage- and calcium-gated potassium channel beta(1) subunit is a lithocholate sensor. FEBS Lett. 582:673-678. doi:10.1016/ j.febslet.2008.01.036
    • (2008) FEBS Lett. , vol.582 , pp. 673-678
    • Bukiya, A.N.1    Vaithianathan, T.2    Toro, L.3    Dopico., A.M.4
  • 16
    • 69249205340 scopus 로고    scopus 로고
    • The BK channel accessory ?1 subunit determines alcohol-induced cerebrovascular constriction
    • doi:10.1016/j.febslet.2009.07.019
    • Bukiya, A.N., J. Liu, and A.M. Dopico. 2009. The BK channel accessory ?1 subunit determines alcohol-induced cerebrovascular constriction. FEBS Lett. 583:2779-2784. doi:10.1016/j.febslet.2009.07.019
    • (2009) FEBS Lett. , vol.583 , pp. 2779-2784
    • Bukiya, A.N.1    Liu, J.2    Dopico., A.M.3
  • 17
    • 33744790291 scopus 로고    scopus 로고
    • Evidence for the role of cell stiffness in modulation of volume-regulated anion channels
    • doi:10.1111/j.1748-1716.2006.01555.x
    • Byfield, F.J., B.D. Hoffman, V.G. Romanenko, Y. Fang, J.C. Crocker, and I. Levitan. 2006. Evidence for the role of cell stiffness in modulation of volume-regulated anion channels. Acta Physiol. (Oxf.). 187:285-294. doi:10.1111/j.1748-1716.2006.01555.x
    • (2006) Acta Physiol. (Oxf.). , vol.187 , pp. 285-294
    • Byfield, F.J.1    Hoffman, B.D.2    Romanenko, V.G.3    Fang, Y.4    Crocker, J.C.5    Levitan., I.6
  • 18
    • 0033028551 scopus 로고    scopus 로고
    • Lipid composition and the lateral pressure profile in bilayers
    • doi:10.1016/S0006- 3495(99)
    • Cantor, R.S. 1999. Lipid composition and the lateral pressure profile in bilayers. Biophys. J. 76:2625-2639. doi:10.1016/S0006- 3495(99)77415-1
    • (1999) Biophys. J. , vol.76 , pp. 2625-2639
    • Cantor, R.S.1
  • 19
    • 0028942821 scopus 로고
    • Attenuation of channel kinetics and conductance by cholesterol: An interpretation using structural stress as a unifying concept
    • Chang, H.M., R. Reitstetter, R.P. Mason, and R. Gruener. 1995. Attenuation of channel kinetics and conductance by cholesterol: an interpretation using structural stress as a unifying concept. J. Membr. Biol. 143:51-63.
    • (1995) J. Membr. Biol. , vol.143 , pp. 51-63
    • Chang, H.M.1    Reitstetter, R.2    Mason, R.P.3    Gruener., R.4
  • 20
    • 0001908198 scopus 로고
    • The principles of the stochastic interpretation of ion-channel mechanisms
    • B. Sakmann and E. Neher, editors Plenum Press, New York
    • Colquhoun, D., and A.G. Hawkes. 1983. The principles of the stochastic interpretation of ion-channel mechanisms. In: Single Channel Recording. B. Sakmann and E. Neher, editors. Plenum Press, New York. 135-175.
    • (1983) Single Channel Recording , pp. 135-175
    • Colquhoun, D.1    Hawkes., A.G.2
  • 22
    • 0041341930 scopus 로고    scopus 로고
    • Cholesterol antagonizes ethanol potentiation of human brain BKCa channels reconstituted into phospholipid bilayers
    • doi:10.1124/mol.64.2.365
    • Crowley, J.J., S.N. Treistman, and A.M. Dopico. 2003. Cholesterol antagonizes ethanol potentiation of human brain BKCa channels reconstituted into phospholipid bilayers. Mol. Pharmacol. 64:365-372. doi:10.1124/mol.64.2.365
    • (2003) Mol. Pharmacol. , vol.64 , pp. 365-372
    • Crowley, J.J.1    Treistman, S.N.2    Dopico., A.M.3
  • 23
    • 22344444877 scopus 로고    scopus 로고
    • Distinct structural features of phospholipids differentially determine ethanol sensitivity and basal function of BK channels
    • Crowley, J.J., S.N. Treistman, and A.M. Dopico. 2005. Distinct structural features of phospholipids differentially determine ethanol sensitivity and basal function of BK channels. Mol. Pharmacol. 68:4-10.
    • (2005) Mol. Pharmacol. , vol.68 , pp. 4-10
    • Crowley, J.J.1    Treistman, S.N.2    Dopico., A.M.3
  • 24
    • 0017192580 scopus 로고
    • The function of sterols in membranes
    • Demel, R.A., and B. De Kruyff. 1976. The function of sterols in membranes. Biochim. Biophys. Acta. 457:109-132.
    • (1976) Biochim. Biophys. Acta. , vol.457 , pp. 109-132
    • Demel, R.A.1    De, B.K.2
  • 25
    • 0015513391 scopus 로고
    • Structural requirements of sterols for the interaction with lecithin at the air water interface
    • doi:10.1016/0005-2736(72)90030-2
    • Demel, R.A., K.R. Bruckdorfer, and L.L. van Deenen. 1972. Structural requirements of sterols for the interaction with lecithin at the air water interface. Biochim. Biophys. Acta. 255:311-320. doi:10.1016/0005-2736(72)90030-2
    • (1972) Biochim. Biophys. Acta. , vol.255 , pp. 311-320
    • Demel, R.A.1    Bruckdorfer, K.R.2    Van, L.L.Deenen.3
  • 26
    • 0035977056 scopus 로고    scopus 로고
    • (Xeno) estrogen sensitivity of smooth muscle BK channels conferred by the regulatory beta1 subunit: A study of beta1 knockout mice
    • doi:10.1074/jbc.M106851200
    • Dick, G.M., and K.M. Sanders. 2001. (Xeno)estrogen sensitivity of smooth muscle BK channels conferred by the regulatory beta1 subunit: a study of beta1 knockout mice. J. Biol. Chem. 276:44835-44840. doi:10.1074/jbc.M106851200
    • (2001) J. Biol. Chem. , vol.276 , pp. 44835-44840
    • Dick, G.M.1    Sanders., K.M.2
  • 27
    • 0038273863 scopus 로고    scopus 로고
    • Ethanol sensitivity of BK(Ca) channels from arterial smooth muscle does not require the presence of the beta 1-subunit
    • Dopico, A.M. 2003. Ethanol sensitivity of BK(Ca) channels from arterial smooth muscle does not require the presence of the beta 1-subunit. Am. J. Physiol. Cell Physiol. 284:C1468-C1480.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Dopico, A.M.1
  • 28
    • 0030039577 scopus 로고    scopus 로고
    • Ethanol increases the activity of large conductance, Ca(2+)-activated K+ channels in isolated neurohypophysial terminals
    • Dopico, A.M., J.R. Lemos, and S.N. Treistman. 1996. Ethanol increases the activity of large conductance, Ca(2+)-activated K+ channels in isolated neurohypophysial terminals. Mol. Pharmacol. 49:40-48.
    • (1996) Mol. Pharmacol. , vol.49 , pp. 40-48
    • Dopico, A.M.1    Lemos, J.R.2    Treistman., S.N.3
  • 29
    • 33744512299 scopus 로고    scopus 로고
    • Cholesterol and the interaction of proteins with membrane domains
    • doi:10.1016/ j.plipres.2006.02.001
    • Epand, R.M. 2006. Cholesterol and the interaction of proteins with membrane domains. Prog. Lipid Res. 45:279-294. doi:10.1016/ j.plipres.2006.02. 001
    • (2006) Prog. Lipid Res. , vol.45 , pp. 279-294
    • Epand, R.M.1
  • 31
    • 33947357066 scopus 로고    scopus 로고
    • Conformation-sensitive steroid and fatty acid sites in the transmembrane domain of the nicotinic acetylcholine receptor
    • doi:10.1021/bi061388z
    • Ferñdez Nievas, G.A., F.J. Barrantes, and S.S. Antollini. 2007. Conformation-sensitive steroid and fatty acid sites in the transmembrane domain of the nicotinic acetylcholine receptor. Biochemistry. 46:3503-3512. doi:10.1021/bi061388z
    • (2007) Biochemistry. , vol.46 , pp. 3503-3512
    • Ferñdez Nievas, G.A.1    Barrantes, F.J.2    Antollini., S.S.3
  • 32
    • 0037429690 scopus 로고    scopus 로고
    • Relationship between cholesterol trafficking and signaling in rafts and caveolae
    • doi:10.1016/S0005-2736(03)00020-8
    • Fielding, C.J., and P.E. Fielding. 2003. Relationship between cholesterol trafficking and signaling in rafts and caveolae. Biochim. Biophys. Acta. 1610:219-228. doi:10.1016/S0005-2736(03)00020-8
    • (2003) Biochim. Biophys. Acta. , vol.1610 , pp. 219-228
    • Fielding, C.J.1    Fielding., P.E.2
  • 33
    • 0022552318 scopus 로고
    • Correlation between acetylcholine receptor function and structural properties of membranes
    • doi:10.1021/bi00352a015
    • Fong, T.M., and M.G. McNamee. 1986. Correlation between acetylcholine receptor function and structural properties of membranes. Biochemistry. 25:830-840. doi:10.1021/bi00352a015
    • (1986) Biochemistry. , vol.25 , pp. 830-840
    • Fong, T.M.1    McNamee., M.G.2
  • 35
    • 0030774729 scopus 로고    scopus 로고
    • Cholesterol as modulator of receptor function
    • doi:10.1021/bi963138w
    • Gimpl, G., K. Burger, and F. Fahrenholz. 1997. Cholesterol as modulator of receptor function. Biochemistry. 36:10959-10974. doi:10.1021/bi963138w
    • (1997) Biochemistry. , vol.36 , pp. 10959-10974
    • Gimpl, G.1    Burger, K.2    Fahrenholz., F.3
  • 36
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94
    • doi:10.1002/(SICI)1096-987X(199604)17:5/6490:: AID-JCC13.0.CO;2-P
    • Halgren, T.A. 1996. Merck molecular force field. I. Basis, form, scope, parameterization, and performance of MMFF94. J. Comput. Chem. 17:490-519. doi:10.1002/(SICI)1096-987X(199604)17:5/63.0.CO;2-P
    • (1996) J. Comput. Chem. , vol.17 , pp. 490-519
    • Halgren, T.A.1
  • 37
    • 0023175459 scopus 로고
    • Structure-activity relationships for steroid interaction with the gamma-aminobutyric acidA receptor complex
    • Harrison, N.L., M.D. Majewska, J.W. Harrington, and J.L. Barker. 1987. Structure-activity relationships for steroid interaction with the gamma-aminobutyric acidA receptor complex. J. Pharmacol. Exp. Ther. 241:346-353.
    • (1987) J. Pharmacol. Exp. Ther. , vol.241 , pp. 346-353
    • Harrison, N.L.1    Majewska, M.D.2    Harrington, J.W.3    Barker., J.L.4
  • 38
    • 0031880699 scopus 로고    scopus 로고
    • Change of motion and localization of cholesterol molecule during L(alpha)-H(II) transition
    • doi:10.1016/S0006-3495(98)74012-3
    • Hayakawa, E., M. Naganuma, K. Mukasa, T. Shimozawa, and T. Araiso. 1998. Change of motion and localization of cholesterol molecule during L(alpha)-H(II) transition. Biophys. J. 74:892-898. doi:10.1016/S0006-3495(98)74012-3
    • (1998) Biophys. J. , vol.74 , pp. 892-898
    • Hayakawa, E.1    Naganuma, M.2    Mukasa, K.3    Shimozawa, T.4    Araiso., T.5
  • 39
    • 34548639993 scopus 로고    scopus 로고
    • Neurosteroid binding sites on GABA(A) receptors
    • doi:10.1016/j.pharmthera.2007.03.011
    • Hosie, A.M., M.E. Wilkins, and T.G. Smart. 2007. Neurosteroid binding sites on GABA(A) receptors. Pharmacol. Ther. 116:7-19. doi:10.1016/j.pharmthera. 2007.03.011
    • (2007) Pharmacol. Ther. , vol.116 , pp. 7-19
    • Hosie, A.M.1    Wilkins, M.E.2    Smart., T.G.3
  • 41
    • 0034902235 scopus 로고    scopus 로고
    • Interactions of cholesterol with lipid bilayers: The preferred configuration and fluctuations
    • doi:10.1016/S0006-3495(01)75729-3
    • Kessel, A., N. Ben-Tal, and S. May. 2001. Interactions of cholesterol with lipid bilayers: the preferred configuration and fluctuations. Biophys. J. 81:643-658. doi:10.1016/S0006-3495(01)75729-3
    • (2001) Biophys. J. , vol.81 , pp. 643-658
    • Kessel, A.1    Ben-Tal, N.2    May., S.3
  • 42
    • 33646182618 scopus 로고    scopus 로고
    • Beta2 and beta4 subunits of BK channels confer differential sensitivity to acute modulation by steroid hormones
    • doi:10.1152/ jn.01352.2005
    • King, J.T., P.V. Lovell, M. Rishniw, M.I. Kotlikoff, M.L. Zeeman, and D.P. McCobb. 2006. Beta2 and beta4 subunits of BK channels confer differential sensitivity to acute modulation by steroid hormones. J. Neurophysiol. 95:2878-2888. doi:10.1152/ jn.01352.2005
    • (2006) J. Neurophysiol. , vol.95 , pp. 2878-2888
    • King, J.T.1    Lovell, P.V.2    Rishniw, M.3    Kotlikoff, M.I.4    Zeeman, M.L.5    McCobb., D.P.6
  • 43
    • 9644254296 scopus 로고    scopus 로고
    • Membrane cholesterol content modulates activation of BK channels in colonic epithelia
    • doi:10.1016/ j.bbamem.2004.11.004
    • Lam, R.S., A.R. Shaw, and M. Duszyk. 2004. Membrane cholesterol content modulates activation of BK channels in colonic epithelia. Biochim. Biophys. Acta. 1667:241-248. doi:10.1016/ j.bbamem.2004.11.004
    • (2004) Biochim. Biophys. Acta. , vol.1667 , pp. 241-248
    • Lam, R.S.1    Shaw, A.R.2    Duszyk., M.3
  • 44
    • 0016741726 scopus 로고
    • Structurally specific effects of some steroid anesthetics on spin-labeled liposomes
    • Lawrence, D.K., and E.W. Gill. 1975. Structurally specific effects of some steroid anesthetics on spin-labeled liposomes. Mol. Pharmacol. 11:280-286.
    • (1975) Mol. Pharmacol. , vol.11 , pp. 280-286
    • Lawrence, D.K.1    Gill., E.W.2
  • 45
    • 0034081627 scopus 로고    scopus 로고
    • Membrane cholesterol content modulates activation of volumeregulated anion current in bovine endothelial cells
    • doi:10.1085/jgp.115.4.405
    • Levitan, I., A.E. Christian, T.N. Tulenko, and G.H. Rothblat. 2000. Membrane cholesterol content modulates activation of volumeregulated anion current in bovine endothelial cells. J. Gen. Physiol. 115:405-416. doi:10.1085/jgp.115.4.405
    • (2000) J. Gen. Physiol. , vol.115 , pp. 405-416
    • Levitan, I.1    Christian, A.E.2    Tulenko, T.N.3    Rothblat., G.H.4
  • 48
    • 50449104476 scopus 로고    scopus 로고
    • Ethanol modulates BKCa channels by acting as an adjuvant of calcium
    • doi:10.1124/ mol.108.048694
    • Liu, J., T. Vaithianathan, K. Manivannan, A. Parrill, and A.M. Dopico. 2008. Ethanol modulates BKCa channels by acting as an adjuvant of calcium. Mol. Pharmacol. 74:628-640. doi:10.1124/ mol.108.048694
    • (2008) Mol. Pharmacol. , vol.74 , pp. 628-640
    • Liu, J.1    Vaithianathan, T.2    Manivannan, K.3    Parrill, A.4    Dopico., A.M.5
  • 49
    • 0030892178 scopus 로고    scopus 로고
    • Dehydroergosterol structural organization in aqueous medium and in a model system of membranes
    • doi:10.1016/S0006- 3495(97)
    • Loura, L.M., and M. Prieto. 1997. Dehydroergosterol structural organization in aqueous medium and in a model system of membranes. Biophys. J. 72:2226-2236. doi:10.1016/S0006- 3495(97)78866-0
    • (1997) Biophys. J. , vol.72 , pp. 2226-2236
    • Loura, L.M.1    Prieto., M.2
  • 50
    • 33645912907 scopus 로고    scopus 로고
    • MaxiK channel partners: Physiological impact
    • doi:10.1113/jphysiol.2005.098913
    • Lu, R., A. Alioua, Y. Kumar, M. Eghbali, E. Stefani, and L. Toro. 2006. MaxiK channel partners: physiological impact. J. Physiol. 570:65-72. doi:10.1113/jphysiol.2005.098913
    • (2006) J. Physiol. , vol.570 , pp. 65-72
    • Lu, R.1    Alioua, A.2    Kumar, Y.3    Eghbali, M.4    Stefani, E.5    Toro., L.6
  • 51
    • 0028053841 scopus 로고
    • Lysophospholipids modulate channel function by altering the mechanical properties of lipid bilayers
    • doi:10.1085/ jgp.104.4.645
    • Lundbaek, J.A., and O.S. Andersen. 1994. Lysophospholipids modulate channel function by altering the mechanical properties of lipid bilayers. J. Gen. Physiol. 104:645-673. doi:10.1085/ jgp.104.4.645
    • (1994) J. Gen. Physiol. , vol.104 , pp. 645-673
    • Lundbaek, J.A.1    Andersen., O.S.2
  • 52
    • 2342469391 scopus 로고    scopus 로고
    • Regulation of sodium channel function by bilayer elasticity: The importance of hydrophobic coupling. Effects of Micelle-forming amphiphiles and cholesterol
    • doi:10.1085/jgp.200308996
    • Lundbaek, J.A., P. Birn, A.J. Hansen, R. Sáard, C. Nielsen, J. Girshman, M.J. Bruno, S.E. Tape, J. Egebjerg, D.V. Greathouse, et al. 2004. Regulation of sodium channel function by bilayer elasticity: the importance of hydrophobic coupling. Effects of Micelle-forming amphiphiles and cholesterol. J. Gen. Physiol. 123:599-621. doi:10.1085/jgp.200308996
    • (2004) J. Gen. Physiol. , vol.123 , pp. 599-621
    • Lundbaek, J.A.1    Birn, P.2    Hansen, A.J.3    Sáard, R.4    Nielsen, C.5    Girshman, J.6    Bruno, M.J.7    Tape, S.E.8    Egebjerg, J.9    Greathouse, D.V.10
  • 53
    • 0037429704 scopus 로고    scopus 로고
    • Condensed complexes of cholesterol and phospholipids
    • doi:10.1016/S0005-2736(03)00015-4
    • McConnell, H.M., and A. Radhakrishnan. 2003. Condensed complexes of cholesterol and phospholipids. Biochim. Biophys. Acta. 1610:159-173. doi:10.1016/S0005-2736(03)00015-4
    • (2003) Biochim. Biophys. Acta. , vol.1610 , pp. 159-173
    • McConnell, H.M.1    Radhakrishnan., A.2
  • 54
    • 0028926916 scopus 로고
    • Functional role of the beta subunit of high conductance calcium-activated potassium channels
    • doi:10.1016/0896-6273(95)90321-6
    • McManus, O.B., L.M. Helms, L. Pallanck, B. Ganetzky, R. Swanson, and R.J. Leonard. 1995. Functional role of the beta subunit of high conductance calcium-activated potassium channels. Neuron. 14:645-650. doi:10.1016/0896- 6273(95)90321-6
    • (1995) Neuron. , vol.14 , pp. 645-650
    • McManus, O.B.1    Helms, L.M.2    Pallanck, L.3    Ganetzky, B.4    Swanson, R.5    Leonard., R.J.6
  • 55
    • 33847768020 scopus 로고    scopus 로고
    • Lipid stress at play: Mechanosensitivity of voltage-gated channels
    • Morris, C.E., and P.F. Juranka. 2007. Lipid stress at play: mechanosensitivity of voltage-gated channels. Current Topics in Membranes. 59:297-338.
    • (2007) Current Topics in Membranes. , vol.59 , pp. 297-338
    • Morris, C.E.1    Juranka., P.F.2
  • 56
    • 0014588913 scopus 로고
    • The electrical capacitance of phospholipid membranes
    • doi:10.1016/S0006-3495 (69)
    • Ohki, S. 1969. The electrical capacitance of phospholipid membranes. Biophys. J. 9:1195-1205. doi:10.1016/S0006-3495 (69)86445-3
    • (1969) Biophys. J. , vol.9 , pp. 1195-1205
    • Ohki, S.1
  • 57
    • 0036027683 scopus 로고    scopus 로고
    • Cholesterol interactions with phospholipids in membranes
    • doi:10.1016/S0163-7827(01)00020-0 Orio, P., P. Rojas, G. Ferreira, and R. Latorre. 2002. New disguises for an old channel: MaxiK channel beta-subunits. News Physiol. Sci. 17156-161
    • Ohvo-Rekil H., B. Ramstedt, P. Leppim?i, and J.P. Slotte. 2002. Cholesterol interactions with phospholipids in membranes. Prog. Lipid Res. 41:66-97. doi:10.1016/S0163-7827(01)00020-0 Orio, P., P. Rojas, G. Ferreira, and R. Latorre. 2002. New disguises for an old channel: MaxiK channel beta-subunits. News Physiol. Sci. 17:156-161.
    • (2002) Prog. Lipid Res. , vol.41 , pp. 66-97
    • Ohvo-Rekil, H.1    Ramstedt, P.B.2    Leppimi3    Slotte., J.P.4
  • 58
    • 0033914742 scopus 로고    scopus 로고
    • Steroid inhibition of rat neuronal nicotinic alpha4beta2 receptors expressed in HEK 293 cells
    • Paradiso, K., K. Sabey, A.S. Evers, C.F. Zorumski, D.F. Covey, and J.H. Steinbach. 2000. Steroid inhibition of rat neuronal nicotinic alpha4beta2 receptors expressed in HEK 293 cells. Mol. Pharmacol. 58:341-351.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 341-351
    • Paradiso, K.1    Sabey, K.2    Evers, A.S.3    Zorumski, C.F.4    Covey, D.F.5    Steinbach., J.H.6
  • 59
    • 0347572922 scopus 로고    scopus 로고
    • Direct evidence for cholesterol crystalline domains in biological membranes: Role in human pathobiology
    • doi:10.1016/S0005-2736(03)00018-X
    • Preston Mason, R., T.N. Tulenko, and R.F. Jacob. 2003. Direct evidence for cholesterol crystalline domains in biological membranes: role in human pathobiology. Biochim. Biophys. Acta. 1610:198-207. doi:10.1016/S0005-2736(03) 00018-X
    • (2003) Biochim. Biophys. Acta. , vol.1610 , pp. 198-207
    • Preston Mason, R.1    Tulenko, T.N.2    Jacob., R.F.3
  • 60
    • 0037340913 scopus 로고    scopus 로고
    • Effects of epicholesterol on the phosphatidylcholine bilayer: A molecular simulation study
    • doi:10.1016/S0006-3495 (03)74989-3
    • Ra, T., and M. Pasenkiewicz-Gierula. 2003. Effects of epicholesterol on the phosphatidylcholine bilayer: a molecular simulation study. Biophys. J. 84:1818-1826. doi:10.1016/S0006-3495 (03)74989-3
    • (2003) Biophys. J. , vol.84 , pp. 1818-1826
    • Ra, T.1    Pasenkiewicz-Gierula, M.2
  • 61
    • 0036924104 scopus 로고    scopus 로고
    • Modulation of endothelial inward-rectifier K+ current by optical isomers of cholesterol
    • doi:10.1016/ S0006-3495(02)75323-X
    • Romanenko, V.G., G.H. Rothblat, and I. Levitan. 2002. Modulation of endothelial inward-rectifier K+ current by optical isomers of cholesterol. Biophys. J. 83:3211-3222. doi:10.1016/ S0006-3495(02)75323-X
    • (2002) Biophys. J. , vol.83 , pp. 3211-3222
    • Romanenko, V.G.1    Rothblat, G.H.2    Levitan., I.3
  • 62
    • 0346462890 scopus 로고    scopus 로고
    • Sensitivity of volume-regulated anion current to cholesterol structural analogues
    • doi:10.1085/jgp.200308882
    • Romanenko, V.G., G.H. Rothblat, and I. Levitan. 2004. Sensitivity of volume-regulated anion current to cholesterol structural analogues. J. Gen. Physiol. 123:77-87. doi:10.1085/jgp.200308882
    • (2004) J. Gen. Physiol. , vol.123 , pp. 77-87
    • Romanenko, V.G.1    Rothblat, G.H.2    Levitan., I.3
  • 63
    • 0001810937 scopus 로고
    • Biological membranes architecture and function
    • R. Lypowsky and E. Sackmann, editors Elsevier, Amsterdam
    • Sackmann, E. 1995. Biological membranes architecture and function. In: Structure and Dynamics of Membranes. R. Lypowsky and E. Sackmann, editors. Elsevier, Amsterdam. 1-63.
    • (1995) Structure and Dynamics of Membranes , pp. 1-63
    • Sackmann, E.1
  • 64
    • 33751180811 scopus 로고    scopus 로고
    • Highconductance potassium channels of the SLO family
    • doi:10.1038/nrn1992
    • Salkoff, L., A. Butler, G. Ferreira, C. Santi, and A. Wei. 2006. Highconductance potassium channels of the SLO family. Nat. Rev. Neurosci. 7:921-931. doi:10.1038/nrn1992
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 921-931
    • Salkoff, L.1    Butler, A.2    Ferreira, G.3    Santi, C.4    Wei., A.5
  • 65
    • 1642402920 scopus 로고    scopus 로고
    • Synthetic copoly(Lys/Phe) and poly(Lys) translocate through lipid bilayer membranes
    • doi:10.1016/j.bbamem.2003.08.003
    • Shibata, A., S. Murata, S. Ueno, S. Liu, S. Futaki, and Y. Baba. 2003. Synthetic copoly(Lys/Phe) and poly(Lys) translocate through lipid bilayer membranes. Biochim. Biophys. Acta. 1616:147-155. doi:10.1016/j.bbamem.2003.08. 003
    • (2003) Biochim. Biophys. Acta. , vol.1616 , pp. 147-155
    • Shibata, A.1    Murata, S.2    Ueno, S.3    Liu, S.4    Futaki, S.5    Baba., Y.6
  • 66
    • 0035218451 scopus 로고    scopus 로고
    • Effects of membrane cholesterol on the sensitivity of the GABA(A) receptor to GABA in acutely dissociated rat hippocampal neurones
    • doi:10.1016/S0028-3908(00)00159-3
    • Sooksawate, T., and M.A. Simmonds. 2001. Effects of membrane cholesterol on the sensitivity of the GABA(A) receptor to GABA in acutely dissociated rat hippocampal neurones. Neuropharmacology. 40:178-184. doi:10.1016/S0028-3908(00) 00159-3
    • (2001) Neuropharmacology. , vol.40 , pp. 178-184
    • Sooksawate, T.1    Simmonds., M.A.2
  • 67
    • 0031899062 scopus 로고    scopus 로고
    • Physical effects of cholesterol on arterial smooth muscle membranes: Evidence of immiscible cholesterol domains and alterations in bilayer width during atherogenesis
    • Tulenko, T.N., M. Chen, P.E. Mason, and R.P. Mason. 1998. Physical effects of cholesterol on arterial smooth muscle membranes: evidence of immiscible cholesterol domains and alterations in bilayer width during atherogenesis. J. Lipid Res. 39:947-956.
    • (1998) J. Lipid Res. , vol.39 , pp. 947-956
    • Tulenko, T.N.1    Chen, M.2    Mason, P.E.3    Mason., R.P.4
  • 68
    • 78650923173 scopus 로고    scopus 로고
    • Cholesterol-ethanol interactions on vascular myocyte BK channels: Contribution to alcohol-induced cerebrovascular constriction
    • doi:10.1016/j.bpj.2008.12.2483
    • Vaithianathan, T., A. Bukiya, J. Liu, and A.M. Dopico. 2009. Cholesterol-ethanol interactions on vascular myocyte BK channels: contribution to alcohol-induced cerebrovascular constriction. Biophys. J. 96:481a-482a. doi:10.1016/j.bpj.2008.12.2483
    • (2009) Biophys. J. , vol.96
    • Vaithianathan, T.1    Bukiya, A.2    Liu, J.3    Dopico., A.M.4
  • 70
    • 14644395532 scopus 로고    scopus 로고
    • The enantiomer of cholesterol
    • doi:10.1007/s00232-004-0714-7
    • Westover, E.J., and D.F. Covey. 2004. The enantiomer of cholesterol. J. Membr. Biol. 202:61-72. doi:10.1007/s00232-004-0714-7
    • (2004) J. Membr. Biol. , vol.202 , pp. 61-72
    • Westover, E.J.1    Covey., D.F.2
  • 71
    • 0030449188 scopus 로고    scopus 로고
    • Enantioselectivity of steroid-induced gamma-aminobutyric acidA receptor modulation and anesthesia
    • Wittmer, L.L., Y. Hu, M. Kalkbrenner, A.S. Evers, C.F. Zorumski, and D.F. Covey. 1996. Enantioselectivity of steroid-induced gamma-aminobutyric acidA receptor modulation and anesthesia. Mol. Pharmacol. 50:1581-1586.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 1581-1586
    • Wittmer, L.L.1    Hu, Y.2    Kalkbrenner, M.3    Evers, A.S.4    Zorumski, C.F.5    Covey., D.F.6
  • 72
    • 0017232478 scopus 로고
    • Structural analysis of hydrated egg lecithin and cholesterol bilayers. II. Neutrol diffraction
    • doi:10.1016/S0022- 2836(76)80068-X
    • Worcester, D.L., and N.P. Franks. 1976. Structural analysis of hydrated egg lecithin and cholesterol bilayers. II. Neutrol diffraction. J. Mol. Biol. 100:359-378. doi:10.1016/S0022- 2836(76)80068-X
    • (1976) J. Mol. Biol. , vol.100 , pp. 359-378
    • Worcester, D.L.1    Franks., N.P.2
  • 73
    • 0034620610 scopus 로고    scopus 로고
    • The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation
    • doi:10.1021/ bi992543v
    • Xu, X., and E. London. 2000. The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation. Biochemistry. 39:843-849. doi:10.1021/ bi992543v
    • (2000) Biochemistry. , vol.39 , pp. 843-849
    • Xu, X.1    London., E.2
  • 74
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle, P.L. 1985. Cholesterol and the cell membrane. Biochim. Biophys. Acta. 822:267-287.
    • (1985) Biochim. Biophys. Acta. , vol.822 , pp. 267-287
    • Yeagle, P.L.1
  • 75
    • 34147179346 scopus 로고    scopus 로고
    • Regulation of the gating of BKCa channel by lipid bilayer thickness
    • doi:10.1074/jbcM607593200
    • Yuan, C., R.J. O'Connell, R.F. Jacob, R.P. Mason, and S.N. Treistman. 2007. Regulation of the gating of BKCa channel by lipid bilayer thickness. J. Biol. Chem. 282:7276-7286. doi:10.1074/jbc .M607593200
    • (2007) J. Biol. Chem. , vol.282 , pp. 7276-7286
    • Yuan, C.1    O'connell, R.J.2    Jacob, R.F.3    Mason, R.P.4    Treistman., S.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.