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Volumn 141, Issue 2, 2013, Pages 243-259

Voltage-dependent gating of the C×32*43E1 hemichannel: Conformational changes at the channel entrances

Author keywords

[No Author keywords available]

Indexed keywords

CONNEXIN 32; GAP JUNCTION PROTEIN;

EID: 84874742226     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210839     Document Type: Article
Times cited : (23)

References (58)
  • 1
    • 0034027222 scopus 로고    scopus 로고
    • Mutations in connexin 32: the molecular and biophysical bases for the X-linked form of Charcot-Marie-Tooth disease
    • Abrams, C.K., S. Oh, Y. Ri, and T.A. Bargiello.; 2000. Mutations in connexin 32: the molecular and biophysical bases for the X-linked form of Charcot-Marie-Tooth disease. Brain Res. Brain Res. Rev. 32:203-214. http://dx.doi.org/10.1016/S0165-0173(99)00082-X.
    • (2000) Brain Res. Brain Res. Rev. , vol.32 , pp. 203-214
    • Abrams, C.K.1    Oh, S.2    Ri, Y.3    Bargiello, T.A.4
  • 2
    • 0037133669 scopus 로고    scopus 로고
    • Voltage opens unopposed gap junction hemichannels formed by a connexin 32 mutant associated with X-linked Charcot-Marie-Tooth disease
    • USA
    • Abrams, C.K., M.V.L. Bennett, V.K. Verselis, and T.A. Bargiello.;2002. Voltage opens unopposed gap junction hemichannels formed by a connexin 32 mutant associated with X-linked Charcot-Marie-Tooth disease. Proc. Natl. Acad. Sci. USA. 99:3980-3984. http://dx.doi.org/10.1073/pnas.261713499.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 3980-3984
    • Abrams, C.K.1    Bennett, M.V.L.2    Verselis, V.K.3    Bargiello, T.A.4
  • 3
    • 84861625594 scopus 로고    scopus 로고
    • Gap junctions in inherited human disorders of the central nervous system
    • Abrams, C.K., and S.S. Scherer.;2012. Gap junctions in inherited human disorders of the central nervous system. Biochim. Biophys. Acta. 1818:2030-2047. http://dx.doi.org/10.1016/j.bbamem.2011.08.015.
    • (2012) Biochim. Biophys. Acta. , vol.1818 , pp. 2030-2047
    • Abrams, C.K.1    Scherer, S.S.2
  • 4
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M.H., D.A. Stauffer, M. Xu, and A. Karlin.; 1992. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science. 258:307-310. http://dx.doi.org/10.1126/science.1384130.
    • (1992) Science. , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 5
    • 79959332086 scopus 로고    scopus 로고
    • Atomic force microscopy of Connexin40 gap junction hemichannels reveals calcium-dependent three-dimensional molecular topography and open-closed conformations of both the extracellular and cytoplasmic faces
    • Allen, M.J., J. Gemel, E.C. Beyer, and R. Lal.;2011. Atomic force microscopy of Connexin40 gap junction hemichannels reveals calcium-dependent three-dimensional molecular topography and open-closed conformations of both the extracellular and cytoplasmic faces. J. Biol. Chem. 286:22139-22146. http://dx.doi.org/10.1074/jbc.M111.240002.
    • (2011) J. Biol. Chem. , vol.286 , pp. 22139-22146
    • Allen, M.J.1    Gemel, J.2    Beyer, E.C.3    Lal, R.4
  • 6
    • 84982336984 scopus 로고
    • Pyridinderivate als Komplexbildner VIII Die Herstellung je eines neuen vier- und sechszähnigen Liganden
    • Anderegg, G., and F. Wenk.; 1967. Pyridinderivate als Komplexbildner VIII Die Herstellung je eines neuen vier- und sechszähnigen Liganden. Helv. Chim. Acta. 50:2330-2332. http://dx.doi.org/10.1002/hlca.19670500817.
    • (1967) Helv. Chim. Acta. , vol.50 , pp. 2330-2332
    • Anderegg, G.1    Wenk, F.2
  • 7
    • 0021895141 scopus 로고
    • Cytosolic Ca2+ homeostasis in Ehrlich and Yoshida carcinomas. A new, membrane-permeant chelator of heavy metals reveals that these ascites tumor cell lines have normal cytosolic free Ca2+
    • Arslan, P., F. Di Virgilio, M. Beltrame, R.Y. Tsien, and T. Pozzan.; 1985. Cytosolic Ca2+ homeostasis in Ehrlich and Yoshida carcinomas. A new, membrane-permeant chelator of heavy metals reveals that these ascites tumor cell lines have normal cytosolic free Ca2+. J. Biol. Chem. 260:2719-2727.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2719-2727
    • Arslan, P.1    Di Virgilio, F.2    Beltrame, M.3    Tsien, R.Y.4    Pozzan, T.5
  • 9
    • 84861618268 scopus 로고    scopus 로고
    • Voltage-dependent conformational changes in connexin channels. Biochim. Biophys
    • Bargiello, T.A., Q. Tang, S. Oh, and T. Kwon.; 2012. Voltage-dependent conformational changes in connexin channels. Biochim. Biophys. Acta. 1818:1807-1822. http://dx.doi.org/10.1016/j.bbamem.2011.09.019.
    • (2012) Acta. , vol.1818 , pp. 1807-1822
    • Bargiello, T.A.1    Tang, Q.2    Oh, S.3    Kwon, T.4
  • 10
    • 0026014463 scopus 로고
    • Gap junctions formed by connexins 26 and 32 alone and in combination are differently affected by applied voltage
    • USA
    • Barrio, L.C., T. Suchyna, T. Bargiello, L.X. Xu, R.S. Roginski, M.V. Bennett, and B.J. Nicholson.;1991. Gap junctions formed by connexins 26 and 32 alone and in combination are differently affected by applied voltage. Proc. Natl. Acad. Sci. USA. 88:8410-8414. http://dx.doi.org/10.1073/pnas.88.19.8410.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 8410-8414
    • Barrio, L.C.1    Suchyna, T.2    Bargiello, T.3    Xu, L.X.4    Roginski, R.S.5    Bennett, M.V.6    Nicholson, B.J.7
  • 12
    • 0001548495 scopus 로고
    • The stability constants of metal complexes of amino acids with polar side chains. Pure Appl
    • Berthon, G. 1995. The stability constants of metal complexes of amino acids with polar side chains. Pure Appl. Chem. 67:1117-1240. http://dx.doi.org/10.1351/pac199567071117.
    • (1995) Chem. , vol.67 , pp. 1117-1240
    • Berthon, G.1
  • 13
    • 33244478285 scopus 로고    scopus 로고
    • Selective defects in channel permeability associated with Cx32 mutations causing X-linked Charcot-Marie-Tooth disease
    • Bicego, M., S. Morassutto, V.H. Hernandez, M. Morgutti, F. Mammano, P. D'Andrea, and R. Bruzzone. 2006. Selective defects in channel permeability associated with Cx32 mutations causing X-linked Charcot-Marie-Tooth disease. Neurobiol. Dis. 21:607-617. http://dx.doi.org/10.1016/j.nbd.2005.09.005.
    • (2006) Neurobiol. Dis. , vol.21 , pp. 607-617
    • Bicego, M.1    Morassutto, S.2    Hernandez, V.H.3    Morgutti, M.4    Mammano, F.5    D'Andrea, P.6    Bruzzone, R.7
  • 14
    • 1642273067 scopus 로고    scopus 로고
    • Gap junction channel gating
    • Bukauskas, F.F., and V.K. Verselis.;2004. Gap junction channel gating. Biochim. Biophys. Acta. 1662:42-60. http://dx.doi.org/10.1016/j.bbamem.2004.01.008.
    • (2004) Biochim. Biophys. Acta. , vol.1662 , pp. 42-60
    • Bukauskas, F.F.1    Verselis, V.K.2
  • 15
    • 58149092631 scopus 로고    scopus 로고
    • Connexin-caused genetic diseases and corresponding mouse models
    • Dobrowolski, R., and K. Willecke.; 2009. Connexin-caused genetic diseases and corresponding mouse models. Antioxid. Redox Signal. 11:283-295. http://dx.doi.org/10.1089/ars.2008.2128.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 283-295
    • Dobrowolski, R.1    Willecke, K.2
  • 16
    • 0037214571 scopus 로고    scopus 로고
    • Effect of external magnesium and calcium on human connexin46 hemichannels
    • Ebihara, L., X. Liu, and J.D. Pal.; 2003. Effect of external magnesium and calcium on human connexin46 hemichannels. Biophys. J. 84:277-286. http://dx.doi.org/10.1016/S0006-3495 (03)74848-6.
    • (2003) Biophys. J. , vol.84 , pp. 277-286
    • Ebihara, L.1    Liu, X.2    Pal, J.D.3
  • 17
    • 15544369856 scopus 로고    scopus 로고
    • Calcium-activated chloride channels: (un)known, (un)loved?
    • Proc. Am. Thorac. Soc.
    • Eggermont, J. 2004. Calcium-activated chloride channels: (un)known, (un)loved? Proc. Am. Thorac. Soc. 1:22-27. http://dx.doi.org/10.1513/pats.2306010.
    • (2004) , vol.1 , pp. 22-27
    • Eggermont, J.1
  • 19
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller, S.E., and A.D. MacKerell.;2000. An improved empirical potential energy function for molecular simulations of phospholipids. J. Phys. Chem. B. 104:7510-7515. http://dx.doi.org/10.1021/jp0007843.
    • (2000) J. Phys. Chem. B. , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerell, A.D.2
  • 21
    • 0035704411 scopus 로고    scopus 로고
    • Emerging issues of connexin channels: biophysics fills the gap
    • Harris, A.L.;2001. Emerging issues of connexin channels: biophysics fills the gap. Q. Rev. Biophys. 34:325-472.
    • (2001) Q. Rev. Biophys. , vol.34 , pp. 325-472
    • Harris, A.L.1
  • 22
    • 15244360606 scopus 로고    scopus 로고
    • Calcium-activated chloride channels
    • Hartzell, C., I. Putzier, and J. Arreola.; 2005. Calcium-activated chloride channels. Annu. Rev. Physiol. 67:719-758. http://dx.doi.org/10.1146/annurev.physiol.67.032003.154341.
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 719-758
    • Hartzell, C.1    Putzier, I.2    Arreola, J.3
  • 23
    • 0032168179 scopus 로고    scopus 로고
    • + channel can be trapped in the open state by an intersubunit metal bridge
    • + channel can be trapped in the open state by an intersubunit metal bridge. Neuron. 21:617-621. http://dx.doi.org/10.1016/S0896-6273(00)80571-1.
    • (1998) Neuron. , vol.21 , pp. 617-621
    • Holmgren, M.1    Shin, K.S.2    Yellen, G.3
  • 24
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • Karlin, A., and M.H. Akabas.;1998. Substituted-cysteine accessibility method. Methods Enzymol. 293:123-145. http://dx.doi.org/10.1016/S0076-6879(98)93011-7.
    • (1998) Methods Enzymol , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 25
    • 77952700991 scopus 로고    scopus 로고
    • Calculation of the gating charge for the Kv1.2 voltage-activated potassium channel
    • Khalili-Araghi, F., V. Jogini, V. Yarov-Yarovoy, E. Tajkhorshid, B. Roux, and K. Schulten.; 2010. Calculation of the gating charge for the Kv1.2 voltage-activated potassium channel. Biophys. J. 98:2189-2198. http://dx.doi.org/10.1016/j.bpj.2010.02.056.
    • (2010) Biophys. J. , vol.98 , pp. 2189-2198
    • Khalili-Araghi, F.1    Jogini, V.2    Yarov-Yarovoy, V.3    Tajkhorshid, E.4    Roux, B.5    Schulten, K.6
  • 26
    • 84855997898 scopus 로고    scopus 로고
    • Molecular dynamics investigation of the -current in the Kv1.2 voltage sensor domains
    • Khalili-Araghi, F., E. Tajkhorshid, B. Roux, and K. Schulten. 2012. Molecular dynamics investigation of the -current in the Kv1.2 voltage sensor domains. Biophys. J. 102:258-267. http://dx.doi.org/10.1016/j.bpj.2011.10.057.
    • (2012) Biophys. J. , vol.102 , pp. 258-267
    • Khalili-Araghi, F.1    Tajkhorshid, E.2    Roux, B.3    Schulten, K.4
  • 27
  • 28
    • 80555135976 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the C×26 hemichannel: evaluation of structural models with Brownian dynamics
    • Kwon, T., A.L. Harris, A. Rossi, and T.A. Bargiello.; 2011. Molecular dynamics simulations of the C×26 hemichannel: evaluation of structural models with Brownian dynamics. J. Gen. Physiol. 138:475-493. http://dx.doi.org/10.1085/jgp.201110679.
    • (2011) J. Gen. Physiol. , vol.138 , pp. 475-493
    • Kwon, T.1    Harris, A.L.2    Rossi, A.3    Bargiello, T.A.4
  • 29
    • 84858777446 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the C×26 hemichannel: insights into voltage-dependent loop-gating
    • Kwon, T., B. Roux, S. Jo, J.B. Klauda, A.L. Harris, and T.A. Bargiello.; 2012. Molecular dynamics simulations of the C×26 hemichannel: insights into voltage-dependent loop-gating. Biophys. J. 102:1341-1351. http://dx.doi.org/10.1016/j.bpj.2012.02.009.
    • (2012) Biophys. J. , vol.102 , pp. 1341-1351
    • Kwon, T.1    Roux, B.2    Jo, S.3    Klauda, J.B.4    Harris, A.L.5    Bargiello, T.A.6
  • 30
    • 75149159657 scopus 로고    scopus 로고
    • The gap junction proteome and its relationship to disease
    • Laird, D.W.;2010. The gap junction proteome and its relationship to disease. Trends Cell Biol. 20:92-101. http://dx.doi.org/10.1016/j.tcb.2009.11.001.
    • (2010) Trends Cell Biol. , vol.20 , pp. 92-101
    • Laird, D.W.1
  • 31
    • 63149198803 scopus 로고    scopus 로고
    • Connexin mutations causing skin disease and deafness increase hemichannel activity and cell death when expressed in Xenopus oocytes
    • Lee, J.R., A.M. Derosa, and T.W. White.;2009. Connexin mutations causing skin disease and deafness increase hemichannel activity and cell death when expressed in Xenopus oocytes. J. Invest. Dermatol. 129:870-878. http://dx.doi.org/10.1038/jid.2008.335.
    • (2009) J. Invest. Dermatol. , vol.129 , pp. 870-878
    • Lee, J.R.1    Derosa, A.M.2    White, T.W.3
  • 32
    • 63849141447 scopus 로고    scopus 로고
    • Structure of the connexin 26 gap junction channel at 3.5 A resolution
    • Maeda, S., S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara.; 2009. Structure of the connexin 26 gap junction channel at 3.5 A resolution. Nature. 458:597-602. http://dx.doi.org/10.1038/nature07869.
    • (2009) Nature. , vol.458 , pp. 597-602
    • Maeda, S.1    Nakagawa, S.2    Suga, M.3    Yamashita, E.4    Oshima, A.5    Fujiyoshi, Y.6    Tsukihara, T.7
  • 33
    • 0037040828 scopus 로고    scopus 로고
    • Role of the carboxyl terminal of connexin43 in transjunctional fast voltage gating
    • Moreno, A.P., M. Chanson, S. Elenes, J. Anumonwo, I. Scerri, H. Gu, S.M. Taffet, and M. Delmar.; 2002. Role of the carboxyl terminal of connexin43 in transjunctional fast voltage gating. Circ. Res. 90:450-457. http://dx.doi.org/10.1161/hh0402.105667.
    • (2002) Circ. Res. , vol.90 , pp. 450-457
    • Moreno, A.P.1    Chanson, M.2    Elenes, S.3    Anumonwo, J.4    Scerri, I.5    Gu, H.6    Taffet, S.M.7    Delmar, M.8
  • 34
    • 0037099393 scopus 로고    scopus 로고
    • Conformational changes in surface structures of isolated connexin 26 gap junctions
    • Müller, D.J., G.M. Hand, A. Engel, and G.E. Sosinsky.;2002. Conformational changes in surface structures of isolated connexin 26 gap junctions. EMBO J. 21:3598-3607. http://dx.doi.org/10.1093/emboj/cdf365.
    • (2002) EMBO J. , vol.21 , pp. 3598-3607
    • Müller, D.J.1    Hand, G.M.2    Engel, A.3    Sosinsky, G.E.4
  • 35
    • 16844385514 scopus 로고
    • Phenomenological Theory of Ion Solvation. Effective Radii of Hydrated Ions
    • Nightingale, E.R.;1959. Phenomenological Theory of Ion Solvation. Effective Radii of Hydrated Ions. J. Phys. Chem. 63:1381-1387. http://dx.doi.org/10.1021/j150579a011.
    • (1959) J. Phys. Chem. , vol.63 , pp. 1381-1387
    • Nightingale, E.R.1
  • 36
    • 0030777706 scopus 로고    scopus 로고
    • Changes in permeability caused by connexin 32 mutations underlie X-linked Charcot-Marie-Tooth disease
    • Oh, S., Y. Ri, M.V. Bennett, E.B. Trexler, V.K. Verselis, and T.A. Bargiello.;1997. Changes in permeability caused by connexin 32 mutations underlie X-linked Charcot-Marie-Tooth disease. Neuron. 19:927-938. http://dx.doi.org/10.1016/S0896-6273 (00)80973-3.
    • (1997) Neuron. , vol.19 , pp. 927-938
    • Oh, S.1    Ri, Y.2    Bennett, M.V.3    Trexler, E.B.4    Verselis, V.K.5    Bargiello, T.A.6
  • 37
    • 0033909785 scopus 로고    scopus 로고
    • Stoichiometry of transjunctional voltage-gating polarity reversal by a negative charge substitution in the amino terminus of a connexin32 chimera
    • Oh, S., C.K. Abrams, V.K. Verselis, and T.A. Bargiello.; 2000. Stoichiometry of transjunctional voltage-gating polarity reversal by a negative charge substitution in the amino terminus of a connexin32 chimera. J. Gen. Physiol. 116:13-31. http://dx.doi.org/10.1085/jgp.116.1.13.
    • (2000) J. Gen. Physiol. , vol.116 , pp. 13-31
    • Oh, S.1    Abrams, C.K.2    Verselis, V.K.3    Bargiello, T.A.4
  • 38
    • 4143088047 scopus 로고    scopus 로고
    • Determinants of gating polarity of a connexin 32 hemichannel
    • Oh, S., S. Rivkin, Q. Tang, V.K. Verselis, and T.A. Bargiello.;2004. Determinants of gating polarity of a connexin 32 hemichannel. Biophys. J. 87:912-928. http://dx.doi.org/10.1529/biophysj.103.038448.
    • (2004) Biophys. J. , vol.87 , pp. 912-928
    • Oh, S.1    Rivkin, S.2    Tang, Q.3    Verselis, V.K.4    Bargiello, T.A.5
  • 39
    • 0030895397 scopus 로고    scopus 로고
    • A chimeric connexin forming gap junction hemichannels
    • Pfahnl, A., X.W. Zhou, R. Werner, and G. Dahl.; 1997. A chimeric connexin forming gap junction hemichannels. Pflugers Arch. 433:773-779. http://dx.doi.org/10.1007/s004240050344.
    • (1997) Pflugers Arch. , vol.433 , pp. 773-779
    • Pfahnl, A.1    Zhou, X.W.2    Werner, R.3    Dahl, G.4
  • 40
    • 0032838486 scopus 로고    scopus 로고
    • Molecular dissection of transjunctional voltage dependence in the connexin-32 and connexin-43 junctions
    • Revilla, A., C. Castro, and L.C. Barrio. 1999. Molecular dissection of transjunctional voltage dependence in the connexin-32 and connexin-43 junctions. Biophys. J. 77:1374-1383. http://dx.doi.org/10.1016/S0006-3495(99)76986-9.
    • (1999) Biophys. J. , vol.77 , pp. 1374-1383
    • Revilla, A.1    Castro, C.2    Barrio, L.C.3
  • 41
    • 0026666944 scopus 로고
    • Molecular analysis of voltage dependence of heterotypic gap junctions formed by connexins 26 and 32
    • discussion: 193-195
    • Rubin, J.B., V.K. Verselis, M.V. Bennett, and T.A. Bargiello.; 1992. Molecular analysis of voltage dependence of heterotypic gap junctions formed by connexins 26 and 32. Biophys. J. 62:183-193, discussion: 193-195. http://dx.doi.org/10.1016/S0006-3495(92) 81804-0.
    • (1992) Biophys J. , vol.62 , pp. 183-193
    • Rubin, J.B.1    Verselis, V.K.2    Bennett, M.V.3    Bargiello, T.A.4
  • 42
    • 77954320871 scopus 로고    scopus 로고
    • 2+ permeability in C×26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome
    • 2+ permeability in C×26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome. J. Gen. Physiol. 136:47-62. http://dx.doi.org/10.1085/jgp.201010433.
    • (2010) J. Gen. Physiol. , vol.136 , pp. 47-62
    • Sánchez, H.A.1    Mese, G.2    Srinivas, M.3    White, T.W.4    Verselis, V.K.5
  • 43
    • 15744376289 scopus 로고    scopus 로고
    • Modifications in the biophysical properties of connexin43 channels by a peptide of the cytoplasmic loop region
    • Seki, A., H.S. Duffy, W. Coombs, D.C. Spray, S.M. Taffet, and M. Delmar.;2004. Modifications in the biophysical properties of connexin43 channels by a peptide of the cytoplasmic loop region. Circ. Res. 95:e22-e28. http://dx.doi.org/10.1161/01.RES.0000140737.62245.c5.
    • (2004) Circ. Res. , vol.95
    • Seki, A.1    Duffy, H.S.2    Coombs, W.3    Spray, D.C.4    Taffet, S.M.5    Delmar, M.6
  • 46
    • 20444397355 scopus 로고    scopus 로고
    • Structural organization of gap junction channels. Biochim. Biophys
    • Sosinsky, G.E., and B.J. Nicholson. 2005. Structural organization of gap junction channels. Biochim. Biophys. Acta. 1711:99-125. http://dx.doi.org/10.1016/j.bbamem.2005.04.001.
    • (2005) Acta. , vol.1711 , pp. 99-125
    • Sosinsky, G.E.1    Nicholson, B.J.2
  • 47
    • 66749118906 scopus 로고    scopus 로고
    • Conformational changes in a pore-forming region underlie voltage- dependent "loop gating" of an unapposed connexin hemichannel
    • Tang, Q., T.L. Dowd, V.K. Verselis, and T.A. Bargiello.;2009. Conformational changes in a pore-forming region underlie voltage- dependent "loop gating" of an unapposed connexin hemichannel. J. Gen. Physiol. 133:555-570. http://dx.doi.org/10.1085/jgp.200910207.
    • (2009) J. Gen. Physiol. , vol.133 , pp. 555-570
    • Tang, Q.1    Dowd, T.L.2    Verselis, V.K.3    Bargiello, T.A.4
  • 48
    • 15444367718 scopus 로고    scopus 로고
    • Calciumdependent open/closed conformations and interfacial energy maps of reconstituted hemichannels
    • Thimm, J., A. Mechler, H. Lin, S. Rhee, and R. Lal.;2005. Calciumdependent open/closed conformations and interfacial energy maps of reconstituted hemichannels. J. Biol. Chem. 280:10646-10654. http://dx.doi.org/10.1074/jbc.M412749200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10646-10654
    • Thimm, J.1    Mechler, A.2    Lin, H.3    Rhee, S.4    Lal, R.5
  • 49
    • 0029905253 scopus 로고    scopus 로고
    • Voltage gating and permeation in a gap junction hemichannel
    • USA.
    • Trexler, E.B., M.V. Bennett, T.A. Bargiello, and V.K. Verselis.;1996. Voltage gating and permeation in a gap junction hemichannel. Proc. Natl. Acad. Sci. USA. 93:5836-5841. http://dx.doi.org/10.1073/pnas.93.12.5836.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 5836-5841
    • Trexler, E.B.1    Bennett, M.V.2    Bargiello, T.A.3    Verselis, V.K.4
  • 50
    • 0021054030 scopus 로고
    • Calcium-mediated changes in gap junction structure: evidence from the low angle X-ray pattern
    • Unwin, P.N., and P.D. Ennis.; 1983. Calcium-mediated changes in gap junction structure: evidence from the low angle X-ray pattern. J. Cell Biol. 97:1459-1466. http://dx.doi.org/10.1083/jcb.97.5.1459.
    • (1983) J. Cell Biol. , vol.97 , pp. 1459-1466
    • Unwin, P.N.1    Ennis, P.D.2
  • 51
    • 0021139243 scopus 로고
    • Two configurations of a channelforming membrane protein
    • Unwin, P.N., and P.D. Ennis.;1984. Two configurations of a channelforming membrane protein. Nature. 307:609-613. http://dx.doi.org/10.1038/307609a0.
    • (1984) Nature. , vol.307 , pp. 609-613
    • Unwin, P.N.1    Ennis, P.D.2
  • 52
    • 83355177269 scopus 로고    scopus 로고
    • In search of a consensus model of the resting state of a voltage-sensing domain
    • Vargas, E., F. Bezanilla, and B. Roux.; 2011. In search of a consensus model of the resting state of a voltage-sensing domain. Neuron. 72:713-720. http://dx.doi.org/10.1016/j.neuron.2011.09.024.
    • (2011) Neuron. , vol.72 , pp. 713-720
    • Vargas, E.1    Bezanilla, F.2    Roux, B.3
  • 53
    • 50449110491 scopus 로고    scopus 로고
    • Divalent cations regulate connexin hemichannels by modulating intrinsic voltage-dependent gating
    • Verselis, V.K., and M. Srinivas.; 2008. Divalent cations regulate connexin hemichannels by modulating intrinsic voltage-dependent gating. J. Gen. Physiol. 132:315-327. http://dx.doi.org/10.1085/jgp.200810029.
    • (2008) J. Gen. Physiol. , vol.132 , pp. 315-327
    • Verselis, V.K.1    Srinivas, M.2
  • 54
    • 0028299152 scopus 로고
    • Opposite voltage gating polarities of two closely related connexins
    • Verselis, V.K., C.S. Ginter, and T.A. Bargiello.;1994. Opposite voltage gating polarities of two closely related connexins. Nature. 368:348-351. http://dx.doi.org/10.1038/368348a0.
    • (1994) Nature , vol.368 , pp. 348-351
    • Verselis, V.K.1    Ginter, C.S.2    Bargiello, T.A.3
  • 55
    • 63249084923 scopus 로고    scopus 로고
    • Loop gating of connexin hemichannels involves movement of pore-lining residues in the first extracellular loop domain
    • Verselis, V.K., M.P. Trelles, C. Rubinos, T.A. Bargiello, and M. Srinivas.;2009. Loop gating of connexin hemichannels involves movement of pore-lining residues in the first extracellular loop domain. J. Biol. Chem. 284:4484-4493. http://dx.doi.org/10.1074/jbc.M807430200.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4484-4493
    • Verselis, V.K.1    Trelles, M.P.2    Rubinos, C.3    Bargiello, T.A.4    Srinivas, M.5
  • 57
    • 0032417420 scopus 로고    scopus 로고
    • The moving parts of voltage-gated ion channels
    • Yellen, G.; 1998. The moving parts of voltage-gated ion channels. Q. Rev. Biophys. 31:239-295. http://dx.doi.org/10.1017/S0033583598003448.
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 239-295
    • Yellen, G.1
  • 58
    • 84859350674 scopus 로고    scopus 로고
    • Permeation pathway of homomeric connexin 26 and connexin 30 channels investigated by molecular dynamics
    • Zonta, F., G. Polles, G. Zanotti, and F. Mammano.; 2012. Permeation pathway of homomeric connexin 26 and connexin 30 channels investigated by molecular dynamics. J. Biomol. Struct. Dyn. 29:985-998. http://dx.doi.org/10.1080/073911012010525027.
    • (2012) J. Biomol. Struct. Dyn. , vol.29 , pp. 985-998
    • Zonta, F.1    Polles, G.2    Zanotti, G.3    Mammano, F.4


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