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Volumn 62, Issue 2, 2004, Pages 378-387

Incorporation of connexins into plasma membranes and gap junctions

Author keywords

Connexin chimeric proteins; Connexins; Trafficking pathways

Indexed keywords

CONNEXIN 26; CONNEXIN 32; CONNEXIN 43; GAP JUNCTION PROTEIN;

EID: 1942438659     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2004.01.016     Document Type: Review
Times cited : (107)

References (122)
  • 1
    • 0035985057 scopus 로고    scopus 로고
    • Structural and functional diversity of connexin genes in the mouse and human genome
    • Willecke K., Eiberger J., Degen J.et al. Structural and functional diversity of connexin genes in the mouse and human genome. Biol. Chem. 383:2002;725-737.
    • (2002) Biol. Chem. , vol.383 , pp. 725-737
    • Willecke, K.1    Eiberger, J.2    Degen, J.3
  • 2
    • 0033033946 scopus 로고    scopus 로고
    • Connexin45 a major connexin of the rabbit sinoatrial mode is co-expressed with connexin43 in a restricted zone at the nodal-crista terminalis border
    • Coppen S.R., Kodama I., Boyett M.R.et al. Connexin45 a major connexin of the rabbit sinoatrial mode is co-expressed with connexin43 in a restricted zone at the nodal-crista terminalis border. J. Histochem. Cytochem. 4:1999;907-918.
    • (1999) J. Histochem. Cytochem. , vol.4 , pp. 907-918
    • Coppen, S.R.1    Kodama, I.2    Boyett, M.R.3
  • 3
    • 1942461519 scopus 로고    scopus 로고
    • Relative expression of connexins 40 and 43 correlates with human atrial conduction properties
    • Kanagaratnam P., Severs N.J., Peters N.S. Relative expression of connexins 40 and 43 correlates with human atrial conduction properties. Circle. 100:1999;4436-4440.
    • (1999) Circle , vol.100 , pp. 4436-4440
    • Kanagaratnam, P.1    Severs, N.J.2    Peters, N.S.3
  • 4
    • 0028093157 scopus 로고
    • Spatiotemporal relation between gap-junctions and fascia adherens junctions during postnatal-development of human ventricular myocardium
    • Peters N.S., Severs N.J., Rothery S.M.et al. Spatiotemporal relation between gap-junctions and fascia adherens junctions during postnatal-development of human ventricular myocardium. Circle. 90:1994;713-725.
    • (1994) Circle , vol.90 , pp. 713-725
    • Peters, N.S.1    Severs, N.J.2    Rothery, S.M.3
  • 5
    • 0034812869 scopus 로고    scopus 로고
    • The role of myocardial gap junctions in electrical conduction and arrhythmogenesis
    • Kanno S., Saffitz J.E. The role of myocardial gap junctions in electrical conduction and arrhythmogenesis. Cardiovasc. Pathol. 10:2001;169-177.
    • (2001) Cardiovasc. Pathol. , vol.10 , pp. 169-177
    • Kanno, S.1    Saffitz, J.E.2
  • 6
    • 17344390158 scopus 로고    scopus 로고
    • Plasma membrane channels formed by connexins: Their regulation and functions
    • Saez J.C., Berthoud V.M., Branes M.C., Martinez A.D., Beyer E.C. Plasma membrane channels formed by connexins: their regulation and functions. Physiol. Rev. 83:2003;1359-1400.
    • (2003) Physiol. Rev. , vol.83 , pp. 1359-1400
    • Saez, J.C.1    Berthoud, V.M.2    Branes, M.C.3    Martinez, A.D.4    Beyer, E.C.5
  • 7
    • 0037184068 scopus 로고    scopus 로고
    • Gap junctions between cells expressing connexin 43 or 32 show inverse permselectivity to adenosine and ATP
    • Goldberg G.S., Moreno A.P., Lampe P.D. Gap junctions between cells expressing connexin 43 or 32 show inverse permselectivity to adenosine and ATP. J. Biol. Chem. 277:2002;36725-36730.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36725-36730
    • Goldberg, G.S.1    Moreno, A.P.2    Lampe, P.D.3
  • 8
    • 0033582686 scopus 로고    scopus 로고
    • Three-dimensional structure of a recombinant gap junction membrane channel
    • Unger V.M., Kumar N.M., Gilula N.B., Yeager M. Three-dimensional structure of a recombinant gap junction membrane channel. Science. 283:1999;1176-1180.
    • (1999) Science , vol.283 , pp. 1176-1180
    • Unger, V.M.1    Kumar, N.M.2    Gilula, N.B.3    Yeager, M.4
  • 9
    • 0035991948 scopus 로고    scopus 로고
    • Gap junction structure and function
    • Evans W.H., Martin P.E.M. Gap junction structure and function. Mol. Membr. Biol. 19:2002;121-136.
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 121-136
    • Evans, W.H.1    Martin, P.E.M.2
  • 10
    • 0027772413 scopus 로고
    • Connexin mutations in X-linked Charcot-Marie-Tooth disease
    • Bergoffen J., Scherer S.S., Wang S.et al. Connexin mutations in X-linked Charcot-Marie-Tooth disease. Science. 262:1993;2039-2042.
    • (1993) Science , vol.262 , pp. 2039-2042
    • Bergoffen, J.1    Scherer, S.S.2    Wang, S.3
  • 11
    • 0031007349 scopus 로고    scopus 로고
    • Connexin 26 mutations in hereditary non-syndromic sensorineural deafness
    • Kelsell D.P., Dunlop J., Stevens H.P.et al. Connexin 26 mutations in hereditary non-syndromic sensorineural deafness. Nature. 387:1997;80-83.
    • (1997) Nature , vol.387 , pp. 80-83
    • Kelsell, D.P.1    Dunlop, J.2    Stevens, H.P.3
  • 13
    • 0031796918 scopus 로고    scopus 로고
    • Mutations in the human connexin gene GJB3 cause erythrokeratodermia variabilis
    • Richard G., Smith L.E., Bailey R.A.et al. Mutations in the human connexin gene GJB3 cause erythrokeratodermia variabilis. Nat. Genet. 20:1998;366-369.
    • (1998) Nat. Genet. , vol.20 , pp. 366-369
    • Richard, G.1    Smith, L.E.2    Bailey, R.A.3
  • 14
    • 0031959735 scopus 로고    scopus 로고
    • A missense mutation in the human connexin50 gene (GJA8) underlies autosomal dominant "zonular pulverulent" cataract on chromosome 1q
    • Shiels A., Mackay D., Ionides A., Berry V., Moore A., Bhattacharya S. A missense mutation in the human connexin50 gene (GJA8) underlies autosomal dominant "zonular pulverulent" cataract on chromosome 1q. Am. J. Hum. Genet. 62:1998;526-532.
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 526-532
    • Shiels, A.1    MacKay, D.2    Ionides, A.3    Berry, V.4    Moore, A.5    Bhattacharya, S.6
  • 15
    • 0035663441 scopus 로고    scopus 로고
    • Mutations in GJA1 (connexin 43) are associated with non-syndromic autosomal recessive deafness
    • Liu X.Z., Xia X.J., Adams J.et al. Mutations in GJA1 (connexin 43) are associated with non-syndromic autosomal recessive deafness. Hum. Mol. Genet. 10:2001;2945-2951.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2945-2951
    • Liu, X.Z.1    Xia, X.J.2    Adams, J.3
  • 16
    • 0034705469 scopus 로고    scopus 로고
    • Gap junctions in cardiovascular disease
    • Jongsma H., Wilders R. Gap junctions in cardiovascular disease. Circ. Res. 86:2000;1193-1197.
    • (2000) Circ. Res. , vol.86 , pp. 1193-1197
    • Jongsma, H.1    Wilders, R.2
  • 17
    • 0027178710 scopus 로고
    • Reduced content of connexin43 gap junctions in ventricular myocardium from hypertrophied and ischemic human hearts
    • Peters N.S., Green C.R., Poole-Wilson P.A., Severs N.J. Reduced content of connexin43 gap junctions in ventricular myocardium from hypertrophied and ischemic human hearts. Circle. 88:1993;864-875.
    • (1993) Circle , vol.88 , pp. 864-875
    • Peters, N.S.1    Green, C.R.2    Poole-Wilson, P.A.3    Severs, N.J.4
  • 18
    • 0141751749 scopus 로고    scopus 로고
    • Preconditioning the myocardium: From cellular physiology to clinical cardiology
    • Yellon D.M., Downey J.M. Preconditioning the myocardium: from cellular physiology to clinical cardiology. Physiol. Rev. 83:2003;1113-1151.
    • (2003) Physiol. Rev. , vol.83 , pp. 1113-1151
    • Yellon, D.M.1    Downey, J.M.2
  • 19
    • 0032617032 scopus 로고    scopus 로고
    • Trafficking pathways leading to the formation of gap junctions. Gap junction-mediated intercellular signalling in health and disease
    • Evans W.H., Ahmad S., Diez J.et al. Trafficking pathways leading to the formation of gap junctions. Gap junction-mediated intercellular signalling in health and disease. Novartis Found. Symp. 219:1999;44-54.
    • (1999) Novartis Found. Symp. , vol.219 , pp. 44-54
    • Evans, W.H.1    Ahmad, S.2    Diez, J.3
  • 20
    • 0028077475 scopus 로고
    • Membrane insertion of gap junction connexins - Polytopic channel-forming membrane-proteins
    • Falk M.M., Kumar N.M., Gilula N.B. Membrane insertion of gap junction connexins - polytopic channel-forming membrane-proteins. J. Cell Biol. 127:1994;343-354.
    • (1994) J. Cell Biol. , vol.127 , pp. 343-354
    • Falk, M.M.1    Kumar, N.M.2    Gilula, N.B.3
  • 21
    • 0033560718 scopus 로고    scopus 로고
    • Synthesis and assembly of connexins in vitro into homomeric and heteromeric functional gap junction hemichannels
    • Ahmad S., Diez J.A., George C.H., Evans W.H. Synthesis and assembly of connexins in vitro into homomeric and heteromeric functional gap junction hemichannels. Biochem. J. 339:1999;247-253.
    • (1999) Biochem. J. , vol.339 , pp. 247-253
    • Ahmad, S.1    Diez, J.A.2    George, C.H.3    Evans, W.H.4
  • 22
    • 0032478623 scopus 로고    scopus 로고
    • Connexin membrane protein biosynthesis is influenced by polypeptide positioning within the translocon and signal peptidase access
    • Falk M.M., Gilula N.B. Connexin membrane protein biosynthesis is influenced by polypeptide positioning within the translocon and signal peptidase access. J. Biol. Chem. 273:1998;7856-7864.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7856-7864
    • Falk, M.M.1    Gilula, N.B.2
  • 23
    • 0036683707 scopus 로고    scopus 로고
    • Post-translational integration and oligomerisation of Cx26 in plasma membranes and evidence of formation of membrane pores. Implications for the assembly of gap junctions
    • Ahmad S., Evans W.H. Post-translational integration and oligomerisation of Cx26 in plasma membranes and evidence of formation of membrane pores. Implications for the assembly of gap junctions. Biochem. J. 365:2002;693-699.
    • (2002) Biochem. J. , vol.365 , pp. 693-699
    • Ahmad, S.1    Evans, W.H.2
  • 24
    • 0029936545 scopus 로고    scopus 로고
    • Membrane integration of in vitro-translated gap junctional proteins - Co- and posttranslational mechanisms
    • Zhang J.T., Chen M.G., Foote C.I., Nicholson B.J. Membrane integration of in vitro-translated gap junctional proteins - co- and posttranslational mechanisms. Mol. Biol. Cell. 7:1996;471-482.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 471-482
    • Zhang, J.T.1    Chen, M.G.2    Foote, C.I.3    Nicholson, B.J.4
  • 25
    • 0029618669 scopus 로고
    • Synthesis and assembly of human beta(1) gap-junctions in BHK cells by DNA transfection with the human beta(1) cDNA
    • Kumar N.M., Friend D.S., Gilula N.B. Synthesis and assembly of human beta(1) gap-junctions in BHK cells by DNA transfection with the human beta(1) cDNA. J. Cell Sci. 108:1995;3725-3734.
    • (1995) J. Cell Sci. , vol.108 , pp. 3725-3734
    • Kumar, N.M.1    Friend, D.S.2    Gilula, N.B.3
  • 26
    • 0033605658 scopus 로고    scopus 로고
    • Intracellular trafficking pathways in the assembly of connexins into gap junctions
    • George C.H., Kendall J.M., Evans W.H. Intracellular trafficking pathways in the assembly of connexins into gap junctions. J. Biol. Chem. 274:1999;8678-8685.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8678-8685
    • George, C.H.1    Kendall, J.M.2    Evans, W.H.3
  • 27
    • 0033563283 scopus 로고    scopus 로고
    • Assembly of heteromeric connexons in guinea-pig liver en route to the Golgi apparatus plasma membrane and gap junctions
    • Diez J.A., Ahmad S., Evans W.H. Assembly of heteromeric connexons in guinea-pig liver en route to the Golgi apparatus plasma membrane and gap junctions. Eur. J. Biochem. 262:1999;142-148.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 142-148
    • Diez, J.A.1    Ahmad, S.2    Evans, W.H.3
  • 28
    • 0027364529 scopus 로고
    • Multisubunit assembly of an integral plasma-membrane channel protein gap junction connexin43 occurs after exit from the ER
    • Musil L.S., Goodenough D.A. Multisubunit assembly of an integral plasma-membrane channel protein gap junction connexin43 occurs after exit from the ER. Cell. 74:1993;1065-1077.
    • (1993) Cell , vol.74 , pp. 1065-1077
    • Musil, L.S.1    Goodenough, D.A.2
  • 29
    • 0030947454 scopus 로고    scopus 로고
    • Connexin46 is retained as monomers in a trans-Golgi compartment of osteoblastic cells
    • Koval M., Harley J.E., Hick E., Steinberg T.H. Connexin46 is retained as monomers in a trans-Golgi compartment of osteoblastic cells. J. Cell Biol. 137:1997;847-857.
    • (1997) J. Cell Biol. , vol.137 , pp. 847-857
    • Koval, M.1    Harley, J.E.2    Hick, E.3    Steinberg, T.H.4
  • 30
    • 0037036426 scopus 로고    scopus 로고
    • Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization
    • DasSarma J.D., Wang F., Koval M. Targeted gap junction protein constructs reveal connexin-specific differences in oligomerization. J. Biol. Chem. 277:2002;20911-20918.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20911-20918
    • Dassarma, J.D.1    Wang, F.2    Koval, M.3
  • 31
    • 0036839258 scopus 로고    scopus 로고
    • Sharing signals: Connecting lung epithelial cells with gap junction channels
    • Koval M. Sharing signals: connecting lung epithelial cells with gap junction channels. Am. J. Physiol., Lung Cell. Mol. Physiol. 283:2002;L875-L893.
    • (2002) Am. J. Physiol., Lung Cell. Mol. Physiol. , vol.283 , pp. 875-L893
    • Koval, M.1
  • 32
    • 0034826706 scopus 로고    scopus 로고
    • Assembly of gap junction hemi-channels. Effects of calmodulin inhibitors and deletion of the cytoplasmic tail on connexin oligomerisation
    • Ahmad S., Martin P.E.M., Evans W.H. Assembly of gap junction hemi-channels. Effects of calmodulin inhibitors and deletion of the cytoplasmic tail on connexin oligomerisation. Eur. J. Biochem. 268:2001;4544-4552.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4544-4552
    • Ahmad, S.1    Martin, P.E.M.2    Evans, W.H.3
  • 33
    • 0030773116 scopus 로고    scopus 로고
    • Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains
    • Torok K., Stauffer K., Evans W.H. Connexin 32 of gap junctions contains two cytoplasmic calmodulin-binding domains. Biochem. J. 326:1997;479-483.
    • (1997) Biochem. J. , vol.326 , pp. 479-483
    • Torok, K.1    Stauffer, K.2    Evans, W.H.3
  • 35
    • 0028918702 scopus 로고
    • Distinct behaviour of connexin56 and connexin46 gap junctional channels can be predicted from the behaviour of their hemi-gap-junctional channels
    • Ebihara L., Berthoud V.M., Beyer E.C. Distinct behaviour of connexin56 and connexin46 gap junctional channels can be predicted from the behaviour of their hemi-gap-junctional channels. Biophys. J. 68:1995;1796-1803.
    • (1995) Biophys. J. , vol.68 , pp. 1796-1803
    • Ebihara, L.1    Berthoud, V.M.2    Beyer, E.C.3
  • 37
    • 0029800089 scopus 로고    scopus 로고
    • Properties and regulation of gap junctional hemichannels in the plasma-membranes of cultured-cells
    • Li H.Y., Liu T.F., Lazrak A., Peracchia C., Goldberg G.S., Lampe P.D.et al. Properties and regulation of gap junctional hemichannels in the plasma-membranes of cultured-cells. J. Cell Biol. 134:1996;1019-1030.
    • (1996) J. Cell Biol. , vol.134 , pp. 1019-1030
    • Li, H.Y.1    Liu, T.F.2    Lazrak, A.3    Peracchia, C.4    Goldberg, G.S.5    Lampe, P.D.6
  • 38
    • 0034611012 scopus 로고    scopus 로고
    • Physiological role of gap-junctional hemichannels: Extracellular calcium-dependent isosmotic volume regulation
    • Quist A.P., Rhee S.K., Lin H., Lal R. Physiological role of gap-junctional hemichannels: extracellular calcium-dependent isosmotic volume regulation. J. Cell Biol. 148:2000;1063-1074.
    • (2000) J. Cell Biol. , vol.148 , pp. 1063-1074
    • Quist, A.P.1    Rhee, S.K.2    Lin, H.3    Lal, R.4
  • 39
    • 0037285683 scopus 로고    scopus 로고
    • Photoliberating inositol145 trisphosphate triggers ATP release that is blocked by the connexin mimetic peptide gap 26
    • Braet K., Vandamme W., Martin P.E., Evans W.H., Leybaert L. Photoliberating inositol145 trisphosphate triggers ATP release that is blocked by the connexin mimetic peptide gap 26. Cell Calcium. 33:2003;37-48.
    • (2003) Cell Calcium , vol.33 , pp. 37-48
    • Braet, K.1    Vandamme, W.2    Martin, P.E.3    Evans, W.H.4    Leybaert, L.5
  • 40
    • 0037039391 scopus 로고    scopus 로고
    • Metabolic inhibition induces opening of unapposed connexin 43 gap junction hemichannels and reduces gap junctional communication in cortical astrocytes in culture
    • Contreas J.E., Sanchez H.A., Eugenin E.A.et al. Metabolic inhibition induces opening of unapposed connexin 43 gap junction hemichannels and reduces gap junctional communication in cortical astrocytes in culture. Proc. Natl. Acad. Sci. 99:2002;495-500.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 495-500
    • Contreas, J.E.1    Sanchez, H.A.2    Eugenin, E.A.3
  • 41
    • 0033745550 scopus 로고    scopus 로고
    • Metabolic inhibition activates a non-selective current through connexin hemichannels in isolated ventricular myocytes
    • Kondo R.P., Wang S.Y., John S.A., Weiss J.N., Goldhaber J.I. Metabolic inhibition activates a non-selective current through connexin hemichannels in isolated ventricular myocytes. J. Mol. Cell. Cardiol. 32:2000;1859-1872.
    • (2000) J. Mol. Cell. Cardiol. , vol.32 , pp. 1859-1872
    • Kondo, R.P.1    Wang, S.Y.2    John, S.A.3    Weiss, J.N.4    Goldhaber, J.I.5
  • 42
    • 0029776697 scopus 로고    scopus 로고
    • The life-cycle of a connexin-gap junction formation removal and degradation
    • Laird D.W. The life-cycle of a connexin-gap junction formation removal and degradation. J. Bioenerg. Biomembr. 28:1996;311-318.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 311-318
    • Laird, D.W.1
  • 43
    • 0031953118 scopus 로고    scopus 로고
    • Assembly of chimeric connexin-aequorin proteins into functional gap junction channels - Reporting intracellular and plasma membrane calcium environments
    • Martin P.E.M., George C.H., Castro C.et al. Assembly of chimeric connexin-aequorin proteins into functional gap junction channels - reporting intracellular and plasma membrane calcium environments. J. Biol. Chem. 273:1998;1719-1726.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1719-1726
    • Martin, P.E.M.1    George, C.H.2    Castro, C.3
  • 44
    • 0033012698 scopus 로고    scopus 로고
    • Trafficking assembly and function of a connexin43-green fluorescent protein chimera in live mammalian cells
    • Jordan K., Solan J.L., Dominguez M.et al. Trafficking assembly and function of a connexin43-green fluorescent protein chimera in live mammalian cells. Mol. Biol. Cell. 10:1999;2033-2050.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2033-2050
    • Jordan, K.1    Solan, J.L.2    Dominguez, M.3
  • 45
    • 0035188530 scopus 로고    scopus 로고
    • Multiple pathways in the trafficking and assembly of Connexin 26 32 and 43 into gap junctional intercellular communication channels
    • Martin P.E.M., Blundell G., Ahmad S., Errington R.J., Evans W.H. Multiple pathways in the trafficking and assembly of Connexin 26 32 and 43 into gap junctional intercellular communication channels. J. Cell Sci. 114:2001;3845-3855.
    • (2001) J. Cell Sci. , vol.114 , pp. 3845-3855
    • Martin, P.E.M.1    Blundell, G.2    Ahmad, S.3    Errington, R.J.4    Evans, W.H.5
  • 46
    • 0034474693 scopus 로고    scopus 로고
    • Connexin-specific distribution within gap junctions revealed in living cells
    • Falk M.M. Connexin-specific distribution within gap junctions revealed in living cells. J. Cell Sci. 113:2000;4109-4120.
    • (2000) J. Cell Sci. , vol.113 , pp. 4109-4120
    • Falk, M.M.1
  • 47
    • 0037134035 scopus 로고    scopus 로고
    • Multicolor electron microscopic imaging of connexin trafficking
    • Gaietta G., Deerinck T.J., Adams S.R.et al. Multicolor electron microscopic imaging of connexin trafficking. Science. 296:2002;503-507.
    • (2002) Science , vol.296 , pp. 503-507
    • Gaietta, G.1    Deerinck, T.J.2    Adams, S.R.3
  • 48
    • 0036793384 scopus 로고    scopus 로고
    • Lighting up gap junctions in a Flash
    • Evans W.H., Martin P.E.M. Lighting up gap junctions in a Flash. BioEssays. 24:2002;876-880.
    • (2002) BioEssays , vol.24 , pp. 876-880
    • Evans, W.H.1    Martin, P.E.M.2
  • 49
    • 0034026936 scopus 로고    scopus 로고
    • Intercellular calcium waves in HeLa cells expressing GFP-labelled connexin 43, 32 or 26
    • Paemeleire K., Martin P.E.M., Coleman S.L.et al. Intercellular calcium waves in HeLa cells expressing GFP-labelled connexin 43, 32 or 26. Mol. Biol. Cell. 11:2000;1815-1827.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1815-1827
    • Paemeleire, K.1    Martin, P.E.M.2    Coleman, S.L.3
  • 50
    • 0034646317 scopus 로고    scopus 로고
    • Clustering of connexin 43-enhanced green fluorescent protein gap junction channels and functional coupling in living cells
    • Bukauskas F.F., Jordan K., Bukauskiene A.et al. Clustering of connexin 43-enhanced green fluorescent protein gap junction channels and functional coupling in living cells. Proc. Natl. Acad. Sci. U. S. A. 97:2000;2556-2561.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 2556-2561
    • Bukauskas, F.F.1    Jordan, K.2    Bukauskiene, A.3
  • 51
    • 0037076384 scopus 로고    scopus 로고
    • Coupling asymmetry of heterotypic connexin 45/ connexin 43-EGFP gap junctions: Properties of fast and slow gating mechanisms
    • Bukauskas F.F., Angele A.B., Verselis V.K., Bennett M.V. Coupling asymmetry of heterotypic connexin 45/ connexin 43-EGFP gap junctions: properties of fast and slow gating mechanisms. Proc. Natl. Acad. Sci. U. S. A. 99:2002;7113-7118.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7113-7118
    • Bukauskas, F.F.1    Angele, A.B.2    Verselis, V.K.3    Bennett, M.V.4
  • 52
    • 0035753879 scopus 로고    scopus 로고
    • Gap junction assembly: Multiple connexin fluorophores identify complex trafficking pathways
    • Martin P.E.M., Errington R.J., Evans W.H. Gap junction assembly: multiple connexin fluorophores identify complex trafficking pathways. Cell Adhes. Commun. 8:2001;243-248.
    • (2001) Cell Adhes. Commun. , vol.8 , pp. 243-248
    • Martin, P.E.M.1    Errington, R.J.2    Evans, W.H.3
  • 53
    • 0029037694 scopus 로고
    • Expression of a connexin-43 beta-galactosidase fusion protein inhibits gap junctional communication in NIH3T3 cells
    • Sullivan R., Lo C.W. Expression of a connexin-43 beta-galactosidase fusion protein inhibits gap junctional communication in NIH3T3 cells. J. Cell Biol. 130:1995;419-429.
    • (1995) J. Cell Biol. , vol.130 , pp. 419-429
    • Sullivan, R.1    Lo, C.W.2
  • 54
    • 0035203507 scopus 로고    scopus 로고
    • Multimeric connexin interactions prior to the trans-Golgi network
    • DasSarma J., Meyer R.A., Wang F.et al. Multimeric connexin interactions prior to the trans-Golgi network. J. Cell Sci. 114:2001;4013-4014.
    • (2001) J. Cell Sci. , vol.114 , pp. 4013-4014
    • Dassarma, J.1    Meyer, R.A.2    Wang, F.3
  • 55
    • 0035370120 scopus 로고    scopus 로고
    • Expression of fluorescently tagged connexins: A novel approach to rescue function of oligomeric DsRed-tagged proteins
    • Lauf U., Lopez P., Falk M.M. Expression of fluorescently tagged connexins: a novel approach to rescue function of oligomeric DsRed-tagged proteins. FEBS Lett. 498:2001;11-15.
    • (2001) FEBS Lett. , vol.498 , pp. 11-15
    • Lauf, U.1    Lopez, P.2    Falk, M.M.3
  • 56
    • 0029176855 scopus 로고
    • Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells
    • Laird D.W., Castillo M., Kasprzak L. Gap junction turnover, intracellular trafficking, and phosphorylation of connexin43 in brefeldin A-treated rat mammary tumor cells. J. Cell Biol. 131:1995;1193-1203.
    • (1995) J. Cell Biol. , vol.131 , pp. 1193-1203
    • Laird, D.W.1    Castillo, M.2    Kasprzak, L.3
  • 57
    • 0035806979 scopus 로고    scopus 로고
    • Gap junction protein connexin-43 interacts directly with microtubules
    • Giepmans B.N., Verlann I., Hengeveld T.et al. Gap junction protein connexin-43 interacts directly with microtubules. Curr. Biol. 11:2001;1364-1368.
    • (2001) Curr. Biol. , vol.11 , pp. 1364-1368
    • Giepmans, B.N.1    Verlann, I.2    Hengeveld, T.3
  • 58
    • 0036343776 scopus 로고    scopus 로고
    • Gap junctions assemble in the presence of cytoskeletal inhibitors but enhanced assembly requires microtubules
    • Johnson R.G., Meyer R.A., Li X.R.et al. Gap junctions assemble in the presence of cytoskeletal inhibitors but enhanced assembly requires microtubules. Exp. Cell Res. 275:2002;67-80.
    • (2002) Exp. Cell Res. , vol.275 , pp. 67-80
    • Johnson, R.G.1    Meyer, R.A.2    Li, X.R.3
  • 59
    • 0036677449 scopus 로고    scopus 로고
    • Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells
    • Lauf U., Giepmans B.N., Lopez P.et al. Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc. Natl. Acad. Sci. U. S. A. 99:2002;10446-10451.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10446-10451
    • Lauf, U.1    Giepmans, B.N.2    Lopez, P.3
  • 60
    • 0035085580 scopus 로고    scopus 로고
    • The origin of annular junctions: A mechanism of gap junction internalisation
    • Jordan K., Chodock R., Hand A.R., Laird D.W. The origin of annular junctions: a mechanism of gap junction internalisation. J. Cell Sci. 114:2001;763-773.
    • (2001) J. Cell Sci. , vol.114 , pp. 763-773
    • Jordan, K.1    Chodock, R.2    Hand, A.R.3    Laird, D.W.4
  • 61
    • 0027252759 scopus 로고
    • Ultrastructural analysis of gap-junctions in C6 glioma-cells transfected with connexin43 cDNA
    • Naus C., Hearn S., Zhu D.G., Nicholson B.J., Shivers R.R. Ultrastructural analysis of gap-junctions in C6 glioma-cells transfected with connexin43 cDNA. Exp. Cell Res. 206:1993;72-84.
    • (1993) Exp. Cell Res. , vol.206 , pp. 72-84
    • Naus, C.1    Hearn, S.2    Zhu, D.G.3    Nicholson, B.J.4    Shivers, R.R.5
  • 63
    • 0031281674 scopus 로고    scopus 로고
    • Degradation of connexin 43 gap junctions involves both the proteasome and the lysosome
    • Laing J.G., Tadros P.N., Westphale E.M., Beyer E.C. Degradation of connexin 43 gap junctions involves both the proteasome and the lysosome. Exp. Cell Res. 236:1997;482-492.
    • (1997) Exp. Cell Res. , vol.236 , pp. 482-492
    • Laing, J.G.1    Tadros, P.N.2    Westphale, E.M.3    Beyer, E.C.4
  • 64
    • 0034047183 scopus 로고    scopus 로고
    • Intracellular transport assembly and degradation of wild-type and disease linked mutant gap junction proteins
    • VanSlyke J.K., Deschenes S.M., Musil L.S. Intracellular transport assembly and degradation of wild-type and disease linked mutant gap junction proteins. Mol. Biol. Cell. 11:2000;1933-1946.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1933-1946
    • Vanslyke, J.K.1    Deschenes, S.M.2    Musil, L.S.3
  • 65
    • 0042030808 scopus 로고    scopus 로고
    • Lysosomal and proteasomal degradation play distinct roles in the life cycle of Cx43 in gap junctional intercellular communication-deficient and -competent breast tumor cells
    • Qin H., Shao Q., Igdoura S.A., Alaoui-Jamali M.A., Laird D.W. Lysosomal and proteasomal degradation play distinct roles in the life cycle of Cx43 in gap junctional intercellular communication-deficient and -competent breast tumor cells. J. Biol. Chem. 278:2003;30005-30014.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30005-30014
    • Qin, H.1    Shao, Q.2    Igdoura, S.A.3    Alaoui-Jamali, M.A.4    Laird, D.W.5
  • 66
    • 1942525831 scopus 로고    scopus 로고
    • Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes
    • Toyofuku T., Yabuki M., Otsu K., Nishida M., Tada M. Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. Circle. 98:1998;52-58.
    • (1998) Circle , vol.98 , pp. 52-58
    • Toyofuku, T.1    Yabuki, M.2    Otsu, K.3    Nishida, M.4    Tada, M.5
  • 67
    • 0037632852 scopus 로고    scopus 로고
    • Lens connexins alpha3Cx46 and alpha8Cx50 interact with zonula occludens protein-1 (ZO-1)
    • Nielsen P.A., Shestopalov V.I., Giepmans B.N.et al. Lens connexins alpha3Cx46 and alpha8Cx50 interact with zonula occludens protein-1 (ZO-1). Mol. Biol. Cell. 14:2003;2470-2481.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2470-2481
    • Nielsen, P.A.1    Shestopalov, V.I.2    Giepmans, B.N.3
  • 68
    • 0036343899 scopus 로고    scopus 로고
    • Cx32 formation and/or Cx32-mediated intercellular communication induces expression and function of tight junctions in hepatocytic cell line
    • Kojima T., Spray D.C., Kokai Y.et al. Cx32 formation and/or Cx32-mediated intercellular communication induces expression and function of tight junctions in hepatocytic cell line. Exp. Cell Res. 276:2002;40-51.
    • (2002) Exp. Cell Res. , vol.276 , pp. 40-51
    • Kojima, T.1    Spray, D.C.2    Kokai, Y.3
  • 69
    • 0037155043 scopus 로고    scopus 로고
    • Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions
    • Barker R.J., Price R.L., Gourdie R.G. Increased association of ZO-1 with connexin43 during remodeling of cardiac gap junctions. Circ. Res. 90:2002;317-324.
    • (2002) Circ. Res. , vol.90 , pp. 317-324
    • Barker, R.J.1    Price, R.L.2    Gourdie, R.G.3
  • 70
    • 0037147288 scopus 로고    scopus 로고
    • Impaired trafficking of connexins in androgen-independent human prostate cancer cell lines and its mitigation by alpha-catenin
    • Govindarajan R., Zhao S., Song X.H.et al. Impaired trafficking of connexins in androgen-independent human prostate cancer cell lines and its mitigation by alpha-catenin. J. Biol. Chem. 277:2002;50087-50097.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50087-50097
    • Govindarajan, R.1    Zhao, S.2    Song, X.H.3
  • 71
    • 0037371343 scopus 로고    scopus 로고
    • Role of catenins in the development of gap junctions in rat cardiomyocytes
    • Wu J.C., Tsai R.Y., Chung T.H. Role of catenins in the development of gap junctions in rat cardiomyocytes. J. Cell. Biochem. 88:2003;823-835.
    • (2003) J. Cell. Biochem. , vol.88 , pp. 823-835
    • Wu, J.C.1    Tsai, R.Y.2    Chung, T.H.3
  • 72
    • 0037035519 scopus 로고    scopus 로고
    • Connexin family members target to lipid raft domains and interact with caveolin-1
    • Schubert A., Schubert W., Spray D.C., Lisanti M.P. Connexin family members target to lipid raft domains and interact with caveolin-1. Biochemistry. 41:2002;5754-5764.
    • (2002) Biochemistry , vol.41 , pp. 5754-5764
    • Schubert, A.1    Schubert, W.2    Spray, D.C.3    Lisanti, M.P.4
  • 73
    • 0034799390 scopus 로고    scopus 로고
    • Gap junction assembly: PTX-sensitive G proteins regulate the distribution of connexin43 within cells
    • Lampe P.D., Qiu Q., Meyer R.A.et al. Gap junction assembly: PTX-sensitive G proteins regulate the distribution of connexin43 within cells. Am. J. Physiol., Cell Physiol. 281:2001;C1211-C1222.
    • (2001) Am. J. Physiol., Cell Physiol. , vol.281 , pp. 1211-C1222
    • Lampe, P.D.1    Qiu, Q.2    Meyer, R.A.3
  • 74
    • 0036094459 scopus 로고    scopus 로고
    • Voltage-sensing and substrate rectification: Moving parts of connexin channels
    • Harris A.L. Voltage-sensing and substrate rectification: moving parts of connexin channels. J. Gen. Physiol. 119:2002;171-185.
    • (2002) J. Gen. Physiol. , vol.119 , pp. 171-185
    • Harris, A.L.1
  • 75
    • 0027297994 scopus 로고
    • Trapping an intermediate form of connexin43 in the Golgi
    • Puranam K.L., Laird D.W., Revel J.P. Trapping an intermediate form of connexin43 in the Golgi. Exp. Cell Res. 206:1993;85-92.
    • (1993) Exp. Cell Res. , vol.206 , pp. 85-92
    • Puranam, K.L.1    Laird, D.W.2    Revel, J.P.3
  • 76
    • 0025789648 scopus 로고
    • Biochemical-analysis of connexin43 intracellular-transport phosphorylation and assembly into gap junctional plaques
    • Musil L.S., Goodenough D.A. Biochemical-analysis of connexin43 intracellular-transport phosphorylation and assembly into gap junctional plaques. J. Cell Biol. 115:1991;1357-1374.
    • (1991) J. Cell Biol. , vol.115 , pp. 1357-1374
    • Musil, L.S.1    Goodenough, D.A.2
  • 77
    • 0034671950 scopus 로고    scopus 로고
    • Regulation of phosphorylation of connexins
    • Lampe P.D., Lau A.F. Regulation of phosphorylation of connexins. Arch. Biochem. Biophys. 384:2000;205-215.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 205-215
    • Lampe, P.D.1    Lau, A.F.2
  • 78
    • 0034717680 scopus 로고    scopus 로고
    • Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication
    • Lampe P.D., TenBroek E.M., Burt J.M.et al. Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication. J. Cell Biol. 149:2000;1503-1552.
    • (2000) J. Cell Biol. , vol.149 , pp. 1503-1552
    • Lampe, P.D.1    Tenbroek, E.M.2    Burt, J.M.3
  • 79
    • 0030722611 scopus 로고    scopus 로고
    • Expression of connexin-43 and connexin-26 in the rat myometrium during pregnancy and labor is differentially regulated by mechanical and hormonal signals
    • Ou C.W., Orsino A., Lye S.J. Expression of connexin-43 and connexin-26 in the rat myometrium during pregnancy and labor is differentially regulated by mechanical and hormonal signals. Endocrinology. 138:1997;5398-5407.
    • (1997) Endocrinology , vol.138 , pp. 5398-5407
    • Ou, C.W.1    Orsino, A.2    Lye, S.J.3
  • 81
    • 0041884855 scopus 로고    scopus 로고
    • Altered connexin expression and wound healing in the epidermis of connexin-deficient mice
    • Kretz M., Euwens C., Hombach S.et al. Altered connexin expression and wound healing in the epidermis of connexin-deficient mice. J. Cell Sci. 116:2003;3443-3452.
    • (2003) J. Cell Sci. , vol.116 , pp. 3443-3452
    • Kretz, M.1    Euwens, C.2    Hombach, S.3
  • 82
    • 0038724475 scopus 로고    scopus 로고
    • Dynamic changes in connexin expression correlate with key events in the wound healing process
    • Coutinho P., Qiu C., Frank S., Tamber K., Becker D. Dynamic changes in connexin expression correlate with key events in the wound healing process. Cell Biol. Int. 27:2003;525-541.
    • (2003) Cell Biol. Int. , vol.27 , pp. 525-541
    • Coutinho, P.1    Qiu, C.2    Frank, S.3    Tamber, K.4    Becker, D.5
  • 83
    • 0030017422 scopus 로고    scopus 로고
    • Functional and structural assessment of intercellular communication-increased conduction-velocity and enhanced connexin expression in dibutyryl cAMP-treated cultured cardiac myocytes
    • Darrow B.J., Fast V.G., Kleber A.G., Beyer E.C., Saffitz J.E. Functional and structural assessment of intercellular communication-increased conduction-velocity and enhanced connexin expression in dibutyryl cAMP-treated cultured cardiac myocytes. Circ. Res. 79:1996;174-183.
    • (1996) Circ. Res. , vol.79 , pp. 174-183
    • Darrow, B.J.1    Fast, V.G.2    Kleber, A.G.3    Beyer, E.C.4    Saffitz, J.E.5
  • 84
    • 0031671378 scopus 로고    scopus 로고
    • Effects of angiotensin II on expression of the gap junction channel protein connexin43 in neonatal rat ventricular myocytes
    • Dodge S.M., Beardslee M.A., Darrow B.J.et al. Effects of angiotensin II on expression of the gap junction channel protein connexin43 in neonatal rat ventricular myocytes. J. Am. Coll. Cardiol. 32:1998;800-807.
    • (1998) J. Am. Coll. Cardiol. , vol.32 , pp. 800-807
    • Dodge, S.M.1    Beardslee, M.A.2    Darrow, B.J.3
  • 86
    • 0033394620 scopus 로고    scopus 로고
    • Dynamics of gap junctions observed in living cells with connexin43-GFP chimeric protein
    • Holm I., Mikhailov A., Jillson T., Rose B. Dynamics of gap junctions observed in living cells with connexin43-GFP chimeric protein. Eur. J. Cell Biol. 78:1999;856-866.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 856-866
    • Holm, I.1    Mikhailov, A.2    Jillson, T.3    Rose, B.4
  • 87
    • 0034644635 scopus 로고    scopus 로고
    • Dephosphorylation and intracellular redistribution of ventricular connexin43 during electrical uncoupling induced by ischemia
    • Beardslee M.A., Lerner D.L., Tadros P.N.et al. Dephosphorylation and intracellular redistribution of ventricular connexin43 during electrical uncoupling induced by ischemia. Circ. Res. 87:2000;656-662.
    • (2000) Circ. Res. , vol.87 , pp. 656-662
    • Beardslee, M.A.1    Lerner, D.L.2    Tadros, P.N.3
  • 88
    • 1942461488 scopus 로고    scopus 로고
    • Different regulation of Connexin 43 in cardiac myocytes by hypoxia and ischemia
    • Turner M., Haywood G.A., Discher D.J.et al. Different regulation of Connexin 43 in cardiac myocytes by hypoxia and ischemia. Circulation. 104(Suppl. I):2001;II-43.
    • (2001) Circulation , vol.104 , Issue.SUPPL. I , pp. 43
    • Turner, M.1    Haywood, G.A.2    Discher, D.J.3
  • 91
    • 0031983038 scopus 로고    scopus 로고
    • Co- and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly
    • Yun L., Xiong X., Helm A.et al. Co- and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly. J. Biol. Chem. 273:1998;568-576.
    • (1998) J. Biol. Chem. , vol.273 , pp. 568-576
    • Yun, L.1    Xiong, X.2    Helm, A.3
  • 92
    • 0041765775 scopus 로고    scopus 로고
    • Peroxisome biogenesis: Advances and conundrums
    • Lazarow P.B. Peroxisome biogenesis: advances and conundrums. Curr. Opin. Cell Biol. 15:2003;489-497.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 489-497
    • Lazarow, P.B.1
  • 94
    • 0037192856 scopus 로고    scopus 로고
    • Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway
    • Yoo J.S., Moyer B.D., Bannykh S.et al. Non-conventional trafficking of the cystic fibrosis transmembrane conductance regulator through the early secretory pathway. J. Biol. Chem. 277:2002;11401-11409.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11401-11409
    • Yoo, J.S.1    Moyer, B.D.2    Bannykh, S.3
  • 95
    • 0038107461 scopus 로고    scopus 로고
    • Involvement of the endoplasmic reticulum in peroxisome formation
    • Geuze H.J., Mark J.L., Stroobants A.K.et al. Involvement of the endoplasmic reticulum in peroxisome formation. Mol. Biol. Cell. 14:2003;2900-2907.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2900-2907
    • Geuze, H.J.1    Mark, J.L.2    Stroobants, A.K.3
  • 96
    • 0032580869 scopus 로고    scopus 로고
    • Heteromeric gap junction channels in rat hepatocytes in which the expression of connexin26 is induced
    • Lee M.J., Rhee S.K. Heteromeric gap junction channels in rat hepatocytes in which the expression of connexin26 is induced. Mol. Cells. 8:1998;295-300.
    • (1998) Mol. Cells , vol.8 , pp. 295-300
    • Lee, M.J.1    Rhee, S.K.2
  • 97
    • 0034796366 scopus 로고    scopus 로고
    • Gap junction expression and cell proliferation in differentiating cultures of Cx32 KO mouse hepatocytes
    • Kojima T., Fort A., Tao M., Yamamoto M., Spray D.C. Gap junction expression and cell proliferation in differentiating cultures of Cx32 KO mouse hepatocytes. Am. J. Physiol., Gastrointest. Liver Physiol. 281:2001;G1004-G1013.
    • (2001) Am. J. Physiol., Gastrointest. Liver Physiol. , vol.281 , pp. 1004-G1013
    • Kojima, T.1    Fort, A.2    Tao, M.3    Yamamoto, M.4    Spray, D.C.5
  • 98
    • 0030962451 scopus 로고    scopus 로고
    • Differential expression of connexins during neocortical development and neuronal circuit formation
    • Nadarajah B., Jones A.M., Evans W.H., Parnavelas J.G. Differential expression of connexins during neocortical development and neuronal circuit formation. J. Neurosci. 17:1997;3096-3111.
    • (1997) J. Neurosci. , vol.17 , pp. 3096-3111
    • Nadarajah, B.1    Jones, A.M.2    Evans, W.H.3    Parnavelas, J.G.4
  • 99
    • 0028556972 scopus 로고
    • Rapid appearance of connexin 26-positive gap-junctions in centrilobular hepatocytes without induction of messenger-RNA and protein-synthesis in isolated-perfused liver of female rat
    • Kojima T., Sawada N., Oyamada M.et al. Rapid appearance of connexin 26-positive gap-junctions in centrilobular hepatocytes without induction of messenger-RNA and protein-synthesis in isolated-perfused liver of female rat. J. Cell Sci. 107:1994;3579-3590.
    • (1994) J. Cell Sci. , vol.107 , pp. 3579-3590
    • Kojima, T.1    Sawada, N.2    Oyamada, M.3
  • 100
  • 101
    • 0032431873 scopus 로고    scopus 로고
    • Gap junctions in normal and neoplastic mammary gland
    • Locke D. Gap junctions in normal and neoplastic mammary gland. J. Pathol. 186:1998;343-349.
    • (1998) J. Pathol. , vol.186 , pp. 343-349
    • Locke, D.1
  • 102
    • 0029083331 scopus 로고
    • Cyclic AMP modifies the cellular distribution of connexin43 and induces a persistent increase in the junctional permeability of mouse mammary tumor cells
    • Atkinson M.M., Lampe P.D., Lin H.H., Kollander R., Li X.R., Kiang D.T. Cyclic AMP modifies the cellular distribution of connexin43 and induces a persistent increase in the junctional permeability of mouse mammary tumor cells. J. Cell Sci. 108:1995;3079-3090.
    • (1995) J. Cell Sci. , vol.108 , pp. 3079-3090
    • Atkinson, M.M.1    Lampe, P.D.2    Lin, H.H.3    Kollander, R.4    Li, X.R.5    Kiang, D.T.6
  • 103
    • 0033828666 scopus 로고    scopus 로고
    • Cyclic AMP and LDL trigger a rapid enhancement in gap junction assembly through a stimulation of connexin trafficking
    • Paulson A.F., Lampe P.D., Meyer R.A.et al. Cyclic AMP and LDL trigger a rapid enhancement in gap junction assembly through a stimulation of connexin trafficking. J. Cell Sci. 113:2000;3037-3049.
    • (2000) J. Cell Sci. , vol.113 , pp. 3037-3049
    • Paulson, A.F.1    Lampe, P.D.2    Meyer, R.A.3
  • 104
    • 0008559128 scopus 로고    scopus 로고
    • Trafficking and targeting of Connexin 32 mutations to gap junctions in Charcot-Marie-Tooth-X Linked disease
    • Martin P.E.M., Evans W.H. Trafficking and targeting of Connexin 32 mutations to gap junctions in Charcot-Marie-Tooth-X Linked disease. Curr. Top. Membr. 49:1999;461-481.
    • (1999) Curr. Top. Membr. , vol.49 , pp. 461-481
    • Martin, P.E.M.1    Evans, W.H.2
  • 105
    • 0037093306 scopus 로고    scopus 로고
    • A mutation in GJB3 is associated with recessive erythrokeratodermia variabilis (EKV) and leads to defective trafficking of the connexin 31 protein
    • Gottfried I., Landau M., Glaser F.et al. A mutation in GJB3 is associated with recessive erythrokeratodermia variabilis (EKV) and leads to defective trafficking of the connexin 31 protein. Hum. Mol. Genet. 11:2002;1311-1316.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1311-1316
    • Gottfried, I.1    Landau, M.2    Glaser, F.3
  • 106
    • 0033963213 scopus 로고    scopus 로고
    • Analysis of gap junction assembly using mutated connexins detected in Charcot Marie Tooth X linked disease
    • Martin P.E.M., Mambetisaeva E.T., Archer D.A., George C.H., Evans W.H. Analysis of gap junction assembly using mutated connexins detected in Charcot Marie Tooth X linked disease. J. Neurochem. 74:2000;711-720.
    • (2000) J. Neurochem. , vol.74 , pp. 711-720
    • Martin, P.E.M.1    Mambetisaeva, E.T.2    Archer, D.A.3    George, C.H.4    Evans, W.H.5
  • 108
    • 0042386448 scopus 로고    scopus 로고
    • Specific amino-acid residues in the N-terminus and TM3 implicated in channel function and oligomerization compatibility of connexin43
    • Lagree V., Brunschwig K., Lopez P.et al. Specific amino-acid residues in the N-terminus and TM3 implicated in channel function and oligomerization compatibility of connexin43. J. Cell Sci. 116:2003;3189-3201.
    • (2003) J. Cell Sci. , vol.116 , pp. 3189-3201
    • Lagree, V.1    Brunschwig, K.2    Lopez, P.3
  • 110
    • 0034234655 scopus 로고    scopus 로고
    • Targeting motifs and functional parameters governing the assembly of connexins into gap junctions
    • Martin P.E.M., Steggles J., Wilson C., Ahmad S., Evans W.H. Targeting motifs and functional parameters governing the assembly of connexins into gap junctions. Biochem. J. 349:2000;281-287.
    • (2000) Biochem. J. , vol.349 , pp. 281-287
    • Martin, P.E.M.1    Steggles, J.2    Wilson, C.3    Ahmad, S.4    Evans, W.H.5
  • 111
    • 0037191101 scopus 로고    scopus 로고
    • Identification of amino acid residues lining the pore of a gap junction channel
    • Skerrett I.M., Aronowitz J., Shin J.H.et al. Identification of amino acid residues lining the pore of a gap junction channel. J. Cell Biol. 159:2002;349-360.
    • (2002) J. Cell Biol. , vol.159 , pp. 349-360
    • Skerrett, I.M.1    Aronowitz, J.2    Shin, J.H.3
  • 112
    • 0037154271 scopus 로고    scopus 로고
    • Function of the voltage gate of gap junction channels: Selective exclusion of molecules
    • Qu Y., Dahl G. Function of the voltage gate of gap junction channels: selective exclusion of molecules. Proc. Natl. Acad. Sci. U. S. A. 99:2002;697-702.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 697-702
    • Qu, Y.1    Dahl, G.2
  • 113
    • 0025946610 scopus 로고
    • Topography of connexin32 in rat-liver gap-junctions - Evidence for an intramolecular disulfide linkage connecting the 2 extracellular peptide loops
    • Rahman S., Evans W.H. Topography of connexin32 in rat-liver gap-junctions - evidence for an intramolecular disulfide linkage connecting the 2 extracellular peptide loops. J. Cell Sci. 100:1991;567-578.
    • (1991) J. Cell Sci. , vol.100 , pp. 567-578
    • Rahman, S.1    Evans, W.H.2
  • 114
    • 0032498942 scopus 로고    scopus 로고
    • The pattern of disulfide linkages in the extracellular loop regions of connexin 32 suggests a model for the docking interface of gap junctions
    • Foote C.I., Zhou L., Zhu X., Nicholson B.J. The pattern of disulfide linkages in the extracellular loop regions of connexin 32 suggests a model for the docking interface of gap junctions. J. Cell Biol. 140:1998;1187-1197.
    • (1998) J. Cell Biol. , vol.140 , pp. 1187-1197
    • Foote, C.I.1    Zhou, L.2    Zhu, X.3    Nicholson, B.J.4
  • 115
    • 0042309578 scopus 로고    scopus 로고
    • Targeted epidermal expression of mutant Connexin 26(D66H) mimics true Vohwinkel syndrome and provides a model for the pathogenesis of dominant connexin disorders
    • Bakirtzis G., Choudhry R., Aasen T.et al. Targeted epidermal expression of mutant Connexin 26(D66H) mimics true Vohwinkel syndrome and provides a model for the pathogenesis of dominant connexin disorders. Hum. Mol. Genet. 12:2003;1737-1744.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1737-1744
    • Bakirtzis, G.1    Choudhry, R.2    Aasen, T.3
  • 116
    • 0242684552 scopus 로고    scopus 로고
    • Mutations in the gene for connexin 26 (GJB2) that cause hearing loss have a dominant negative effect on connexin 30
    • Marziano N.K., Casalotti S.O., Portelli A.E., Becker D.L., Forge A. Mutations in the gene for connexin 26 (GJB2) that cause hearing loss have a dominant negative effect on connexin 30. Hum. Mol. Genet. 12:2003;805-812.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 805-812
    • Marziano, N.K.1    Casalotti, S.O.2    Portelli, A.E.3    Becker, D.L.4    Forge, A.5
  • 117
    • 0036451762 scopus 로고    scopus 로고
    • Diverse trafficking abnormalities of connexin32 mutants causing CMTX
    • Yum S.W., Kleopa K.A., Shumas S., Scherer S.S. Diverse trafficking abnormalities of connexin32 mutants causing CMTX. Neurobiol. Dis. 11:2002;43-52.
    • (2002) Neurobiol. Dis. , vol.11 , pp. 43-52
    • Yum, S.W.1    Kleopa, K.A.2    Shumas, S.3    Scherer, S.S.4
  • 118
    • 0032491419 scopus 로고    scopus 로고
    • Connexin-aequorin chimerae report cytoplasmic calcium environments along trafficking pathways leading to gap junction biogenesis in living COS-7 cells
    • George C.H., Kendall J.M., Campbell A.K., Evans W.H. Connexin-aequorin chimerae report cytoplasmic calcium environments along trafficking pathways leading to gap junction biogenesis in living COS-7 cells. J. Biol. Chem. 273:1998;29822-29829.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29822-29829
    • George, C.H.1    Kendall, J.M.2    Campbell, A.K.3    Evans, W.H.4
  • 119
    • 0035853435 scopus 로고    scopus 로고
    • The carboxyl terminal domain regulates the unitary conductance and voltage dependence of connexin40 gap junction channels
    • Anumonwo J.M., Taffet S.M., Gu H.et al. The carboxyl terminal domain regulates the unitary conductance and voltage dependence of connexin40 gap junction channels. Circ. Res. 88:2001;666-673.
    • (2001) Circ. Res. , vol.88 , pp. 666-673
    • Anumonwo, J.M.1    Taffet, S.M.2    Gu, H.3
  • 120
    • 0033612181 scopus 로고    scopus 로고
    • Hetero-domain interactions as a mechanism for the regulation of connexin channels
    • Stergiopoulos K., Alvarado J.L., Mastroianni M.et al. Hetero-domain interactions as a mechanism for the regulation of connexin channels. Circ. Res. 84:1999;1144-1155.
    • (1999) Circ. Res. , vol.84 , pp. 1144-1155
    • Stergiopoulos, K.1    Alvarado, J.L.2    Mastroianni, M.3
  • 121
    • 0036634865 scopus 로고    scopus 로고
    • Pharmacological modification of gap junction coupling by an antiarrhythmic peptide via protein kinase C activation
    • Weng S., Lauven M., Schaefer T., Polontchouk L., Grover R., Dhein S. Pharmacological modification of gap junction coupling by an antiarrhythmic peptide via protein kinase C activation. FASEB J. 16:2002;114-116.
    • (2002) FASEB J. , vol.16 , pp. 114-116
    • Weng, S.1    Lauven, M.2    Schaefer, T.3    Polontchouk, L.4    Grover, R.5    Dhein, S.6
  • 122
    • 0036213942 scopus 로고    scopus 로고
    • Cardiac gap junctions and connexins: Their role in atrail fibrilation and potential as therapeutic targets
    • vanderVelden H.M., Jongsma H. Cardiac gap junctions and connexins: their role in atrail fibrilation and potential as therapeutic targets. Cardiovasc. Res. 54:2002;270-279.
    • (2002) Cardiovasc. Res. , vol.54 , pp. 270-279
    • Vandervelden, H.M.1    Jongsma, H.2


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