메뉴 건너뛰기




Volumn 75, Issue , 2013, Pages 583-593

The bizarre pharmacology of the ATP release channel pannexin1

Author keywords

Apoptosis; Gap junction; Glibenclamide; Inflammasome; Malaria; Mitochondrium; Pannexin; Probenecid

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTIMALARIAL AGENT; CHLORIDE CHANNEL BLOCKING AGENT; GAP JUNCTION PROTEIN; INFLAMMASOME INHIBITOR; LIGAND; MITOCHONDRIAL INHIBITOR; P2X7 RECEPTOR LIGAND; PANNEXIN1; PROTEIN INHIBITOR; THIOL DERIVATIVE; TRANSPORT INHIBITOR; UNCLASSIFIED DRUG;

EID: 84890427145     PISSN: 00283908     EISSN: 18737064     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2013.02.019     Document Type: Review
Times cited : (104)

References (92)
  • 1
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • P.M. Abou-Sleiman, M.M. Muqit, and N.W. Wood Expanding insights of mitochondrial dysfunction in Parkinson's disease Nat. Rev. Neurosci. 7 2006 207 219
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 3
    • 4143127920 scopus 로고    scopus 로고
    • Pannexin membrane channels are mechanosensitive conduits for ATP
    • L. Bao, S. Locovei, and G. Dahl Pannexin membrane channels are mechanosensitive conduits for ATP FEBS Lett. 572 2004 65 68
    • (2004) FEBS Lett. , vol.572 , pp. 65-68
    • Bao, L.1    Locovei, S.2    Dahl, G.3
  • 4
    • 35748965595 scopus 로고    scopus 로고
    • Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane
    • D. Boassa, C. Ambrosi, F. Qiu, G. Dahl, G. Gaietta, and G. Sosinsky Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane J. Biol. Chem. 282 2007 31733 31743
    • (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
  • 5
    • 42649085323 scopus 로고    scopus 로고
    • Trafficking dynamics of glycosylated pannexin 1 proteins
    • D. Boassa, F. Qiu, G. Dahl, and G. Sosinsky Trafficking dynamics of glycosylated pannexin 1 proteins Cell. Commun. Adhes. 15 2008 119 132
    • (2008) Cell. Commun. Adhes. , vol.15 , pp. 119-132
    • Boassa, D.1    Qiu, F.2    Dahl, G.3    Sosinsky, G.4
  • 6
    • 0037285683 scopus 로고    scopus 로고
    • Photoliberating inositol-1,4,5-trisphosphate triggers ATP release that is blocked by the connexin mimetic peptide gap 26
    • K. Braet, W. Vandamme, P.E. Martin, W.H. Evans, and L. Leybaert Photoliberating inositol-1,4,5-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
  • 7
    • 14844334146 scopus 로고    scopus 로고
    • Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes
    • R. Bruzzone, M.T. Barbe, N.J. Jakob, and H. Monyer Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes J. Neurochem. 92 2005 1033 1043
    • (2005) J. Neurochem. , vol.92 , pp. 1033-1043
    • Bruzzone, R.1    Barbe, M.T.2    Jakob, N.J.3    Monyer, H.4
  • 9
    • 0027404826 scopus 로고
    • Multiple conductance states of newly formed single gap junction channels between insect cells
    • F.F. Bukauskas, and R. Weingart Multiple conductance states of newly formed single gap junction channels between insect cells Pflugers Archiv - Eur. J. Physiol. 423 1993 152 154
    • (1993) Pflugers Archiv - Eur. J. Physiol. , vol.423 , pp. 152-154
    • Bukauskas, F.F.1    Weingart, R.2
  • 10
    • 70349948843 scopus 로고    scopus 로고
    • The potassium channel subunit Kvbeta3 interacts with pannexin 1 and attenuates its sensitivity to changes in redox potentials
    • S. Bunse, S. Locovei, M. Schmidt, F. Qiu, G. Zoidl, G. Dahl, and R. Dermietzel The potassium channel subunit Kvbeta3 interacts with pannexin 1 and attenuates its sensitivity to changes in redox potentials FEBS J. 276 2009 6258 6270
    • (2009) FEBS J. , vol.276 , pp. 6258-6270
    • Bunse, S.1    Locovei, S.2    Schmidt, M.3    Qiu, F.4    Zoidl, G.5    Dahl, G.6    Dermietzel, R.7
  • 11
    • 78649684422 scopus 로고    scopus 로고
    • Intracellular cysteine 346 is essentially involved in regulating Panx1 channel activity
    • S. Bunse, M. Schmidt, N. Prochnow, G. Zoidl, and R. Dermietzel Intracellular cysteine 346 is essentially involved in regulating Panx1 channel activity J. Biol. Chem. 285 2010 38444 38452
    • (2010) J. Biol. Chem. , vol.285 , pp. 38444-38452
    • Bunse, S.1    Schmidt, M.2    Prochnow, N.3    Zoidl, G.4    Dermietzel, R.5
  • 14
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • M. Crompton The mitochondrial permeability transition pore and its role in cell death Biochem. J. 341 Pt 2 1999 233 249
    • (1999) Biochem. J. , vol.341 , Issue.PT 2 , pp. 233-249
    • Crompton, M.1
  • 15
    • 33745254724 scopus 로고    scopus 로고
    • The inflammatory process of gout and its treatment
    • B.N. Cronstein, and R. Terkeltaub The inflammatory process of gout and its treatment Arthritis Res. Ther. 8 Suppl. 1 2006 S3
    • (2006) Arthritis Res. Ther. , vol.8 , Issue.SUPPL. 1 , pp. 3
    • Cronstein, B.N.1    Terkeltaub, R.2
  • 17
    • 42149157824 scopus 로고    scopus 로고
    • Gap junction-mimetic peptides do work, but in unexpected ways
    • G. Dahl Gap junction-mimetic peptides do work, but in unexpected ways Cell. Commun. Adhes. 14 2007 259 264
    • (2007) Cell. Commun. Adhes. , vol.14 , pp. 259-264
    • Dahl, G.1
  • 18
    • 84869494557 scopus 로고    scopus 로고
    • Pannexin: From discovery to bedside in 11+/-4 years?
    • PMID: 22771709
    • G. Dahl, and R.W. Keane Pannexin: from discovery to bedside in 11+/-4 years? PMID: 22771709 Brain Res. 2012 150 159
    • (2012) Brain Res. , pp. 150-159
    • Dahl, G.1    Keane, R.W.2
  • 19
    • 33745712366 scopus 로고    scopus 로고
    • Pannexin: To Gap or not to Gap, is that a question?
    • G. Dahl, and S. Locovei Pannexin: to Gap or not to Gap, is that a question? IUBMB Life 58 2006 409 419
    • (2006) IUBMB Life , vol.58 , pp. 409-419
    • Dahl, G.1    Locovei, S.2
  • 20
    • 0028089678 scopus 로고
    • Attempts to define functional domains of gap junction proteins with synthetic peptides
    • G. Dahl, W. Nonner, and R. Werner Attempts to define functional domains of gap junction proteins with synthetic peptides Biophysical J. 67 1994 1816 1822
    • (1994) Biophysical J. , vol.67 , pp. 1816-1822
    • Dahl, G.1    Nonner, W.2    Werner, R.3
  • 21
    • 0026780731 scopus 로고
    • Mutational analysis of gap junction formation
    • discussion 180-172
    • G. Dahl, R. Werner, E. Levine, and C. Rabadan-Diehl Mutational analysis of gap junction formation Biophysical J. 62 1992 172 180 discussion 180-172
    • (1992) Biophysical J. , vol.62 , pp. 172-180
    • Dahl, G.1    Werner, R.2    Levine, E.3    Rabadan-Diehl, C.4
  • 23
    • 84856018136 scopus 로고    scopus 로고
    • Mitochondrial adenine nucleotide transport and cardioprotection
    • S. Das, and C. Steenbergen Mitochondrial adenine nucleotide transport and cardioprotection J. Mol. Cell. Cardiol. 52 2012 448 453
    • (2012) J. Mol. Cell. Cardiol. , vol.52 , pp. 448-453
    • Das, S.1    Steenbergen, C.2
  • 24
    • 0022620229 scopus 로고
    • Reversible inhibition of intercellular junctional communication by glycyrrhetinic acid
    • J.S. Davidson, I.M. Baumgarten, and E.H. Harley Reversible inhibition of intercellular junctional communication by glycyrrhetinic acid Biochem. Biophys. Res. Commun. 134 1986 29 36
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 29-36
    • Davidson, J.S.1    Baumgarten, I.M.2    Harley, E.H.3
  • 28
    • 80855130801 scopus 로고    scopus 로고
    • Mitochondrial calcium handling during ischemia-induced cell death in neurons
    • Y. Gouriou, N. Demaurex, P. Bijlenga, and U. De Marchi Mitochondrial calcium handling during ischemia-induced cell death in neurons Biochimie 93 2011 2060 2067
    • (2011) Biochimie , vol.93 , pp. 2060-2067
    • Gouriou, Y.1    Demaurex, N.2    Bijlenga, P.3    De Marchi, U.4
  • 31
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore complex: Another view
    • A.P. Halestrap, G.P. McStay, and S.J. Clarke The permeability transition pore complex: another view Biochimie 84 2002 153 166
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 32
    • 0030612880 scopus 로고    scopus 로고
    • Interleukin-1beta secretion is impaired by inhibitors of the Atp binding cassette transporter, ABC1
    • Y. Hamon, M.F. Luciani, F. Becq, B. Verrier, A. Rubartelli, and G. Chimini Interleukin-1beta secretion is impaired by inhibitors of the Atp binding cassette transporter, ABC1 Blood 90 1997 2911 2915
    • (1997) Blood , vol.90 , pp. 2911-2915
    • Hamon, Y.1    Luciani, M.F.2    Becq, F.3    Verrier, B.4    Rubartelli, A.5    Chimini, G.6
  • 35
    • 33751572168 scopus 로고    scopus 로고
    • Pannexin1 is expressed by neurons and glia but does not form functional gap junctions
    • Y. Huang, J.B. Grinspan, C.K. Abrams, and S.S. Scherer Pannexin1 is expressed by neurons and glia but does not form functional gap junctions Glia 55 2007 46 56
    • (2007) Glia , vol.55 , pp. 46-56
    • Huang, Y.1    Grinspan, J.B.2    Abrams, C.K.3    Scherer, S.S.4
  • 36
    • 66149173401 scopus 로고    scopus 로고
    • Pannexin 1: The molecular substrate of astrocyte hemichannels
    • R. Iglesias, G. Dahl, F. Qiu, D.C. Spray, and E. Scemes Pannexin 1: the molecular substrate of astrocyte hemichannels J. Neurosci. 29 2009 7092 7097
    • (2009) J. Neurosci. , vol.29 , pp. 7092-7097
    • Iglesias, R.1    Dahl, G.2    Qiu, F.3    Spray, D.C.4    Scemes, E.5
  • 37
    • 77951101287 scopus 로고    scopus 로고
    • Mefloquine blockade of Pannexin1 currents: Resolution of a conflict
    • R. Iglesias, D.C. Spray, and E. Scemes Mefloquine blockade of Pannexin1 currents: resolution of a conflict Cell. Commun. Adhes. 16 2009 131 137
    • (2009) Cell. Commun. Adhes. , vol.16 , pp. 131-137
    • Iglesias, R.1    Spray, D.C.2    Scemes, E.3
  • 38
    • 34547594520 scopus 로고    scopus 로고
    • Stimulation of rat erythrocyte P2X7 receptor induces the release of epoxyeicosatrienoic acids
    • H. Jiang, A.G. Zhu, M. Mamczur, J.R. Falck, K.M. Lerea, and J.C. McGiff Stimulation of rat erythrocyte P2X7 receptor induces the release of epoxyeicosatrienoic acids Br. J. Pharmacol. 151 2007 1033 1040
    • (2007) Br. J. Pharmacol. , vol.151 , pp. 1033-1040
    • Jiang, H.1    Zhu, A.G.2    Mamczur, M.3    Falck, J.R.4    Lerea, K.M.5    McGiff, J.C.6
  • 39
    • 0019302480 scopus 로고
    • Interaction of anaesthetics with electrical synapses
    • M.F. Johnston, S.A. Simon, and F. Ramon Interaction of anaesthetics with electrical synapses Nature 286 1980 498 500
    • (1980) Nature , vol.286 , pp. 498-500
    • Johnston, M.F.1    Simon, S.A.2    Ramon, F.3
  • 40
    • 78650944898 scopus 로고    scopus 로고
    • Pannexin1 constitutes the large conductance cation channel of cardiac myocytes
    • M.C. Kienitz, K. Bender, R. Dermietzel, L. Pott, and G. Zoidl Pannexin1 constitutes the large conductance cation channel of cardiac myocytes J. Biol. Chem. 286 2011 290 298
    • (2011) J. Biol. Chem. , vol.286 , pp. 290-298
    • Kienitz, M.C.1    Bender, K.2    Dermietzel, R.3    Pott, L.4    Zoidl, G.5
  • 43
    • 77249118801 scopus 로고    scopus 로고
    • The inflammasomes: Mechanisms of activation and function
    • E. Latz The inflammasomes: mechanisms of activation and function Curr. Opin. Immunol. 22 2010 28 33
    • (2010) Curr. Opin. Immunol. , vol.22 , pp. 28-33
    • Latz, E.1
  • 44
    • 33646748700 scopus 로고    scopus 로고
    • Pannexin1 in erythrocytes: Function without a gap
    • S. Locovei, L. Bao, and G. Dahl Pannexin1 in erythrocytes: function without a gap Proc. Natl. Acad. Sci. USA 103 2006 7655 7659
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7655-7659
    • Locovei, S.1    Bao, L.2    Dahl, G.3
  • 45
    • 29344452180 scopus 로고    scopus 로고
    • Activation of pannexin1 channels by ATP through P2Y receptors and by cytoplasmic calcium
    • S. Locovei, J. Wang, and G. Dahl Activation of pannexin1 channels by ATP through P2Y receptors and by cytoplasmic calcium FEBS Lett. 580 2006 239 244
    • (2006) FEBS Lett. , vol.580 , pp. 239-244
    • Locovei, S.1    Wang, J.2    Dahl, G.3
  • 46
    • 33846438625 scopus 로고    scopus 로고
    • Pannexin1 is part of the pore forming unit of the P2X7 receptor death complex
    • S. Locovei, E. Scemes, F. Qiu, D.C. Spray, and G. Dahl Pannexin1 is part of the pore forming unit of the P2X7 receptor death complex FEBS Lett. 581 2007 483 488
    • (2007) FEBS Lett. , vol.581 , pp. 483-488
    • Locovei, S.1    Scemes, E.2    Qiu, F.3    Spray, D.C.4    Dahl, G.5
  • 48
    • 59649088329 scopus 로고    scopus 로고
    • Pharmacological characterization of pannexin-1 currents expressed in mammalian cells
    • W. Ma, H. Hui, P. Pelegrin, and A. Surprenant Pharmacological characterization of pannexin-1 currents expressed in mammalian cells J. Pharmacol. Exp. Ther. 328 2009 409 418
    • (2009) J. Pharmacol. Exp. Ther. , vol.328 , pp. 409-418
    • Ma, W.1    Hui, H.2    Pelegrin, P.3    Surprenant, A.4
  • 49
    • 44849136632 scopus 로고    scopus 로고
    • Pannexin-1-mediated intracellular delivery of muramyl dipeptide induces caspase-1 activation via cryopyrin/NLRP3 independently of Nod2
    • N. Marina-Garcia, L. Franchi, Y.G. Kim, D. Miller, C. McDonald, G.J. Boons, and G. Nunez Pannexin-1-mediated intracellular delivery of muramyl dipeptide induces caspase-1 activation via cryopyrin/NLRP3 independently of Nod2 J. Immunol. 180 2008 4050 4057
    • (2008) J. Immunol. , vol.180 , pp. 4050-4057
    • Marina-Garcia, N.1    Franchi, L.2    Kim, Y.G.3    Miller, D.4    McDonald, C.5    Boons, G.J.6    Nunez, G.7
  • 50
    • 14844354847 scopus 로고    scopus 로고
    • ATP binding cassette transporter ABC1 is required for the release of interleukin-1beta by P2X7-stimulated and lipopolysaccharide-primed mouse Schwann cells
    • V. Marty, C. Medina, C. Combe, P. Parnet, and T. Amedee ATP binding cassette transporter ABC1 is required for the release of interleukin-1beta by P2X7-stimulated and lipopolysaccharide-primed mouse Schwann cells Glia 49 2005 511 519
    • (2005) Glia , vol.49 , pp. 511-519
    • Marty, V.1    Medina, C.2    Combe, C.3    Parnet, P.4    Amedee, T.5
  • 51
    • 0035876102 scopus 로고    scopus 로고
    • Molecular structure of the glibenclamide binding site of the beta-cell K(ATP) channel
    • M.V. Mikhailov, E.A. Mikhailova, and S.J. Ashcroft Molecular structure of the glibenclamide binding site of the beta-cell K(ATP) channel FEBS Lett. 499 2001 154 160
    • (2001) FEBS Lett. , vol.499 , pp. 154-160
    • Mikhailov, M.V.1    Mikhailova, E.A.2    Ashcroft, S.J.3
  • 53
    • 0345599926 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide/ATP-induced release of interleukin-18 by KN-62 and glyburide
    • H. Muhl, S. Hofler, and J. Pfeilschifter Inhibition of lipopolysaccharide/ATP-induced release of interleukin-18 by KN-62 and glyburide Eur. J. Pharmacol. 482 2003 325 328
    • (2003) Eur. J. Pharmacol. , vol.482 , pp. 325-328
    • Muhl, H.1    Hofler, S.2    Pfeilschifter, J.3
  • 54
    • 20644444992 scopus 로고    scopus 로고
    • Bongkrekic acid ameliorates ischemic neuronal death in the cortex by preventing cytochrome c release and inhibiting astrocyte activation
    • M. Muranyi, and P.A. Li Bongkrekic acid ameliorates ischemic neuronal death in the cortex by preventing cytochrome c release and inhibiting astrocyte activation Neurosci. Lett. 384 2005 277 281
    • (2005) Neurosci. Lett. , vol.384 , pp. 277-281
    • Muranyi, M.1    Li, P.A.2
  • 56
    • 0027364529 scopus 로고
    • Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ER
    • L.S. Musil, and D.A. Goodenough 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
  • 57
    • 51449124322 scopus 로고    scopus 로고
    • Colchicine: Its mechanism of action and efficacy in crystal-induced inflammation
    • G. Nuki Colchicine: its mechanism of action and efficacy in crystal-induced inflammation Curr. Rheumatol. Rep. 10 2008 218 227
    • (2008) Curr. Rheumatol. Rep. , vol.10 , pp. 218-227
    • Nuki, G.1
  • 59
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • P. Pelegrin, and A. Surprenant Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor Embo J. 25 2006 5071 5082
    • (2006) Embo J. , vol.25 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 60
    • 67349102910 scopus 로고    scopus 로고
    • The P2X(7) receptor-pannexin connection to dye uptake and IL-1beta release
    • P. Pelegrin, and A. Surprenant The P2X(7) receptor-pannexin connection to dye uptake and IL-1beta release Purinergic Signal. 5 2009 129 137
    • (2009) Purinergic Signal. , vol.5 , pp. 129-137
    • Pelegrin, P.1    Surprenant, A.2
  • 61
    • 36549084087 scopus 로고    scopus 로고
    • Pannexin 1 and pannexin3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins
    • S. Penuela, R. Bhalla, X.Q. Gong, K.N. Cowan, S.J. Celetti, B.J. Cowan, D. Bai, Q. Shao, and D.W. Laird Pannexin 1 and pannexin3 are glycoproteins that exhibit many distinct characteristics from the connexin family of gap junction proteins J. Cell. Sci. 120 2007 3772 3783
    • (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
  • 62
    • 70350112277 scopus 로고    scopus 로고
    • Glycosylation regulates pannexin intermixing and cellular localization
    • S. Penuela, R. Bhalla, K. Nag, and D.W. Laird Glycosylation regulates pannexin intermixing and cellular localization Mol. Biol. Cell. 20 2009 4313 4323
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 4313-4323
    • Penuela, S.1    Bhalla, R.2    Nag, K.3    Laird, D.W.4
  • 64
    • 60849084461 scopus 로고    scopus 로고
    • A permeant regulating its permeation pore: Inhibition of pannexin1 channels by ATP
    • F. Qiu, and G. Dahl A permeant regulating its permeation pore: inhibition of pannexin1 channels by ATP Am. J. Physiol. Cell. Physiol. 296 2009 C250 C255
    • (2009) Am. J. Physiol. Cell. Physiol. , vol.296
    • Qiu, F.1    Dahl, G.2
  • 65
    • 84857685160 scopus 로고    scopus 로고
    • Alanine substitution scanning of pannexin1 reveals amino acid residues mediating ATP sensitivity
    • F. Qiu, J. Wang, and G. Dahl Alanine substitution scanning of pannexin1 reveals amino acid residues mediating ATP sensitivity Purinergic Signal. 8 2012 81 90
    • (2012) Purinergic Signal. , vol.8 , pp. 81-90
    • Qiu, F.1    Wang, J.2    Dahl, G.3
  • 66
    • 80255138754 scopus 로고    scopus 로고
    • Two non-vesicular ATP release pathways in the mouse erythrocyte membrane
    • F. Qiu, J. Wang, D.C. Spray, E. Scemes, and G. Dahl Two non-vesicular ATP release pathways in the mouse erythrocyte membrane FEBS Lett. 585 2011 3430 3435
    • (2011) FEBS Lett. , vol.585 , pp. 3430-3435
    • Qiu, F.1    Wang, J.2    Spray, D.C.3    Scemes, E.4    Dahl, G.5
  • 68
    • 33748323257 scopus 로고    scopus 로고
    • Glutamate acts at NMDA receptors on fresh bovine and on cultured human retinal pigment epithelial cells to trigger release of ATP
    • D. Reigada, W. Lu, and C.H. Mitchell Glutamate acts at NMDA receptors on fresh bovine and on cultured human retinal pigment epithelial cells to trigger release of ATP J. Physiol. 575 2006 707 720
    • (2006) J. Physiol. , vol.575 , pp. 707-720
    • Reigada, D.1    Lu, W.2    Mitchell, C.H.3
  • 69
    • 0034853407 scopus 로고    scopus 로고
    • Volume-dependent ATP-conductive large-conductance anion channel as a pathway for swelling-induced ATP release
    • R.Z. Sabirov, A.K. Dutta, and Y. Okada Volume-dependent ATP-conductive large-conductance anion channel as a pathway for swelling-induced ATP release J. Gen. Physiol. 118 2001 251 266
    • (2001) J. Gen. Physiol. , vol.118 , pp. 251-266
    • Sabirov, R.Z.1    Dutta, A.K.2    Okada, Y.3
  • 71
    • 84861582003 scopus 로고    scopus 로고
    • Nature of plasmalemmal functional "hemichannels"
    • E. Scemes Nature of plasmalemmal functional "hemichannels" Biochim. Biophys. Acta 1818 2011 1863 1880
    • (2011) Biochim. Biophys. Acta , vol.1818 , pp. 1863-1880
    • Scemes, E.1
  • 73
    • 74549184092 scopus 로고    scopus 로고
    • The NLRP3 inflammasome: A sensor for metabolic danger?
    • K. Schroder, R. Zhou, and J. Tschopp The NLRP3 inflammasome: a sensor for metabolic danger? Science 327 2010 296 300
    • (2010) Science , vol.327 , pp. 296-300
    • Schroder, K.1    Zhou, R.2    Tschopp, J.3
  • 79
    • 0018615322 scopus 로고
    • Inhibitors of the adenine nucleotide translocase
    • M. Stubbs Inhibitors of the adenine nucleotide translocase Pharmacol. Ther. 7 1979 329 350
    • (1979) Pharmacol. Ther. , vol.7 , pp. 329-350
    • Stubbs, M.1
  • 80
    • 0021840516 scopus 로고
    • The sulphonylurea receptor may be an ATP-sensitive potassium channel
    • N.C. Sturgess, M.L. Ashford, D.L. Cook, and C.N. Hales The sulphonylurea receptor may be an ATP-sensitive potassium channel Lancet 2 1985 474 475
    • (1985) Lancet , vol.2 , pp. 474-475
    • Sturgess, N.C.1    Ashford, M.L.2    Cook, D.L.3    Hales, C.N.4
  • 81
    • 84860658309 scopus 로고    scopus 로고
    • ATP signaling is deficient in cultured pannexin1-null mouse astrocytes
    • S.O. Suadicani, R. Iglesias, J. Wang, G. Dahl, D.C. Spray, and E. Scemes ATP signaling is deficient in cultured pannexin1-null mouse astrocytes Glia 60 2012 1106 1116
    • (2012) Glia , vol.60 , pp. 1106-1116
    • Suadicani, S.O.1    Iglesias, R.2    Wang, J.3    Dahl, G.4    Spray, D.C.5    Scemes, E.6
  • 82
    • 52649150872 scopus 로고    scopus 로고
    • Pannexins are new molecular candidates for assembling gap junctions in the cochlea
    • W. Tang, S. Ahmad, V.I. Shestopalov, and X. Lin Pannexins are new molecular candidates for assembling gap junctions in the cochlea Neuroreport 19 2008 1253 1257
    • (2008) Neuroreport , vol.19 , pp. 1253-1257
    • Tang, W.1    Ahmad, S.2    Shestopalov, V.I.3    Lin, X.4
  • 84
    • 33646584876 scopus 로고    scopus 로고
    • Ischemia opens neuronal gap junction hemichannels
    • R.J. Thompson, N. Zhou, and B.A. MacVicar Ischemia opens neuronal gap junction hemichannels Science 312 2006 924 927
    • (2006) Science , vol.312 , pp. 924-927
    • Thompson, R.J.1    Zhou, N.2    Macvicar, B.A.3
  • 86
    • 84862675016 scopus 로고    scopus 로고
    • P53 opens the mitochondrial permeability transition pore to trigger necrosis
    • A.V. Vaseva, N.D. Marchenko, K. Ji, S.E. Tsirka, S. Holzmann, and U.M. Moll p53 opens the mitochondrial permeability transition pore to trigger necrosis Cell 149 2012 1536 1548
    • (2012) Cell , vol.149 , pp. 1536-1548
    • Vaseva, A.V.1    Marchenko, N.D.2    Ji, K.3    Tsirka, S.E.4    Holzmann, S.5    Moll, U.M.6
  • 87
    • 78649480274 scopus 로고    scopus 로고
    • SCAM analysis of Panx1 suggests a peculiar pore structure
    • J. Wang, and G. Dahl SCAM analysis of Panx1 suggests a peculiar pore structure J. Gen. Physiol. 136 2010 515 527
    • (2010) J. Gen. Physiol. , vol.136 , pp. 515-527
    • Wang, J.1    Dahl, G.2
  • 88
    • 34548764500 scopus 로고    scopus 로고
    • Modulation of membrane channel currents by gap junction protein mimetic peptides: Size matters
    • J. Wang, M. Ma, S. Locovei, R.W. Keane, and G. Dahl Modulation of membrane channel currents by gap junction protein mimetic peptides: size matters Am. J. Physiol. Cell. Physiol. 293 2007 C1112 C1119
    • (2007) Am. J. Physiol. Cell. Physiol. , vol.293
    • Wang, J.1    Ma, M.2    Locovei, S.3    Keane, R.W.4    Dahl, G.5
  • 89
    • 0028819911 scopus 로고
    • Specific motifs in the external loops of connexin proteins can determine gap junction formation between chick heart myocytes [published erratum appears in J Physiol (Lond) 1996 Feb 1;490(Pt 3):827]
    • A. Warner, D.K. Clements, S. Parikh, W.H. Evans, and R.L. DeHaan Specific motifs in the external loops of connexin proteins can determine gap junction formation between chick heart myocytes [published erratum appears in J Physiol (Lond) 1996 Feb 1;490(Pt 3):827] J. Physiol. 488 1995 721 728
    • (1995) J. Physiol. , vol.488 , pp. 721-728
    • Warner, A.1    Clements, D.K.2    Parikh, S.3    Evans, W.H.4    Dehaan, R.L.5
  • 91
    • 84861005703 scopus 로고    scopus 로고
    • Neurons respond directly to mechanical deformation with pannexin-mediated ATP release and autostimulation of P2X7 receptors
    • J. Xia, J.C. Lim, W. Lu, J.M. Beckel, E.J. Macarak, A.M. Laties, and C.H. Mitchell Neurons respond directly to mechanical deformation with pannexin-mediated ATP release and autostimulation of P2X7 receptors J. Physiol. 590 2012 2285 2304
    • (2012) J. Physiol. , vol.590 , pp. 2285-2304
    • Xia, J.1    Lim, J.C.2    Lu, W.3    Beckel, J.M.4    Macarak, E.J.5    Laties, A.M.6    Mitchell, C.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.