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Volumn 136, Issue 5, 2010, Pages 515-527

SCAM analysis of Panx1 suggests a peculiar pore structure

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GAP JUNCTION PROTEIN; NERVE PROTEIN; PANX1 PROTEIN, MOUSE;

EID: 78649480274     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201010440     Document Type: Article
Times cited : (72)

References (45)
  • 1
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • doi:10.1126/science.1384130
    • 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. doi: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
  • 2
    • 4143127920 scopus 로고    scopus 로고
    • Pannexin membrane channels are mechanosensitive conduits for ATP
    • doi:10.1016/j.febslet.2004.07.009
    • Bao, L., S. Locovei, and G. Dahl. 2004. Pannexin membrane channels are mechanosensitive conduits for ATP. FEBS Lett. 572:65-68. doi:10.1016/j.febslet. 2004.07.009
    • (2004) FEBS Lett. , vol.572 , pp. 65-68
    • Bao, L.1    Locovei, S.2    Dahl, G.3
  • 3
    • 36549024942 scopus 로고    scopus 로고
    • Innexins form two types of channels
    • doi:10.1016/j.febslet.2007.11.030
    • Bao, L., S. Samuels, S. Locovei, E.R. Macagno, K.J. Muller, and G. Dahl. 2007. Innexins form two types of channels. FEBS Lett. 581:5703-5708. doi:10.1016/j.febslet.2007.11.030
    • (2007) FEBS Lett. , vol.581 , pp. 5703-5708
    • Bao, L.1    Samuels, S.2    Locovei, S.3    MacAgno, E.R.4    Muller, K.J.5    Dahl, G.6
  • 4
    • 0025963272 scopus 로고
    • Gap junctions: New tools, new answers, new questions
    • doi:10.1016/0896-6273(91)90241-Q
    • Bennett, M.V., L.C. Barrio, T.A. Bargiello, D.C. Spray, E. Hertzberg, and J.C. Sáez. 1991. Gap junctions: new tools, new answers, new questions. Neuron. 6:305-320. doi:10.1016/0896-6273(91)90241-Q
    • (1991) Neuron , vol.6 , pp. 305-320
    • Bennett, M.V.1    Barrio, L.C.2    Bargiello, T.A.3    Spray, D.C.4    Hertzberg, E.5    Sáez, J.C.6
  • 5
    • 35748965595 scopus 로고    scopus 로고
    • Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane
    • doi:10.1074/jbc.M702422200
    • Boassa, D., C. Ambrosi, F. Qiu, G. Dahl, G. Gaietta, and G. Sosinsky. 2007. Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. J. Biol. Chem. 282:31733-31743. doi:10.1074/jbc. M702422200
    • (2007) J. Biol. Chem. , vol.282 , pp. 31733-31743
    • Boassa, D.1    Ambrosi, C.2    Qiu, F.3    Dahl, G.4    Gaietta, G.5    Sosinsky, G.6
  • 6
    • 42649085323 scopus 로고    scopus 로고
    • Trafficking dynamics of glycosylated pannexin 1 proteins
    • doi:10.1080/15419060802013885
    • Boassa, D., F. Qiu, G. Dahl, and G. Sosinsky. 2008. Trafficking dynamics of glycosylated pannexin 1 proteins. Cell Commun. Adhes. 15:119-132. doi:10.1080/15419060802013885
    • (2008) Cell Commun. Adhes. , vol.15 , pp. 119-132
    • Boassa, D.1    Qiu, F.2    Dahl, G.3    Sosinsky, G.4
  • 7
    • 0345255097 scopus 로고    scopus 로고
    • Pannexins, a family of gap junction proteins expressed in brain
    • doi:10.1073/pnas.2233464100
    • Bruzzone, R., S.G. Hormuzdi, M.T. Barbe, A. Herb, and H. Monyer. 2003. Pannexins, a family of gap junction proteins expressed in brain. Proc. Natl. Acad. Sci. USA. 100:13644-13649. doi:10.1073/pnas.2233464100
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 13644-13649
    • Bruzzone, R.1    Hormuzdi, S.G.2    Barbe, M.T.3    Herb, A.4    Monyer, H.5
  • 8
    • 14844334146 scopus 로고    scopus 로고
    • Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes
    • doi:10.1111/j.1471-4159.2004.02947.x
    • Bruzzone, R., M.T. Barbe, N.J. Jakob, and H. Monyer. 2005. Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes. J. Neurochem. 92:1033-1043. doi:10.1111/j.1471- 4159.2004.02947.x
    • (2005) J. Neurochem. , vol.92 , pp. 1033-1043
    • Bruzzone, R.1    Barbe, M.T.2    Jakob, N.J.3    Monyer, H.4
  • 9
    • 34249030531 scopus 로고    scopus 로고
    • An innexin-dependent cell network establishes left-right neuronal asymmetry in C. Elegans
    • doi:10.1016/j.cell.2007.02.052
    • Chuang, C.F., M.K. Vanhoven, R.D. Fetter, V.K. Verselis, and C.I. Bargmann. 2007. An innexin-dependent cell network establishes left-right neuronal asymmetry in C. elegans. Cell. 129:787-799. doi:10.1016/j.cell.2007.02. 052
    • (2007) Cell. , vol.129 , pp. 787-799
    • Chuang, C.F.1    Vanhoven, M.K.2    Fetter, R.D.3    Verselis, V.K.4    Bargmann, C.I.5
  • 10
    • 0002941572 scopus 로고
    • The Xenopus oocyte cell-cell channel assay for functional analysis of gap junction proteins
    • B. Stevenson, W. Gallin, and D. Paul, editors. Oxford University Press, Oxford, UK
    • Dahl, G. 1992. The Xenopus oocyte cell-cell channel assay for functional analysis of gap junction proteins. In Cell-Cell Interactions: A Practical Approach. B. Stevenson, W. Gallin, and D. Paul, editors. Oxford University Press, Oxford, UK. 143-165.
    • (1992) Cell-Cell Interactions: A Practical Approach , pp. 143-165
    • Dahl, G.1
  • 11
    • 33745712366 scopus 로고    scopus 로고
    • Pannexin: To gap or not to gap, is that a questionè
    • doi:10.1080/15216540600794526
    • Dahl, G., and S. Locovei. 2006. Pannexin: to gap or not to gap, is that a questionè IUBMB Life. 58:409-419. doi:10.1080/15216540600794526
    • (2006) IUBMB Life. , vol.58 , pp. 409-419
    • Dahl, G.1    Locovei, S.2
  • 12
    • 1942470893 scopus 로고    scopus 로고
    • Structural bases for the chemical regulation of Connexin43 channels
    • doi:10.1016/j.cardiores.2003.12.030
    • Delmar, M., W. Coombs, P. Sorgen, H.S. Duffy, and S.M. Taffet. 2004. Structural bases for the chemical regulation of Connexin43 channels. Cardiovasc. Res. 62:268-275. doi:10.1016/j.cardiores.2003.12.030
    • (2004) Cardiovasc. Res. , vol.62 , pp. 268-275
    • Delmar, M.1    Coombs, W.2    Sorgen, P.3    Duffy, H.S.4    Taffet, S.M.5
  • 13
    • 0024110268 scopus 로고
    • Topological distribution of two connexin32 antigenic sites in intact and split rodent hepatocyte gap junctions
    • doi:10.1083/jcb.107.5.1817
    • Goodenough, D.A., D.L. Paul, and L. Jesaitis. 1988. Topological distribution of two connexin32 antigenic sites in intact and split rodent hepatocyte gap junctions. J. Cell Biol. 107:1817-1824. doi:10.1083/jcb.107.5. 1817
    • (1988) J. Cell Biol. , vol.107 , pp. 1817-1824
    • Goodenough, D.A.1    Paul, D.L.2    Jesaitis, L.3
  • 14
    • 0029860763 scopus 로고    scopus 로고
    • On the use of thiolmodifying agents to determine channel topology
    • doi:10.1016/0028-3908(96)00129-3
    • Holmgren, M., Y. Liu, Y. Xu, and G. Yellen. 1996. On the use of thiolmodifying agents to determine channel topology. Neuropharmacology. 35:797-804. doi:10.1016/0028-3908(96)00129-3
    • (1996) Neuropharmacology. , vol.35 , pp. 797-804
    • Holmgren, M.1    Liu, Y.2    Xu, Y.3    Yellen, G.4
  • 15
    • 0032942633 scopus 로고    scopus 로고
    • Exchange of conductance and gating properties between gap junction hemichannels
    • doi:10.1016/S0014-5793(99)00558-X
    • Hu, X., and G. Dahl. 1999. Exchange of conductance and gating properties between gap junction hemichannels. FEBS Lett. 451:113-117. doi:10.1016/S0014- 5793(99)00558-X
    • (1999) FEBS Lett. , vol.451 , pp. 113-117
    • Hu, X.1    Dahl, G.2
  • 16
    • 33646137561 scopus 로고    scopus 로고
    • Conductance of connexin hemichannels segregates with the first transmembrane segment
    • doi:10.1529/biophysj.105.066373
    • Hu, X., M. Ma, and G. Dahl. 2006. Conductance of connexin hemichannels segregates with the first transmembrane segment. Biophys. J. 90:140-150. doi:10.1529/biophysj.105.066373
    • (2006) Biophys. J. , vol.90 , pp. 140-150
    • Hu, X.1    Ma, M.2    Dahl, G.3
  • 17
    • 66149173401 scopus 로고    scopus 로고
    • Pannexin 1: The molecular substrate of astrocyte "hemichannels"
    • doi:10.1523/JNEUROSCI.6062-08.2009
    • Iglesias, R., G. Dahl, F. Qiu, D.C. Spray, and E. Scemes. 2009. Pannexin 1: the molecular substrate of astrocyte "hemichannels". J. Neurosci. 29:7092-7097. doi:10.1523/JNEUROSCI.6062-08.2009
    • (2009) J. Neurosci. , vol.29 , pp. 7092-7097
    • Iglesias, R.1    Dahl, G.2    Qiu, F.3    Spray, D.C.4    Scemes, E.5
  • 18
    • 0034697284 scopus 로고    scopus 로고
    • The yeast mitochondrial citrate transport protein. Probing the secondary structure of transmembrane domain iv and identification of residues that likely comprise a portion of the citrate translocation pathway
    • doi:10.1074/jbc.275.16.12009
    • Kaplan, R.S., J.A. Mayor, D. Brauer, R. Kotaria, D.E. Walters, and A.M. Dean. 2000. The yeast mitochondrial citrate transport protein. Probing the secondary structure of transmembrane domain iv and identification of residues that likely comprise a portion of the citrate translocation pathway. J. Biol. Chem. 275:12009-12016. doi:10.1074/jbc.275.16.12009
    • (2000) J. Biol. Chem. , vol.275 , pp. 12009-12016
    • Kaplan, R.S.1    Mayor, J.A.2    Brauer, D.3    Kotaria, R.4    Walters, D.E.5    Dean, A.M.6
  • 19
    • 0141919839 scopus 로고    scopus 로고
    • Single-channel SCAM identifies pore-lining residues in the first extracellular loop and first transmembrane domains of Cx46 hemichannels
    • doi:10.1085/jgp.200308861
    • Kronengold, J., E.B. Trexler, F.F. Bukauskas, T.A. Bargiello, and V.K. Verselis. 2003. Single-channel SCAM identifies pore-lining residues in the first extracellular loop and first transmembrane domains of Cx46 hemichannels. J. Gen. Physiol. 122:389-405. doi:10.1085/jgp.200308861
    • (2003) J. Gen. Physiol. , vol.122 , pp. 389-405
    • Kronengold, J.1    Trexler, E.B.2    Bukauskas, F.F.3    Bargiello, T.A.4    Verselis, V.K.5
  • 20
    • 0029990996 scopus 로고    scopus 로고
    • Dynamic rearrangement of the outer mouth of a K+ channel during gating
    • doi:10.1016/S0896-6273(00)80106-3
    • Liu, Y., M.E. Jurman, and G. Yellen. 1996. Dynamic rearrangement of the outer mouth of a K+ channel during gating. Neuron. 16:859-867. doi:10.1016/S0896-6273(00)80106-3
    • (1996) Neuron. , vol.16 , pp. 859-867
    • Liu, Y.1    Jurman, M.E.2    Yellen, G.3
  • 21
    • 33646748700 scopus 로고    scopus 로고
    • Pannexin 1 in erythrocytes: Function without a gap
    • doi:10.1073/pnas.0601037103
    • Locovei, S., L. Bao, and G. Dahl. 2006a. Pannexin 1 in erythrocytes: function without a gap. Proc. Natl. Acad. Sci. USA. 103:7655-7659. doi:10.1073/pnas.0601037103
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 7655-7659
    • Locovei, S.1    Bao, L.2    Dahl, G.3
  • 22
    • 29344452180 scopus 로고    scopus 로고
    • Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium
    • doi:10.1016/j.febslet.2005.12.004
    • Locovei, S., J. Wang, and G. Dahl. 2006b. Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium. FEBS Lett. 580:239-244. doi:10.1016/j.febslet.2005.12.004
    • (2006) FEBS Lett. , vol.580 , pp. 239-244
    • Locovei, S.1    Wang, J.2    Dahl, G.3
  • 23
    • 33846438625 scopus 로고    scopus 로고
    • Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex
    • doi:10.1016/j.febslet.2006.12.056
    • Locovei, S., E. Scemes, F. Qiu, D.C. Spray, and G. Dahl. 2007. Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex. FEBS Lett. 581:483-488. doi:10.1016/j.febslet.2006.12.056
    • (2007) FEBS Lett. , vol.581 , pp. 483-488
    • Locovei, S.1    Scemes, E.2    Qiu, F.3    Spray, D.C.4    Dahl, G.5
  • 24
    • 0028960949 scopus 로고
    • Silver as a probe of pore-forming residues in a potassium channel
    • doi:10.1126/science.7716526
    • Lü, Q., and C. Miller. 1995. Silver as a probe of pore-forming residues in a potassium channel. Science. 268:304-307. doi:10.1126/science. 7716526
    • (1995) Science. , vol.268 , pp. 304-307
    • Lü, Q.1    Miller, C.2
  • 25
    • 33646145304 scopus 로고    scopus 로고
    • Cosegregation of permeability and single-channel conductance in chimeric connexins
    • doi:10.1529/biophysj.105.066381
    • Ma, M., and G. Dahl. 2006. Cosegregation of permeability and single-channel conductance in chimeric connexins. Biophys. J. 90:151-163. doi:10.1529/biophysj.105.066381
    • (2006) Biophys. J. , vol.90 , pp. 151-163
    • Ma, M.1    Dahl, G.2
  • 26
    • 63849141447 scopus 로고    scopus 로고
    • Structure of the connexin 26 gap junction channel at 3.5 Å resolution
    • doi:10.1038/nature07869
    • 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 Å resolution. Nature. 458:597-602. doi: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
  • 27
    • 0035968321 scopus 로고    scopus 로고
    • Brefeldin A block of integrindependent mechanosensitive ATP release from Xenopus oocytes reveals a novel mechanism of mechanotransduction
    • doi:10.1074/jbc.M101500200
    • Maroto, R., and O.P. Hamill. 2001. Brefeldin A block of integrindependent mechanosensitive ATP release from Xenopus oocytes reveals a novel mechanism of mechanotransduction. J. Biol. Chem. 276:23867-23872. doi:10.1074/jbc.M101500200
    • (2001) J. Biol. Chem. , vol.276 , pp. 23867-23872
    • Maroto, R.1    Hamill, O.P.2
  • 28
    • 43749106037 scopus 로고    scopus 로고
    • Charges dispersed over the permeation pathway determine the charge selectivity and conductance of a Cx32 chimeric hemichannel
    • doi:10.1113/jphysiol.2008.150805
    • Oh, S., V.K. Verselis, and T.A. Bargiello. 2008. Charges dispersed over the permeation pathway determine the charge selectivity and conductance of a Cx32 chimeric hemichannel. J. Physiol. 586:2445-2461. doi:10.1113/jphysiol.2008. 150805
    • (2008) J. Physiol. , vol.586 , pp. 2445-2461
    • Oh, S.1    Verselis, V.K.2    Bargiello, T.A.3
  • 29
    • 18944394972 scopus 로고    scopus 로고
    • Evolution of gap junction proteins-The pannexin alternative
    • doi:10.1242/jeb.01547
    • Panchin, Y.V. 2005. Evolution of gap junction proteins-the pannexin alternative. J. Exp. Biol. 208:1415-1419. doi:10.1242/jeb.01547
    • (2005) J. Exp. Biol. , Issue.208 , pp. 1415-1419
    • Panchin, Y.V.1
  • 30
    • 0034729660 scopus 로고    scopus 로고
    • A ubiquitous family of putative gap junction molecules
    • doi:10.1016/S0960-9822(00)00576-5
    • Panchin, Y., I. Kelmanson, M. Matz, K. Lukyanov, N. Usman, and S. Lukyanov. 2000. A ubiquitous family of putative gap junction molecules. Curr. Biol. 10:R473-R474. doi:10.1016/S0960-9822(00)00576-5
    • (2000) Curr. Biol. , vol.10
    • Panchin, Y.1    Kelmanson, I.2    Matz, M.3    Lukyanov, K.4    Usman, N.5    Lukyanov, S.6
  • 31
    • 36549084087 scopus 로고    scopus 로고
    • Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins
    • doi:10.1242/jcs.009514
    • Penuela, S., R. Bhalla, X.Q. Gong, K.N. Cowan, S.J. Celetti, B.J. Cowan, D. Bai, Q. Shao, and D.W. Laird. 2007. Pannexin 1 and pannexin 3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins. J. Cell Sci. 120:3772-3783. doi:10.1242/jcs.009514
    • (2007) J. Cell Sci. , vol.120 , pp. 3772-3783
    • Penuela, S.1    Bhalla, R.2    Gong, X.Q.3    Cowan, K.N.4    Celetti, S.J.5    Cowan, B.J.6    Bai, D.7    Shao, Q.8    Laird, D.W.9
  • 32
    • 0031755597 scopus 로고    scopus 로고
    • Localization of a voltage gate in connexin46 gap junction hemichannels
    • doi:10.1016/S0006-3495(98)77676-3
    • Pfahnl, A., and G. Dahl. 1998. Localization of a voltage gate in connexin46 gap junction hemichannels. Biophys. J. 75:2323-2331. doi:10.1016/S0006-3495(98)77676-3
    • (1998) Biophys. J. , vol.75 , pp. 2323-2331
    • Pfahnl, A.1    Dahl, G.2
  • 33
    • 60849084461 scopus 로고    scopus 로고
    • A permeant regulating its permeation pore: Inhibition of pannexin 1 channels by ATP
    • doi:10.1152/ajpcell.00433.2008
    • Qiu, F., and G. Dahl. 2009. A permeant regulating its permeation pore: inhibition of pannexin 1 channels by ATP. Am. J. Physiol. Cell Physiol. 296:C250-C255. doi:10.1152/ajpcell.00433.2008
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296
    • Qiu, F.1    Dahl, G.2
  • 34
    • 0028018109 scopus 로고
    • A connexin-32 mutation associated with Charcot-Marie-Tooth disease does not affect channel formation in oocytes
    • doi:10.1016/0014-5793(94)00819-1
    • Rabadan-Diehl, C., G. Dahl, and R. Werner. 1994. A connexin-32 mutation associated with Charcot-Marie-Tooth disease does not affect channel formation in oocytes. FEBS Lett. 351:90-94. doi:10.1016/0014-5793(94)00819-1
    • (1994) FEBS Lett. , vol.351 , pp. 90-94
    • Rabadan-Diehl, C.1    Dahl, G.2    Werner, R.3
  • 36
    • 0030031307 scopus 로고    scopus 로고
    • Selected cysteine point mutations confer mercurial sensitivity to the mercurial-insensitive water channel MIWC/AQP-4
    • doi:10.1021/bi9520038
    • Shi, L.B., and A.S. Verkman. 1996. Selected cysteine point mutations confer mercurial sensitivity to the mercurial-insensitive water channel MIWC/AQP-4. Biochemistry. 35:538-544. doi:10.1021/bi9520038
    • (1996) Biochemistry. , vol.35 , pp. 538-544
    • Shi, L.B.1    Verkman, A.S.2
  • 37
    • 53449101616 scopus 로고    scopus 로고
    • Probenecid, a gout remedy, inhibits pannexin 1 channels
    • doi:10.1152/ajpcell.00227.2008
    • Silverman, W., S. Locovei, and G. Dahl. 2008. Probenecid, a gout remedy, inhibits pannexin 1 channels. Am. J. Physiol. Cell Physiol. 295:C761-C767. doi:10.1152/ajpcell.00227.2008
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Silverman, W.1    Locovei, S.2    Dahl, G.3
  • 39
    • 0037191101 scopus 로고    scopus 로고
    • Identification of amino acid residues lining the pore of a gap junction channel
    • doi:10.1083/jcb.200207060
    • Skerrett, I.M., J. Aronowitz, J.H. Shin, G. Cymes, E. Kasperek, F.L. Cao, and B.J. Nicholson. 2002. Identification of amino acid residues lining the pore of a gap junction channel. J. Cell Biol. 159:349-360. doi:10.1083/jcb.200207060
    • (2002) J. Cell Biol. , vol.159 , pp. 349-360
    • Skerrett, I.M.1    Aronowitz, J.2    Shin, J.H.3    Cymes, G.4    Kasperek, E.5    Cao, F.L.6    Nicholson, B.J.7
  • 40
    • 0029905253 scopus 로고    scopus 로고
    • Voltage gating and permeation in a gap junction hemichannel
    • doi:10.1073/pnas.93.12.5836
    • 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. doi:10.1073/pnas.93.12.5836
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 5836-5841
    • Trexler, E.B.1    Bennett, M.V.2    Bargiello, T.A.3    Verselis, V.K.4
  • 41
    • 0024848780 scopus 로고
    • The structure of ion channels in membranes of excitable cells
    • doi:10.1016/0896-6273(89)90235-3
    • Unwin, N. 1989. The structure of ion channels in membranes of excitable cells. Neuron. 3:665-676. doi:10.1016/0896-6273(89)90235-3
    • (1989) Neuron. , vol.3 , pp. 665-676
    • Unwin, N.1
  • 42
    • 34548764500 scopus 로고    scopus 로고
    • Modulation of membrane channel currents by gap junction protein mimetic peptides: Size matters
    • doi:10.1152/ajpcell.00097.2007
    • Wang, J., M. Ma, S. Locovei, R.W. Keane, and G. Dahl. 2007. Modulation of membrane channel currents by gap junction protein mimetic peptides: size matters. Am. J. Physiol. Cell Physiol. 293:C1112-C1119. doi:10.1152/ajpcell. 00097.2007
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Wang, J.1    Ma, M.2    Locovei, S.3    Keane, R.W.4    Dahl, G.5
  • 43
    • 34249060921 scopus 로고    scopus 로고
    • Gap junctional proteins of animals: The innexin/pannexin superfamily
    • doi:10.1016/j.pbiomolbio.2007.03.006
    • Yen, M.R., and M.H. Saier Jr. 2007. Gap junctional proteins of animals: the innexin/pannexin superfamily. Prog. Biophys. Mol. Biol. 94:5-14. doi:10.1016/j.pbiomolbio.2007.03.006
    • (2007) Prog. Biophys. Mol. Biol. , vol.94 , pp. 5-14
    • Yen, M.R.1    Saier Jr., M.H.2
  • 44
    • 0031456382 scopus 로고    scopus 로고
    • Identification of acetylcholine receptor channel-lining residues in the M1 segment of the beta-subunit
    • doi:10.1021/bi972357u
    • Zhang, H., and A. Karlin. 1997. Identification of acetylcholine receptor channel-lining residues in the M1 segment of the beta-subunit. Biochemistry. 36:15856-15864. doi:10.1021/bi972357u
    • (1997) Biochemistry. , vol.36 , pp. 15856-15864
    • Zhang, H.1    Karlin, A.2
  • 45
    • 0030897850 scopus 로고    scopus 로고
    • Identification of a pore lining segment in gap junction hemichannels
    • doi:10.1016/S0006-3495(97)78840-4
    • Zhou, X.W., A. Pfahnl, R. Werner, A. Hudder, A. Llanes, A. Luebke, and G. Dahl. 1997. Identification of a pore lining segment in gap junction hemichannels. Biophys. J. 72:1946-1953. doi:10.1016/S0006-3495(97)78840-4
    • (1997) Biophys. J. , vol.72 , pp. 1946-1953
    • Zhou, X.W.1    Pfahnl, A.2    Werner, R.3    Hudder, A.4    Llanes, A.5    Luebke, A.6    Dahl, G.7


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