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Volumn 370, Issue 1672, 2015, Pages 1-11

ATP release through pannexon channels

Author keywords

Allosteric; ATP; Conductance; Pannexin; Permeability; Potassium

Indexed keywords

APOPTOSIS; BRAIN; CALCIUM; CONDUCTIVITY; MEMBRANE; OXYGEN; PERMEABILITY; PHOSPHATE (ORGANIC); PHYSIOLOGY; POTASSIUM; PROTEIN; SIGNAL;

EID: 84930982265     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2014.0191     Document Type: Article
Times cited : (187)

References (110)
  • 1
    • 0025569752 scopus 로고
    • Overview. Purinergic mechanisms
    • discussion 8
    • Burnstock G. 1990 Overview. Purinergic mechanisms. Ann. N.Y. Acad. Sci. 603, 1-17; discussion 8. (doi:10.1111/j.1749-6632.1990.tb37657.x)
    • (1990) Ann. N.Y. Acad. Sci , vol.603 , pp. 1-17
    • Burnstock, G.1
  • 2
    • 0028998316 scopus 로고
    • Current state of purinoceptor research. Pharm
    • Burnstock G. 1995 Current state of purinoceptor research. Pharm. Acta Helv. 69, 231-242. (doi:10.1016/0031-6865(94)00043-U)
    • (1995) Acta Helv , vol.69 , pp. 231-242
    • Burnstock, G.1
  • 3
    • 46449134214 scopus 로고    scopus 로고
    • Purinergic signalling and disorders of the central nervous system. Nat
    • Burnstock G. 2008 Purinergic signalling and disorders of the central nervous system. Nat. Rev. Drug Discov. 7, 575-590. (doi:10.1038/nrd2605)
    • (2008) Rev. Drug Discov , vol.7 , pp. 575-590
    • Burnstock, G.1
  • 4
    • 84940815279 scopus 로고
    • The physiological activity of adenine compounds with especial reference to their action upon the mammalian heart
    • Drury AN, Szent-Gyorgyi A. 1929 The physiological activity of adenine compounds with especial reference to their action upon the mammalian heart. J. Physiol. 68, 213-237. (doi:10.1113/jphysiol.1929.sp002608)
    • (1929) J. Physiol , vol.68 , pp. 213-237
    • Drury, A.N.1    Szent-Gyorgyi, A.2
  • 5
    • 4243340417 scopus 로고
    • The possibility that ATP is a transmitter at sensory nerve endings
    • Holton FA, Holton P. 1953 The possibility that ATP is a transmitter at sensory nerve endings. J. Physiol. 119, 50P-51P.
    • (1953) J. Physiol , vol.119 , pp. 50P-51P
    • Holton, F.A.1    Holton, P.2
  • 6
    • 0000563758 scopus 로고
    • The capillary dilator substances in dry powders of spinal roots; a possible role of adenosine triphosphate in chemical transmission from nerve endings
    • Holton FA, Holton P. 1954 The capillary dilator substances in dry powders of spinal roots; a possible role of adenosine triphosphate in chemical transmission from nerve endings. J. Physiol. 126, 124-140. (doi:10.1113/jphysiol.1954.sp005198)
    • (1954) J. Physiol , vol.126 , pp. 124-140
    • Holton, F.A.1    Holton, P.2
  • 7
    • 0014891847 scopus 로고
    • Evidence that adenosine triphosphate or a related nucleotide is the transmitter substance released by non-adrenergic inhibitory nerves in the gut
    • Burnstock G, Campbell G, Satchell D, Smythe A. 1970 Evidence that adenosine triphosphate or a related nucleotide is the transmitter substance released by non-adrenergic inhibitory nerves in the gut. Br. J. Pharmacol. 40, 668-688. (doi:10.1111/j.1476-5381.1970.tb10646.x)
    • (1970) Br. J. Pharmacol , vol.40 , pp. 668-688
    • Burnstock, G.1    Campbell, G.2    Satchell, D.3    Smythe, A.4
  • 8
    • 0015235864 scopus 로고
    • Neural nomenclature
    • Burnstock G. 1971 Neural nomenclature. Nature 229, 282-283. (doi:10.1038/229282d0)
    • (1971) Nature , vol.229 , pp. 282-283
    • Burnstock, G.1
  • 9
    • 0015237341 scopus 로고
    • [3H]adenosine triphosphate: Release during stimulation of enteric nerves
    • Su C, Bevan JA, Burnstock G. 1971 [3H]adenosine triphosphate: release during stimulation of enteric nerves. Science 173, 336-338. (doi:10.1126/science.173.3994.336)
    • (1971) Science , vol.173 , pp. 336-338
    • Su, C.1    Bevan, J.A.2    Burnstock, G.3
  • 10
    • 0020079880 scopus 로고
    • The effects of purified botulinum neurotoxin type A on cholinergic, adrenergic and non-adrenergic, atropine-resistant autonomic neuromuscular transmission
    • MacKenzie I, Burnstock G, Dolly JO. 1982 The effects of purified botulinum neurotoxin type A on cholinergic, adrenergic and non-adrenergic, atropine-resistant autonomic neuromuscular transmission. Neuroscience 7, 997-1006. (doi:10.1016/0306-4522(82)90056-2)
    • (1982) Neuroscience , vol.7 , pp. 997-1006
    • Mackenzie, I.1    Burnstock, G.2    Dolly, J.O.3
  • 11
    • 0018100288 scopus 로고
    • Chemical and physical characterization of cholinergic synaptic vesicles
    • Wagner JA, Carlson SS, Kelly RB. 1978 Chemical and physical characterization of cholinergic synaptic vesicles. Biochemistry 17, 1199-1206. (doi:10.1021/bi00600a010)
    • (1978) Biochemistry , vol.17 , pp. 1199-1206
    • Wagner, J.A.1    Carlson, S.S.2    Kelly, R.B.3
  • 12
    • 0016741237 scopus 로고
    • On the association between transmitter secretion and the release of adenine nucleotides from mammalian motor nerve terminals
    • Silinsky EM. 1975 On the association between transmitter secretion and the release of adenine nucleotides from mammalian motor nerve terminals. J. Physiol. 247, 145-162. (doi:10.1113/jphysiol.1975.sp010925)
    • (1975) J. Physiol , vol.247 , pp. 145-162
    • Silinsky, E.M.1
  • 13
    • 0025060145 scopus 로고
    • Acetylcholine and ATP are coreleased from the electromotor nerve terminals of Narcine brasiliensis by an exocytotic mechanism
    • Unsworth CD, Johnson RG. 1990 Acetylcholine and ATP are coreleased from the electromotor nerve terminals of Narcine brasiliensis by an exocytotic mechanism. Proc. Natl Acad. Sci. USA 87, 553-557. (doi:10.1073/pnas.87.2.553)
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 553-557
    • Unsworth, C.D.1    Johnson, R.G.2
  • 15
    • 84860144966 scopus 로고    scopus 로고
    • Functional and anatomical identification of a vesicular transporter mediating neuronal ATP release. Cereb
    • Larsson M, Sawada K, Morland C, Hiasa M, Ormel L, Moriyama Y, Gundersen V. 2011 Functional and anatomical identification of a vesicular transporter mediating neuronal ATP release. Cereb. Cortex 22, 1203-1214. (doi:10.1093/cercor/bhr203)
    • (2011) Cortex , vol.22 , pp. 1203-1214
    • Larsson, M.1    Sawada, K.2    Morland, C.3    Hiasa, M.4    Ormel, L.5    Moriyama, Y.6    Gundersen, V.7
  • 16
    • 0030220030 scopus 로고    scopus 로고
    • Neuronal synthesis, storage and release of ATP
    • Sperlágh B, Vizi SE. 1996 Neuronal synthesis, storage and release of ATP. The Neurosciences 8, 175-186. (doi:10.1006/smns.1996.0023)
    • (1996) The Neurosciences , vol.8 , pp. 175-186
    • Sperlágh, B.1    Vizi, S.E.2
  • 17
    • 0027264923 scopus 로고
    • ATP: A fast neurotransmitter
    • Edwards FA, Gibb AJ. 1993 ATP: a fast neurotransmitter. FEBS Lett. 325, 86-89. (doi:10.1016/0014-5793(93)81419-Z)
    • (1993) FEBS Lett , vol.325 , pp. 86-89
    • Edwards, F.A.1    Gibb, A.J.2
  • 18
    • 85047676379 scopus 로고
    • Release of ATP from human erythrocytes in response to a brief period of hypoxia and hypercapnia. Cardiovasc
    • Bergfeld GR, Forrester T. 1992 Release of ATP from human erythrocytes in response to a brief period of hypoxia and hypercapnia. Cardiovasc. Res. 26, 40-47. (doi:10.1093/cvr/26.1.40)
    • (1992) Res , vol.26 , pp. 40-47
    • Bergfeld, G.R.1    Forrester, T.2
  • 19
    • 0030013341 scopus 로고    scopus 로고
    • Non-synaptic release of ATP by electrical stimulation in slices of rat hippocampus, cerebellum and habenula
    • Hamann M, Attwell D. 1996 Non-synaptic release of ATP by electrical stimulation in slices of rat hippocampus, cerebellum and habenula. Eur. J. Neurosci. 8, 1510-1515. (doi:10.1111/j.1460-9568.1996.tb01613.x)
    • (1996) Eur. J. Neurosci , vol.8 , pp. 1510-1515
    • Hamann, M.1    Attwell, D.2
  • 20
    • 0346496120 scopus 로고    scopus 로고
    • Connexin channels, connexin mimetic peptides and ATP release. Cell. Commun
    • Leybaert L, Braet K, Vandamme W, Cabooter L, Martin PE, Evans WH. 2003 Connexin channels, connexin mimetic peptides and ATP release. Cell. Commun. Adhes. 10, 251-257. (doi:10.1080/cac.10.4-6.251.257)
    • (2003) Adhes , vol.10 , pp. 251-257
    • Leybaert, L.1    Braet, K.2    Vandamme, W.3    Cabooter, L.4    Martin, P.E.5    Evans, W.H.6
  • 21
    • 33646748700 scopus 로고    scopus 로고
    • Pannexin 1 in erythrocytes: Function without a gap
    • Locovei S, Bao L, Dahl G. 2006 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
    • 84901841296 scopus 로고    scopus 로고
    • Biology of purinergic signalling: Its ancient evolutionary roots, its omnipresence and its multiple functional significance
    • Verkhratsky A, Burnstock G. 2014 Biology of purinergic signalling: its ancient evolutionary roots, its omnipresence and its multiple functional significance. Bioessays 36, 697-705. (doi:10.1002/bies.201400024)
    • (2014) Bioessays , vol.36 , pp. 697-705
    • Verkhratsky, A.1    Burnstock, G.2
  • 24
    • 53449101616 scopus 로고    scopus 로고
    • Probenecid, a gout remedy, inhibits pannexin 1 channels
    • Silverman W, Locovei S, Dahl G. 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 , pp. C761-C767
    • Silverman, W.1    Locovei, S.2    Dahl, G.3
  • 25
    • 35748965595 scopus 로고    scopus 로고
    • Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane
    • Boassa D, Ambrosi C, Qiu F, Dahl G, Gaietta G, Sosinsky G. 2007 Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane. J. Biol. Chem. 282, 31 733-31 743. (doi:10.1074/jbc.M702422200)
    • (2007) J. Biol. Chem , vol.282 , Issue.31-743 , pp. 733-831
    • Boassa, D.1    Ambrosi, C.2    Qiu, F.3    Dahl, G.4    Gaietta, G.5    Sosinsky, G.6
  • 26
    • 33745712366 scopus 로고    scopus 로고
    • Pannexin: To gap or not to gap, is that a question?
    • Dahl G, Locovei S. 2006 Pannexin: to gap or not to gap, is that a question? IUBMB Life 58, 409-419. (doi:10.1080/15216540600794526)
    • (2006) IUBMB Life , vol.58 , pp. 409-419
    • Dahl, G.1    Locovei, S.2
  • 27
    • 0027937589 scopus 로고
    • The cystic fibrosis transmembrane conductance regulator is a dual ATP and chloride channel
    • 591
    • Reisin IL et al. 1994 The cystic fibrosis transmembrane conductance regulator is a dual ATP and chloride channel. J. Biol. Chem. 269, 20 584-20 591.
    • (1994) J. Biol. Chem , vol.269 , Issue.20 , pp. 584-620
    • Reisin, I.L.1
  • 28
    • 43049105822 scopus 로고    scopus 로고
    • Maxi-anion channel as a candidate pathway for osmosensitive ATP release from mouse astrocytes in primary culture
    • Liu HT, Toychiev AH, Takahashi N, Sabirov RZ, Okada Y. 2008 Maxi-anion channel as a candidate pathway for osmosensitive ATP release from mouse astrocytes in primary culture. Cell Res. 18, 558-565. (doi:10.1038/cr.2008.49)
    • (2008) Cell Res , vol.18 , pp. 558-565
    • Liu, H.T.1    Toychiev, A.H.2    Takahashi, N.3    Sabirov, R.Z.4    Okada, Y.5
  • 30
    • 84874956365 scopus 로고    scopus 로고
    • CALHM1 ion channel mediates purinergic neurotransmission of sweet, bitter and umami tastes
    • Taruno A et al. 2013 CALHM1 ion channel mediates purinergic neurotransmission of sweet, bitter and umami tastes. Nature 495, 223-226. (doi:10.1038/nature11906)
    • (2013) Nature , vol.495 , pp. 223-226
    • Taruno, A.1
  • 31
    • 4143127920 scopus 로고    scopus 로고
    • Pannexin membrane channels are mechanosensitive conduits for ATP
    • Bao L, Locovei S, Dahl G. 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
  • 32
    • 0029882509 scopus 로고    scopus 로고
    • CFTR channels expressed in CHO cells do not have detectable ATP conductance
    • Grygorczyk R, Tabcharani JA, Hanrahan JW. 1996 CFTR channels expressed in CHO cells do not have detectable ATP conductance. J. Membr. Biol. 151, 139-148. (doi:10.1007/s002329900065)
    • (1996) J. Membr. Biol , vol.151 , pp. 139-148
    • Grygorczyk, R.1    Tabcharani, J.A.2    Hanrahan, J.W.3
  • 34
    • 14844334146 scopus 로고    scopus 로고
    • Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes
    • Bruzzone R, Barbe MT, Jakob NJ, Monyer H. 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
  • 35
    • 84890427145 scopus 로고    scopus 로고
    • The bizarre pharmacology of the ATP release channel pannexin1
    • Dahl G, Qiu F, Wang J. 2013 The bizarre pharmacology of the ATP release channel pannexin1. Neuropharmacology 75, 150-159. (doi:10.1016/j.neuropharm.2013.02.019)
    • (2013) Neuropharmacology , vol.75 , pp. 150-159
    • Dahl, G.1    Qiu, F.2    Wang, J.3
  • 38
    • 84869200750 scopus 로고    scopus 로고
    • Intrarenal localization of the plasma membrane ATP channel pannexin1
    • Hanner F, Lam L, Nguyen MT, Yu A, Peti-Peterdi J. 2012 Intrarenal localization of the plasma membrane ATP channel pannexin1. Am. J. Physiol. Renal Physiol. 303, F1454-F1459. (doi:10.1152/ajprenal.00206.2011)
    • (2012) Am. J. Physiol. Renal Physiol , vol.303 , pp. F1454-F1459
    • Hanner, F.1    Lam, L.2    Nguyen, M.T.3    Yu, A.4    Peti-Peterdi, J.5
  • 39
    • 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
    • Penuela S, Bhalla R, Gong XQ, Cowan KN, Celetti SJ, Cowan BJ, Bai D, Shao Q, Laird DW. 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
  • 40
    • 0345255097 scopus 로고    scopus 로고
    • Pannexins, a family of gap junction proteins expressed in brain
    • 649
    • Bruzzone R, Hormuzdi SG, Barbe MT, Herb A, Monyer H. 2003 Pannexins, a family of gap junction proteins expressed in brain. Proc. Natl Acad. Sci. USA 100, 13 644-13 649. (doi:10.1073/pnas.2233464100)
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , Issue.13 , pp. 644-713
    • Bruzzone, R.1    Hormuzdi, S.G.2    Barbe, M.T.3    Herb, A.4    Monyer, H.5
  • 41
    • 34548764500 scopus 로고    scopus 로고
    • Modulation of membrane channel currents by gap junction protein mimetic peptides: Size matters
    • Wang J, Ma M, Locovei S, Keane RW, Dahl G. 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 , pp. C1112-C1119
    • Wang, J.1    Ma, M.2    Locovei, S.3    Keane, R.W.4    Dahl, G.5
  • 43
    • 77957834139 scopus 로고    scopus 로고
    • Neuroglial ATP release through innexin channels controls microglial cell movement to a nerve injury
    • Samuels SE, Lipitz JB, Dahl G, Muller KJ. 2010 Neuroglial ATP release through innexin channels controls microglial cell movement to a nerve injury. J. Gen. Physiol. 136, 425-442. (doi:10.1085/jgp.201010476)
    • (2010) J. Gen. Physiol , vol.136 , pp. 425-442
    • Samuels, S.E.1    Lipitz, J.B.2    Dahl, G.3    Muller, K.J.4
  • 44
    • 84880319581 scopus 로고    scopus 로고
    • Arachidonic acid closes innexin/pannexin channels and thereby inhibits microglia cell movement to a nerve injury. Dev
    • Samuels SE, Lipitz JB, Wang J, Dahl G, Muller KJ. 2013 Arachidonic acid closes innexin/pannexin channels and thereby inhibits microglia cell movement to a nerve injury. Dev. Neurobiol. 73, 621-631. (doi:10.1002/dneu.22088)
    • (2013) Neurobiol , vol.73 , pp. 621-631
    • Samuels, S.E.1    Lipitz, J.B.2    Wang, J.3    Dahl, G.4    Muller, K.J.5
  • 45
    • 84898891936 scopus 로고    scopus 로고
    • Innexin and pannexin channels and their signaling
    • Dahl G, Muller KJ. 2014 Innexin and pannexin channels and their signaling. FEBS Lett. 588, 1396-1402. (doi:10.1016/j.febslet.2014.03.007)
    • (2014) FEBS Lett , vol.588 , pp. 1396-1402
    • Dahl, G.1    Muller, K.J.2
  • 46
    • 80255138754 scopus 로고    scopus 로고
    • Two non-vesicular ATP release pathways in the mouse erythrocyte membrane
    • Qiu F, Wang J, Spray DC, Scemes E, Dahl G. 2011 Two non-vesicular ATP release pathways in the mouse erythrocyte membrane. FEBS Lett. 585, 3430-3435. (doi:10.1016/j.febslet.2011.09.033)
    • (2011) FEBS Lett , vol.585 , pp. 3430-3435
    • Qiu, F.1    Wang, J.2    Spray, D.C.3    Scemes, E.4    Dahl, G.5
  • 47
    • 84860658309 scopus 로고    scopus 로고
    • ATP signaling is deficient in cultured pannexin1-null mouse astrocytes
    • Suadicani SO, Iglesias R, Wang J, Dahl G, Spray DC, Scemes E. 2012 ATP signaling is deficient in cultured pannexin1-null mouse astrocytes. Glia 60, 1106-1116. (doi:10.1002/glia.22338)
    • (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
  • 48
    • 79960694399 scopus 로고    scopus 로고
    • Rho signaling regulates pannexin 1-mediated ATP release from airway epithelia
    • Seminario-Vidal L et al. 2011 Rho signaling regulates pannexin 1-mediated ATP release from airway epithelia. J. Biol. Chem. 286, 26 277-26 286. (doi:10.1074/jbc.M111.260562)
    • (2011) J. Biol. Chem. 286 , vol.277-26 , Issue.286 , pp. 26
    • Seminario-Vidal, L.1
  • 50
    • 79956336722 scopus 로고    scopus 로고
    • Expression and roles of pannexins in ATP release in the pituitary gland
    • Li S, Bjelobaba I, Yan Z, Kucka M, Tomic M, Stojilkovic SS. 2011 Expression and roles of pannexins in ATP release in the pituitary gland. Endocrinology 152, 2342-2352. (doi:10.1210/en.2010-1216)
    • (2011) Endocrinology , vol.152 , pp. 2342-2352
    • Li, S.1    Bjelobaba, I.2    Yan, Z.3    Kucka, M.4    Tomic, M.5    Stojilkovic, S.S.6
  • 51
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • Pelegrin P, Surprenant A. 2006 Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor. EMBO J. 25, 5071-5082. (doi:10.1038/sj.emboj.7601378)
    • (2006) EMBO J , vol.25 , pp. 5071-5082
    • Pelegrin, P.1    Surprenant, A.2
  • 52
    • 29344452180 scopus 로고    scopus 로고
    • Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium
    • Locovei S, Wang J, Dahl G. 2006 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
  • 53
    • 33846438625 scopus 로고    scopus 로고
    • Pannexin1 is part of the pore forming unit of the P2X receptor death complex
    • Locovei S, Scemes E, Qiu F, Spray DC, Dahl G. 2007 Pannexin1 is part of the pore forming unit of the P2X 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
  • 54
    • 60849084461 scopus 로고    scopus 로고
    • A permeant regulating its permeation pore: Inhibition of pannexin 1 channels by ATP
    • Qiu F, Dahl G. 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 , pp. C250-C255
    • Qiu, F.1    Dahl, G.2
  • 55
    • 84857685160 scopus 로고    scopus 로고
    • Alanine substitution scanning of pannexin1 reveals amino acid residues mediating ATP sensitivity
    • Qiu F, Wang J, Dahl G. 2012 Alanine substitution scanning of pannexin1 reveals amino acid residues mediating ATP sensitivity. Purinergic Signal. 8, 81-90. (doi:10.1007/s11302-011-9263-6)
    • (2012) Purinergic Signal , vol.8 , pp. 81-90
    • Qiu, F.1    Wang, J.2    Dahl, G.3
  • 56
    • 78649480274 scopus 로고    scopus 로고
    • SCAM analysis of Panx1 suggests a peculiar pore structure
    • Wang J, Dahl G. 2010 SCAM analysis of Panx1 suggests a peculiar pore structure. J. Gen. Physiol. 136, 515-527. (doi:10.1085/jgp.201010440)
    • (2010) J. Gen. Physiol , vol.136 , pp. 515-527
    • Wang, J.1    Dahl, G.2
  • 57
    • 33646584876 scopus 로고    scopus 로고
    • Ischemia opens neuronal gap junction hemichannels
    • Thompson RJ, Zhou N, MacVicar BA. 2006 Ischemia opens neuronal gap junction hemichannels. Science 312, 924-927. (doi:10.1126/science.1126241)
    • (2006) Science , vol.312 , pp. 924-927
    • Thompson, R.J.1    Zhou, N.2    Macvicar, B.A.3
  • 58
    • 84906827762 scopus 로고    scopus 로고
    • The membrane protein Pannexin1 forms two open-channel conformations depending on the mode of activation
    • ra69
    • Wang J, Ambrosi C, Qiu F, Jackson DG, Sosinsky G, Dahl G. 2014 The membrane protein Pannexin1 forms two open-channel conformations depending on the mode of activation. Sci. Signal. 7, ra69. (doi:10.1126/scisignal.2005431)
    • (2014) Sci. Signal , vol.7
    • Wang, J.1    Ambrosi, C.2    Qiu, F.3    Jackson, D.G.4    Sosinsky, G.5    Dahl, G.6
  • 59
    • 34547594520 scopus 로고    scopus 로고
    • Stimulation of rat erythrocyte P2X7 receptor induces the release of epoxyeicosatrienoic acids
    • Jiang H, Zhu AG, Mamczur M, Falck JR, Lerea KM, McGiff JC. 2007 Stimulation of rat erythrocyte P2X7 receptor induces the release of epoxyeicosatrienoic acids. Br. J. Pharmacol. 151, 1033-1040. (doi:10.1038/sj.bjp.0707311)
    • (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
  • 62
    • 84863393008 scopus 로고    scopus 로고
    • Activation of neuronal P2X7 receptor-pannexin-1 mediates death of enteric neurons during colitis. Nat
    • Gulbransen BD et al. 2012 Activation of neuronal P2X7 receptor-pannexin-1 mediates death of enteric neurons during colitis. Nat. Med. 18, 600-604. (doi:10.1038/nm.2679)
    • (2012) Med , vol.18 , pp. 600-604
    • Gulbransen, B.D.1
  • 64
    • 77955293473 scopus 로고    scopus 로고
    • Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other
    • Ambrosi C, Gassmann O, Pranskevich JN, Boassa D, Smock A, Wang J, Dahl G, Steinem C, Sosinsky GE. 2010 Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other. J. Biol. Chem. 285, 24 420-24 431. (doi:10.1074/jbc.M110.115444)
    • (2010) J. Biol. Chem. 285 , vol.420-24 , Issue.431 , pp. 24
    • Ambrosi, C.1    Gassmann, O.2    Pranskevich, J.N.3    Boassa, D.4    Smock, A.5    Wang, J.6    Dahl, G.7    Steinem, C.8    Sosinsky, G.E.9
  • 65
    • 33751572168 scopus 로고    scopus 로고
    • Pannexin1 is expressed by neurons and glia but does not form functional gap junctions
    • Huang Y, Grinspan JB, Abrams CK, Scherer SS. 2007 Pannexin1 is expressed by neurons and glia but does not form functional gap junctions. Glia 55, 46-56. (doi:10.1002/glia.20435)
    • (2007) Glia , vol.55 , pp. 46-56
    • Huang, Y.1    Grinspan, J.B.2    Abrams, C.K.3    Scherer, S.S.4
  • 66
    • 84879258844 scopus 로고    scopus 로고
    • A comparative antibody analysis of pannexin1 expression in four rat brain regions reveals varying subcellular localizations. Front
    • Cone AC, Ambrosi C, Scemes E, Martone ME, Sosinsky GE. 2013 A comparative antibody analysis of pannexin1 expression in four rat brain regions reveals varying subcellular localizations. Front. Pharmacol. 4, 6. (doi:10.3389/fphar.2013.00006)
    • (2013) Pharmacol , vol.4 , pp. 6
    • Cone, A.C.1    Ambrosi, C.2    Scemes, E.3    Martone, M.E.4    Sosinsky, G.E.5
  • 67
    • 70349948843 scopus 로고    scopus 로고
    • The potassium channel subunit Kvbeta3 interacts with pannexin 1 and attenuates its sensitivity to changes in redox potentials
    • Bunse S, Locovei S, Schmidt M, Qiu F, Zoidl G, Dahl G, Dermietzel R. 2009 The potassium channel subunit Kvbeta3 interacts with pannexin 1 and attenuates its sensitivity to changes in redox potentials. FEBS J. 276, 6258-6270. (doi:10.1111/j.1742-4658.2009.07334.x)
    • (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
  • 69
    • 84866516383 scopus 로고    scopus 로고
    • Pannexin 1 in the regulation of vascular tone. Trends Cardiovasc
    • Billaud M, Sandilos JK, Isakson BE. 2012 Pannexin 1 in the regulation of vascular tone. Trends Cardiovasc. Med. 22, 68-72. (doi:10.1016/j.tcm.2012.06.014)
    • (2012) Med , vol.22 , pp. 68-72
    • Billaud, M.1    Sandilos, J.K.2    Isakson, B.E.3
  • 70
    • 84928568592 scopus 로고    scopus 로고
    • Angiotensin II mobilizes intracellular calcium and activates pannexin-1 channels in rat carotid body type II cells via AT1 receptors
    • Murali S, Zhang M, Nurse CA. 2014 Angiotensin II mobilizes intracellular calcium and activates pannexin-1 channels in rat carotid body type II cells via AT1 receptors. J. Physiol. 592, 4747-4762. (doi:10.1113/jphysiol.2014.279299)
    • (2014) J. Physiol , vol.592 , pp. 4747-4762
    • Murali, S.1    Zhang, M.2    Nurse, C.A.3
  • 71
    • 84855745647 scopus 로고    scopus 로고
    • Hyposmotic stress causes ATP release and stimulates Na,K-ATPase activity in porcine lens
    • Shahidullah M, Mandal A, Beimgraben C, Delamere NA. 2011 Hyposmotic stress causes ATP release and stimulates Na,K-ATPase activity in porcine lens. J. Cell Physiol. 227, 1428-1437. (doi:10.1002/jcp.22858)
    • (2011) J. Cell Physiol , vol.227 , pp. 1428-1437
    • Shahidullah, M.1    Mandal, A.2    Beimgraben, C.3    Delamere, N.A.4
  • 72
    • 84861005703 scopus 로고    scopus 로고
    • Neurons respond directly to mechanical deformation with pannexin-mediated ATP release and autostimulation of P2X7 receptors
    • Xia J, Lim JC, Lu W, Beckel JM, Macarak EJ, Laties AM, Mitchell CH. 2012 Neurons respond directly to mechanical deformation with pannexin-mediated ATP release and autostimulation of P2X7 receptors. J. Physiol. 590, 2285-2304. (doi:10.1113/jphysiol.2012.227983)
    • (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
  • 73
    • 84904395911 scopus 로고    scopus 로고
    • Mechanosensitive release of adenosine 50-triphosphate through pannexin channels and mechanosensitive upregulation of pannexin channels in optic nerve head astrocytes: A mechanism for purinergic involvement in chronic strain
    • Beckel JM et al. 2014 Mechanosensitive release of adenosine 50-triphosphate through pannexin channels and mechanosensitive upregulation of pannexin channels in optic nerve head astrocytes: a mechanism for purinergic involvement in chronic strain. Glia 62, 1486-1501. (doi:10.1002/glia.22695)
    • (2014) Glia , vol.62 , pp. 1486-1501
    • Beckel, J.M.1
  • 74
    • 78649663488 scopus 로고    scopus 로고
    • Pathways for ATP release by bovine ciliary epithelial cells, the initial step in purinergic regulation of aqueous humor inflow
    • Li A, Leung CT, Peterson-Yantorno K, Mitchell CH, Civan MM. 2010 Pathways for ATP release by bovine ciliary epithelial cells, the initial step in purinergic regulation of aqueous humor inflow. Am. J. Physiol. Cell Physiol. 299, C1308-C1317. (doi:10.1152/ajpcell.00333.2010)
    • (2010) Am. J. Physiol. Cell Physiol , vol.299 , pp. C1308-C1317
    • Li, A.1    Leung, C.T.2    Peterson-Yantorno, K.3    Mitchell, C.H.4    Civan, M.M.5
  • 75
    • 84868327319 scopus 로고    scopus 로고
    • Maxi-anion channel and pannexin 1 hemichannel constitute separate pathways for swelling-induced ATP release in murine L929 fibrosarcoma cells
    • Islam MR, Uramoto H, Okada T, Sabirov RZ, Okada Y. 2012 Maxi-anion channel and pannexin 1 hemichannel constitute separate pathways for swelling-induced ATP release in murine L929 fibrosarcoma cells. Am. J. Physiol. Cell Physiol. 303, C924-C935. (doi:10.1152/ajpcell.00459.2011)
    • (2012) Am. J. Physiol. Cell Physiol , vol.303 , pp. C924-C935
    • Islam, M.R.1    Uramoto, H.2    Okada, T.3    Sabirov, R.Z.4    Okada, Y.5
  • 77
    • 0141963861 scopus 로고    scopus 로고
    • Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels
    • Tang XD, Xu R, Reynolds MF, Garcia ML, Heinemann SH, Hoshi T. 2003 Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels. Nature 425, 531-535. (doi:10.1038/nature02003)
    • (2003) Nature , vol.425 , pp. 531-535
    • Tang, X.D.1    Xu, R.2    Reynolds, M.F.3    Garcia, M.L.4    Heinemann, S.H.5    Hoshi, T.6
  • 78
    • 84865592969 scopus 로고    scopus 로고
    • P2Y2 receptor activation opens pannexin-1 channels in rat carotid body type II cells: Potential role in amplifying the neurotransmitter ATP
    • Zhang M, Piskuric NA, Vollmer C, Nurse CA. 2012 P2Y2 receptor activation opens pannexin-1 channels in rat carotid body type II cells: potential role in amplifying the neurotransmitter ATP. J. Physiol. 590, 4335-4350. (doi:10.1113/jphysiol.2012. 236265)
    • (2012) J. Physiol , vol.590 , pp. 4335-4350
    • Zhang, M.1    Piskuric, N.A.2    Vollmer, C.3    Nurse, C.A.4
  • 79
    • 59649088329 scopus 로고    scopus 로고
    • Pharmacological characterization of pannexin-1 currents expressed in mammalian cells
    • Ma W, Hui H, Pelegrin P, Surprenant A. 2009 Pharmacological characterization of pannexin-1 currents expressed in mammalian cells. J. Pharmacol. Exp. Ther. 328, 409-418. (doi:10.1124/jpet.108.146365)
    • (2009) J. Pharmacol. Exp. Ther , vol.328 , pp. 409-418
    • Ma, W.1    Hui, H.2    Pelegrin, P.3    Surprenant, A.4
  • 80
    • 84880825336 scopus 로고    scopus 로고
    • P2X4 assembles with P2X7 and pannexin-1 in gingival epithelial cells and modulates ATP-induced reactive oxygen species production and inflammasome activation
    • Hung SC, Choi CH, Said-Sadier N, Johnson L, Atanasova KR, Sellami H, Yilmaz O., Ojcius DM. 2013 P2X4 assembles with P2X7 and pannexin-1 in gingival epithelial cells and modulates ATP-induced reactive oxygen species production and inflammasome activation. PLoS ONE 8, e70210. (doi:10.1371/journal.pone.0070210)
    • (2013) Plos ONE , vol.8
    • Hung, S.C.1    Choi, C.H.2    Said-Sadier, N.3    Johnson, L.4    Atanasova, K.R.5    Sellami, H.6    Yilmaz, O.7    Ojcius, D.M.8
  • 81
    • 80054112857 scopus 로고    scopus 로고
    • Characterization of novel Pannexin 1 isoforms from rat pituitary cells and their association with ATP-gated P2X channels. Gen. Comp
    • Li S, Tomic M, Stojilkovic SS. 2011 Characterization of novel Pannexin 1 isoforms from rat pituitary cells and their association with ATP-gated P2X channels. Gen. Comp. Endocrinol. 174, 202-210. (doi:10.1016/j.ygcen.2011.08.019)
    • (2011) Endocrinol , vol.174 , pp. 202-210
    • Li, S.1    Tomic, M.2    Stojilkovic, S.S.3
  • 83
    • 0035253835 scopus 로고    scopus 로고
    • Nucleotide receptors: An emerging family of regulatory molecules in blood cells
    • Di Virgilio F et al. 2001 Nucleotide receptors: an emerging family of regulatory molecules in blood cells. Blood 97, 587-600. (doi:10.1182/blood.V97.3.587)
    • (2001) Blood , vol.97 , pp. 587-600
    • Di Virgilio, F.1
  • 84
    • 0029801974 scopus 로고    scopus 로고
    • Rat astroglial P2Z (P2X7) receptors regulate intracellular calcium and purine release
    • Ballerini P et al. 1996 Rat astroglial P2Z (P2X7) receptors regulate intracellular calcium and purine release. Neuroreport 7, 2533-2537. (doi:10.1097/00001756-199611040-00026)
    • (1996) Neuroreport , vol.7 , pp. 2533-2537
    • Ballerini, P.1
  • 85
    • 0029951639 scopus 로고    scopus 로고
    • ATP-stimulated release of ATP by human endothelial cells
    • Bodin P, Burnstock G. 1996 ATP-stimulated release of ATP by human endothelial cells. J. Cardiovasc. Pharmacol. 27, 872-875. (doi:10.1097/00005344-199606000-00015)
    • (1996) J. Cardiovasc. Pharmacol , vol.27 , pp. 872-875
    • Bodin, P.1    Burnstock, G.2
  • 86
    • 84869494557 scopus 로고    scopus 로고
    • Pannexin: From discovery to bedside in 11+4 years?
    • Dahl G, Keane RW. 2012 Pannexin: from discovery to bedside in 11+4 years? Brain Res. 1487, 150-159. (doi:10.1016/j.brainres.2012.04.058)
    • (2012) Brain Res , vol.1487 , pp. 150-159
    • Dahl, G.1    Keane, R.W.2
  • 87
    • 84865708285 scopus 로고    scopus 로고
    • Anoxiainduced NMDA receptor activation opens pannexin channels via Src family kinases
    • Weilinger NL, Tang PL, Thompson RJ. 2012 Anoxiainduced NMDA receptor activation opens pannexin channels via Src family kinases. J. Neurosci. 32, 12 579-12 588. (doi:10.1523/JNEUROSCI.1267-12.2012)
    • (2012) J. Neurosci. 32 , vol.579-12 , Issue.588 , pp. 12
    • Weilinger, N.L.1    Tang, P.L.2    Thompson, R.J.3
  • 88
    • 84901417217 scopus 로고    scopus 로고
    • Pannexin-1 as a potentiator of ligand-gated receptor signaling
    • Isakson BE, Thompson RJ. 2014 Pannexin-1 as a potentiator of ligand-gated receptor signaling. Channels (Austin) 8, 118-123. (doi:10.4161/chan.27978)
    • (2014) Channels (Austin) , vol.8 , pp. 118-123
    • Isakson, B.E.1    Thompson, R.J.2
  • 89
    • 68949110210 scopus 로고    scopus 로고
    • Thrombin promotes release of ATP from lung epithelial cells through coordinated activation of Rho- and Ca2þdependent signaling pathways
    • 648
    • Seminario-Vidal L, Kreda S, Jones L, O’Neal W, Trejo J, Boucher RC, Lazarowski ER. 2009 Thrombin promotes release of ATP from lung epithelial cells through coordinated activation of Rho- and Ca2þdependent signaling pathways. J. Biol. Chem. 284, 20 638-20 648. (doi:10.1074/jbc.M109.004762)
    • (2009) J. Biol. Chem , vol.284 , Issue.20 , pp. 638-720
    • Seminario-Vidal, L.1    Kreda, S.2    Jones, L.3    O’Neal, W.4    Trejo, J.5    Boucher, R.C.6    Lazarowski, E.R.7
  • 90
    • 84884192964 scopus 로고    scopus 로고
    • Bradykinin-induced Ca2þ signaling in human subcutaneous fibroblasts involves ATP release via hemichannels leading to P2Y12 receptors activation. Cell Commun
    • Pinheiro AR, Paramos-de-Carvalho D, Certal M, Costa C, Magalhaes-Cardoso MT, Ferreirinha F, Costa M, Correia-de-Sa´ P. 2013 Bradykinin-induced Ca2þ signaling in human subcutaneous fibroblasts involves ATP release via hemichannels leading to P2Y12 receptors activation. Cell Commun. Signal. 11, 70. (doi:10.1186/1478-811X-11-70)
    • (2013) Signal , vol.11 , pp. 70
    • Pinheiro, A.R.1    Paramos-De-Carvalho, D.2    Certal, M.3    Costa, C.4    Magalhaes-Cardoso, M.T.5    Ferreirinha, F.6    Costa, M.7    Correia-De-Sa´, P.8
  • 91
    • 84884575578 scopus 로고    scopus 로고
    • Histamine induces ATP release from human subcutaneous fibroblasts, via pannexin-1 hemichannels, leading to Ca2þ mobilization and cell proliferation
    • Pinheiro AR et al. 2013 Histamine induces ATP release from human subcutaneous fibroblasts, via pannexin-1 hemichannels, leading to Ca2þ mobilization and cell proliferation. J. Biol. Chem. 288, 27 571-27 583. (doi:10.1074/jbc.M113.460865)
    • (2013) J. Biol. Chem. 288 , vol.571-27 , Issue.583 , pp. 27
    • Pinheiro, A.R.1
  • 92
    • 84907158809 scopus 로고    scopus 로고
    • Inhibitors of the 5-lipoxygenase pathway activate pannexin1 channels in macrophages via the thromboxane receptor
    • da Silva-Souza HA, de Lira MN, Patel NK, Spray DC, Persechini PM, Scemes E. 2014 Inhibitors of the 5-lipoxygenase pathway activate pannexin1 channels in macrophages via the thromboxane receptor. Am. J. Physiol. Cell Physiol. 307,C571-C579. (doi:10.1152/ajpcell.00087.2014)
    • (2014) Am. J. Physiol. Cell Physiol , vol.307 , pp. C571-C579
    • Da Silva-Souza, H.A.1    De Lira, M.N.2    Patel, N.K.3    Spray, D.C.4    Persechini, P.M.5    Scemes, E.6
  • 93
    • 84908313648 scopus 로고    scopus 로고
    • Pannexin 1 channels: New actors in the regulation of catecholamine release from adrenal chromaffin cells. Front
    • Momboisse F et al. 2014 Pannexin 1 channels: new actors in the regulation of catecholamine release from adrenal chromaffin cells. Front. Cell Neurosci. 8, 270. (doi:10.3389/fncel.2014.00270)
    • (2014) Cell Neurosci , vol.8 , pp. 270
    • Momboisse, F.1
  • 94
    • 84897504567 scopus 로고    scopus 로고
    • ATP and potassium ions: A deadly combination for astrocytes. Sci
    • Jackson DG, Wang J, Keane RW, Scemes E, Dahl G. 2014 ATP and potassium ions: a deadly combination for astrocytes. Sci. Rep. 4, 4576. (doi:10.1038/srep04576)
    • (2014) Rep , vol.4 , pp. 4576
    • Jackson, D.G.1    Wang, J.2    Keane, R.W.3    Scemes, E.4    Dahl, G.5
  • 95
    • 77957942834 scopus 로고    scopus 로고
    • Pannexin 1 channels mediate ‘find-me’ signal release and membrane permeability during apoptosis
    • Chekeni FB et al. 2010 Pannexin 1 channels mediate ‘find-me’ signal release and membrane permeability during apoptosis. Nature 467, 863-867. (doi:10.1038/nature09413)
    • (2010) Nature , vol.467 , pp. 863-867
    • Chekeni, F.B.1
  • 97
    • 58149335525 scopus 로고    scopus 로고
    • ATP and NO dually control migration of microglia to nerve lesions. Dev
    • Duan Y, Sahley CL, Muller KJ. 2009 ATP and NO dually control migration of microglia to nerve lesions. Dev. Neurobiol. 69, 60-72. (doi:10.1002/dneu.20689)
    • (2009) Neurobiol , vol.69 , pp. 60-72
    • Duan, Y.1    Sahley, C.L.2    Muller, K.J.3
  • 98
    • 84901445139 scopus 로고    scopus 로고
    • Intrinsic properties and regulation of Pannexin 1 channel
    • Chiu YH, Ravichandran KS, Bayliss DA. 2014 Intrinsic properties and regulation of Pannexin 1 channel. Channels (Austin) 8, 103-109. (doi:10.4161/chan.27545)
    • (2014) Channels (Austin) , vol.8 , pp. 103-109
    • Chiu, Y.H.1    Ravichandran, K.S.2    Bayliss, D.A.3
  • 100
    • 84859514212 scopus 로고    scopus 로고
    • Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region
    • 311
    • Sandilos JK, Chiu YH, Chekeni FB, Armstrong AJ, Walk SF, Ravichandran KS, Bayliss DA. 2012 Pannexin 1, an ATP release channel, is activated by caspase cleavage of its pore-associated C-terminal autoinhibitory region. J. Biol. Chem. 287, 11 303-11 311. (doi:10.1074/jbc.M111.323378)
    • (2012) J. Biol. Chem , vol.287 , Issue.11 , pp. 303-311
    • Sandilos, J.K.1    Chiu, Y.H.2    Chekeni, F.B.3    Armstrong, A.J.4    Walk, S.F.5    Ravichandran, K.S.6    Bayliss, D.A.7
  • 101
    • 75749152627 scopus 로고    scopus 로고
    • Non-junction functions of pannexin-1 channels
    • MacVicar BA, Thompson RJ. 2010 Non-junction functions of pannexin-1 channels. Trends Neurosci. 33, 93-102. (doi:10.1016/j.tins.2009.11.007)
    • (2010) Trends Neurosci , vol.33 , pp. 93-102
    • Macvicar, B.A.1    Thompson, R.J.2
  • 103
    • 84873530701 scopus 로고    scopus 로고
    • The ATP permeability of pannexin 1 channels in a heterologous system and in mammalian taste cells is dispensable
    • Romanov RA, Bystrova MF, Rogachevskaya OA, Sadovnikov VB, Shestopalov VI, Kolesnikov SS. 2012 The ATP permeability of pannexin 1 channels in a heterologous system and in mammalian taste cells is dispensable. J. Cell Sci. 125, 5514-5523. (doi:10.1242/jcs.111062)
    • (2012) J. Cell Sci , vol.125 , pp. 5514-5523
    • Romanov, R.A.1    Bystrova, M.F.2    Rogachevskaya, O.A.3    Sadovnikov, V.B.4    Shestopalov, V.I.5    Kolesnikov, S.S.6
  • 104
    • 84886639238 scopus 로고    scopus 로고
    • Role of connexin 32 hemichannels in the release of ATP from peripheral nerves
    • Nualart-Marti A et al. 2013 Role of connexin 32 hemichannels in the release of ATP from peripheral nerves. Glia 61, 1976-1989. (doi:10.1002/glia.22568)
    • (2013) Glia , vol.61 , pp. 1976-1989
    • Nualart-Marti, A.1
  • 106
    • 84878558857 scopus 로고    scopus 로고
    • The food dye FD&C Blue No. 1 is a selective inhibitor of the ATP release channel Panx1
    • Wang J, Jackson DG, Dahl G. 2013 The food dye FD&C Blue No. 1 is a selective inhibitor of the ATP release channel Panx1. J. Gen. Physiol. 141,649-656. (doi:10.1085/jgp.201310966)
    • (2013) J. Gen. Physiol , vol.141 , pp. 649-656
    • Wang, J.1    Jackson, D.G.2    Dahl, G.3
  • 108
    • 77953319991 scopus 로고    scopus 로고
    • Pannexin 3 regulates intracellular ATP/cAMP levels and promotes chondrocyte differentiation
    • 958
    • Iwamoto T, Nakamura T, Doyle A, Ishikawa M, de Vega S, Fukumoto S, Yamada Y. 2010 Pannexin 3 regulates intracellular ATP/cAMP levels and promotes chondrocyte differentiation. J. Biol. Chem. 285, 18 948-18 958. (doi:10.1074/jbc.M110.127027)
    • (2010) J. Biol. Chem , vol.285 , Issue.18 , pp. 948-1018
    • Iwamoto, T.1    Nakamura, T.2    Doyle, A.3    Ishikawa, M.4    De Vega, S.5    Fukumoto, S.6    Yamada, Y.7
  • 109
    • 79960212462 scopus 로고    scopus 로고
    • Pannexin 3 functions as an ER Ca2þ channel, hemichannel, and gap junction to promote osteoblast differentiation
    • Ishikawa M, Iwamoto T, Nakamura T, Doyle A, Fukumoto S, Yamada Y. 2011 Pannexin 3 functions as an ER Ca2þ channel, hemichannel, and gap junction to promote osteoblast differentiation. J. Cell Biol. 193, 1257-1274. (doi:10.1083/jcb.201101050)
    • (2011) J. Cell Biol , vol.193 , pp. 1257-1274
    • Ishikawa, M.1    Iwamoto, T.2    Nakamura, T.3    Doyle, A.4    Fukumoto, S.5    Yamada, Y.6
  • 110
    • 12144288999 scopus 로고    scopus 로고
    • The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins
    • Baranova A et al. 2004 The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins. Genomics 83, 706-716. (doi:10.1016/j.ygeno.2003.09.025)
    • (2004) Genomics , vol.83 , pp. 706-716
    • Baranova, A.1


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