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Volumn 435, Issue 3, 2011, Pages 711-722

Molecular interaction and functional regulation of connexin50 gap junctions by calmodulin

Author keywords

Calcium; Calmodulin; Connexin50; Gap junction; Junctional conductance; Protein protein interaction

Indexed keywords

CALCIUM ION; CALMIDAZOLIUM; CALMODULIN; CONNEXIN 43; CONNEXIN 46; CONNEXIN 50; GAP JUNCTION PROTEIN; UNCLASSIFIED DRUG;

EID: 79954540639     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101726     Document Type: Article
Times cited : (42)

References (61)
  • 1
    • 0029974655 scopus 로고    scopus 로고
    • Connections with connexins: The molecular basis of direct intercellular signaling
    • Bruzzone, R., White, T. W. and Paul, D. L. (1996) Connections with connexins: the molecular basis of direct intercellular signaling. Eur. J. Biochem. 238, 1-27
    • (1996) Eur. J. Biochem. , vol.238 , pp. 1-27
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 2
    • 0035991948 scopus 로고    scopus 로고
    • Gap junctions: Structure and function
    • Evans, W. H. and Martin, P. E. (2002) Gap junctions: structure and function. Mol. Membr. Biol. 19, 121-136
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 121-136
    • Evans, W.H.1    Martin, P.E.2
  • 4
    • 0025181954 scopus 로고
    • Mammalian lens inter-fiber resistance is modulated by calcium and calmodulin
    • Gandolfi, S. A., Duncan, G., Tomlinson, J. and Maraini, G. (1990) Mammalian lens inter-fiber resistance is modulated by calcium and calmodulin. Curr. Eye Res. 9, 533-541
    • (1990) Curr. Eye Res. , vol.9 , pp. 533-541
    • Gandolfi, S.A.1    Duncan, G.2    Tomlinson, J.3    Maraini, G.4
  • 5
    • 0027930117 scopus 로고
    • Micromolar levels of intracellular calcium reduce gap junctional permeability in lens cultures
    • Crow, J. M., Atkinson, M. M. and Johnson, R. G. (1994) Micromolar levels of intracellular calcium reduce gap junctional permeability in lens cultures. Invest. Ophthalmol. Visual Sci. 35, 3332-3341
    • (1994) Invest. Ophthalmol. Visual Sci. , vol.35 , pp. 3332-3341
    • Crow, J.M.1    Atkinson, M.M.2    Johnson, R.G.3
  • 7
    • 0242426633 scopus 로고    scopus 로고
    • Calmodulin and protein kinase C regulate gap junctional coupling in lens epithelial cells
    • Lurtz, M. M. and Louis, C. F. (2003) Calmodulin and protein kinase C regulate gap junctional coupling in lens epithelial cells. Am. J. Physiol. Cell Physiol. 285, C1475-C1482
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Lurtz, M.M.1    Louis, C.F.2
  • 9
    • 0030773116 scopus 로고    scopus 로고
    • Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains
    • Török, K., Stauffer, K. and Evans, W. H. (1997) Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains. Biochem. J. 326, 479-483
    • (1997) Biochem. J. , vol.326 , pp. 479-483
    • Török, K.1    Stauffer, K.2    Evans, W.H.3
  • 10
    • 55249113183 scopus 로고    scopus 로고
    • Calmodulin association with connexin32-derived peptides suggests trans-domain interaction in chemical gating of gap junction channels
    • Dodd, R., Peracchia, C., Stolady, D. and Török, K. (2008) Calmodulin association with connexin32-derived peptides suggests trans-domain interaction in chemical gating of gap junction channels. J. Biol. Chem. 283, 26911-26920
    • (2008) J. Biol. Chem. , vol.283 , pp. 26911-26920
    • Dodd, R.1    Peracchia, C.2    Stolady, D.3    Török, K.4
  • 13
    • 0037399919 scopus 로고    scopus 로고
    • CaMBOT: Profiling and characterizing calmodulin-binding proteins
    • O'Day, D. H. (2003) CaMBOT: profiling and characterizing calmodulin-binding proteins. Cell. Signalling 15, 347-354
    • (2003) Cell. Signalling , vol.15 , pp. 347-354
    • O'Day, D.H.1
  • 15
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones, D. T., Taylor, W. R. and Thornton, J. M. (1994) A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry 33, 3038-3049
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 16
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G. and Sonnhammer, E. L. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305, 567-580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 17
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnady, G. E. and Simon, I. (1998) Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J. Mol. Biol. 283, 489-506
    • (1998) J. Mol. Biol. , vol.283 , pp. 489-506
    • Tusnady, G.E.1    Simon, I.2
  • 18
    • 0000207681 scopus 로고
    • TMbase: A database of membrane spanning protein segments
    • Hofmann, K. and Stoffel, W. (1993) TMbase: a database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 374, 166
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 19
    • 0035999985 scopus 로고    scopus 로고
    • Amphiphilicity index index of polar amino acids as an aid in the characterization of amino acid preference at membrane-water interfaces
    • Mitaku, S., Hirokawa, T. and Tsuji, T. (2002) Amphiphilicity index of polar amino acids as an aid in the characterization of amino acid preference at membrane-water interfaces. Bioinformatics 18, 608-616 (Pubitemid 34521049)
    • (2002) Bioinformatics , vol.18 , Issue.4 , pp. 608-616
    • Mitaku, S.1    Hirokawa, T.2    Tsuji, T.3
  • 20
    • 0032570779 scopus 로고    scopus 로고
    • Do transmembrane protein superfolds exist?
    • Jones, D. T. (1998) Do transmembrane protein superfolds exist? FEBS Lett. 423, 281-285
    • (1998) FEBS Lett. , vol.423 , pp. 281-285
    • Jones, D.T.1
  • 21
    • 0034786532 scopus 로고    scopus 로고
    • The HMMTOP transmembrane topology prediction server
    • Tusnady, G. E. and Simon, I. (2001) The HMMTOP transmembrane topology prediction server. Bioinformatics 17, 849-850 (Pubitemid 32970487)
    • (2001) Bioinformatics , vol.17 , Issue.9 , pp. 849-850
    • Tusnady, G.E.1    Simon, I.2
  • 22
    • 0020549669 scopus 로고
    • A fluorescent calmodulin that reports the binding of hydrophobic inhibitory ligands
    • Johnson, J. D. and Wittenauer, L. A. (1983) A fluorescent calmodulin that reports the binding of hydrophobic inhibitory ligands. Biochem. J. 211, 473-479
    • (1983) Biochem. J. , vol.211 , pp. 473-479
    • Johnson, J.D.1    Wittenauer, L.A.2
  • 24
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 25
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D. K., Grimshaw, S. B., Receveur, V., Dobson, C. M., Jones, J. A. and Smith, L. J. (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 38, 16424-16431
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 26
    • 0037194384 scopus 로고    scopus 로고
    • Isolated EF-loop III of calmodulin in a scaffold protein remains unpaired in solution using pulsed-field-gradient NMR spectroscopy
    • Lee, H. W., Yang, W., Ye, Y., Liu, Z. R., Glushka, J. and Yang, J. J. (2002) Isolated EF-loop III of calmodulin in a scaffold protein remains unpaired in solution using pulsed-field-gradient NMR spectroscopy. Biochim. Biophys. Acta 1598, 80-87
    • (2002) Biochim. Biophys. Acta , vol.1598 , pp. 80-87
    • Lee, H.W.1    Yang, W.2    Ye, Y.3    Liu, Z.R.4    Glushka, J.5    Yang, J.J.6
  • 27
    • 0042936805 scopus 로고
    • Self-diffusion in normal and heavy water in the range 1-45°
    • Mills, R. (1973) Self-diffusion in normal and heavy water in the range 1-45°. J. Phys. Chem. 77, 685-688
    • (1973) J. Phys. Chem. , vol.77 , pp. 685-688
    • Mills, R.1
  • 28
    • 0019874687 scopus 로고
    • Preparation of a fluorescent-labeled derivative of calmodulin which retains its affinity for calmodulin binding proteins
    • LaPorte, D. C., Keller, C. H., Olwin, B. B. and Storm, D. R. (1981) Preparation of a fluorescent-labeled derivative of calmodulin which retains its affinity for calmodulin binding proteins. Biochemistry 20, 3965-3972
    • (1981) Biochemistry , vol.20 , pp. 3965-3972
    • LaPorte, D.C.1    Keller, C.H.2    Olwin, B.B.3    Storm, D.R.4
  • 29
    • 37849028920 scopus 로고    scopus 로고
    • The neuronal voltage-dependent sodium channel type II IQ motif lowers the calcium affinity of the C-domain of calmodulin
    • Theoharis, N. T., Sorensen, B. R., Theisen-Toupal, J. and Shea, M. A. (2008) The neuronal voltage-dependent sodium channel type II IQ motif lowers the calcium affinity of the C-domain of calmodulin. Biochemistry 47, 112-123
    • (2008) Biochemistry , vol.47 , pp. 112-123
    • Theoharis, N.T.1    Sorensen, B.R.2    Theisen-Toupal, J.3    Shea, M.A.4
  • 30
    • 0036841137 scopus 로고    scopus 로고
    • Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence
    • VanScyoc, W. S., Sorensen, B. R., Rusinova, E., Laws, W. R., Ross, J. B. and Shea, M. A. (2002) Calcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence. Biophys. J. 83, 2767-2780
    • (2002) Biophys. J. , vol.83 , pp. 2767-2780
    • VanScyoc, W.S.1    Sorensen, B.R.2    Rusinova, E.3    Laws, W.R.4    Ross, J.B.5    Shea, M.A.6
  • 31
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L. and Wallace, B. A. (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-W673
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 32
    • 0028873081 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • Munoz, V. and Serrano, L. (1995) Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. J. Mol. Biol. 245, 275-296
    • (1995) J. Mol. Biol. , vol.245 , pp. 275-296
    • Munoz, V.1    Serrano, L.2
  • 33
    • 0028834210 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence
    • Munoz, V. and Serrano, L. (1995) Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence. J. Mol. Biol. 245, 297-308
    • (1995) J. Mol. Biol. , vol.245 , pp. 297-308
    • Munoz, V.1    Serrano, L.2
  • 34
    • 0028447768 scopus 로고
    • Elucidating the folding problem of helical peptides using empirical parameters
    • Munoz, V. and Serrano, L. (1994) Elucidating the folding problem of helical peptides using empirical parameters. Nat. Struct. Biol. 1, 399-409
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 399-409
    • Munoz, V.1    Serrano, L.2
  • 35
    • 0030609908 scopus 로고    scopus 로고
    • 2+-dependent interaction with calmodulin is conserved in the synapsin family: Identification of a high-affinity site
    • DOI 10.1021/bi970709r
    • Nicol, S., Rahman, D. and Baines, A. J. (1997) Ca2+-dependent interaction with calmodulin is conserved in the synapsin family: identification of a high-affinity site. Biochemistry 36, 11487-11495 (Pubitemid 27408632)
    • (1997) Biochemistry , vol.36 , Issue.38 , pp. 11487-11495
    • Nicol, S.1    Rahman, D.2    Baines, A.J.3
  • 37
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador, W. E., Means, A. R. and Quiocho, F. A. (1993) Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262, 1718-1721
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 38
    • 4444270810 scopus 로고    scopus 로고
    • The role of electrostatic interactions in calmodulin-peptide complex formation
    • DOI 10.1529/biophysj.104.040998
    • Andre, I., Kesvatera, T., Jonsson, B., Akerfeldt, K. S. and Linse, S. (2004) The role of electrostatic interactions in calmodulin-peptide complex formation. Biophys. J. 87, 1929-1938 (Pubitemid 39167047)
    • (2004) Biophysical Journal , vol.87 , Issue.3 , pp. 1929-1938
    • Andre, I.1    Kesvatera, T.2    Jonsson, B.3    Akerfeldt, K.S.4    Linse, S.5
  • 39
    • 37149018110 scopus 로고    scopus 로고
    • Intracellular calcium regulation of connexin43
    • Lurtz, M. M. and Louis, C. F. (2007) Intracellular calcium regulation of connexin43. Am. J. Physiol. Cell Physiol. 293, C1806-C1813
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Lurtz, M.M.1    Louis, C.F.2
  • 40
    • 0033854573 scopus 로고    scopus 로고
    • Molecular cloning of ovine connexin44 and temporal expression of gap junction proteins in a lens cell culture
    • Yang, D. I. and Louis, C. F. (2000) Molecular cloning of ovine connexin44 and temporal expression of gap junction proteins in a lens cell culture. Invest. Ophthalmol. Visual Sci. 41, 2658-2664
    • (2000) Invest. Ophthalmol. Visual Sci. , vol.41 , pp. 2658-2664
    • Yang, D.I.1    Louis, C.F.2
  • 41
    • 0026688138 scopus 로고
    • Calmidazolium, a calmodulin inhibitor, inhibits endothelium-dependent relaxations resistant to nitro-L-arginine in the canine coronary artery
    • Illiano, S., Nagao, T. and Vanhoutte, P. M. (1992) Calmidazolium, a calmodulin inhibitor, inhibits endothelium-dependent relaxations resistant to nitro-L-arginine in the canine coronary artery. Br. J. Pharmacol. 107, 387-392
    • (1992) Br. J. Pharmacol. , vol.107 , pp. 387-392
    • Illiano, S.1    Nagao, T.2    Vanhoutte, P.M.3
  • 42
    • 0037256228 scopus 로고    scopus 로고
    • NMR methods for the determination of protein-ligand dissociation constants
    • Fielding, L. (2003) NMR methods for the determination of protein-ligand dissociation constants. Curr. Top. Med. Chem. 3, 39-53
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 39-53
    • Fielding, L.1
  • 43
    • 0037307080 scopus 로고    scopus 로고
    • Protein conformational changes studied by diffusion NMR spectroscopy: Application to helix-loop-helix calcium binding proteins
    • DOI 10.1110/ps.0226203
    • Weljie, A. M., Yamniuk, A. P., Yoshino, H., Izumi, Y. and Vogel, H. J. (2003) Protein conformational changes studied by diffusion NMR spectroscopy: application to helix-loop-helix calcium binding proteins. Protein Sci. 12, 228-236 (Pubitemid 36120335)
    • (2003) Protein Science , vol.12 , Issue.2 , pp. 228-236
    • Weljie, A.M.1    Yamniuk, A.P.2    Yoshino, H.3    Izumi, Y.4    Vogel, H.J.5
  • 45
    • 0023786585 scopus 로고
    • Rotational dynamics of the single tryptophan of porcine pancreatic phospholipase A2, its zymogen, and an enzyme/micelle complex: A steady-state and time-resolved anisotropy study
    • Ludescher, R. D., Johnson, I. D., Volwerk, J. J., de Haas, G. H., Jost, P. C. and Hudson, B. S. (1988) Rotational dynamics of the single tryptophan of porcine pancreatic phospholipase A2, its zymogen, and an enzyme/micelle complex: a steady-state and time-resolved anisotropy study. Biochemistry 27, 6618-6628
    • (1988) Biochemistry , vol.27 , pp. 6618-6628
    • Ludescher, R.D.1    Johnson, I.D.2    Volwerk, J.J.3    De Haas, G.H.4    Jost, P.C.5    Hudson, B.S.6
  • 46
    • 0028025010 scopus 로고
    • Selective dye and ionic permeability of gap junction channels formed by connexin45
    • Veenstra, R. D., Wang, H. Z., Beyer, E. C. and Brink, P. R. (1994) Selective dye and ionic permeability of gap junction channels formed by connexin45. Circ. Res. 75, 483-490
    • (1994) Circ. Res. , vol.75 , pp. 483-490
    • Veenstra, R.D.1    Wang, H.Z.2    Beyer, E.C.3    Brink, P.R.4
  • 47
    • 0029095038 scopus 로고
    • Unique conductance, gating, and selective permeability properties of gap junction channels formed by connexin40
    • Beblo, D. A., Wang, H. Z., Beyer, E. C., Westphale, E. M. and Veenstra, R. D. (1995) Unique conductance, gating, and selective permeability properties of gap junction channels formed by connexin40. Circ. Res. 77, 813-822
    • (1995) Circ. Res. , vol.77 , pp. 813-822
    • Beblo, D.A.1    Wang, H.Z.2    Beyer, E.C.3    Westphale, E.M.4    Veenstra, R.D.5
  • 48
    • 0026722204 scopus 로고
    • Reconstitution of channels from preparations enriched in lens gap junction protein MP70
    • Donaldson, P. and Kistler, J. (1992) Reconstitution of channels from preparations enriched in lens gap junction protein MP70. J. Membr. Biol. 129, 155-165
    • (1992) J. Membr. Biol. , vol.129 , pp. 155-165
    • Donaldson, P.1    Kistler, J.2
  • 49
    • 0033564511 scopus 로고    scopus 로고
    • Voltage dependence of macroscopic and unitary currents of gap junction channels formed by mouse connexin50 expressed in rat neuroblastoma cells
    • Srinivas, M., Costa, M., Gao, Y., Fort, A., Fishman, G. I. and Spray, D. C. (1999) Voltage dependence of macroscopic and unitary currents of gap junction channels formed by mouse connexin50 expressed in rat neuroblastoma cells. J. Physiol. 517, 673-689
    • (1999) J. Physiol. , vol.517 , pp. 673-689
    • Srinivas, M.1    Costa, M.2    Gao, Y.3    Fort, A.4    Fishman, G.I.5    Spray, D.C.6
  • 50
    • 0037087452 scopus 로고    scopus 로고
    • Functional role of the carboxyl terminal domain of human connexin 50 in gap junctional channels
    • Xu, X., Berthoud, V. M., Beyer, E. C. and Ebihara, L. (2002) Functional role of the carboxyl terminal domain of human connexin 50 in gap junctional channels. J. Membr. Biol. 186, 101-112
    • (2002) J. Membr. Biol. , vol.186 , pp. 101-112
    • Xu, X.1    Berthoud, V.M.2    Beyer, E.C.3    Ebihara, L.4
  • 51
    • 0031132747 scopus 로고    scopus 로고
    • Connexin domains relevant to the chemical gating of gap junction channels
    • Peracchia, C. and Wang, X. C. (1997) Connexin domains relevant to the chemical gating of gap junction channels. Braz. J. Med. Biol. Res. 30, 577-590
    • (1997) Braz. J. Med. Biol. Res. , vol.30 , pp. 577-590
    • Peracchia, C.1    Wang, X.C.2
  • 52
    • 55249113183 scopus 로고    scopus 로고
    • Calmodulin association with connexin32-derived peptides suggests trans-domain interaction in chemical gating of gap junction channels
    • Dodd, R., Peracchia, C., Stolady, D. and Török, K. (2008) Calmodulin association with connexin32-derived peptides suggests trans-domain interaction in chemical gating of gap junction channels. J. Biol. Chem. 283, 26911-26920
    • (2008) J. Biol. Chem. , vol.283 , pp. 26911-26920
    • Dodd, R.1    Peracchia, C.2    Stolady, D.3    Török, K.4
  • 53
    • 0034826706 scopus 로고    scopus 로고
    • Assembly of gap junction channels: Mechanism, effects of calmodulin antagonists and identification of connexin oligomerization determinants
    • Ahmad, S., Martin, P. E. and Evans, W. H. (2001) Assembly of gap junction channels: mechanism, effects of calmodulin antagonists and identification of connexin oligomerization determinants. Eur. J. Biochem. 268, 4544-4552
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4544-4552
    • Ahmad, S.1    Martin, P.E.2    Evans, W.H.3
  • 54
    • 0037623211 scopus 로고    scopus 로고
    • Calmodulin antagonists suppress gap junction coupling in isolated Hensen cells of the guinea pig cochlea
    • Blodow, A., Ngezahayo, A., Ernst, A. and Kolb, H. A. (2003) Calmodulin antagonists suppress gap junction coupling in isolated Hensen cells of the guinea pig cochlea. Pflügers Arch. 446, 36-41
    • (2003) Pflügers Arch. , vol.446 , pp. 36-41
    • Blodow, A.1    Ngezahayo, A.2    Ernst, A.3    Kolb, H.A.4
  • 56
    • 0036218448 scopus 로고    scopus 로고
    • Hemichannel and junctional properties of connexin 50
    • Beahm, D. L. and Hall, J. E. (2002) Hemichannel and junctional properties of connexin 50. Biophys. J. 82, 2016-2031
    • (2002) Biophys. J. , vol.82 , pp. 2016-2031
    • Beahm, D.L.1    Hall, J.E.2
  • 57
    • 48449089054 scopus 로고    scopus 로고
    • Site-directed mutagenesis reveals putative regions of protein interaction within the transmembrane domains of connexins
    • Toloue, M. M., Woolwine, Y., Karcz, J. A., Kasperek, E. M., Nicholson, B. J. and Skerett, I. M. (2008) Site-directed mutagenesis reveals putative regions of protein interaction within the transmembrane domains of connexins. Cell Commun. Adhes. 15, 95-105
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 95-105
    • Toloue, M.M.1    Woolwine, Y.2    Karcz, J.A.3    Kasperek, E.M.4    Nicholson, B.J.5    Skerett, I.M.6
  • 60
    • 34547224262 scopus 로고    scopus 로고
    • Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule
    • Oshima, A., Tani, K., Hiroaki, Y., Fujiyoshi, Y. and Sosinsky, G. E. (2007) Three-dimensional structure of a human connexin26 gap junction channel reveals a plug in the vestibule. Proc. Natl. Acad. Sci. U.S.A. 104, 10034-10039
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 10034-10039
    • Oshima, A.1    Tani, K.2    Hiroaki, Y.3    Fujiyoshi, Y.4    Sosinsky, G.E.5
  • 61
    • 0034107588 scopus 로고    scopus 로고
    • Chemical gating of gap junction channels
    • Peracchia, C., Wang, X. G. and Peracchia, L. L. (2000) Chemical gating of gap junction channels. Methods 20, 188-195
    • (2000) Methods , vol.20 , pp. 188-195
    • Peracchia, C.1    Wang, X.G.2    Peracchia, L.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.