메뉴 건너뛰기




Volumn 1838, Issue 2, 2014, Pages 521-531

Membrane channels as integrators of G-protein-mediated signaling

Author keywords

G protein signaling; Inward rectifier K+ channels; Membrane channels

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN BETA SUBUNIT; GUANINE NUCLEOTIDE BINDING PROTEIN GAMMA SUBUNIT; INWARDLY RECTIFYING POTASSIUM CHANNEL; PHOSPHATIDYLINOSITIDE; RGS PROTEIN;

EID: 84892163683     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.08.018     Document Type: Review
Times cited : (24)

References (270)
  • 1
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • A.G. Gilman G proteins: transducers of receptor-generated signals Annu. Rev. Biochem. 56 1987 615 649
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 2
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • DOI 10.1146/annurev.biochem.66.1.639
    • S.R. Sprang G protein mechanisms: insights from structural analysis Annu. Rev. Biochem. 66 1997 639 678 (Pubitemid 27274670)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 3
    • 37549016836 scopus 로고    scopus 로고
    • Heterotrimeric G protein activation by G-protein-coupled receptors
    • W.M. Oldham, and H.E. Hamm Heterotrimeric G protein activation by G-protein-coupled receptors Nat. Rev. Mol. Cell Biol. 9 2008 60 71
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 60-71
    • Oldham, W.M.1    Hamm, H.E.2
  • 4
    • 33747754105 scopus 로고    scopus 로고
    • Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse
    • DOI 10.1016/j.ygeno.2006.04.001, PII S0888754306001054
    • T.K. Bjarnadottir, D.E. Gloriam, S.H. Hellstrand, H. Kristiansson, R. Fredriksson, and H.B. Schioth Comprehensive repertoire and phylogenetic analysis of the G protein-coupled receptors in human and mouse Genomics 88 2006 263 273 (Pubitemid 44278529)
    • (2006) Genomics , vol.88 , Issue.3 , pp. 263-273
    • Bjarnadottir, T.K.1    Gloriam, D.E.2    Hellstrand, S.H.3    Kristiansson, H.4    Fredriksson, R.5    Schioth, H.B.6
  • 5
    • 0342433231 scopus 로고
    • 2 dopamine receptors in acutely dissociated neurons from rat corpus striatum
    • 2 dopamine receptors in acutely dissociated neurons from rat corpus striatum Proc. Natl. Acad. Sci. U.S.A. 85 1988 3618 3622
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 3618-3622
    • Freedman, J.E.1    Weight, F.F.2
  • 8
    • 0030032001 scopus 로고    scopus 로고
    • EGL-10 regulates G protein signaling in the C. Elegans nervous system and shares a conserved domain with many mammalian proteins
    • DOI 10.1016/S0092-8674(00)80998-8
    • M.R. Koelle, and H.R. Horvitz EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins Cell 84 1996 115 125 (Pubitemid 26031466)
    • (1996) Cell , vol.84 , Issue.1 , pp. 115-125
    • Koelle, M.R.1    Horvitz, H.R.2
  • 9
    • 0036733358 scopus 로고    scopus 로고
    • Cellular regulation of RGS proteins: Modulators and integrators of G protein signaling
    • S. Hollinger, and J.R. Hepler Cellular regulation of RGS proteins: modulators and integrators of G protein signaling Pharmacol. Rev. 54 2002 527 559
    • (2002) Pharmacol. Rev. , vol.54 , pp. 527-559
    • Hollinger, S.1    Hepler, J.R.2
  • 10
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins
    • E.M. Ross, and T.M. Wilkie GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins Annu. Rev. Biochem. 69 2000 795 827
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2
  • 11
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPase-activating proteins for the G(i) subfamily of G protein α subunits
    • DOI 10.1016/S0092-8674(00)80117-8
    • i subfamily of G protein α subunits Cell 86 1996 445 452 (Pubitemid 26272084)
    • (1996) Cell , vol.86 , Issue.3 , pp. 445-452
    • Berman, D.M.1    Wilkie, T.M.2    Gilman, A.G.3
  • 12
    • 79960671811 scopus 로고    scopus 로고
    • Regulators of G-protein signaling and their Gα substrates: Promises and challenges in their use as drug discovery targets
    • A.J. Kimple, D.E. Bosch, P.M. Giguére, and D.P. Siderovski Regulators of G-protein signaling and their Gα substrates: promises and challenges in their use as drug discovery targets Pharmacol. Rev. 63 2011 728 749
    • (2011) Pharmacol. Rev. , vol.63 , pp. 728-749
    • Kimple, A.J.1    Bosch, D.E.2    Giguére, P.M.3    Siderovski, D.P.4
  • 13
    • 14844343100 scopus 로고    scopus 로고
    • Multi-tasking RGS proteins in the heart: The next therapeutic target?
    • DOI 10.1161/01.RES.0000158287.49872.4e
    • E.L. Riddle, R.A. Schwartzman, M. Bond, and P.A. Insel Multi-tasking RGS proteins in the heart: the next therapeutic target? Circ. Res. 96 2005 401 411 (Pubitemid 40354533)
    • (2005) Circulation Research , vol.96 , Issue.4 , pp. 401-411
    • Riddle, E.L.1    Schwartzman, R.A.2    Bond, M.3    Insel, P.A.4
  • 14
    • 0038143228 scopus 로고    scopus 로고
    • Palmitoylation regulates regulators of G-protein signaling (RGS) 16 function: I. Mutation of amino-terminal cysteine residues on RGS16 prevents its targeting to lipid rafts and palmitoylation of an internal cysteine residue
    • DOI 10.1074/jbc.M210123200
    • A. Hiol, P.C. Davey, J.L. Osterhout, A.A. Waheed, E.R. Fischer, C.K. Chen, G. Milligan, K.M. Druey, and T.L. Jones Palmitoylation regulates regulators of G-protein signaling (RGS) 16 function. I. Mutation of amino-terminal cysteine residues on RGS16 prevents its targeting to lipid rafts and palmitoylation of an internal cysteine residue J. Biol. Chem. 278 2003 19301 19308 (Pubitemid 36799323)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.21 , pp. 19301-19308
    • Hiol, A.1    Davey, P.C.2    Osterhout, J.L.3    Waheed, A.A.4    Fischer, E.R.5    Chen, C.-K.6    Milligan, G.7    Druey, K.M.8    Jones, T.L.Z.9
  • 17
    • 0033621480 scopus 로고    scopus 로고
    • Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10
    • DOI 10.1074/jbc.274.53.38260
    • Y. Tu, S. Popov, C. Slaughter, and E.M. Ross Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10 J. Biol. Chem. 274 1999 38260 38267 (Pubitemid 30026902)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.53 , pp. 38260-38267
    • Tu, Y.1    Popov, S.2    Slaughter, C.3    Ross, E.M.4
  • 18
    • 0035827527 scopus 로고    scopus 로고
    • Binding of regulator of G protein signaling (RGS) proteins to phospholipid bilayers. Contribution of location and/or orientation to Gtpase-activating protein activity
    • Y. Tu, J. Woodson, and E.M. Ross Binding of regulator of G protein signaling (RGS) proteins to phospholipid bilayers. Contribution of location and/or orientation to Gtpase-activating protein activity J. Biol. Chem. 276 2001 20160 20166
    • (2001) J. Biol. Chem. , vol.276 , pp. 20160-20166
    • Tu, Y.1    Woodson, J.2    Ross, E.M.3
  • 20
    • 0027509511 scopus 로고
    • Cardiac pacemaking in the sinoatrial node
    • H. Irisawa, H.F. Brown, and W. Giles Cardiac pacemaking in the sinoatrial node Physiol. Rev. 73 1993 197 227 (Pubitemid 23065438)
    • (1993) Physiological Reviews , vol.73 , Issue.1 , pp. 197-227
    • Irisawa, H.1    Brown, H.F.2    Giles, W.3
  • 21
    • 0019497754 scopus 로고
    • The time course of the muscarinic response to ionophoretic acetylcholine application to the S-A node of the rabbit heart
    • DOI 10.1007/BF00584791
    • W. Osterrieder, Q.F. Yang, and W. Trautwein The time course of the muscarinic response to ionophoretic acetylcholine application to the S-A node of the rabbit heart Pflugers Arch. 389 1981 283 291 (Pubitemid 11150180)
    • (1981) Pflugers Archiv European Journal of Physiology , vol.389 , Issue.3 , pp. 283-291
    • Osterrieder, W.1    Yang, Q.F.2    Trautwein, W.3
  • 22
    • 0027198392 scopus 로고
    • Differential phosphorylation of two size forms of the neuronal class C L- type calcium channel α1 subunit
    • J.W. Hell, C.T. Yokoyama, S.T. Wong, C. Warner, T.P. Snutch, and W.A. Catterall Differential phosphorylation of two size forms of the neuronal class C l-type calcium channel alpha 1 subunit J. Biol. Chem. 268 1993 19451 19457 (Pubitemid 23270725)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.26 , pp. 19451-19457
    • Hell, J.W.1    Yokoyama, C.T.2    Wong, S.T.3    Warner, C.4    Snutch, T.P.5    Catterall, W.A.6
  • 23
    • 0017358578 scopus 로고
    • A study of the ion selectivity and the kinetic properties of the calcium dependent slow inward current in mammalian cardiac muscle
    • H. Reuter, and H. Scholz A study of the ion selectivity and the kinetic properties of the calcium dependent slow inward current in mammalian cardiac muscle J. Physiol. 264 1977 17 47 (Pubitemid 8029819)
    • (1977) Journal of Physiology , vol.264 , Issue.1 , pp. 17-47
    • Reuter, H.1    Scholz, H.2
  • 24
    • 0017143158 scopus 로고
    • A metabolic control mechanism for calcium ion influx that may protect the ventricular myocardial cell
    • N. Sperelakis, and J.A. Schneider A metabolic control mechanism for calcium ion influx that may protect the ventricular myocardial cell Am. J. Cardiol. 37 1976 1079 1085
    • (1976) Am. J. Cardiol. , vol.37 , pp. 1079-1085
    • Sperelakis, N.1    Schneider, J.A.2
  • 25
    • 0034623827 scopus 로고    scopus 로고
    • Regulation of cardiac l-type calcium channels by protein kinase A and protein kinase C
    • T.J. Kamp, and J.W. Hell Regulation of cardiac l-type calcium channels by protein kinase A and protein kinase C Circ. Res. 87 2000 1095 1102
    • (2000) Circ. Res. , vol.87 , pp. 1095-1102
    • Kamp, T.J.1    Hell, J.W.2
  • 26
    • 0028297589 scopus 로고
    • Regulation and modulation of calcium channels in cardiac, skeletal, and smooth muscle cells
    • T.F. McDonald, S. Pelzer, W. Trautwein, and D.J. Pelzer Regulation and modulation of calcium channels in cardiac, skeletal, and smooth muscle cells Physiol. Rev. 74 1994 365 507 (Pubitemid 24127646)
    • (1994) Physiological Reviews , vol.74 , Issue.2 , pp. 365-507
    • Mcdonald, T.F.1    Pelzer, S.2    Trautwein, W.3    Pelzer, D.J.4
  • 27
    • 0025963987 scopus 로고
    • Isoproterenol antagonizes prolongation of refractory period by the class III antiarrhythmic agent E-4031 in guinea pig myocytes. Mechanism of action
    • M.C. Sanguinetti, N.K. Jurkiewicz, A. Scott, and P.K. Siegl Isoproterenol antagonizes prolongation of refractory period by the class III antiarrhythmic agent E-4031 in guinea pig myocytes. Mechanism of action Circ. Res. 68 1991 77 84
    • (1991) Circ. Res. , vol.68 , pp. 77-84
    • Sanguinetti, M.C.1    Jurkiewicz, N.K.2    Scott, A.3    Siegl, P.K.4
  • 28
    • 0037127028 scopus 로고    scopus 로고
    • Requirement of a macromolecular signaling complex for β adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel
    • DOI 10.1126/science.1066843
    • S.O. Marx, J. Kurokawa, S. Reiken, H. Motoike, J. D'Armiento, A.R. Marks, and R.S. Kass Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel Science 295 2002 496 499 (Pubitemid 34101639)
    • (2002) Science , vol.295 , Issue.5554 , pp. 496-499
    • Marx, S.O.1    Kurokawa, J.2    Reiken, S.3    Motoike, H.4    D'Armiento, J.5    Marks, A.R.6    Kass, R.S.7
  • 29
    • 0024280882 scopus 로고
    • Regulation of a heart potassium channel by protein kinase A and C
    • K.B. Walsh, and R.S. Kass Regulation of a heart potassium channel by protein kinase A and C Science 242 1988 67 69
    • (1988) Science , vol.242 , pp. 67-69
    • Walsh, K.B.1    Kass, R.S.2
  • 30
    • 0021677187 scopus 로고
    • Inactivation of calcium channel current in the calf cardiac Purkinje fiber. Evidence for voltage- and calcium-mediated mechanisms
    • DOI 10.1085/jgp.84.5.705
    • R.S. Kass, and M.C. Sanguinetti Inactivation of calcium channel current in the calf cardiac Purkinje fiber. Evidence for voltage- and calcium-mediated mechanisms J. Gen. Physiol. 84 1984 705 726 (Pubitemid 15208316)
    • (1984) Journal of General Physiology , vol.84 , Issue.5 , pp. 705-726
    • Kass, R.S.1    Sanguinetti, M.C.2
  • 31
    • 0021891161 scopus 로고
    • Inactivation of calcium channels in mammalian heart cells: Joint dependence on membrane potential and intracellular calcium
    • K.S. Lee, E. Marban, and R.W. Tsien Inactivation of calcium channels in mammalian heart cells: joint dependence on membrane potential and intracellular calcium J. Physiol. 364 1985 395 411 (Pubitemid 15067221)
    • (1985) Journal of Physiology , vol.VOL. 364 , pp. 395-411
    • Lee, K.S.1    Marban, E.2    Tsien, R.W.3
  • 33
  • 34
    • 45549093780 scopus 로고    scopus 로고
    • Kv7 channels: Interaction with dopaminergic and serotonergic neurotransmission in the CNS
    • DOI 10.1113/jphysiol.2007.149450
    • H.H. Hansen, O. Waroux, V. Seutin, T.J. Jentsch, S. Aznar, and J.D. Mikkelsen Kv7 channels: interaction with dopaminergic and serotonergic neurotransmission in the CNS J. Physiol. 586 2008 1823 1832 (Pubitemid 351997511)
    • (2008) Journal of Physiology , vol.586 , Issue.7 , pp. 1823-1832
    • Hansen, H.H.1    Waroux, O.2    Seutin, V.3    Jentsch, T.J.4    Aznar, S.5    Mikkelsen, J.D.6
  • 35
    • 84873410833 scopus 로고    scopus 로고
    • 1 corticospinal mirror neurons and their role in movement suppression during action observation
    • 1 corticospinal mirror neurons and their role in movement suppression during action observation Curr. Biol. 23 2013 236 243
    • (2013) Curr. Biol. , vol.23 , pp. 236-243
    • Vigneswaran, G.1    Philipp, R.2    Lemon, R.N.3    Kraskov, A.4
  • 36
    • 0018886033 scopus 로고
    • + current in a vertebrate neurone
    • + current in a vertebrate neurone Nature 283 1980 673 676 (Pubitemid 10099998)
    • (1980) Nature , vol.283 , Issue.5748 , pp. 673-676
    • Brown, D.A.1    Adams, P.R.2
  • 38
    • 0034303612 scopus 로고    scopus 로고
    • Neuronal KCNQ potassium channels: Physiology and role in disease
    • T.J. Jentsch Neuronal KCNQ potassium channels: physiology and role in disease Nat. Rev. Neurosci. 1 2000 21 30
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 21-30
    • Jentsch, T.J.1
  • 39
    • 0034929557 scopus 로고    scopus 로고
    • KCNQ potassium channels: Physiology, pathophysiology, and pharmacology
    • DOI 10.1016/S0163-7258(01)00116-4, PII S0163725801001164
    • J. Robbins KCNQ potassium channels: physiology, pathophysiology, and pharmacology Pharmacol. Ther. 90 2001 1 19 (Pubitemid 32622837)
    • (2001) Pharmacology and Therapeutics , vol.90 , Issue.1 , pp. 1-19
    • Robbins, J.1
  • 40
    • 0029831984 scopus 로고    scopus 로고
    • 2
    • 2 + exchange and KATP potassium channels by PIP2 Science 273 1996 956 959 (Pubitemid 26275172)
    • (1996) Science , vol.273 , Issue.5277 , pp. 956-959
    • Hilgemann, D.W.1    Ball, R.2
  • 41
    • 0032491439 scopus 로고    scopus 로고
    • Membrane phospholipid control of nucleotide sensitivity of K(ATP) channels
    • ATP channels Science 282 1998 1138 1141 (Pubitemid 28516245)
    • (1998) Science , vol.282 , Issue.5391 , pp. 1138-1141
    • Shyng, S.-L.1    Nichols, C.G.2
  • 44
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • DOI 10.1038/nature02196
    • D.E. Clapham TRP channels as cellular sensors Nature 426 2003 517 524 (Pubitemid 37522633)
    • (2003) Nature , vol.426 , Issue.6966 , pp. 517-524
    • Clapham, D.E.1
  • 45
    • 0037040395 scopus 로고    scopus 로고
    • The TRP channels, a remarkably functional family
    • DOI 10.1016/S0092-8674(02)00670-0
    • C. Montell, L. Birnbaumer, and V. Flockerzi The TRP channels, a remarkably functional family Cell 108 2002 595 598 (Pubitemid 34241421)
    • (2002) Cell , vol.108 , Issue.5 , pp. 595-598
    • Montell, C.1    Birnbaumer, L.2    Flockerzi, V.3
  • 46
    • 84866483657 scopus 로고    scopus 로고
    • TRP channels: Sensors and transducers of gasotransmitter signals
    • N. Takahashi, D. Kozai, and Y. Mori TRP channels: sensors and transducers of gasotransmitter signals Front. Physiol. 3 2012 324
    • (2012) Front. Physiol. , vol.3 , pp. 324
    • Takahashi, N.1    Kozai, D.2    Mori, Y.3
  • 51
    • 0024457676 scopus 로고
    • The mechanism of protein kinase C activation
    • K.P. Huang The mechanism of protein kinase C activation Trends Neurosci. 12 1989 425 432
    • (1989) Trends Neurosci. , vol.12 , pp. 425-432
    • Huang, K.P.1
  • 52
    • 0021269612 scopus 로고
    • Calcium-activated potassium channels and their role in secretion
    • O.H. Petersen, and Y. Maruyama Calcium-activated potassium channels and their role in secretion Nature 307 1984 693 696 (Pubitemid 14133937)
    • (1984) Nature , vol.307 , Issue.5953 , pp. 693-696
    • Petersen, O.H.1    Maruyama, Y.2
  • 55
    • 83455199984 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. LXXXV: Calcium-activated chloride channels
    • F. Huang, X. Wong, and L.Y. Jan International Union of Basic and Clinical Pharmacology. LXXXV: calcium-activated chloride channels Pharmacol. Rev. 64 2012 1 15
    • (2012) Pharmacol. Rev. , vol.64 , pp. 1-15
    • Huang, F.1    Wong, X.2    Jan, L.Y.3
  • 57
    • 0842344647 scopus 로고    scopus 로고
    • 2+ channels: One switch
    • DOI 10.1113/jphysiol.2003.047902
    • 2 + channels: one switch J. Physiol. 554 2004 275 283 (Pubitemid 38181342)
    • (2004) Journal of Physiology , vol.554 , Issue.2 , pp. 275-283
    • Findlay, I.1
  • 58
    • 33751314569 scopus 로고    scopus 로고
    • Angiotensin II activates two cation conductances with distinct TRPC1 and TRPC6 channel properties in rabbit mesenteric artery myocytes
    • DOI 10.1113/jphysiol.2006.119305
    • S.N. Saleh, A.P. Albert, C.M. Peppiatt, and W.A. Large Angiotensin II activates two cation conductances with distinct TRPC1 and TRPC6 channel properties in rabbit mesenteric artery myocytes J. Physiol. 577 2006 479 495 (Pubitemid 44804007)
    • (2006) Journal of Physiology , vol.577 , Issue.2 , pp. 479-495
    • Saleh, S.N.1    Albert, A.P.2    Peppiatt, C.M.3    Large, W.A.4
  • 59
    • 0025359287 scopus 로고
    • Acetylcholine activates nonselective cation channels in guinea pig ileum through a G protein
    • R. Inoue, and G. Isenberg Acetylcholine activates nonselective cation channels in guinea pig ileum through a G protein Am. J. Physiol. 258 1990 C1173 C1178
    • (1990) Am. J. Physiol. , vol.258
    • Inoue, R.1    Isenberg, G.2
  • 60
    • 2342467414 scopus 로고    scopus 로고
    • G-protein-gated TRP-like cationic channel activated by muscarinic receptors: Effect of potential on single-channel gating
    • DOI 10.1085/jgp.200309002
    • A.V. Zholos, A.A. Zholos, and T.B. Bolton G-protein-gated TRP-like cationic channel activated by muscarinic receptors: effect of potential on single-channel gating J. Gen. Physiol. 123 2004 581 598 (Pubitemid 38590860)
    • (2004) Journal of General Physiology , vol.123 , Issue.5 , pp. 581-598
    • Zholos, A.V.1    Zholos, A.A.2    Bolton, T.B.3
  • 66
    • 37149016771 scopus 로고    scopus 로고
    • Vasopressin: Behavioral roles of an "original" neuropeptide
    • DOI 10.1016/j.pneurobio.2007.10.007, PII S030100820700192X
    • H.K. Caldwell, H.J. Lee, A.H. Macbeth, and W.S. Young III Vasopressin: behavioral roles of an "original" neuropeptide Prog. Neurobiol. 84 2008 1 24 (Pubitemid 350256874)
    • (2008) Progress in Neurobiology , vol.84 , Issue.1 , pp. 1-24
    • Caldwell, H.K.1    Lee, H.-J.2    Macbeth, A.H.3    Young III, W.S.4
  • 67
    • 0031726939 scopus 로고    scopus 로고
    • Aquaporins (water channels): Role in vasopressin-activated water transport
    • A.I. Dibas, A.J. Mia, and T. Yorio Aquaporins (water channels): role in vasopressin-activated water transport Proc. Soc. Exp. Biol. Med. 219 1998 183 199
    • (1998) Proc. Soc. Exp. Biol. Med. , vol.219 , pp. 183-199
    • Dibas, A.I.1    Mia, A.J.2    Yorio, T.3
  • 68
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • DOI 10.1038/nrm1527
    • W. Wong, and J.D. Scott AKAP signalling complexes: focal points in space and time Nat. Rev. Mol. Cell Biol. 5 2004 959 970 (Pubitemid 39611533)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.12 , pp. 959-970
    • Wong, W.1    Scott, J.D.2
  • 70
    • 0032520827 scopus 로고    scopus 로고
    • Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1
    • J.W. Lin, M. Wyszynski, R. Madhavan, R. Sealock, J.U. Kim, and M. Sheng Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1 J. Neurosci. 18 1998 2017 2027 (Pubitemid 28141409)
    • (1998) Journal of Neuroscience , vol.18 , Issue.6 , pp. 2017-2027
    • Lin, J.W.1    Wyszynski, M.2    Madhavan, R.3    Sealock, R.4    Kim, J.U.5    Sheng, M.6
  • 74
    • 3042543544 scopus 로고    scopus 로고
    • 2+-dependent BK channel signaling complex by binding to β2 adrenergic receptor
    • DOI 10.1038/sj.emboj.7600228
    • 2 +-dependent BK channel signaling complex by binding to β2 adrenergic receptor EMBO J. 23 2004 2196 2205 (Pubitemid 38833229)
    • (2004) EMBO Journal , vol.23 , Issue.11 , pp. 2196-2205
    • Liu, G.1    Shi, J.2    Yang, L.3    Cao, L.4    Park, S.M.5    Cui, J.6    Marx, S.O.7
  • 75
    • 0022924198 scopus 로고
    • Noradrenaline modulates calcium channels in avian dorsal root ganglion cells through tight receptor-channel coupling
    • P. Forscher, G.S. Oxford, and D. Schulz Noradrenaline modulates calcium channels in avian dorsal root ganglion cells through tight receptor-channel coupling J. Physiol. 379 1986 131 144 (Pubitemid 17175910)
    • (1986) Journal of Physiology , vol.379 , pp. 131-144
    • Forscher, P.1    Oxford, G.S.2    Schulz, D.3
  • 76
    • 0024354817 scopus 로고
    • Neurotransmitter inhibition of neuronal calcium currents by changes in channel voltage dependence
    • DOI 10.1038/340153a0
    • B.P. Bean Neurotransmitter inhibition of neuronal calcium currents by changes in channel voltage dependence Nature 340 1989 153 156 (Pubitemid 19175368)
    • (1989) Nature , vol.340 , Issue.6229 , pp. 153-156
    • Bean, B.P.1
  • 77
    • 0027008759 scopus 로고
    • 2+ channels in rat sympathetic neurones is mediated by guanine nucleotide binding proteins
    • 2 + channels in rat sympathetic neurones is mediated by guanine nucleotide binding proteins J. Physiol. 458 1992 339 359 (Pubitemid 23024597)
    • (1992) Journal of Physiology , vol.458 , pp. 339-359
    • Ikeda, S.R.1
  • 78
    • 0026803223 scopus 로고
    • G protein-coupled mechanisms and nervous signaling
    • B. Hille G protein-coupled mechanisms and nervous signaling Neuron 9 1992 187 195
    • (1992) Neuron , vol.9 , pp. 187-195
    • Hille, B.1
  • 79
    • 0029201897 scopus 로고
    • Voltage-dependent calcium channels and their modulation by neurotransmitters and G proteins
    • A.C. Dolphin Voltage-dependent calcium channels and their modulation by neurotransmitters and G proteins Exp. Physiol. 80 1995 1 36
    • (1995) Exp. Physiol. , vol.80 , pp. 1-36
    • Dolphin, A.C.1
  • 80
    • 0028258190 scopus 로고
    • 2 + channels in supporting hippocampal synaptic transmission
    • 2 + channels in supporting hippocampal synaptic transmission Science 264 1994 107 111
    • (1994) Science , vol.264 , pp. 107-111
    • Wheeler, D.B.1    Randall, A.2    Tsien, R.W.3
  • 82
    • 0029921401 scopus 로고    scopus 로고
    • Voltage-dependent modulation of N-type calcium channels by G-protein beta gamma subunits
    • S.R. Ikeda Voltage-dependent modulation of N-type calcium channels by G-protein beta gamma subunits Nature 380 1996 255 258
    • (1996) Nature , vol.380 , pp. 255-258
    • Ikeda, S.R.1
  • 83
    • 0034306154 scopus 로고    scopus 로고
    • G protein modulation of recombinant P/Q-type calcium channels by regulators of G protein signalling proteins
    • M.D. Mark, S. Wittemann, and S. Herlitze G protein modulation of recombinant P/Q-type calcium channels by regulators of G protein signalling proteins J. Physiol. 528 Pt 1 2000 65 77
    • (2000) J. Physiol. , vol.528 , Issue.PART 1 , pp. 65-77
    • Mark, M.D.1    Wittemann, S.2    Herlitze, S.3
  • 84
    • 0024381039 scopus 로고
    • Modulation of Ca-channel current by an adenosine analog mediated by a GTP-binding protein in chick sensory neurons
    • DOI 10.1007/BF00580956
    • H. Kasai, and T. Aosaki Modulation of Ca-channel current by an adenosine analog mediated by a GTP-binding protein in chick sensory neurons Pflugers Arch. 414 1989 145 149 (Pubitemid 19154694)
    • (1989) Pflugers Archiv European Journal of Physiology , vol.414 , Issue.2 , pp. 145-149
    • Kasai, H.1    Aosaki, T.2
  • 85
    • 0024375987 scopus 로고
    • α-Adrenergic inhibition of sympathetic neurotransmitter release mediated by modulation of N-type calcium-channel gating
    • DOI 10.1038/340639a0
    • D. Lipscombe, S. Kongsamut, and R.W. Tsien Alpha-adrenergic inhibition of sympathetic neurotransmitter release mediated by modulation of N-type calcium-channel gating Nature 340 1989 639 642 (Pubitemid 19202573)
    • (1989) Nature , vol.340 , Issue.6235 , pp. 639-642
    • Lipscombe, D.1    Kongsamut, S.2    Tsien, R.W.3
  • 86
    • 0033566706 scopus 로고    scopus 로고
    • Identification of residues in the N terminus of α1B critical for inhibition of the voltage-dependent calcium channel by Gβγ
    • 1B critical for inhibition of the voltage-dependent calcium channel by Gβγ J. Neurosci. 19 1999 6855 6864 (Pubitemid 29380114)
    • (1999) Journal of Neuroscience , vol.19 , Issue.16 , pp. 6855-6864
    • Canti, C.1    Page, K.M.2    Stephens, G.J.3    Dolphin, A.C.4
  • 88
    • 0032525072 scopus 로고    scopus 로고
    • Structural features determining differential receptor regulation of neuronal Ca channels
    • A.A. Simen, and R.J. Miller Structural features determining differential receptor regulation of neuronal Ca channels J. Neurosci. 18 1998 3689 3698 (Pubitemid 28225676)
    • (1998) Journal of Neuroscience , vol.18 , Issue.10 , pp. 3689-3698
    • Simen, A.A.1    Miller, R.J.2
  • 90
    • 0031033757 scopus 로고    scopus 로고
    • Direct binding of G-protein βγ complex to voltage-dependent calcium channels
    • DOI 10.1038/385446a0
    • M. De Waard, H. Liu, D. Walker, V.E. Scott, C.A. Gurnett, and K.P. Campbell Direct binding of G-protein betagamma complex to voltage-dependent calcium channels Nature 385 1997 446 450 (Pubitemid 27065931)
    • (1997) Nature , vol.385 , Issue.6615 , pp. 446-450
    • De Waard, M.1    Liu, H.2    Walker, D.3    Scott, V.E.S.4    Gurnett, C.A.5    Campbell, K.P.6
  • 91
    • 0031022543 scopus 로고    scopus 로고
    • 1 subunit
    • DOI 10.1038/385442a0
    • G.W. Zamponi, E. Bourinet, D. Nelson, J. Nargeot, and T.P. Snutch Crosstalk between G proteins and protein kinase C mediated by the calcium channel α1 subunit Nature 385 1997 442 446 (Pubitemid 27065930)
    • (1997) Nature , vol.385 , Issue.6615 , pp. 442-446
    • Zamponi, G.W.1    Bourinet, E.2    Nelson, D.3    Nargeot, J.4    Snutch, T.P.5
  • 92
    • 0034688225 scopus 로고    scopus 로고
    • Direct protein-protein coupling enables cross-talk between dopamine D5 and γ-aminobutyric acid A receptors
    • DOI 10.1038/35002014
    • F. Liu, Q. Wan, Z.B. Pristupa, X.M. Yu, Y.T. Wang, and H.B. Niznik Direct protein-protein coupling enables cross-talk between dopamine D5 and γ-aminobutyric acid A receptors Nature 403 2000 274 280 (Pubitemid 30062376)
    • (2000) Nature , vol.403 , Issue.6767 , pp. 274-280
    • Liu, F.1    Wan, Q.2    Pristupa, Z.B.3    Yu, X.-M.4    Wang, Y.T.5    Niznik, H.B.6
  • 97
    • 0034666058 scopus 로고    scopus 로고
    • Interaction between G proteins and accessory subunits in the regulation of 1B calcium channels in Xenopus oocytes
    • C. Canti, Y. Bogdanov, and A.C. Dolphin Interaction between G proteins and accessory subunits in the regulation of 1B calcium channels in Xenopus oocytes J. Physiol. 527 Pt 3 2000 419 432
    • (2000) J. Physiol. , vol.527 , Issue.PART 3 , pp. 419-432
    • Canti, C.1    Bogdanov, Y.2    Dolphin, A.C.3
  • 98
    • 0035977069 scopus 로고    scopus 로고
    • Calcium channel β subunits differentially regulate the inhibition of N-type channels by individual Gβ isoforms
    • Z.P. Feng, M.I. Arnot, C.J. Doering, and G.W. Zamponi Calcium channel β subunits differentially regulate the inhibition of N-type channels by individual Gβ isoforms J. Biol. Chem. 276 2001 45051 45058
    • (2001) J. Biol. Chem. , vol.276 , pp. 45051-45058
    • Feng, Z.P.1    Arnot, M.I.2    Doering, C.J.3    Zamponi, G.W.4
  • 107
    • 84861848301 scopus 로고    scopus 로고
    • G-protein-mediated inhibition of the Trp channel TRPM1 requires the Gβγ dimer
    • Y. Shen, M.A. Rampino, R.C. Carroll, and S. Nawy G-protein-mediated inhibition of the Trp channel TRPM1 requires the Gβγ dimer Proc. Natl. Acad. Sci. U.S.A. 109 2012 8752 8757
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 8752-8757
    • Shen, Y.1    Rampino, M.A.2    Carroll, R.C.3    Nawy, S.4
  • 111
    • 22944473967 scopus 로고    scopus 로고
    • Physiology and pharmacology of two-pore domain potassium channels
    • DOI 10.2174/1381612054546824
    • D. Kim Physiology and pharmacology of two-pore domain potassium channels Curr. Pharm. Des. 11 2005 2717 2736 (Pubitemid 41051880)
    • (2005) Current Pharmaceutical Design , vol.11 , Issue.21 , pp. 2717-2736
    • Kim, D.1
  • 112
    • 0033679959 scopus 로고    scopus 로고
    • Molecular and functional properties of two-pore-domain potassium channels
    • F. Lesage, and M. Lazdunski Molecular and functional properties of two-pore-domain potassium channels Am. J. Physiol. Renal Physiol. 279 2000 F793 F801
    • (2000) Am. J. Physiol. Renal Physiol. , vol.279
    • Lesage, F.1    Lazdunski, M.2
  • 113
    • 34548363326 scopus 로고    scopus 로고
    • Biophysical, pharmacological, and functional characteristics of cloned and native mammalian two-pore domain K+ channels
    • DOI 10.1007/s12013-007-0007-8
    • + channels Cell Biochem. Biophys. 47 2007 209 256 (Pubitemid 47338363)
    • (2007) Cell Biochemistry and Biophysics , vol.47 , Issue.2 , pp. 209-256
    • Lotshaw, D.P.1
  • 117
    • 10444252700 scopus 로고
    • Über humorale Übertragbarkeit der Herznervenwirkung
    • O. Loewi Über humorale Übertragbarkeit der Herznervenwirkung Pflugers Arch. 189 1921 239 242
    • (1921) Pflugers Arch. , vol.189 , pp. 239-242
    • Loewi, O.1
  • 118
    • 9644295236 scopus 로고
    • Über humorale Übertragbarkeit der Herznervenwirkung. VI. der Angriffspunkt des Atropins
    • O. Loewi, and E. Navratil Über humorale Übertragbarkeit der Herznervenwirkung. VI. Der Angriffspunkt des Atropins Pflugers Arch. 214 1926 678 688
    • (1926) Pflugers Arch. , vol.214 , pp. 678-688
    • Loewi, O.1    Navratil, E.2
  • 119
    • 0001097450 scopus 로고
    • Production of membrane potential changes in the frog's heart by inhibitory nerve impulses
    • J. Del Castillo, and B. Katz Production of membrane potential changes in the frog's heart by inhibitory nerve impulses Nature 175 1955 1035
    • (1955) Nature , vol.175 , pp. 1035
    • Del Castillo, J.1    Katz, B.2
  • 120
    • 0000732951 scopus 로고
    • Vagal and sympathetic effects on the pacemaker fibers in the sinus venosus of the heart
    • O.F. Hutter, and W. Trautwein Vagal and sympathetic effects on the pacemaker fibers in the sinus venosus of the heart J. Gen. Physiol. 39 1956 715 733
    • (1956) J. Gen. Physiol. , vol.39 , pp. 715-733
    • Hutter, O.F.1    Trautwein, W.2
  • 121
    • 0000241873 scopus 로고
    • Mechanism of membrane effect of acetylcholine on myocardial fibers
    • W. Trautwein, and J. Dudel Mechanism of membrane effect of acetylcholine on myocardial fibers Pflugers Arch. 266 1958 324 334
    • (1958) Pflugers Arch. , vol.266 , pp. 324-334
    • Trautwein, W.1    Dudel, J.2
  • 122
    • 0018075372 scopus 로고
    • Relaxation of the ACh-induced potassium current in the rabbit sinoatrial node cell
    • A. Noma, and W. Trautwein Relaxation of the ACh-induced potassium current in the rabbit sinoatrial node cell Pflugers Arch. 377 1978 193 200 (Pubitemid 9041066)
    • (1978) Pflugers Archiv European Journal of Physiology , vol.377 , Issue.3 , pp. 193-200
    • Noma, A.1    Trautwein, W.2
  • 123
    • 0022350208 scopus 로고
    • Uncoupling of cardiac muscarinic and β-adrenergic receptors from ion channels by a guanine nucleotide analogue
    • DOI 10.1038/317538a0
    • G.E. Breitwieser, and G. Szabo Uncoupling of cardiac muscarinic and β-adrenergic receptors from ion channels by a guanine nucleotide analogue Nature 317 1985 538 540 (Pubitemid 16224161)
    • (1985) Nature , vol.317 , Issue.6037 , pp. 538-540
    • Breitwieser, G.E.1    Szabo, G.2
  • 124
    • 0022365717 scopus 로고
    • GTP-binding proteins couple cardiac muscarinic receptors to a K channel
    • DOI 10.1038/317536a0
    • P.J. Pfaffinger, J.M. Martin, D.D. Hunter, N.M. Nathanson, and B. Hille GTP-binding proteins couple cardiac muscarinic receptors to a K channel Nature 317 1985 536 538 (Pubitemid 16224160)
    • (1985) Nature , vol.317 , Issue.6037 , pp. 536-538
    • Pfaffinger, P.J.1    Martin, J.M.2    Hunter, D.D.3
  • 127
    • 74949143771 scopus 로고    scopus 로고
    • Inwardly rectifying potassium channels: Their structure, function, and physiological roles
    • H. Hibino, A. Inanobe, K. Furutani, S. Murakami, I. Findlay, and Y. Kurachi Inwardly rectifying potassium channels: their structure, function, and physiological roles Physiol. Rev. 90 2010 291 366
    • (2010) Physiol. Rev. , vol.90 , pp. 291-366
    • Hibino, H.1    Inanobe, A.2    Furutani, K.3    Murakami, S.4    Findlay, I.5    Kurachi, Y.6
  • 128
    • 77951498231 scopus 로고    scopus 로고
    • Emerging roles for G protein-gated inwardly rectifying potassium (GIRK) channels in health and disease
    • C. Lüscher, and P.A. Slesinger Emerging roles for G protein-gated inwardly rectifying potassium (GIRK) channels in health and disease Nat. Rev. Neurosci. 11 2010 301 315
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 301-315
    • Lüscher, C.1    Slesinger, P.A.2
  • 129
    • 0032415101 scopus 로고    scopus 로고
    • G protein regulation of potassium ion channels
    • M. Yamada, A. Inanobe, and Y. Kurachi G protein regulation of potassium ion channels Pharmacol. Rev. 50 1998 723 760
    • (1998) Pharmacol. Rev. , vol.50 , pp. 723-760
    • Yamada, M.1    Inanobe, A.2    Kurachi, Y.3
  • 132
    • 3042695848 scopus 로고    scopus 로고
    • A family of putative Kir potassium channels in prokaryotes
    • S.R. Durell, and H.R. Guy A family of putative Kir potassium channels in prokaryotes BMC Evol. Biol. 1 2001 14
    • (2001) BMC Evol. Biol. , vol.1 , pp. 14
    • Durell, S.R.1    Guy, H.R.2
  • 133
    • 0029563444 scopus 로고
    • Immunological and physical characterization of the brain G protein-gated muscarinic potassium channel
    • DOI 10.1006/bbrc.1995.2901
    • A. Inanobe, H. Ito, M. Ito, Y. Hosoya, and Y. Kurachi Immunological and physical characterization of the brain G protein-gated muscarinic potassium channel Biochem. Biophys. Res. Commun. 217 1995 1238 1244 (Pubitemid 26019784)
    • (1995) Biochemical and Biophysical Research Communications , vol.217 , Issue.3 , pp. 1238-1244
    • Inanobe, A.1    Ito, H.2    Ito, M.3    Hosoya, Y.4    Karachi, Y.5
  • 134
    • 0032584662 scopus 로고    scopus 로고
    • Tetrameric subunit structure of the native brain inwardly rectifying potassium channel K(ir) 2.2
    • DOI 10.1074/jbc.273.31.19699
    • K.F. Raab-Graham, and C.A. Vandenberg Tetrameric subunit structure of the native brain inwardly rectifying potassium channel Kir 2.2 J. Biol. Chem. 273 1998 19699 19707 (Pubitemid 28367028)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.31 , pp. 19699-19707
    • Raab-Graham, K.F.1    Vandenberg, C.A.2
  • 137
    • 0342806880 scopus 로고    scopus 로고
    • + channel proteins GIRK1 and GIRK2 and their altered expression in weaver brain
    • + channel proteins GIRK1 and GIRK2 and their altered expression in weaver brain J. Neurosci. 16 1996 7137 7150 (Pubitemid 26382891)
    • (1996) Journal of Neuroscience , vol.16 , Issue.22 , pp. 7137-7150
    • Liao, Y.J.1    Jan, Y.N.2    Jan, L.Y.3
  • 144
    • 30544431963 scopus 로고    scopus 로고
    • Molecular and cellular diversity of neuronal G-protein-gated potassium channels
    • DOI 10.1523/JNEUROSCI.3484-05.2005
    • L. Koyrakh, R. Lujan, J. Colon, C. Karschin, Y. Kurachi, A. Karschin, and K. Wickman Molecular and cellular diversity of neuronal G-protein-gated potassium channels J. Neurosci. 25 2005 11468 11478 (Pubitemid 43083718)
    • (2005) Journal of Neuroscience , vol.25 , Issue.49 , pp. 11468-11478
    • Koyrakh, L.1    Lujan, R.2    Colon, J.3    Karschin, C.4    Kurachi, Y.5    Karschin, A.6    Wickman, K.7
  • 147
    • 0031909974 scopus 로고    scopus 로고
    • Abnormal heart rate regulation in GIRK4 knockout mice
    • DOI 10.1016/S0896-6273(00)80438-9
    • K. Wickman, J. Nemec, S.J. Gendler, and D.E. Clapham Abnormal heart rate regulation in GIRK4 knockout mice Neuron 20 1998 103 114 (Pubitemid 28078353)
    • (1998) Neuron , vol.20 , Issue.1 , pp. 103-114
    • Wickman, K.1    Nemec, J.2    Gendler, S.J.3    Clapham, D.E.4
  • 148
    • 0036616477 scopus 로고    scopus 로고
    • G-Protein-Gated Potassium Channels Containing Kir3.2 and Kir3.3 Subunits Mediate the Acute Inhibitory Effects of Opioids on Locus Ceruleus Neurons
    • M. Torrecilla, C.L. Marker, S.C. Cintora, M. Stoffel, J.T. Williams, and K. Wickman G-protein-gated potassium channels containing Kir3.2 and Kir3.3 subunits mediate the acute inhibitory effects of opioids on locus ceruleus neurons J. Neurosci. 22 2002 4328 4334 (Pubitemid 37465648)
    • (2002) Journal of Neuroscience , vol.22 , Issue.11 , pp. 4328-4334
    • Torrecilla, M.1    Marker, C.L.2    Cintora, S.C.3    Stoffel, M.4    Williams, J.T.5    Wickman, K.6
  • 149
    • 46149084039 scopus 로고    scopus 로고
    • Behavioral characterization of mice lacking GIRK/Kir3 channel subunits
    • DOI 10.1111/j.1601-183X.2008.00388.x
    • M. Pravetoni, and K. Wickman Behavioral characterization of mice lacking GIRK/Kir3 channel subunits Genes Brain Behav. 7 2008 523 531 (Pubitemid 351991487)
    • (2008) Genes, Brain and Behavior , vol.7 , Issue.5 , pp. 523-531
    • Pravetoni, M.1    Wickman, K.2
  • 150
    • 70349126720 scopus 로고    scopus 로고
    • Mapping a barbiturate withdrawal locus to a 0.44 Mb interval and analysis of a novel null mutant identify a role for Kcnj9 (GIRK3) in withdrawal from pentobarbital, zolpidem, and ethanol
    • L.B. Kozell, N.A. Walter, L.C. Milner, K. Wickman, and K.J. Buck Mapping a barbiturate withdrawal locus to a 0.44 Mb interval and analysis of a novel null mutant identify a role for Kcnj9 (GIRK3) in withdrawal from pentobarbital, zolpidem, and ethanol J. Neurosci. 29 2009 11662 11673
    • (2009) J. Neurosci. , vol.29 , pp. 11662-11673
    • Kozell, L.B.1    Walter, N.A.2    Milner, L.C.3    Wickman, K.4    Buck, K.J.5
  • 151
    • 0037184996 scopus 로고    scopus 로고
    • Structural basis of inward rectification: Cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 AA; resolution
    • DOI 10.1016/S0092-8674(02)01227-8
    • M. Nishida, and R. MacKinnon Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 Å resolution Cell 111 2002 957 965 (Pubitemid 36044688)
    • (2002) Cell , vol.111 , Issue.7 , pp. 957-965
    • Nishida, M.1    MacKinnon, R.2
  • 153
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • R. MacKinnon Potassium channels FEBS Lett. 555 2003 62 65
    • (2003) FEBS Lett. , vol.555 , pp. 62-65
    • Mackinnon, R.1
  • 154
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • DOI 10.1038/417523a
    • Y. Jiang, A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon The open pore conformation of potassium channels Nature 417 2002 523 526 (Pubitemid 34595913)
    • (2002) Nature , vol.417 , Issue.6888 , pp. 523-526
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 157
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • DOI 10.1038/417515a
    • Y. Jiang, A. Lee, J. Chen, M. Cadene, B.T. Chait, and R. MacKinnon Crystal structure and mechanism of a calcium-gated potassium channel Nature 417 2002 515 522 (Pubitemid 34595912)
    • (2002) Nature , vol.417 , Issue.6888 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 160
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • DOI 10.1038/nature06265, PII NATURE06265
    • + channel in a lipid membrane-like environment Nature 450 2007 376 382 (Pubitemid 350126743)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 162
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • J. Payandeh, T. Scheuer, N. Zheng, and W.A. Catterall The crystal structure of a voltage-gated sodium channel Nature 475 2012 353 358
    • (2012) Nature , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 163
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • A.I. Sobolevsky, M.P. Rosconi, and E. Gouaux X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor Nature 462 2009 745 756
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 165
    • 58149250085 scopus 로고    scopus 로고
    • High-resolution structure of the open NaK channel
    • A. Alam, and Y. Jiang High-resolution structure of the open NaK channel Nat. Struct. Mol. Biol. 16 2009 30 34
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 30-34
    • Alam, A.1    Jiang, Y.2
  • 166
    • 58149213832 scopus 로고    scopus 로고
    • Structural analysis of ion selectivity in the NaK channel
    • A. Alam, and Y. Jiang Structural analysis of ion selectivity in the NaK channel Nat. Struct. Mol. Biol. 16 2009 35 41
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 35-41
    • Alam, A.1    Jiang, Y.2
  • 167
    • 0035950089 scopus 로고    scopus 로고
    • Ion conduction pore is conserved among potassium channels
    • DOI 10.1038/35101535
    • Z. Lu, A.M. Klem, and Y. Ramu Ion conduction pore is conserved among potassium channels Nature 413 2001 809 813 (Pubitemid 33026842)
    • (2001) Nature , vol.413 , Issue.6858 , pp. 809-813
    • Lu, Z.1    Klem, A.M.2    Ramu, Y.3
  • 170
    • 0035868661 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1111/j.1469-7793.2001.0645h.x
    • + channel J. Physiol. 531 2001 645 660 (Pubitemid 32243746)
    • (2001) Journal of Physiology , vol.531 , Issue.3 , pp. 645-660
    • Kubo, Y.1    Murata, Y.2
  • 173
    • 0027984375 scopus 로고
    • Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification
    • DOI 10.1038/372366a0
    • A.N. Lopatin, E.N. Makhina, and C.G. Nichols Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification Nature 372 1994 366 369 (Pubitemid 24363439)
    • (1994) Nature , vol.372 , Issue.6504 , pp. 366-369
    • Lopatin, A.N.1    Makhina, E.N.2    Nichols, C.G.3
  • 174
    • 66849091683 scopus 로고    scopus 로고
    • Mutational and in silico analyses for antidepressant block of astroglial inward-rectifier Kir4.1 channel
    • K. Furutani, Y. Ohno, A. Inanobe, H. Hibino, and Y. Kurachi Mutational and in silico analyses for antidepressant block of astroglial inward-rectifier Kir4.1 channel Mol. Pharmacol. 75 2009 1287 1295
    • (2009) Mol. Pharmacol. , vol.75 , pp. 1287-1295
    • Furutani, K.1    Ohno, Y.2    Inanobe, A.3    Hibino, H.4    Kurachi, Y.5
  • 175
    • 35448954314 scopus 로고    scopus 로고
    • Inhibition of astroglial Kir4.1 channels by selective serotonin reuptake inhibitors
    • DOI 10.1016/j.brainres.2007.08.018, PII S0006899307018574
    • Y. Ohno, H. Hibino, C. Lossin, A. Inanobe, and Y. Kurachi Inhibition of astroglial Kir4.1 channels by selective serotonin reuptake inhibitors Brain Res. 1178 2007 44 51 (Pubitemid 47625356)
    • (2007) Brain Research , vol.1178 , Issue.1 , pp. 44-51
    • Ohno, Y.1    Hibino, H.2    Lossin, C.3    Inanobe, A.4    Kurachi, Y.5
  • 177
    • 0017258698 scopus 로고
    • Single-channel currents recorded from membrane of denervated frog muscle fibres
    • E. Neher, and B. Sakmann Single-channel currents recorded from membrane of denervated frog muscle fibres Nature 260 1976 799 802
    • (1976) Nature , vol.260 , pp. 799-802
    • Neher, E.1    Sakmann, B.2
  • 178
    • 0019143565 scopus 로고
    • + channel currents observed in cultured rat muscle cells
    • + channel currents observed in cultured rat muscle cells Nature 287 1980 447 449 (Pubitemid 11250353)
    • (1980) Nature , vol.287 , Issue.5781 , pp. 447-449
    • Sigworth, F.J.1    Neher, E.2
  • 179
    • 0023478292 scopus 로고
    • Data transformations for improved display and fitting of single-channel dwell time histograms
    • F.J. Sigworth, and S.M. Sine Data transformations for improved display and fitting of single-channel dwell time histograms Biophys. J. 52 1987 1047 1054
    • (1987) Biophys. J. , vol.52 , pp. 1047-1054
    • Sigworth, F.J.1    Sine, S.M.2
  • 181
    • 0030479238 scopus 로고    scopus 로고
    • + channel in guinea pig atrial myocytes: Spectral analysis of the effect of GTP on single-channel kinetics
    • DOI 10.1085/jgp.108.6.485
    • + channel in guinea pig atrial myocytes. Spectral analysis of the effect of GTP on single-channel kinetics J. Gen. Physiol. 108 1996 485 495 (Pubitemid 26427116)
    • (1996) Journal of General Physiology , vol.108 , Issue.6 , pp. 485-495
    • Hosoya, Y.1    Yamada, M.2    Ito, H.3    Kurachi, Y.4
  • 183
    • 0032606702 scopus 로고    scopus 로고
    • Gβγ binding increases the open time of I(KACh): Kinetic evidence for multiple Gβγ binding sites
    • KACh: kinetic evidence for multiple Gβγ binding sites Biophys. J. 76 1999 246 252 (Pubitemid 29202453)
    • (1999) Biophysical Journal , vol.76 , Issue.1 I , pp. 246-252
    • Nemec, J.1    Wickman, K.2    Clapham, D.E.3
  • 184
    • 0033761774 scopus 로고    scopus 로고
    • Single channel studies of inward rectifier potassium channel regulation by muscarinic acetylcholine receptors
    • J. Bard, M.T. Kunkel, and E.G. Peralta Single channel studies of inward rectifier potassium channel regulation by muscarinic acetylcholine receptors J. Gen. Physiol. 116 2000 645 652
    • (2000) J. Gen. Physiol. , vol.116 , pp. 645-652
    • Bard, J.1    Kunkel, M.T.2    Peralta, E.G.3
  • 186
    • 0020575547 scopus 로고
    • + channels in isolated pacemaker cells of the mammalian heart
    • + channels in isolated pacemaker cells of the mammalian heart Nature 303 1983 250 253 (Pubitemid 13135529)
    • (1983) Nature , vol.303 , Issue.5914 , pp. 250-253
    • Sakmann, B.1    Noma, A.2    Trautwein, W.3
  • 187
    • 0030045421 scopus 로고    scopus 로고
    • Single-channel properties of a G-protein-coupled inward rectifier potassium channel in brain neurons
    • J.J. Grigg, T. Kozasa, Y. Nakajima, and S. Nakajima Single-channel properties of a G-protein-coupled inward rectifier potassium channel in brain neurons J. Neurophysiol. 75 1996 318 328 (Pubitemid 26072042)
    • (1996) Journal of Neurophysiology , vol.75 , Issue.1 , pp. 318-328
    • Grigg, J.J.1    Kozasa, T.2    Nakajima, Y.3    Nakajima, S.4
  • 188
    • 0031058470 scopus 로고    scopus 로고
    • Effector contributions to GβΥ-mediated signaling as revealed by muscarinic potassium channel gating
    • DOI 10.1085/jgp.109.2.245
    • T.T. Ivanova-Nikolova, and G.E. Breitwieser Effector contributions to Gβγ-mediated signaling as revealed by muscarinic potassium channel gating J. Gen. Physiol. 109 1997 245 253 (Pubitemid 27078410)
    • (1997) Journal of General Physiology , vol.109 , Issue.2 , pp. 245-253
    • Ivanova-Nikolova, T.T.1    Breitwieser, G.E.2
  • 189
    • 0032546013 scopus 로고    scopus 로고
    • 2 and its stabilization by Gβγ
    • DOI 10.1038/35882
    • 2 and its stabilization by Gβγ 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
  • 190
    • 0025825595 scopus 로고
    • + channel function in rat atrial cells by phosphorylation
    • + channel function in rat atrial cells by phosphorylation J. Physiol. 437 1991 133 155
    • (1991) J. Physiol. , vol.437 , pp. 133-155
    • Kim, D.1
  • 199
    • 0027219695 scopus 로고
    • Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel
    • DOI 10.1038/364802a0
    • Y. Kubo, E. Reuveny, P.A. Slesinger, Y.N. Jan, and L.Y. Jan Primary structure and functional expression of a rat G-protein-coupled muscarinic potassium channel Nature 364 1993 802 806 (Pubitemid 23261760)
    • (1993) Nature , vol.364 , Issue.6440 , pp. 802-806
    • Kubo, Y.1    Reuveny, E.2    Slesinger, P.A.3    Jan, Y.N.4    Jan, L.Y.5
  • 202
    • 0037183977 scopus 로고    scopus 로고
    • Distinct sites on G protein βγ subunits regulate different effector functions
    • T. Mirshahi, V. Mittal, H. Zhang, M.E. Linder, and D.E. Logothetis Distinct sites on G protein βγ subunits regulate different effector functions J. Biol. Chem. 277 2002 36345 36350
    • (2002) J. Biol. Chem. , vol.277 , pp. 36345-36350
    • Mirshahi, T.1    Mittal, V.2    Zhang, H.3    Linder, M.E.4    Logothetis, D.E.5
  • 205
    • 0030973605 scopus 로고    scopus 로고
    • + channels
    • DOI 10.1016/S0014-5793(97)00197-X, PII S001457939700197X
    • + channels FEBS Lett. 405 1997 291 298 (Pubitemid 27138494)
    • (1997) FEBS Letters , vol.405 , Issue.3 , pp. 291-298
    • Huang, C.-L.1    Jan, Y.N.2    Jan, L.Y.3
  • 206
    • 0028792376 scopus 로고
    • Identification of structural elements involved in G protein gating of the GIRK1 potassium channel
    • P.A. Slesinger, E. Reuveny, Y.N. Jan, and J.Y. Jan Identification of structural elements involved in G protein gating of the GIRK1 potassium channel Neuron 15 1995 1145 1156
    • (1995) Neuron , vol.15 , pp. 1145-1156
    • Slesinger, P.A.1    Reuveny, E.2    Jan, Y.N.3    Jan, J.Y.4
  • 209
    • 78751530099 scopus 로고    scopus 로고
    • NMR analyses of the Gβγ binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1)
    • M. Yokogawa, M. Osawa, K. Takeuchi, Y. Mase, and I. Shimada NMR analyses of the Gβγ binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1) J. Biol. Chem. 286 2011 2215 2223
    • (2011) J. Biol. Chem. , vol.286 , pp. 2215-2223
    • Yokogawa, M.1    Osawa, M.2    Takeuchi, K.3    Mase, Y.4    Shimada, I.5
  • 210
    • 34547129073 scopus 로고    scopus 로고
    • Diverse Kir modulators act in close proximity to residues implicated in phosphoinositide binding
    • DOI 10.1113/jphysiol.2007.133157
    • D.E. Logothetis, D. Lupyan, and A. Rosenhouse-Dantsker Diverse Kir modulators act in close proximity to residues implicated in phosphoinositide binding J. Physiol. 582 2007 953 965 (Pubitemid 47104332)
    • (2007) Journal of Physiology , vol.582 , Issue.3 , pp. 953-965
    • Logothetis, D.E.1    Lupyan, D.2    Rosenhouse-Dantsker, A.3
  • 213
    • 4444359501 scopus 로고    scopus 로고
    • Characteristic interactions with phosphatidylinositol 4,5-bisphosphate determine regulation of Kir channels by diverse modulators
    • DOI 10.1074/jbc.M403413200
    • X. Du, H. Zhang, C. Lopes, T. Mirshahi, T. Rohacs, and D.E. Logothetis Characteristic interactions with phosphatidylinositol 4,5-bisphosphate determine regulation of Kir channels by diverse modulators J. Biol. Chem. 279 2004 37271 37281 (Pubitemid 39195433)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37271-37281
    • Du, X.1    Zhang, H.2    Lopes, C.3    Mirshahi, T.4    Rohacs, T.5    Logothetis, D.E.6
  • 214
    • 34548605730 scopus 로고    scopus 로고
    • 2 signals: When, where, and how?
    • 2 signals: when, where, and how? Pflugers Arch. 455 2007 55 67
    • (2007) Pflugers Arch. , vol.455 , pp. 55-67
    • Hilgemann, D.W.1
  • 215
    • 0035957619 scopus 로고    scopus 로고
    • Novel signalling events mediated by muscarinic receptor subtypes
    • DOI 10.1016/S0024-3205(01)01048-7, PII S0024320501010487
    • M. Bunemann, and M.M. Hosey Novel signalling events mediated by muscarinic receptor subtypes Life Sci. 68 2001 2525 2533 (Pubitemid 32455691)
    • (2001) Life Sciences , vol.68 , Issue.22-23 , pp. 2525-2533
    • Bunemann, M.1    Hosey, M.M.2
  • 218
    • 78650643884 scopus 로고    scopus 로고
    • + (GIRK) channels to caveolae determines receptor specificity of phosphatidylinositol 4,5-bisphosphate signaling
    • + (GIRK) channels to caveolae determines receptor specificity of phosphatidylinositol 4,5-bisphosphate signaling J. Biol. Chem. 285 2010 41732 41739
    • (2010) J. Biol. Chem. , vol.285 , pp. 41732-41739
    • Cui, S.1    Ho, W.K.2    Kim, S.T.3    Cho, H.4
  • 220
    • 0031055885 scopus 로고    scopus 로고
    • Anionic phospholipids activate ATP-sensitive potassium channels
    • DOI 10.1074/jbc.272.9.5388
    • Z. Fan, and J.C. Makielski Anionic phospholipids activate ATP-sensitive potassium channels J. Biol. Chem. 272 1997 5388 5395 (Pubitemid 27102355)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.9 , pp. 5388-5395
    • Fan, Z.1    Makielski, J.C.2
  • 228
    • 13444254031 scopus 로고    scopus 로고
    • α subunits selectively bind to C-terminal domain of neuronal GIRK channels: Evidence for a heterotrimeric G-protein-channel complex
    • DOI 10.1016/j.mcn.2004.10.009
    • S.M. Clancy, C.E. Fowler, M. Finley, K.F. Suen, C. Arrabit, F. Berton, T. Kosaza, P.J. Casey, and P.A. Slesinger Pertussis-toxin-sensitive Gα subunits selectively bind to C-terminal domain of neuronal GIRK channels: evidence for a heterotrimeric G-protein-channel complex Mol. Cell. Neurosci. 28 2005 375 389 (Pubitemid 40202597)
    • (2005) Molecular and Cellular Neuroscience , vol.28 , Issue.2 , pp. 375-389
    • Clancy, S.M.1    Fowler, C.E.2    Finley, M.3    Suen, K.F.4    Arrabit, C.5    Berton, F.6    Kosaza, T.7    Casey, P.J.8    Slesinger, P.A.9
  • 229
    • 0038664388 scopus 로고    scopus 로고
    • Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy
    • DOI 10.1016/S0896-6273(03)00193-4
    • I. Riven, E. Kalmanzon, L. Segev, and E. Reuveny Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy Neuron 38 2003 225 235 (Pubitemid 36555649)
    • (2003) Neuron , vol.38 , Issue.2 , pp. 225-235
    • Riven, I.1    Kalmanzon, E.2    Segev, L.3    Reuveny, E.4
  • 232
    • 0033151730 scopus 로고    scopus 로고
    • New roles for RGS2, 5 and 8 on the ratio-dependent modulation of recombinant GIRK channels expressed in Xenopus oocytes
    • DOI 10.1111/j.1469-7793.1999.0341t.x
    • S. Herlitze, J.P. Ruppersberg, and M.D. Mark New roles for RGS2, 5 and 8 on the ratio-dependent modulation of recombinant GIRK channels expressed in Xenopus oocytes J. Physiol. 517 Pt 2 1999 341 352 (Pubitemid 29294881)
    • (1999) Journal of Physiology , vol.517 , Issue.2 , pp. 341-352
    • Herlitze, S.1    Ruppersberg, J.P.2    Mark, M.D.3
  • 235
    • 0035880976 scopus 로고    scopus 로고
    • Interaction between the RGS domain of RGS4 with G protein α subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel
    • DOI 10.1111/j.1469-7793.2001.t01-1-00133.x
    • A. Inanobe, S. Fujita, Y. Makino, K. Matsushita, M. Ishii, M. Chachin, and Y. Kurachi Interaction between the RGS domain of RGS4 with G protein α subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel J. Physiol. 535 2001 133 143 (Pubitemid 32782731)
    • (2001) Journal of Physiology , vol.535 , Issue.1 , pp. 133-143
    • Inanobe, A.1    Fujita, S.2    Makino, Y.3    Matsushita, K.4    Ishii, M.5    Chachin, M.6    Kurachi, Y.7
  • 236
    • 0034721832 scopus 로고    scopus 로고
    • Rapid kinetics of regulator of G-protein signaling (RGS)-mediated Galphai and Galphao deactivation. Galpha specificity of RGS4 and RGS7
    • K.L. Lan, H. Zhong, M. Nanamori, and R.R. Neubig Rapid kinetics of regulator of G-protein signaling (RGS)-mediated Galphai and Galphao deactivation. Galpha specificity of RGS4 AND RGS7 J. Biol. Chem. 275 2000 33497 33503
    • (2000) J. Biol. Chem. , vol.275 , pp. 33497-33503
    • Lan, K.L.1    Zhong, H.2    Nanamori, M.3    Neubig, R.R.4
  • 237
    • 12244309566 scopus 로고    scopus 로고
    • 1-coupled muscarinic m2 receptors in Xenopus oocytes: The role of receptor precoupling in RGS modulation
    • DOI 10.1113/jphysiol.2002.032151
    • i-coupled muscarinic m2 receptors in Xenopus oocytes: the role of receptor precoupling in RGS modulation J. Physiol. 545 2002 355 373 (Pubitemid 36004372)
    • (2002) Journal of Physiology , vol.545 , Issue.2 , pp. 355-373
    • Zhang, Q.1    Pacheco, M.A.2    Doupnik, C.A.3
  • 239
    • 18744376919 scopus 로고    scopus 로고
    • Real-time monitoring of receptor and G-protein interactions in living cells
    • DOI 10.1038/nmeth743
    • C. Gales, R.V. Rebois, M. Hogue, P. Trieu, A. Breit, T.E. Hebert, and M. Bouvier Real-time monitoring of receptor and G-protein interactions in living cells Nat. Methods 2 2005 177 184 (Pubitemid 41122124)
    • (2005) Nature Methods , vol.2 , Issue.3 , pp. 177-184
    • Gales, C.1    Rebois, R.V.2    Hogue, M.3    Trieu, P.4    Breit, A.5    Hebert, T.E.6    Bouvier, M.7
  • 240
    • 28644443374 scopus 로고    scopus 로고
    • Dynamics of receptor/G protein coupling in living cells
    • DOI 10.1038/sj.emboj.7600870
    • P. Hein, M. Frank, C. Hoffmann, M.J. Lohse, and M. Bunemann Dynamics of receptor/G protein coupling in living cells EMBO J. 24 2005 4106 4114 (Pubitemid 41752879)
    • (2005) EMBO Journal , vol.24 , Issue.23 , pp. 4106-4114
    • Hein, P.1    Frank, M.2    Hoffmann, C.3    Lohse, M.J.4    Bunemann, M.5
  • 242
    • 33845942736 scopus 로고    scopus 로고
    • RGS3 and RGS4 differentially associate with G protein-coupled receptor-Kir3 channel signaling complexes revealing two modes of RGS modulation: Precoupling and collision coupling
    • DOI 10.1074/jbc.M603177200
    • C. Jaen, and C.A. Doupnik RGS3 and RGS4 differentially associate with G protein-coupled receptor-Kir3 channel signaling complexes revealing two modes of RGS modulation. Precoupling and collision coupling J. Biol. Chem. 281 2006 34549 34560 (Pubitemid 46036662)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34549-34560
    • Jaen, C.1    Doupnik, C.A.2
  • 244
    • 33947532316 scopus 로고    scopus 로고
    • B receptors with Kir3 channels and regulators of G protein signalling (RGS4) proteins
    • DOI 10.1113/jphysiol.2006.123216
    • B receptors with Kir3 channels and regulators of G protein signalling (RGS4) proteins J. Physiol. 580 2007 51 65 (Pubitemid 46470644)
    • (2007) Journal of Physiology , vol.580 , Issue.1 , pp. 51-65
    • Fowler, C.E.1    Aryal, P.2    Suen, K.F.3    Slesinger, P.A.4
  • 250
    • 34548386717 scopus 로고    scopus 로고
    • Crystal structure of a Kir3.1-prokaryotic Kir channel chimera
    • DOI 10.1038/sj.emboj.7601828, PII 7601828
    • M. Nishida, M. Cadene, B.T. Chait, and R. MacKinnon Crystal structure of a Kir3.1-prokaryotic Kir channel chimera EMBO J. 26 2007 4005 4015 (Pubitemid 47367496)
    • (2007) EMBO Journal , vol.26 , Issue.17 , pp. 4005-4015
    • Nishida, M.1    Cadene, M.2    Chait, B.T.3    MacKinnon, R.4
  • 251
    • 14544298750 scopus 로고    scopus 로고
    • Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification
    • DOI 10.1038/nn1411
    • S. Pegan, C. Arrabit, W. Zhou, W. Kwiatkowski, A. Collins, P.A. Slesinger, and S. Choe Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification Nat. Neurosci. 8 2005 279 287 (Pubitemid 40300184)
    • (2005) Nature Neuroscience , vol.8 , Issue.3 , pp. 279-287
    • Pegan, S.1    Arrabit, C.2    Zhou, W.3    Kwiatkowski, W.4    Collins, A.5    Slesinger, P.A.6    Choe, S.7
  • 252
    • 77953714921 scopus 로고    scopus 로고
    • Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels
    • O.B. Clarke, A.T. Caputo, A.P. Hill, J.I. Vandenberg, B.J. Smith, and J.M. Gulbis Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels Cell 141 2010 1018 1029
    • (2010) Cell , vol.141 , pp. 1018-1029
    • Clarke, O.B.1    Caputo, A.T.2    Hill, A.P.3    Vandenberg, J.I.4    Smith, B.J.5    Gulbis, J.M.6
  • 254
    • 84878996278 scopus 로고    scopus 로고
    • X-ray structure of the mammalian GIRK2-βγ G-protein complex
    • M.R. Whorton, and R. MacKinnon X-ray structure of the mammalian GIRK2-βγ G-protein complex Nature 498 2013 190 197
    • (2013) Nature , vol.498 , pp. 190-197
    • Whorton, M.R.1    Mackinnon, R.2
  • 255
    • 26444584556 scopus 로고    scopus 로고
    • Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography
    • DOI 10.1016/j.str.2005.07.011, PII S0969212605002704
    • A. Kuo, C. Domene, L.N. Johnson, D.A. Doyle, and C. Venien-Bryan Two different conformational states of the KirBac3.1 potassium channel revealed by electron crystallography Structure 13 2005 1463 1472 (Pubitemid 41427586)
    • (2005) Structure , vol.13 , Issue.10 , pp. 1463-1472
    • Kuo, A.1    Domene, C.2    Johnson, L.N.3    Doyle, D.A.4    Venien-Bryan, C.5
  • 256
    • 35548982646 scopus 로고    scopus 로고
    • Direct visualization of kirbac3.1 potassium channel gating by atomic force microscopy
    • DOI 10.1016/j.jmb.2007.09.043, PII S0022283607012314
    • S. Jaroslawski, B. Zadek, F. Ashcroft, C. Venien-Bryan, and S. Scheuring Direct visualization of KirBac3.1 potassium channel gating by atomic force microscopy J. Mol. Biol. 374 2007 500 505 (Pubitemid 350007655)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.2 , pp. 500-505
    • Jaroslawski, S.1    Zadek, B.2    Ashcroft, F.3    Venien-Bryan, C.4    Scheuring, S.5
  • 258
    • 33645325379 scopus 로고    scopus 로고
    • Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1
    • Y. Fujiwara, and Y. Kubo Functional roles of charged amino acid residues on the wall of the cytoplasmic pore of Kir2.1 J. Gen. Physiol. 127 2006 401 419
    • (2006) J. Gen. Physiol. , vol.127 , pp. 401-419
    • Fujiwara, Y.1    Kubo, Y.2
  • 259
    • 59649091228 scopus 로고    scopus 로고
    • Long-pore electrostatics in inward-rectifier potassium channels
    • J.L. Robertson, L.G. Palmer, and B. Roux Long-pore electrostatics in inward-rectifier potassium channels J. Gen. Physiol. 132 2008 613 632
    • (2008) J. Gen. Physiol. , vol.132 , pp. 613-632
    • Robertson, J.L.1    Palmer, L.G.2    Roux, B.3
  • 260
    • 84864652652 scopus 로고    scopus 로고
    • Multi-ion distributions in the cytoplasmic domain of inward rectifier potassium channels
    • J.L. Robertson, L.G. Palmer, and B. Roux Multi-ion distributions in the cytoplasmic domain of inward rectifier potassium channels Biophys. J. 103 2012 434 443
    • (2012) Biophys. J. , vol.103 , pp. 434-443
    • Robertson, J.L.1    Palmer, L.G.2    Roux, B.3
  • 262
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core
    • N. Armstrong, and E. Gouaux Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core Neuron 28 2000 165 181
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 263
    • 33748622291 scopus 로고    scopus 로고
    • + Channels
    • DOI 10.1016/j.cell.2006.08.029, PII S0092867406010981
    • + channels Cell 126 2006 1161 1173 (Pubitemid 44380293)
    • (2006) Cell , vol.126 , Issue.6 , pp. 1161-1173
    • Ye, S.1    Li, Y.2    Chen, L.3    Jiang, Y.4
  • 265
    • 33746047139 scopus 로고    scopus 로고
    • Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1
    • DOI 10.1021/bi060653d
    • S. Pegan, C. Arrabit, P.A. Slesinger, and S. Choe Andersen's syndrome mutation effects on the structure and assembly of the cytoplasmic domains of Kir2.1 Biochemistry 45 2006 8599 8606 (Pubitemid 44078880)
    • (2006) Biochemistry , vol.45 , Issue.28 , pp. 8599-8606
    • Pegan, S.1    Arrabit, C.2    Slesinger, P.A.3    Choe, S.4
  • 267
    • 84871261368 scopus 로고    scopus 로고
    • The cytosolic GH loop regulates the phosphatidylinositol 4,5-bisphosphate-induced gating kinetics of Kir2 channels
    • H.L. An, S.Q. Lu, J.W. Li, X.Y. Meng, Y. Zhan, M. Cui, M. Long, H.L. Zhang, and D.E. Logothetis The cytosolic GH loop regulates the phosphatidylinositol 4,5-bisphosphate-induced gating kinetics of Kir2 channels J. Biol. Chem. 287 2012 42278 42287
    • (2012) J. Biol. Chem. , vol.287 , pp. 42278-42287
    • An, H.L.1    Lu, S.Q.2    Li, J.W.3    Meng, X.Y.4    Zhan, Y.5    Cui, M.6    Long, M.7    Zhang, H.L.8    Logothetis, D.E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.