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Volumn 30, Issue 5, 1997, Pages 577-590

Connexin domains relevant to the chemical gating of gap junction channels

Author keywords

Calcium; Calmodulin; Cell junctions; Cell cell interaction; Gap junctions; Membrane channels

Indexed keywords

ARACHIDONIC ACID; ARGININE; ASPARAGINE; CALCIUM; CALMODULIN; GAP JUNCTION PROTEIN; ION CHANNEL; THREONINE;

EID: 0031132747     PISSN: 0100879X     EISSN: None     Source Type: Journal    
DOI: 10.1590/S0100-879X1997000500003     Document Type: Article
Times cited : (27)

References (80)
  • 1
    • 0029974655 scopus 로고    scopus 로고
    • Connections with connexins: The molecular basis of direct intercellular signaling
    • Bruzzone R, White TW & Paul DL (1996). Connections with connexins: The molecular basis of direct intercellular signaling. European Journal of Biochemistry, 238: 1-27.
    • (1996) European Journal of Biochemistry , vol.238 , pp. 1-27
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 4
    • 0028088839 scopus 로고
    • Point mutations of the connexin32 (GJB1) gene in X-linked dominant Charcot-Marie-Tooth neuropathy
    • Ionasescu V, Searby C & Ionasescu R (1994). Point mutations of the connexin32 (GJB1) gene in X-linked dominant Charcot-Marie-Tooth neuropathy. Human Molecular Genetics, 3: 355-358.
    • (1994) Human Molecular Genetics , vol.3 , pp. 355-358
    • Ionasescu, V.1    Searby, C.2    Ionasescu, R.3
  • 6
    • 0028203576 scopus 로고
    • CMTX1: A gap junction genetic disease
    • Spray DC (1994). CMTX1: A gap junction genetic disease. Lancet, 343: 1111-1112.
    • (1994) Lancet , vol.343 , pp. 1111-1112
    • Spray, D.C.1
  • 7
    • 0029060788 scopus 로고
    • Mutations of the connexin43 gap-junction gene in patients with heart malformations and defects of laterality
    • Britz-Cunningham SH, Shah MM, Zuppan CW & Fletcher WH (1995). Mutations of the connexin43 gap-junction gene in patients with heart malformations and defects of laterality. New England Journal of Medicine, 332: 1323-1329.
    • (1995) New England Journal of Medicine , vol.332 , pp. 1323-1329
    • Britz-Cunningham, S.H.1    Shah, M.M.2    Zuppan, C.W.3    Fletcher, W.H.4
  • 8
    • 0028343428 scopus 로고
    • Modulation of gap junctional mechanisms during calcium-free induced field burst activity: A possible role for electrotonic coupling in epileptogenesis
    • Perez-Velazquez JL, Valiante TA & Carlen PL (1994). Modulation of gap junctional mechanisms during calcium-free induced field burst activity: A possible role for electrotonic coupling in epileptogenesis. Journal of Neuroscience, 14: 4308-4317.
    • (1994) Journal of Neuroscience , vol.14 , pp. 4308-4317
    • Perez-Velazquez, J.L.1    Valiante, T.A.2    Carlen, P.L.3
  • 9
    • 0028863734 scopus 로고
    • Gap junctions are required for the propagation of spreading depression
    • Nedergaard M, Cooper AJL & Goldman SA (1995). Gap junctions are required for the propagation of spreading depression. Journal of Neurobiology, 28: 433-444.
    • (1995) Journal of Neurobiology , vol.28 , pp. 433-444
    • Nedergaard, M.1    Cooper, A.J.L.2    Goldman, S.A.3
  • 11
    • 0019230279 scopus 로고
    • Structural correlates of gap junction permeation
    • Peracchia C (1980). Structural correlates of gap junction permeation. International Review of Cytology, 66: 81-146.
    • (1980) International Review of Cytology , vol.66 , pp. 81-146
    • Peracchia, C.1
  • 13
    • 0023644895 scopus 로고
    • Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures
    • Zimmer DB, Green CR, Evans WH & Gilula NB (1987). Topological analysis of the major protein in isolated intact rat liver gap junctions and gap junction-derived single membrane structures. Journal of Biological Chemistry, 262: 7751-7763.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 7751-7763
    • Zimmer, D.B.1    Green, C.R.2    Evans, W.H.3    Gilula, N.B.4
  • 15
    • 0024095587 scopus 로고
    • Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations
    • Milks LC, Kumar NM, Houghten R, Unwin N & Gilula NB (1988). Topology of the 32-kd liver gap junction protein determined by site-directed antibody localizations. EMBO Journal, 7: 2967-2975.
    • (1988) EMBO Journal , vol.7 , pp. 2967-2975
    • Milks, L.C.1    Kumar, N.M.2    Houghten, R.3    Unwin, N.4    Gilula, N.B.5
  • 16
    • 0024110268 scopus 로고
    • Topological distribution of two connexin32 antigenic sites in intact and split rodent hepatocyte gap junctions
    • Goodenough DA, Paul DL & Jesaitis L (1988). Topological distribution of two connexin32 antigenic sites in intact and split rodent hepatocyte gap junctions. Journal of Cell Biology, 107: 1817-1824.
    • (1988) Journal of Cell Biology , vol.107 , pp. 1817-1824
    • Goodenough, D.A.1    Paul, D.L.2    Jesaitis, L.3
  • 17
    • 0024356206 scopus 로고
    • The 43-kD polypeptide of heart gap junctions: Immunolocalization, topology, and functional domains
    • Yancey SB, John SA, Lal R, Austin BJ & Revel J-P (1989). The 43-kD polypeptide of heart gap junctions: Immunolocalization, topology, and functional domains. Journal of Cell Biology, 108: 2241-2254.
    • (1989) Journal of Cell Biology , vol.108 , pp. 2241-2254
    • Yancey, S.B.1    John, S.A.2    Lal, R.3    Austin, B.J.4    Revel, J.-P.5
  • 18
    • 0025569290 scopus 로고
    • Biochemical and immunochemical analysis of the arrangement of connexin43 in rat heart gap junction membranes
    • Laird DW & Revel J-P (1990). Biochemical and immunochemical analysis of the arrangement of connexin43 in rat heart gap junction membranes. Journal of Cell Science, 97: 109-117.
    • (1990) Journal of Cell Science , vol.97 , pp. 109-117
    • Laird, D.W.1    Revel, J.-P.2
  • 19
    • 0026671599 scopus 로고
    • Inhibition of gap junction and adherent junction assembly by connexin and A-CAM antibodies
    • Meyer RA, Laird DW, Revel JP & Johnson RG (1992). Inhibition of gap junction and adherent junction assembly by connexin and A-CAM antibodies. Journal of Cell Biology, 119: 179-189.
    • (1992) Journal of Cell Biology , vol.119 , pp. 179-189
    • Meyer, R.A.1    Laird, D.W.2    Revel, J.P.3    Johnson, R.G.4
  • 20
    • 0026515179 scopus 로고
    • Membrane topology and quaternary structure of cardiac gap junction ion channels
    • Yeager M & Gilula NB (1992). Membrane topology and quaternary structure of cardiac gap junction ion channels. Journal of Molecular Biology, 223: 929-948.
    • (1992) Journal of Molecular Biology , vol.223 , pp. 929-948
    • Yeager, M.1    Gilula, N.B.2
  • 21
    • 0028256347 scopus 로고
    • The topological structure of connexin 26 and its distribution compared to connexin 32 in hepatic gap junctions
    • Zhang J-T & Nicholson BJ (1994). The topological structure of connexin 26 and its distribution compared to connexin 32 in hepatic gap junctions. Journal of Membrane Biology, 139: 15-29.
    • (1994) Journal of Membrane Biology , vol.139 , pp. 15-29
    • Zhang, J.-T.1    Nicholson, B.J.2
  • 22
    • 0028906886 scopus 로고
    • The topogenic fate of the polytopic transmembrane proteins, synaptophysin and connexin, is determined by their membrane-spanning domains
    • Leube RE (1995). The topogenic fate of the polytopic transmembrane proteins, synaptophysin and connexin, is determined by their membrane-spanning domains. Journal of Cell Science, 108: 883-894.
    • (1995) Journal of Cell Science , vol.108 , pp. 883-894
    • Leube, R.E.1
  • 23
    • 0025092104 scopus 로고
    • Increase in gap junction resistance with acidification in crayfish septate axons is closely related to changes in intracellular calcium but not hydrogen ion concentration
    • Peracchia C (1990). Increase in gap junction resistance with acidification in crayfish septate axons is closely related to changes in intracellular calcium but not hydrogen ion concentration. Journal of Membrane Biology, 113: 75-92.
    • (1990) Journal of Membrane Biology , vol.113 , pp. 75-92
    • Peracchia, C.1
  • 24
    • 0027448843 scopus 로고
    • Gap junction gating sensitivity to physiological internal calcium regardless of pH in Novikoff hepatoma cells
    • Lazrak A & Peracchia C (1993). Gap junction gating sensitivity to physiological internal calcium regardless of pH in Novikoff hepatoma cells. Biophysical Journal, 65: 2002-2012.
    • (1993) Biophysical Journal , vol.65 , pp. 2002-2012
    • Lazrak, A.1    Peracchia, C.2
  • 25
    • 0028141842 scopus 로고
    • Ca-mediated and independent effects of arachidonic acid on gap junctions and Ca-independent effects of oleic acid and halothane
    • Lazrak A, Peres A, Giovannardi S & Peracchia C (1994). Ca-mediated and independent effects of arachidonic acid on gap junctions and Ca-independent effects of oleic acid and halothane. Biophysical Journal, 67: 1052-1059.
    • (1994) Biophysical Journal , vol.67 , pp. 1052-1059
    • Lazrak, A.1    Peres, A.2    Giovannardi, S.3    Peracchia, C.4
  • 26
    • 0029101240 scopus 로고
    • Magnitude and modulation of pancreatic ß-cell gap junction electrical conductance in situ
    • Mears D, Sheppard Jr NF, Atwater I & Rojas E (1995). Magnitude and modulation of pancreatic ß-cell gap junction electrical conductance in situ. Journal of Membrane Biology, 146: 163-176.
    • (1995) Journal of Membrane Biology , vol.146 , pp. 163-176
    • Mears, D.1    Sheppard Jr., N.F.2    Atwater, I.3    Rojas, E.4
  • 27
    • 0027930117 scopus 로고
    • Micromolar levels of intracellular calcium reduce gap junctional permeability in lens cultures
    • Crow JM, Atkinson MM & Johnson RG (1994). Micromolar levels of intracellular calcium reduce gap junctional permeability in lens cultures. Investigative Ophthalmology and Visual Science, 35: 3332-3341.
    • (1994) Investigative Ophthalmology and Visual Science , vol.35 , pp. 3332-3341
    • Crow, J.M.1    Atkinson, M.M.2    Johnson, R.G.3
  • 28
    • 0029964362 scopus 로고    scopus 로고
    • Inhibition of calmodulin expression prevents low-pH-induced gap junction uncoupling in Xenopus oocytes
    • Peracchia C, Wang XG, Li LQ & Peracchia LL (1996). Inhibition of calmodulin expression prevents low-pH-induced gap junction uncoupling in Xenopus oocytes. Pflügers Archiv, 431: 379-387.
    • (1996) Pflügers Archiv , vol.431 , pp. 379-387
    • Peracchia, C.1    Wang, X.G.2    Li, L.Q.3    Peracchia, L.L.4
  • 30
    • 1542389995 scopus 로고
    • Calcium ions and the healing-over in heart fibers
    • Taccardi T & Marchetti C (Editors), Pergamon Press, Elmsford, New York
    • Délèze J (1965). Calcium ions and the healing-over in heart fibers. In: Taccardi T & Marchetti C (Editors), Electrophysiology of the Heart. Pergamon Press, Elmsford, New York, 147-148.
    • (1965) Electrophysiology of the Heart , pp. 147-148
    • Délèze, J.1
  • 31
    • 0017079650 scopus 로고
    • Permeability of a cell junction during intracellular injection of divalent cations
    • Délèze J & Loewenstein WR (1976). Permeability of a cell junction during intracellular injection of divalent cations. Journal of Membrane Biology, 28: 71-86.
    • (1976) Journal of Membrane Biology , vol.28 , pp. 71-86
    • Délèze, J.1    Loewenstein, W.R.2
  • 32
    • 0017125140 scopus 로고
    • Permeability of a cell junction and the local cytoplasmic free ionized calcium concentration: A study with aequorin
    • Rose B & Loewenstein WR (1976). Permeability of a cell junction and the local cytoplasmic free ionized calcium concentration: a study with aequorin. Journal of Membrane Biology, 28: 87-119.
    • (1976) Journal of Membrane Biology , vol.28 , pp. 87-119
    • Rose, B.1    Loewenstein, W.R.2
  • 33
    • 0016825329 scopus 로고
    • Effect of intracellular injection of calcium and strontium on cell communication in heart
    • De Mello WC (1975). Effect of intracellular injection of calcium and strontium on cell communication in heart. Journal of Physiology, 250: 231-245.
    • (1975) Journal of Physiology , vol.250 , pp. 231-245
    • De Mello, W.C.1
  • 34
    • 0017761775 scopus 로고
    • Carbon dioxide reversibly abolishes ionic communication between cells of early amphibian embryo
    • Turin L & Warner AE (1977). Carbon dioxide reversibly abolishes ionic communication between cells of early amphibian embryo. Nature, 270: 56-57.
    • (1977) Nature , vol.270 , pp. 56-57
    • Turin, L.1    Warner, A.E.2
  • 35
    • 0018908753 scopus 로고
    • Intracellular pH in early Xenopus embryos: Its effect on current flow between blastomeres
    • Turin L & Warner AE (1980). Intracellular pH in early Xenopus embryos: its effect on current flow between blastomeres. Journal of Physiology, 300: 489-504.
    • (1980) Journal of Physiology , vol.300 , pp. 489-504
    • Turin, L.1    Warner, A.E.2
  • 36
    • 0019471073 scopus 로고
    • Gap junctional conductance is a simple and sensitive function of intracellular pH
    • Spray DC, Harris AL & Bennett MV (1981). Gap junctional conductance is a simple and sensitive function of intracellular pH. Science, 211: 712-715.
    • (1981) Science , vol.211 , pp. 712-715
    • Spray, D.C.1    Harris, A.L.2    Bennett, M.V.3
  • 38
    • 0009749819 scopus 로고
    • Permeability and regulation of gap junction channels in cells and in artificial lipid bilayers
    • De Mello WC (Editor), Plenum Press, New York
    • Peracchia C (1987). Permeability and regulation of gap junction channels in cells and in artificial lipid bilayers. In: De Mello WC (Editor), Cell-to-Cell Communication. Plenum Press, New York, 65-102.
    • (1987) Cell-to-Cell Communication , pp. 65-102
    • Peracchia, C.1
  • 39
    • 0024545772 scopus 로고
    • Intracellular pH and cell-to-cell transmission in sheep Purkinje fibers
    • Pressler ML (1989). Intracellular pH and cell-to-cell transmission in sheep Purkinje fibers. Biophysical Journal, 55: 53-65.
    • (1989) Biophysical Journal , vol.55 , pp. 53-65
    • Pressler, M.L.1
  • 40
    • 0027172696 scopus 로고
    • A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: The carboxyl tail length
    • Liu S, Taffet S, Stoner L, Delmar M, Vallano ML & Jalife J (1993). A structural basis for the unequal sensitivity of the major cardiac and liver gap junctions to intracellular acidification: The carboxyl tail length. Biophysical Journal, 64: 1422-1433.
    • (1993) Biophysical Journal , vol.64 , pp. 1422-1433
    • Liu, S.1    Taffet, S.2    Stoner, L.3    Delmar, M.4    Vallano, M.L.5    Jalife, J.6
  • 41
    • 0025334768 scopus 로고
    • i-induced changes in gap junction conductance and calcium concentration in crayfish septate axons
    • i-induced changes in gap junction conductance and calcium concentration in crayfish septate axons. Journal of Membrane Biology, 117: 79-89.
    • (1990) Journal of Membrane Biology , vol.117 , pp. 79-89
    • Peracchia, C.1
  • 44
    • 0017364846 scopus 로고
    • Action of ouabain on intercellular coupling and conduction-velocity in mammalian ventricular muscle
    • Weingart R (1977). Action of ouabain on intercellular coupling and conduction-velocity in mammalian ventricular muscle. Journal of Physiology, 264: 341-365.
    • (1977) Journal of Physiology , vol.264 , pp. 341-365
    • Weingart, R.1
  • 45
    • 0018870828 scopus 로고
    • Decoupling of heart muscle cells: Correlation with increased cytoplasmic calcium activity and with changes of nexus ultrastructure
    • Dahl G & lsenberg G (1980). Decoupling of heart muscle cells: correlation with increased cytoplasmic calcium activity and with changes of nexus ultrastructure. Journal of Membrane Biology, 53: 63-75.
    • (1980) Journal of Membrane Biology , vol.53 , pp. 63-75
    • Dahl, G.1    Lsenberg, G.2
  • 46
    • 0022526707 scopus 로고
    • Physiological modulation of gap junction permeability
    • Neyton J & Trautmann A (1986). Physiological modulation of gap junction permeability. Journal of Experimental Biology, 124: 93-114.
    • (1986) Journal of Experimental Biology , vol.124 , pp. 93-114
    • Neyton, J.1    Trautmann, A.2
  • 48
    • 0023161934 scopus 로고
    • Dependence of junctional conductance on proton, calcium and magnesium ions in cardiac paired cells of guinea-pig
    • Noma A & Tsuboi N (1987). Dependence of junctional conductance on proton, calcium and magnesium ions in cardiac paired cells of guinea-pig. Journal of Physiology, 382: 193-211.
    • (1987) Journal of Physiology , vol.382 , pp. 193-211
    • Noma, A.1    Tsuboi, N.2
  • 49
    • 0023838610 scopus 로고
    • Cardiac gap junction channel activity in embryonic chick ventricle cells
    • Veenstra RD & DeHaan RL (1988). Cardiac gap junction channel activity in embryonic chick ventricle cells. American Journal of Physiology, 254: H170-H180.
    • (1988) American Journal of Physiology , vol.254
    • Veenstra, R.D.1    DeHaan, R.L.2
  • 51
    • 0024710511 scopus 로고
    • Intercellular signaling as visualized by endogenous calcium-dependent bioluminescence
    • Brehm P, Lechleiter J, Smith S & Dunlap K (1989). Intercellular signaling as visualized by endogenous calcium-dependent bioluminescence. Neuron, 3: 191-198.
    • (1989) Neuron , vol.3 , pp. 191-198
    • Brehm, P.1    Lechleiter, J.2    Smith, S.3    Dunlap, K.4
  • 52
    • 0023243246 scopus 로고
    • Activation of a calcium-dependent photoprotein by chemical signaling through gap junctions
    • Dunlap K, Takeda K & Brehm P (1987). Activation of a calcium-dependent photoprotein by chemical signaling through gap junctions. Nature, 325: 60-62.
    • (1987) Nature , vol.325 , pp. 60-62
    • Dunlap, K.1    Takeda, K.2    Brehm, P.3
  • 53
    • 0019731424 scopus 로고
    • Electrotonic coupling in internally perfused crayfish segmented axons
    • Johnston MF & Ramón F (1981). Electrotonic coupling in internally perfused crayfish segmented axons. Journal of Physiology, 317: 509-518.
    • (1981) Journal of Physiology , vol.317 , pp. 509-518
    • Johnston, M.F.1    Ramón, F.2
  • 54
    • 0003324793 scopus 로고
    • A calmodulin inhibitor prevents gap junction crystallization and electrical uncoupling
    • Abstract
    • Peracchia C, Bernardini G & Peracchia LL (1981). A calmodulin inhibitor prevents gap junction crystallization and electrical uncoupling. Journal of Cell Biology, 91: 124 (Abstract).
    • (1981) Journal of Cell Biology , vol.91 , pp. 124
    • Peracchia, C.1    Bernardini, G.2    Peracchia, L.L.3
  • 55
    • 0021063967 scopus 로고
    • Is calmodulin involved in the regulation of gap junction permeability?
    • Peracchia C, Bernardini G & Peracchia LL (1983). Is calmodulin involved in the regulation of gap junction permeability? Pflügers Archiv, 399: 152-154.
    • (1983) Pflügers Archiv , vol.399 , pp. 152-154
    • Peracchia, C.1    Bernardini, G.2    Peracchia, L.L.3
  • 56
    • 0020399716 scopus 로고
    • Liver gap junctions and lens fiber junctions: Comparative analysis and calmodulin interaction
    • Hertzberg EL & Gilula NB (1981). Liver gap junctions and lens fiber junctions: comparative analysis and calmodulin interaction. Cold Spring Harbor Symposia on Quantitative Biology, 46: 639-645.
    • (1981) Cold Spring Harbor Symposia on Quantitative Biology , vol.46 , pp. 639-645
    • Hertzberg, E.L.1    Gilula, N.B.2
  • 57
    • 0021148916 scopus 로고
    • Communicating junctions and calmodulin: Inhibition of electrical uncoupling in Xenopus embryo by calmidazolium
    • Peracchia C (1984). Communicating junctions and calmodulin: inhibition of electrical uncoupling in Xenopus embryo by calmidazolium. Journal of Membrane Biology, 81: 49-58.
    • (1984) Journal of Membrane Biology , vol.81 , pp. 49-58
    • Peracchia, C.1
  • 58
    • 0023127381 scopus 로고
    • Calmodulin-like proteins and communicating junctions. Electrical uncoupling of crayfish septate axons is inhibited by the calmodulin inhibitor W7 and is not affected by cyclic nucleotides
    • Peracchia C (1987). Calmodulin-like proteins and communicating junctions. Electrical uncoupling of crayfish septate axons is inhibited by the calmodulin inhibitor W7 and is not affected by cyclic nucleotides. Pflügers Archiv, 408: 379-385.
    • (1987) Pflügers Archiv , vol.408 , pp. 379-385
    • Peracchia, C.1
  • 59
    • 0004337115 scopus 로고
    • Electrical uncoupling induced by general anesthetics: A calcium-independent process?
    • Bennett MVL & Spray DC (Editors), Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • Wojtczak JA (1985). Electrical uncoupling induced by general anesthetics: a calcium-independent process? In: Bennett MVL & Spray DC (Editors), Gap Junctions. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 167-175.
    • (1985) Gap Junctions , pp. 167-175
    • Wojtczak, J.A.1
  • 60
    • 0024393057 scopus 로고
    • Effects of calmidazolium and dibutyryl cyclic AMP on the longitudinal internal resistance in sinus node strips
    • Tuganowski W, Korczynska I, Wasik K & Piatek G (1989). Effects of calmidazolium and dibutyryl cyclic AMP on the longitudinal internal resistance in sinus node strips. Pflügers Archiv, 414: 351-353.
    • (1989) Pflügers Archiv , vol.414 , pp. 351-353
    • Tuganowski, W.1    Korczynska, I.2    Wasik, K.3    Piatek, G.4
  • 61
    • 0025181954 scopus 로고
    • Mammalian lens inter-fiber resistance is modulated by calcium and calmodulin
    • Gandolfi SA, Duncan G, Tomlinson J & Maraini G (1990). Mammalian lens inter-fiber resistance is modulated by calcium and calmodulin. Current Eye Research, 9: 533-541.
    • (1990) Current Eye Research , vol.9 , pp. 533-541
    • Gandolfi, S.A.1    Duncan, G.2    Tomlinson, J.3    Maraini, G.4
  • 62
    • 0023852621 scopus 로고
    • Calmodulin acts as an intermediary for the effects of calcium on gap junctions from crayfish lateral axons
    • Arellano RO, Ramón F, Rivera A & Zampighi GA (1988). Calmodulin acts as an intermediary for the effects of calcium on gap junctions from crayfish lateral axons. Journal of Membrane Biology, 101: 119-131.
    • (1988) Journal of Membrane Biology , vol.101 , pp. 119-131
    • Arellano, R.O.1    Ramón, F.2    Rivera, A.3    Zampighi, G.A.4
  • 64
    • 0024496650 scopus 로고
    • Ultracytochemistry of calmodulin binding sites in myocardial cells by staining of frozen thin sections with colloidal gold-labeled calmodulin
    • Fujimoto K, Araki N, Ogawa K-S, Kondo S, Kitaoka T & Ogawa K (1989). Ultracytochemistry of calmodulin binding sites in myocardial cells by staining of frozen thin sections with colloidal gold-labeled calmodulin. Journal of Histochemistry and Cytochemistry, 37: 249-256.
    • (1989) Journal of Histochemistry and Cytochemistry , vol.37 , pp. 249-256
    • Fujimoto, K.1    Araki, N.2    Ogawa, K.-S.3    Kondo, S.4    Kitaoka, T.5    Ogawa, K.6
  • 67
    • 0025155347 scopus 로고
    • Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines
    • Musil LS, Cunningham BA, Edelman GM & Goodenough DA (1990). Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines. Journal of Cell Biology, 111: 2077-2088.
    • (1990) Journal of Cell Biology , vol.111 , pp. 2077-2088
    • Musil, L.S.1    Cunningham, B.A.2    Edelman, G.M.3    Goodenough, D.A.4
  • 68
    • 0013975093 scopus 로고
    • +-induced anomalous rectification in squid giant axons
    • +-induced anomalous rectification in squid giant axons. Journal of General Physiology, 50: 491-503.
    • (1966) Journal of General Physiology , vol.50 , pp. 491-503
    • Armstrong, C.M.1
  • 69
    • 0025245612 scopus 로고
    • Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB
    • Zagotta WN, Hoshi T & Aldrich RW (1990). Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science, 250: 568-571.
    • (1990) Science , vol.250 , pp. 568-571
    • Zagotta, W.N.1    Hoshi, T.2    Aldrich, R.W.3
  • 70
    • 0030050142 scopus 로고    scopus 로고
    • Intramolecular interactions mediate pH regulation of connexin43 channels
    • Morley GE, Taffet SM & Delmar M (1996). Intramolecular interactions mediate pH regulation of connexin43 channels. Biophysical Journal, 70: 1294-1302.
    • (1996) Biophysical Journal , vol.70 , pp. 1294-1302
    • Morley, G.E.1    Taffet, S.M.2    Delmar, M.3
  • 73
    • 0343453471 scopus 로고    scopus 로고
    • Molecular domains relevant for chemical gating in gap junction channels made of connexin32
    • Abstract
    • Wang XG & Peracchia C (1996). Molecular domains relevant for chemical gating in gap junction channels made of connexin32. Molecular Biology of the Cell, 7: 462 (Abstract).
    • (1996) Molecular Biology of the Cell , vol.7 , pp. 462
    • Wang, X.G.1    Peracchia, C.2
  • 74
    • 0029961752 scopus 로고    scopus 로고
    • Chimeric evidence for a role of the connexin cytoplasmic loop in gap junction channel gating
    • Wang XG, Li LQ, Peracchia LL & Peracchia C (1996). Chimeric evidence for a role of the connexin cytoplasmic loop in gap junction channel gating. Pflügers Archiv, 431: 844-852.
    • (1996) Pflügers Archiv , vol.431 , pp. 844-852
    • Wang, X.G.1    Li, L.Q.2    Peracchia, L.L.3    Peracchia, C.4
  • 75
    • 0000909950 scopus 로고    scopus 로고
    • Connexin32/38 chimeras suggest a role for the second half of the inner loop in gap junction gating by low pH
    • Wang XG & Peracchia C (1996). Connexin32/38 chimeras suggest a role for the second half of the inner loop in gap junction gating by low pH. American Journal of Physiology, 271: C1743-C1749.
    • (1996) American Journal of Physiology , vol.271
    • Wang, X.G.1    Peracchia, C.2
  • 76
    • 0025246161 scopus 로고
    • Structure-activity relations of the cardiac gap junction channel
    • Spray DC & Burt JM (1990). Structure-activity relations of the cardiac gap junction channel. American Journal of Physiology, 258: C195-C205.
    • (1990) American Journal of Physiology , vol.258
    • Spray, D.C.1    Burt, J.M.2
  • 77
    • 0028284598 scopus 로고
    • Role of histidine 95 on pH gating of the cardiac gap junction protein connexin43
    • Ek JF, Delmar M, Perzova R & Taffet SM (1994). Role of histidine 95 on pH gating of the cardiac gap junction protein connexin43. Circulation Research, 74: 1058-1064.
    • (1994) Circulation Research , vol.74 , pp. 1058-1064
    • Ek, J.F.1    Delmar, M.2    Perzova, R.3    Taffet, S.M.4
  • 78
    • 0342583569 scopus 로고    scopus 로고
    • The role of histidine residues on pH sensitivity of the gap junction protein connexin 43
    • Abstract
    • Hermans MMP, Kortekaas P, Jongsma HJ & Rook MB (1996). The role of histidine residues on pH sensitivity of the gap junction protein connexin 43. Molecular Biology of the Cell, 7: 91 (Abstract).
    • (1996) Molecular Biology of the Cell , vol.7 , pp. 91
    • Hermans, M.M.P.1    Kortekaas, P.2    Jongsma, H.J.3    Rook, M.B.4
  • 80
    • 2542570658 scopus 로고    scopus 로고
    • Is connexin cooperativity necessary for chemical gating of gap junction channels?
    • Wang XG & Peracchia C (1997). Is connexin cooperativity necessary for chemical gating of gap junction channels? Biophysical Journal, 72: A 292.
    • (1997) Biophysical Journal , vol.72
    • Wang, X.G.1    Peracchia, C.2


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