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Volumn 8, Issue FEB, 2014, Pages

Principles and properties of ion flow in P2X receptors

Author keywords

ATP; Gating; Mutagenesis; P2X; Permeability; SCAM; Selectivity

Indexed keywords

IONOTROPIC RECEPTOR; PURINERGIC P2X RECEPTOR;

EID: 84893635581     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2014.00006     Document Type: Review
Times cited : (84)

References (157)
  • 3
    • 58249113980 scopus 로고    scopus 로고
    • Mammalian nicotinic acetylcholine receptors: From structure to function
    • doi: 10.1152/physrev.00015.2008
    • Albuquerque, E. X., Pereira, E. F., Alkondon, M., and Rogers, S. W. (2009). Mammalian nicotinic acetylcholine receptors: from structure to function. Physiol. Rev. 89, 73-120. doi: 10.1152/physrev.00015.2008
    • (2009) Physiol. Rev , vol.89 , pp. 73-120
    • Albuquerque, E.X.1    Pereira, E.F.2    Alkondon, M.3    Rogers, S.W.4
  • 4
    • 80051696222 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: Mapping agonist binding and channel gating
    • doi: 10.1074/jbc.M111.260364
    • Allsopp, R. C., El Ajouz, S., Schmid, R., and Evans, R. J. (2011). Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gating. J. Biol. Chem. 286, 29207-29217. doi: 10.1074/jbc.M111.260364
    • (2011) J. Biol. Chem , vol.286 , pp. 29207-29217
    • Allsopp, R.C.1    El Ajouz, S.2    Schmid, R.3    Evans, R.J.4
  • 5
    • 4143136452 scopus 로고    scopus 로고
    • Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes
    • doi: 10.1016/j.jmb.2004.06.092
    • Aschrafi, A., Sadtler, S., Niculescu, C., Rettinger, J., and Schmalzing, G. (2004). Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes. J. Mol. Biol. 342, 333-343. doi: 10.1016/j.jmb.2004.06.092
    • (2004) J. Mol. Biol , vol.342 , pp. 333-343
    • Aschrafi, A.1    Sadtler, S.2    Niculescu, C.3    Rettinger, J.4    Schmalzing, G.5
  • 6
    • 84866519244 scopus 로고    scopus 로고
    • Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes
    • doi: 10.1038/nature11375
    • Baconguis, I., and Gouaux, E. (2012). Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature 489, 400-405. doi: 10.1038/nature11375
    • (2012) Nature , vol.489 , pp. 400-405
    • Baconguis, I.1    Gouaux, E.2
  • 7
    • 77952650740 scopus 로고    scopus 로고
    • Dynamic changes in the TRPA1 selectivity filter lead to progressive but reversible pore dilation
    • doi: 10.1152/ajpcell.00489.2009
    • Banke, T. G., Chaplan, S. R., and Wickenden, A. D. (2010). Dynamic changes in the TRPA1 selectivity filter lead to progressive but reversible pore dilation. Am. J. Physiol. Cell Physiol. 298, C1457-C1468. doi: 10.1152/ajpcell.00489.2009
    • (2010) Am. J. Physiol. Cell Physiol , vol.298
    • Banke, T.G.1    Chaplan, S.R.2    Wickenden, A.D.3
  • 8
    • 15444372454 scopus 로고    scopus 로고
    • AFM imaging demonstrates that P2X2 receptors are trimers, but that P2X6 receptor subunits do not oligomerize
    • doi: 10.1074/jbc.M412265200
    • Barrera, N. P., Ormond, S. J., Henderson, R. M., Murrell-Lagnado, R. D., and Edwardson, J. M. (2005). AFM imaging demonstrates that P2X2 receptors are trimers, but that P2X6 receptor subunits do not oligomerize. J. Biol. Chem. 280, 10759-10765. doi: 10.1074/jbc.M412265200
    • (2005) J. Biol. Chem , vol.280 , pp. 10759-10765
    • Barrera, N.P.1    Ormond, S.J.2    Henderson, R.M.3    Murrell-Lagnado, R.D.4    Edwardson, J.M.5
  • 9
    • 0026336870 scopus 로고
    • Changes in cytoplasmic calcium induced by purinergic P2x receptor activation in vascular smooth muscle cells and sensory neurons
    • doi: 10.1007/978-1-4684-6003-2_19
    • Benham, C. D., Bouvier, M. M., and Evans, M. L. (1991). Changes in cytoplasmic calcium induced by purinergic P2x receptor activation in vascular smooth muscle cells and sensory neurons. Adv. Exp. Med. Biol. 304, 229-239. doi: 10.1007/978-1-4684-6003-2_19
    • (1991) Adv. Exp. Med. Biol , vol.304 , pp. 229-239
    • Benham, C.D.1    Bouvier, M.M.2    Evans, M.L.3
  • 10
    • 84858070953 scopus 로고    scopus 로고
    • P2X4 receptor channels form large noncytolytic pores in resting and activated microglia
    • doi: 10.1002/glia.22301
    • Bernier, L. P., Ase, A. R., Boue-Grabot, E., and Seguela, P. (2012). P2X4 receptor channels form large noncytolytic pores in resting and activated microglia. Glia 60, 728-737. doi: 10.1002/glia.22301
    • (2012) Glia , vol.60 , pp. 728-737
    • Bernier, L.P.1    Ase, A.R.2    Boue-Grabot, E.3    Seguela, P.4
  • 11
    • 34948819283 scopus 로고    scopus 로고
    • Inhibition of nociceptors by TRPV1-mediated entry of impermeant sodium channel blockers
    • doi: 10.1038/nature06191
    • Binshtok, A. M., Bean, B. P., and Woolf, C. J. (2007). Inhibition of nociceptors by TRPV1-mediated entry of impermeant sodium channel blockers. Nature 449, 607-610. doi: 10.1038/nature06191
    • (2007) Nature , vol.449 , pp. 607-610
    • Binshtok, A.M.1    Bean, B.P.2    Woolf, C.J.3
  • 12
    • 0038441333 scopus 로고    scopus 로고
    • Pharmacological and biophysical properties of the human P2X5 receptor
    • doi: 10.1124/mol.63.6.1407
    • Bo, X., Jiang, L. H., Wilson, H. L., Kim, M., Burnstock, G., Surprenant, A., et al. (2003). Pharmacological and biophysical properties of the human P2X5 receptor. Mol. Pharmacol. 63, 1407-1416. doi: 10.1124/mol.63.6.1407
    • (2003) Mol. Pharmacol , vol.63 , pp. 1407-1416
    • Bo, X.1    Jiang, L.H.2    Wilson, H.L.3    Kim, M.4    Burnstock, G.5    Surprenant, A.6
  • 13
    • 0033555821 scopus 로고    scopus 로고
    • ATP stimulates sympathetic transmitter release via presynaptic P2X purinoceptors
    • Boehm, S. (1999). ATP stimulates sympathetic transmitter release via presynaptic P2X purinoceptors. J. Neurosci. 19, 737-746.
    • (1999) J. Neurosci , vol.19 , pp. 737-746
    • Boehm, S.1
  • 14
    • 0040609340 scopus 로고    scopus 로고
    • A protein kinase C site highly conserved in P2X subunits controls the desensitization kinetics of P2X(2) ATP-gated channels
    • doi: 10.1074/jbc.275.14.10190
    • Boue-Grabot, E., Archambault, V., and Seguela, P. (2000). A protein kinase C site highly conserved in P2X subunits controls the desensitization kinetics of P2X(2) ATP-gated channels. J. Biol. Chem. 275, 10190-10195. doi: 10.1074/jbc.275.14.10190
    • (2000) J. Biol. Chem , vol.275 , pp. 10190-10195
    • Boue-Grabot, E.1    Archambault, V.2    Seguela, P.3
  • 15
    • 0348133543 scopus 로고    scopus 로고
    • The sources and sequestration of Ca(2+) contributing to neuroeffector Ca(2+) transients in the mouse vas deferens
    • doi: 10.1113/jphysiol.2003.049734
    • Brain, K. L., Cuprian, A. M., Williams, D. J., and Cunnane, T. C. (2003). The sources and sequestration of Ca(2+) contributing to neuroeffector Ca(2+) transients in the mouse vas deferens. J. Physiol. 553, 627-635. doi: 10.1113/jphysiol.2003.049734
    • (2003) J. Physiol , vol.553 , pp. 627-635
    • Brain, K.L.1    Cuprian, A.M.2    Williams, D.J.3    Cunnane, T.C.4
  • 16
    • 0028025001 scopus 로고
    • New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor
    • doi: 10.1038/371519a0
    • Brake, A. J., Wagenbach, M. J., and Julius, D. (1994). New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor. Nature 371, 519-523. doi: 10.1038/371519a0
    • (1994) Nature , vol.371 , pp. 519-523
    • Brake, A.J.1    Wagenbach, M.J.2    Julius, D.3
  • 17
    • 0028937070 scopus 로고
    • Nonselective cationic currents elicited by extracellular ATP in human B-lymphocytes
    • doi: 10.1007/BF00373990
    • Bretschneider, F., Klapperstuck, M., Lohn, M., and Markwardt, F. (1995). Nonselective cationic currents elicited by extracellular ATP in human B-lymphocytes. Pflugers Arch. 429, 691-698. doi: 10.1007/BF00373990
    • (1995) Pflugers Arch , vol.429 , pp. 691-698
    • Bretschneider, F.1    Klapperstuck, M.2    Lohn, M.3    Markwardt, F.4
  • 18
    • 78650677994 scopus 로고    scopus 로고
    • P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance
    • doi: 10.1038/nn.2705
    • Browne, L. E., Cao, L., Broomhead, H. E., Bragg, L., Wilkinson, W. J., and North, R. A. (2011). P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance. Nat. Neurosci. 14, 17-18. doi: 10.1038/nn.2705
    • (2011) Nat. Neurosci , vol.14 , pp. 17-18
    • Browne, L.E.1    Cao, L.2    Broomhead, H.E.3    Bragg, L.4    Wilkinson, W.J.5    North, R.A.6
  • 19
    • 84874195644 scopus 로고    scopus 로고
    • P2X7 receptor channels allow direct permeation of nanometer-sized dyes
    • doi: 10.1523/JNEUROSCI.2235-12.2013
    • Browne, L. E., Compan, V., Bragg, L., and North, R. A. (2013). P2X7 receptor channels allow direct permeation of nanometer-sized dyes. J. Neurosci. 33, 3557-3566. doi: 10.1523/JNEUROSCI.2235-12.2013
    • (2013) J. Neurosci , vol.33 , pp. 3557-3566
    • Browne, L.E.1    Compan, V.2    Bragg, L.3    North, R.A.4
  • 20
    • 0032420182 scopus 로고    scopus 로고
    • Calcium permeability of ligand-gated channels
    • doi: 10.1016/S0143-4160(98)90056-2
    • Burnashev, N. (1998). Calcium permeability of ligand-gated channels. Cell Calcium 24, 325-332. doi: 10.1016/S0143-4160(98)90056-2
    • (1998) Cell Calcium , vol.24 , pp. 325-332
    • Burnashev, N.1
  • 21
    • 79955957628 scopus 로고    scopus 로고
    • P2X receptors in health and disease
    • doi: 10.1016/B978-0-12-385526-8.00011-4
    • Burnstock, G., and Kennedy, C. (2011). P2X receptors in health and disease. Adv. Pharmacol. 61, 333-372. doi: 10.1016/B978-0-12-385526-8.00011-4
    • (2011) Adv. Pharmacol , vol.61 , pp. 333-372
    • Burnstock, G.1    Kennedy, C.2
  • 22
    • 73149109743 scopus 로고    scopus 로고
    • P2X7 receptor activates multiple selective dye-permeation pathways in RAW 264.7 and human embryonic kidney 293 cells
    • doi: 10.1124/mol.109.059923
    • Cankurtaran-Sayar, S., Sayar, K., and Ugur, M. (2009). P2X7 receptor activates multiple selective dye-permeation pathways in RAW 264.7 and human embryonic kidney 293 cells. Mol. Pharmacol. 76, 1323-1332. doi: 10.1124/mol.109.059923
    • (2009) Mol. Pharmacol , vol.76 , pp. 1323-1332
    • Cankurtaran-Sayar, S.1    Sayar, K.2    Ugur, M.3
  • 23
    • 84859757951 scopus 로고    scopus 로고
    • Contribution of residues in second transmembrane domain of ASIC1a protein to ion selectivity
    • doi: 10.1074/jbc.M111.329284
    • Carattino, M. D., and Della Vecchia, M. C. (2012). Contribution of residues in second transmembrane domain of ASIC1a protein to ion selectivity. J. Biol. Chem. 287, 12927-12934. doi: 10.1074/jbc.M111.329284
    • (2012) J. Biol. Chem , vol.287 , pp. 12927-12934
    • Carattino, M.D.1    Della Vecchia, M.C.2
  • 24
    • 84861716984 scopus 로고    scopus 로고
    • Voltage-gated sodium channels at 60: Structure, function and pathophysiology
    • doi: 10.1113/jphysiol.2011.224204
    • Catterall, W. A. (2012). Voltage-gated sodium channels at 60: structure, function and pathophysiology. J. Physiol. 590, 2577-2589. doi: 10.1113/jphysiol.2011.224204
    • (2012) J. Physiol , vol.590 , pp. 2577-2589
    • Catterall, W.A.1
  • 25
    • 84867240374 scopus 로고    scopus 로고
    • The Hodgkin-Huxley heritage: From channels to circuits
    • doi: 10.1523/JNEUROSCI.3403-12.2012
    • Catterall, W. A., Raman, I. M., Robinson, H. P., Sejnowski, T. J., and Paulsen, O. (2012). The Hodgkin-Huxley heritage: from channels to circuits. J. Neurosci. 32, 14064-14073. doi: 10.1523/JNEUROSCI.3403-12.2012
    • (2012) J. Neurosci , vol.32 , pp. 14064-14073
    • Catterall, W.A.1    Raman, I.M.2    Robinson, H.P.3    Sejnowski, T.J.4    Paulsen, O.5
  • 26
    • 58149237912 scopus 로고    scopus 로고
    • Regulation of P2X2 receptors by the neuronal calcium sensor VILIP1
    • doi: 10.1126/scisignal.1162329
    • Chaumont, S., Compan, V., Toulme, E., Richler, E., Housley, G. D., Rassendren, F., et al. (2008) Regulation of P2X2 receptors by the neuronal calcium sensor VILIP1. Sci. Signal. 1, ra8. doi: 10.1126/scisignal.1162329
    • (2008) Sci. Signal , vol.1
    • Chaumont, S.1    Compan, V.2    Toulme, E.3    Richler, E.4    Housley, G.D.5    Rassendren, F.6
  • 27
    • 42649095142 scopus 로고    scopus 로고
    • TRPV1 shows dynamic ionic selectivity during agonist stimulation
    • doi: 10.1038/nn.2102
    • Chung, M. K., Guler, A. D., and Caterina, M. J. (2008). TRPV1 shows dynamic ionic selectivity during agonist stimulation. Nat. Neurosci. 11, 555-564. doi: 10.1038/nn.2102
    • (2008) Nat. Neurosci , vol.11 , pp. 555-564
    • Chung, M.K.1    Guler, A.D.2    Caterina, M.J.3
  • 28
    • 79955950645 scopus 로고    scopus 로고
    • Activation and regulation of purinergic P2X receptor channels
    • doi: 10.1124/pr.110.003129
    • Coddou, C., Yan, Z., Obsil, T., Huidobro-Toro, J. P., and Stojilkovic, S. S. (2011). Activation and regulation of purinergic P2X receptor channels. Pharmacol. Rev. 63, 641-683. doi: 10.1124/pr.110.003129
    • (2011) Pharmacol. Rev , vol.63 , pp. 641-683
    • Coddou, C.1    Yan, Z.2    Obsil, T.3    Huidobro-Toro, J.P.4    Stojilkovic, S.S.5
  • 29
    • 84858408591 scopus 로고    scopus 로고
    • P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties
    • doi: 10.1523/JNEUROSCI.6332-11.2012
    • Compan, V., Ulmann, L., Stelmashenko, O., Chemin, J., Chaumont, S., and Rassendren, F. (2012). P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties J. Neurosci. 32, 4284-4296. doi: 10.1523/JNEUROSCI.6332-11.2012
    • (2012) J. Neurosci , vol.32 , pp. 4284-4296
    • Compan, V.1    Ulmann, L.2    Stelmashenko, O.3    Chemin, J.4    Chaumont, S.5    Rassendren, F.6
  • 30
    • 0030922667 scopus 로고    scopus 로고
    • Distinct ATP receptors on pain-sensing and stretch-sensing neurons
    • doi: 10.1038/387505a0
    • Cook, S. P., Vulchanova, L., Hargreaves, K. M., Elde, R., and McCleskey, E. W. (1997). Distinct ATP receptors on pain-sensing and stretch-sensing neurons. Nature 387, 505-508. doi: 10.1038/387505a0
    • (1997) Nature , vol.387 , pp. 505-508
    • Cook, S.P.1    Vulchanova, L.2    Hargreaves, K.M.3    Elde, R.4    McCleskey, E.W.5
  • 31
    • 79953161602 scopus 로고    scopus 로고
    • Terminus of the P2X7 receptor: Treasure hunting
    • doi: 10.1007/s11302-011-9215-1
    • Costa-Junior, H. M., Sarmento Vieira, F., and Coutinho-Silva, R. (2011). Terminus of the P2X7 receptor: treasure hunting. Purinergic Signal. 7, 7-19. doi: 10.1007/s11302-011-9215-1
    • (2011) Purinergic Signal , vol.7 , pp. 7-19
    • Costa-Junior, H.M.1    Sarmento Vieira, F.2    Coutinho-Silva, R.3
  • 32
    • 0032732474 scopus 로고    scopus 로고
    • Ion permeation and block of P2X(2) purinoceptors: Single channel recordings
    • doi: 10.1007/s002329900598
    • Ding, S., and Sachs, F. (1999a). Ion permeation and block of P2X(2) purinoceptors: single channel recordings. J. Membr. Biol. 172, 215-223. doi: 10.1007/s002329900598
    • (1999) J. Membr. Biol , vol.172 , pp. 215-223
    • Ding, S.1    Sachs, F.2
  • 33
    • 0032940264 scopus 로고    scopus 로고
    • Single channel properties of P2X2 purinoceptors
    • doi: 10.1085/jgp.113.5.695
    • Ding, S., and Sachs, F. (1999b). Single channel properties of P2X2 purinoceptors. J. Gen. Physiol. 113, 695-720. doi: 10.1085/jgp.113.5.695
    • (1999) J. Gen. Physiol , vol.113 , pp. 695-720
    • Ding, S.1    Sachs, F.2
  • 34
    • 84868248487 scopus 로고    scopus 로고
    • Purines, purinergic receptors, and cance
    • doi: 10.1158/0008-5472.CAN-12-1600
    • Di Virgilio, F. (2012). Purines, purinergic receptors, and cance. Cancer Res. 72, 5441-5447. doi: 10.1158/0008-5472.CAN-12-1600
    • (2012) Cancer Res , vol.72 , pp. 5441-5447
    • Di Virgilio, F.1
  • 35
    • 40449114454 scopus 로고    scopus 로고
    • Metals in proteins: Correlation between the metal-ion type, coordination number and the amino-acid residues involved in the coordination
    • doi: 10.1107/S090744490706595X
    • Dokmanic, I., Sikic, M., and Tomic, S. (2008). Metals in proteins: correlation between the metal-ion type, coordination number and the amino-acid residues involved in the coordination. Acta Crystallogr. D Biol. Crystallogr. 64, 257-263. doi: 10.1107/S090744490706595X
    • (2008) Acta Crystallogr. D Biol. Crystallogr , vol.64 , pp. 257-263
    • Dokmanic, I.1    Sikic, M.2    Tomic, S.3
  • 36
    • 1342323323 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase and caspase signaling pathways are required for P2X7 receptor (P2X7R)-induced pore formation in human THP-1 cells
    • doi: 10.1124/jpet.103.059600
    • Donnelly-Roberts, D. L., Namovic, M. T., Faltynek, C. R., and Jarvis, M. F. (2004). Mitogen-activated protein kinase and caspase signaling pathways are required for P2X7 receptor (P2X7R)-induced pore formation in human THP-1 cells. J. Pharmacol. Exp. Ther. 308, 1053-1061. doi: 10.1124/jpet.103.059600
    • (2004) J. Pharmacol. Exp. Ther , vol.308 , pp. 1053-1061
    • Donnelly-Roberts, D.L.1    Namovic, M.T.2    Faltynek, C.R.3    Jarvis, M.F.4
  • 37
    • 0031689402 scopus 로고    scopus 로고
    • P2X receptor-mediated excitation of nociceptive afferents in the normal and arthritic rat knee joint
    • doi: 10.1038/sj.bjp.0702080
    • Dowd, E., McQueen, D. S., Chessell, I. P., and Humphrey, P. P. (1998). P2X receptor-mediated excitation of nociceptive afferents in the normal and arthritic rat knee joint. Br. J. Pharmacol. 125, 341-346. doi: 10.1038/sj.bjp.0702080
    • (1998) Br. J. Pharmacol , vol.125 , pp. 341-346
    • Dowd, E.1    McQueen, D.S.2    Chessell, I.P.3    Humphrey, P.P.4
  • 38
    • 2542464972 scopus 로고    scopus 로고
    • Structural changes during ion channel gating
    • doi: 10.1016/j.tins.2004.04.004
    • Doyle, D. A. (2004). Structural changes during ion channel gating. Trends Neurosci. 27, 298-302. doi: 10.1016/j.tins.2004.04.004
    • (2004) Trends Neurosci , vol.27 , pp. 298-302
    • Doyle, D.A.1
  • 39
    • 0032053981 scopus 로고    scopus 로고
    • A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method
    • Egan, T. M., Haines, W. R., and Voigt, M. M. (1998). A domain contributing to the ion channel of ATP-gated P2X2 receptors identified by the substituted cysteine accessibility method. J. Neurosci. 18, 2350-2359.
    • (1998) J. Neurosci , vol.18 , pp. 2350-2359
    • Egan, T.M.1    Haines, W.R.2    Voigt, M.M.3
  • 40
    • 1842558753 scopus 로고    scopus 로고
    • Contribution of calcium ions to P2X channel responses
    • doi: 10.1523/JNEUROSCI.5429-03.2004
    • Egan, T. M., and Khakh, B. S. (2004). Contribution of calcium ions to P2X channel responses. J. Neurosci. 24, 3413-3420. doi: 10.1523/JNEUROSCI.5429-03.2004
    • (2004) J. Neurosci , vol.24 , pp. 3413-3420
    • Egan, T.M.1    Khakh, B.S.2
  • 41
    • 33745753599 scopus 로고    scopus 로고
    • Biophysics of P2X receptors
    • doi: 10.1007/s00424-006-0078-1
    • Egan, T. M., Samways, D. S., and Li, Z. (2006). Biophysics of P2X receptors. Pflugers Arch. 452, 501-512. doi: 10.1007/s00424-006-0078-1
    • (2006) Pflugers Arch , vol.452 , pp. 501-512
    • Egan, T.M.1    Samways, D.S.2    Li, Z.3
  • 42
    • 0023061436 scopus 로고
    • An introduction to molecular architecture and permeability of ion channels
    • doi: 10.1146/annurev.bb.16.060187.001225
    • Eisenman, G., and Dani, J. A. (1987). An introduction to molecular architecture and permeability of ion channels. Annu. Rev. Biophys. Biophys. Chem. 16, 205-226. doi: 10.1146/annurev.bb.16.060187.001225
    • (1987) Annu. Rev. Biophys. Biophys. Chem , vol.16 , pp. 205-226
    • Eisenman, G.1    Dani, J.A.2
  • 43
    • 0021070747 scopus 로고
    • Ionic selectivity revisited: The role of kinetic and equilibrium processes in ion permeation through channels
    • doi: 10.1007/BF01870364
    • Eisenman, G., and Horn, R. (1983). Ionic selectivity revisited: the role of kinetic and equilibrium processes in ion permeation through channels. J. Membr. Biol. 76, 197-225. doi: 10.1007/BF01870364
    • (1983) J. Membr. Biol , vol.76 , pp. 197-225
    • Eisenman, G.1    Horn, R.2
  • 44
    • 0036290377 scopus 로고    scopus 로고
    • P2X(1) Receptor subunit contribution to gating revealed by a dominant negative PKC mutant
    • doi: 10.1006/bbrc.2002.6488
    • Ennion, S. J., and Evans, R. J. (2002). P2X(1) Receptor subunit contribution to gating revealed by a dominant negative PKC mutant. Biochem. Biophys. Res. Commun. 291, 611-616. doi: 10.1006/bbrc.2002.6488
    • (2002) Biochem. Biophys. Res. Commun , vol.291 , pp. 611-616
    • Ennion, S.J.1    Evans, R.J.2
  • 45
    • 0030593493 scopus 로고    scopus 로고
    • Single channel properties of ATP-gated cation channels (P2X receptors) heterologously expressed in Chinese hamster ovary cells
    • doi: 10.1016/0304-3940(96)12804-4
    • Evans, R. J. (1996). Single channel properties of ATP-gated cation channels (P2X receptors) heterologously expressed in Chinese hamster ovary cells. Neurosci. Lett. 212, 212-214. doi: 10.1016/0304-3940(96)12804-4
    • (1996) Neurosci. Lett , vol.212 , pp. 212-214
    • Evans, R.J.1
  • 46
    • 0029955763 scopus 로고    scopus 로고
    • Ionic permeability of, and divalent cation effects on, two ATP-gated cation channels (P2X receptors) expressed in mammalian cells
    • Evans, R. J., Lewis, C., Virginio, C., Lundstrom, K., Buell, G., Surprenant, A., et al. (1996). Ionic permeability of, and divalent cation effects on, two ATP-gated cation channels (P2X receptors) expressed in mammalian cells. J. Physiol. 497(Pt 2), 413-422.
    • (1996) J. Physiol , vol.497 , Issue.PART 2 , pp. 413-422
    • Evans, R.J.1    Lewis, C.2    Virginio, C.3    Lundstrom, K.4    Buell, G.5    Surprenant, A.6
  • 47
    • 12144283595 scopus 로고    scopus 로고
    • Are second messengers crucial for opening the pore associated with P2X7 receptor?
    • doi: 10.1152/ajpcell.00215.2004
    • Faria, R. X., Defarias, F. P., and Alves, L. A. (2005). Are second messengers crucial for opening the pore associated with P2X7 receptor? Am. J. Physiol. Cell Physiol. 288, C260-C271. doi: 10.1152/ajpcell.00215.2004
    • (2005) Am. J. Physiol. Cell Physiol , vol.288
    • Faria, R.X.1    Defarias, F.P.2    Alves, L.A.3
  • 49
    • 47249090581 scopus 로고    scopus 로고
    • Permeation properties of a P2X receptor in the green algae Ostreococcus tauri
    • doi: 10.1074/jbc.M801512200
    • Fountain, S. J., Cao, L., Young, M. T., and North, R. A. (2008). Permeation properties of a P2X receptor in the green algae Ostreococcus tauri. J. Biol. Chem. 283, 15122-15126. doi: 10.1074/jbc.M801512200
    • (2008) J. Biol. Chem , vol.283 , pp. 15122-15126
    • Fountain, S.J.1    Cao, L.2    Young, M.T.3    North, R.A.4
  • 50
    • 0347359010 scopus 로고    scopus 로고
    • Ca2+ permeability of nicotinic acetylcholine receptors
    • doi: 10.1016/j.ceca.2003.08.006
    • Fucile, S. (2004). Ca2+ permeability of nicotinic acetylcholine receptors. Cell Calcium 35, 1-8. doi: 10.1016/j.ceca.2003.08.006
    • (2004) Cell Calcium , vol.35 , pp. 1-8
    • Fucile, S.1
  • 51
    • 0031033013 scopus 로고    scopus 로고
    • Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue
    • Garcia-Guzman, M., Soto, F., Gomez-Hernandez, J. M., Lund, P. E., and Stuhmer, W. (1997). Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue. Mol. Pharmacol. 51, 109-118.
    • (1997) Mol. Pharmacol , vol.51 , pp. 109-118
    • Garcia-Guzman, M.1    Soto, F.2    Gomez-Hernandez, J.M.3    Lund, P.E.4    Stuhmer, W.5
  • 52
    • 84863393008 scopus 로고    scopus 로고
    • Activation of neuronal P2X7 receptor-pannexin-1 mediates death of enteric neurons during colitis
    • doi: 10.1038/nm.2679
    • Gulbransen, B. D., Bashashati, M., Hirota, S. A., Gui, X., Roberts, J. A., MacDonald, J. A., 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) Nat. Med , vol.18 , pp. 600-604
    • Gulbransen, B.D.1    Bashashati, M.2    Hirota, S.A.3    Gui, X.4    Roberts, J.A.5    McDonald, J.A.6
  • 53
    • 0035980064 scopus 로고    scopus 로고
    • The first transmembrane domain of the P2X receptor subunit participates in the agonist-induced gating of the channel
    • doi: 10.1074/jbc.M104216200
    • Haines, W. R., Migita, K., Cox, J. A., Egan, T. M., and Voigt, M. M. (2001). The first transmembrane domain of the P2X receptor subunit participates in the agonist-induced gating of the channel. J. Biol. Chem. 276, 32793-32798. doi: 10.1074/jbc.M104216200
    • (2001) J. Biol. Chem , vol.276 , pp. 32793-32798
    • Haines, W.R.1    Migita, K.2    Cox, J.A.3    Egan, T.M.4    Voigt, M.M.5
  • 54
    • 84860785529 scopus 로고    scopus 로고
    • Molecular mechanism of ATP binding and ion channel activation in P2X receptors
    • doi: 10.1038/nature11010
    • Hattori, M., and Gouaux, E. (2012). Molecular mechanism of ATP binding and ion channel activation in P2X receptors. Nature 485, 207-212. doi: 10.1038/nature11010
    • (2012) Nature , vol.485 , pp. 207-212
    • Hattori, M.1    Gouaux, E.2
  • 55
    • 84885767038 scopus 로고    scopus 로고
    • Inter-and intrasubunit interactions between transmembrane helices in the open state of P2X receptor channels
    • doi: 10.1073/pnas.1311071110
    • Heymann, G., Dai, J., Li, M., Silberberg, S. D., Zhou, H. X., and Swartz, K. J. (2013). Inter-and intrasubunit interactions between transmembrane helices in the open state of P2X receptor channels. Proc. Natl. Acad. Sci. U.S.A. 110, E4045-E4054. doi: 10.1073/pnas.1311071110
    • (2013) Proc. Natl. Acad. Sci. U.S. A , vol.110
    • Heymann, G.1    Dai, J.2    Li, M.3    Silberberg, S.D.4    Zhou, H.X.5    Swartz, K.J.6
  • 56
    • 0003443746 scopus 로고    scopus 로고
    • 3nd Edn. Sunderland, MA: Sinauer Associates
    • Hille, B. (2001). Ion Channels of Excitable Membranes, 3nd Edn. Sunderland, MA: Sinauer Associates, 441-574.
    • (2001) Ion Channels of Excitable Membranes , pp. 441-574
    • Hille, B.1
  • 57
    • 0032168179 scopus 로고    scopus 로고
    • The activation gate of a voltage-gated K+ channel can be trapped in the open state by an intersubunit metal bridge
    • doi: 10.1016/S0896-6273(00)80571-1
    • Holmgren, M., Shin, K. S., and Yellen, G. (1998). The activation gate of a voltage-gated K+ channel can be trapped in the open state by an intersubunit metal bridge. Neuron 21, 617-621. doi: 10.1016/S0896-6273(00)80571-1
    • (1998) Neuron , vol.21 , pp. 617-621
    • Holmgren, M.1    Shin, K.S.2    Yellen, G.3
  • 58
    • 0036400557 scopus 로고    scopus 로고
    • Voltage and concentration dependence of Ca(2+) permeability in recombinant glutamate receptor subtypes
    • doi: 10.1113/jphysiol.2001.012897
    • Jatzke, C., Watanabe, J., and Wollmuth, L. P. (2002). Voltage and concentration dependence of Ca(2+) permeability in recombinant glutamate receptor subtypes. J. Physiol. 538, 25-39. doi: 10.1113/jphysiol.2001.012897
    • (2002) J. Physiol , vol.538 , pp. 25-39
    • Jatzke, C.1    Watanabe, J.2    Wollmuth, L.P.3
  • 60
    • 26844570488 scopus 로고    scopus 로고
    • N-methyl-D-glucamine and propidium dyes utilize different permeation pathways at rat P2X(7) receptors
    • doi: 10.1152/ajpcell.00253.2005
    • Jiang, L. H., Rassendren, F., Mackenzie, A., Zhang, Y. H., Surprenant, A., and North, R. A. (2005). N-methyl-D-glucamine and propidium dyes utilize different permeation pathways at rat P2X(7) receptors. Am. J. Physiol. Cell Physiol. 289, C1295-C1302. doi: 10.1152/ajpcell.00253.2005
    • (2005) Am. J. Physiol. Cell Physiol , vol.289
    • Jiang, L.H.1    Rassendren, F.2    McKenzie, A.3    Zhang, Y.H.4    Surprenant, A.5    North, R.A.6
  • 61
    • 0035805612 scopus 로고    scopus 로고
    • Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X(2) receptor
    • doi: 10.1074/jbc.M011327200
    • Jiang, L. H., Rassendren, F., Spelta, V., Surprenant, A., and North, R. A. (2001). Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X(2) receptor. J. Biol. Chem. 276, 14902-14908. doi: 10.1074/jbc.M011327200
    • (2001) J. Biol. Chem , vol.276 , pp. 14902-14908
    • Jiang, L.H.1    Rassendren, F.2    Spelta, V.3    Surprenant, A.4    North, R.A.5
  • 62
    • 77952373276 scopus 로고    scopus 로고
    • A putative extracellular salt bridge at the subunit interface contributes to the ion channel function of the ATP-gated P2X2 receptor
    • doi: 10.1074/jbc.M110.101980
    • Jiang, R., Martz, A., Gonin, S., Taly, A., de Carvalho, L. P., and Grutter, T. (2010). A putative extracellular salt bridge at the subunit interface contributes to the ion channel function of the ATP-gated P2X2 receptor. J. Biol. Chem. 285, 15805-15815. doi: 10.1074/jbc.M110.101980
    • (2010) J. Biol. Chem , vol.285 , pp. 15805-15815
    • Jiang, R.1    Martz, A.2    Gonin, S.3    Taly, A.4    de Carvalho, L.P.5    Grutter, T.6
  • 63
    • 84861526394 scopus 로고    scopus 로고
    • Molecular and functional properties of P2X receptors-recent progress and persisting challenges
    • doi: 10.1007/s11302-012-9314-7
    • Kaczmarek-Hajek, K., Lorinczi, E., Hausmann, R., and Nicke, A. (2012). Molecular and functional properties of P2X receptors-recent progress and persisting challenges. Purinergic Signal. 8, 375-417. doi: 10.1007/s11302-012-9314-7
    • (2012) Purinergic Signal , vol.8 , pp. 375-417
    • Kaczmarek-Hajek, K.1    Lorinczi, E.2    Hausmann, R.3    Nicke, A.4
  • 64
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • doi: 10.1038/nature08198
    • Kawate, T., Michel, J. C., Birdsong, W. T., and Gouaux, E. (2009). Crystal structure of the ATP-gated P2X(4) ion channel in the closed state. Nature 460, 592-598. doi: 10.1038/nature08198
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 65
    • 79958024000 scopus 로고    scopus 로고
    • Ion access pathway to the transmembrane pore in P2X receptor channels
    • doi: 10.1085/jgp.201010593
    • Kawate, T., Robertson, J. L., Li, M., Silberberg, S. D., and Swartz, K. J. (2011). Ion access pathway to the transmembrane pore in P2X receptor channels. J. Gen. Physiol. 137, 579-590. doi: 10.1085/jgp.201010593
    • (2011) J. Gen. Physiol , vol.137 , pp. 579-590
    • Kawate, T.1    Robertson, J.L.2    Li, M.3    Silberberg, S.D.4    Swartz, K.J.5
  • 66
    • 3543062342 scopus 로고    scopus 로고
    • Ligand-gated ion channels: Mechanisms underlying ion selectivity
    • doi: 10.1016/j.pbiomolbio.2003.09.002
    • Keramidas, A., Moorhouse, A. J., Schofield, P. R., and Barry, P. H. (2004). Ligand-gated ion channels: mechanisms underlying ion selectivity. Prog. Biophys. Mol. Biol. 86, 161-204. doi: 10.1016/j.pbiomolbio.2003.09.002
    • (2004) Prog. Biophys. Mol. Biol , vol.86 , pp. 161-204
    • Keramidas, A.1    Moorhouse, A.J.2    Schofield, P.R.3    Barry, P.H.4
  • 67
    • 0033366463 scopus 로고    scopus 로고
    • Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds
    • doi: 10.1038/7233
    • Khakh, B. S., Bao, X. R., Labarca, C., and Lester, H. A. (1999a). Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds. Nat. Neurosci. 2, 322-330. doi: 10.1038/7233
    • (1999) Nat. Neurosci , vol.2 , pp. 322-330
    • Khakh, B.S.1    Bao, X.R.2    Labarca, C.3    Lester, H.A.4
  • 68
    • 0033198189 scopus 로고    scopus 로고
    • Allosteric control of gating and kinetics at P2X(4) receptor channels
    • Khakh, B. S., Proctor, W. R., Dunwiddie, T. V., Labarca, C., and Lester, H. A. (1999b). Allosteric control of gating and kinetics at P2X(4) receptor channels. J. Neurosci. 19, 7289-7299.
    • (1999) J. Neurosci , vol.19 , pp. 7289-7299
    • Khakh, B.S.1    Proctor, W.R.2    Dunwiddie, T.V.3    Labarca, C.4    Lester, H.A.5
  • 69
    • 14044274324 scopus 로고    scopus 로고
    • Contribution of transmembrane regions to ATP-gated P2X2 channel permeability dynamics
    • doi: 10.1074/jbc.M411324200
    • Khakh, B. S., and Egan, T. M. (2005). Contribution of transmembrane regions to ATP-gated P2X2 channel permeability dynamics. J. Biol. Chem. 280, 6118-6129. doi: 10.1074/jbc.M411324200
    • (2005) J. Biol. Chem , vol.280 , pp. 6118-6129
    • Khakh, B.S.1    Egan, T.M.2
  • 70
    • 0031848216 scopus 로고    scopus 로고
    • ATP receptor-mediated enhancement of fast excitatory neurotransmitter release in the brain
    • Khakh, B. S., and Henderson, G. (1998). ATP receptor-mediated enhancement of fast excitatory neurotransmitter release in the brain. Mol. Pharmacol. 54, 372-378.
    • (1998) Mol. Pharmacol , vol.54 , pp. 372-378
    • Khakh, B.S.1    Henderson, G.2
  • 71
    • 0034601288 scopus 로고    scopus 로고
    • Modulation of fast synaptic transmission by presynaptic ligand-gated cation channels
    • doi: 10.1016/S0165-1838(00)00111-9
    • Khakh, B. S., and Henderson, G. (2000). Modulation of fast synaptic transmission by presynaptic ligand-gated cation channels. J. Auton. Nerv. Syst. 81, 110-121. doi: 10.1016/S0165-1838(00)00111-9
    • (2000) J. Auton. Nerv. Syst , vol.81 , pp. 110-121
    • Khakh, B.S.1    Henderson, G.2
  • 72
    • 0033180224 scopus 로고    scopus 로고
    • Dynamic selectivity filters in ion channels
    • doi: 10.1016/S0896-6273(01)80025-8
    • Khakh, B. S., and Lester, H. A. (1999). Dynamic selectivity filters in ion channels. Neuron 23, 653-658. doi: 10.1016/S0896-6273(01)80025-8
    • (1999) Neuron , vol.23 , pp. 653-658
    • Khakh, B.S.1    Lester, H.A.2
  • 73
    • 33746701380 scopus 로고    scopus 로고
    • P2X receptors as cell-surface ATP sensors in health and disease
    • doi: 10.1038/nature04886
    • Khakh, B. S., and North, R. A. (2006). P2X receptors as cell-surface ATP sensors in health and disease. Nature 442, 527-532. doi: 10.1038/nature04886
    • (2006) Nature , vol.442 , pp. 527-532
    • Khakh, B.S.1    North, R.A.2
  • 75
    • 0033569461 scopus 로고    scopus 로고
    • Excitatory effect of P2X receptor activation on mesenteric afferent nerves in the anaesthetised rat
    • doi: 10.1111/j.1469-7793.1999.00551.x
    • Kirkup, A. J., Booth, C. E., Chessell, I. P., Humphrey, P. P., and Grundy, D. (1999). Excitatory effect of P2X receptor activation on mesenteric afferent nerves in the anaesthetised rat. J. Physiol. 520(Pt 2), 551-563. doi: 10.1111/j.1469-7793.1999.00551.x
    • (1999) J. Physiol , vol.520 , Issue.PART 2 , pp. 551-563
    • Kirkup, A.J.1    Booth, C.E.2    Chessell, I.P.3    Humphrey, P.P.4    Grundy, D.5
  • 76
    • 0034714006 scopus 로고    scopus 로고
    • Characteristics of P2X7 receptors from human B lymphocytes expressed in Xenopus oocytes
    • doi: 10.1016/S0005-2736(00)00245-5
    • Klapperstuck, M., Buttner, C., Bohm, T., Schmalzing, G., and Markwardt, F. (2000). Characteristics of P2X7 receptors from human B lymphocytes expressed in Xenopus oocytes. Biochim. Biophys. Acta. 1467, 444-456. doi: 10.1016/S0005-2736(00)00245-5
    • (2000) Biochim. Biophys. Acta , vol.1467 , pp. 444-456
    • Klapperstuck, M.1    Buttner, C.2    Bohm, T.3    Schmalzing, G.4    Markwardt, F.5
  • 77
    • 77951213527 scopus 로고    scopus 로고
    • Gated access to the pore of a P2X receptor: Structural implications for closed-open transitions
    • doi: 10.1074/jbc.M109.089185
    • Kracun, S., Chaptal, V., Abramson, J., and Khakh, B. S. (2010). Gated access to the pore of a P2X receptor: structural implications for closed-open transitions. J. Biol. Chem. 285, 10110-10121. doi: 10.1074/jbc.M109.089185
    • (2010) J. Biol. Chem , vol.285 , pp. 10110-10121
    • Kracun, S.1    Chaptal, V.2    Abramson, J.3    Khakh, B.S.4
  • 78
    • 0031030226 scopus 로고    scopus 로고
    • Atomic distance estimates from disulfides and high-affinity metal-binding sites in a K+ channel pore
    • doi: 10.1016/S0006-3495(97)78651-X
    • Krovetz, H. S., VanDongen, H. M., and VanDongen, A. M. (1997). Atomic distance estimates from disulfides and high-affinity metal-binding sites in a K+ channel pore. Biophys. J. 72, 117-126. doi: 10.1016/S0006-3495(97)78651-X
    • (1997) Biophys. J , vol.72 , pp. 117-126
    • Krovetz, H.S.1    VanDongen, H.M.2    VanDongen, A.M.3
  • 79
    • 0028941130 scopus 로고
    • Side-chain accessibilities in the pore of a K+ channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis
    • doi: 10.1016/S0006-3495(95)80266-3
    • Kurz, L. L., Zuhlke, R. D., Zhang, H. J., and Joho, R. H. (1995). Side-chain accessibilities in the pore of a K+ channel probed by sulfhydryl-specific reagents after cysteine-scanning mutagenesis. Biophys. J. 68, 900-905. doi: 10.1016/S0006-3495(95)80266-3
    • (1995) Biophys. J , vol.68 , pp. 900-905
    • Kurz, L.L.1    Zuhlke, R.D.2    Zhang, H.J.3    Joho, R.H.4
  • 80
    • 84866327243 scopus 로고    scopus 로고
    • Structural changes during HCN channel gating defined by high affinity metal bridges
    • doi: 10.1085/jgp.201210838
    • Kwan, D. C., Prole, D. L., and Yellen, G. (2012). Structural changes during HCN channel gating defined by high affinity metal bridges. J. Gen. Physiol. 140, 279-291. doi: 10.1085/jgp.201210838
    • (2012) J. Gen. Physiol , vol.140 , pp. 279-291
    • Kwan, D.C.1    Prole, D.L.2    Yellen, G.3
  • 81
    • 0037144622 scopus 로고    scopus 로고
    • Evoked and spontaneous purinergic junctional Ca2+ transients (jCaTs) in rat small arteries
    • doi: 10.1161/01.RES.0000035060.98415.4B
    • Lamont, C., and Wier, W. G. (2002). Evoked and spontaneous purinergic junctional Ca2+ transients (jCaTs) in rat small arteries. Circ. Res. 91, 454-456. doi: 10.1161/01.RES.0000035060.98415.4B
    • (2002) Circ. Res , vol.91 , pp. 454-456
    • Lamont, C.1    Wier, W.G.2
  • 82
    • 0032032383 scopus 로고    scopus 로고
    • Sensory presynaptic and widespread somatodendritic immunolocalization of central ionotropic P2X ATP receptors
    • doi: 10.1016/S0306-4522(97)00365-5
    • Le, K. T., Villeneuve, P., Ramjaun, A. R., McPherson, P. S., Beaudet, A., and Seguela, P. (1998). Sensory presynaptic and widespread somatodendritic immunolocalization of central ionotropic P2X ATP receptors Neuroscience 83, 177-190. doi: 10.1016/S0306-4522(97)00365-5
    • (1998) Neuroscience , vol.83 , pp. 177-190
    • Le, K.T.1    Villeneuve, P.2    Ramjaun, A.R.3    McPherson, P.S.4    Beaudet, A.5    Seguela, P.6
  • 83
    • 0028982205 scopus 로고
    • Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons
    • doi: 10.1038/377432a0
    • Lewis, C., Neidhart, S., Holy, C., North, R. A., Buell, G., and Surprenant, A. (1995). Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons Nature 377, 432-435. doi: 10.1038/377432a0
    • (1995) Nature , vol.377 , pp. 432-435
    • Lewis, C.1    Neidhart, S.2    Holy, C.3    North, R.A.4    Buell, G.5    Surprenant, A.6
  • 84
    • 79957733084 scopus 로고    scopus 로고
    • Activity-dependent targeting of TRPV1 with a pore-permeating capsaicin analog
    • doi: 10.1073/pnas.1018550108
    • Li, H., Wang, S., Chuang, A. Y., Cohen, B. E., and Chuang, H. H. (2011). Activity-dependent targeting of TRPV1 with a pore-permeating capsaicin analog. Proc. Natl. Acad. Sci. U.S.A. 108, 8497-8502. doi: 10.1073/pnas.1018550108
    • (2011) Proc. Natl. Acad. Sci. U.S. A , vol.108 , pp. 8497-8502
    • Li, H.1    Wang, S.2    Chuang, A.Y.3    Cohen, B.E.4    Chuang, H.H.5
  • 85
    • 48149111510 scopus 로고    scopus 로고
    • Gating the pore of P2X receptor channels
    • doi: 10.1038/nn.2151
    • Li, M., Chang, T. H., Silberberg, S. D., and Swartz, K. J. (2008). Gating the pore of P2X receptor channels. Nat. Neurosci. 11, 883-887. doi: 10.1038/nn.2151
    • (2008) Nat. Neurosci , vol.11 , pp. 883-887
    • Li, M.1    Chang, T.H.2    Silberberg, S.D.3    Swartz, K.J.4
  • 86
    • 84880308941 scopus 로고    scopus 로고
    • Pore-opening mechanism in trimeric P2X receptor channels
    • doi: 10.1038/ncomms1048
    • Li, M., Kawate, T., Silberberg, S. D., and Swartz, K. J. (2010). Pore-opening mechanism in trimeric P2X receptor channels. Nat. Commun. 1, 44. doi: 10.1038/ncomms1048
    • (2010) Nat. Commun , vol.1 , pp. 44
    • Li, M.1    Kawate, T.2    Silberberg, S.D.3    Swartz, K.J.4
  • 87
    • 0030709246 scopus 로고    scopus 로고
    • A modulatory subunit of acid sensing ion channels in brain and dorsal root ganglion cells
    • doi: 10.1074/jbc.272.47.29778
    • Lingueglia, E., de Weille, J. R., Bassilana, F., Heurteaux, C., Sakai, H., Waldmann, R., et al. (1997). A modulatory subunit of acid sensing ion channels in brain and dorsal root ganglion cells. J. Biol. Chem. 272, 29778-29783. doi: 10.1074/jbc.272.47.29778
    • (1997) J. Biol. Chem , vol.272 , pp. 29778-29783
    • Lingueglia, E.1    de Weille, J.R.2    Bassilana, F.3    Heurteaux, C.4    Sakai, H.5    Waldmann, R.6
  • 88
    • 0030795112 scopus 로고    scopus 로고
    • Gated access to the pore of a voltage-dependent K+ channel
    • doi: 10.1016/S0896-6273(00)80357-8
    • Liu, Y., Holmgren, M., Jurman, M. E., and Yellen, G. (1997). Gated access to the pore of a voltage-dependent K+ channel. Neuron 19, 175-184. doi: 10.1016/S0896-6273(00)80357-8
    • (1997) Neuron , vol.19 , pp. 175-184
    • Liu, Y.1    Holmgren, M.2    Jurman, M.E.3    Yellen, G.4
  • 89
    • 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., Scemes, E., Qiu, F., Spray, D. C., and Dahl, G. (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
  • 90
    • 0028960949 scopus 로고
    • Silver as a probe of pore-forming residues in a potassium channel
    • doi: 10.1126/science.7716526
    • Lu, Q., and Miller, C. (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
    • Lu, Q.1    Miller, C.2
  • 91
    • 84862615541 scopus 로고    scopus 로고
    • Pannexin 1 forms an anion-selective channel
    • doi: 10.1007/s00424-012-1077-z
    • Ma, W., Compan, V., Zheng, W., Martin, E., North, R. A., Verkhratsky, A., et al. (2012). Pannexin 1 forms an anion-selective channel. Pflugers Arch. 463, 585-592. doi: 10.1007/s00424-012-1077-z
    • (2012) Pflugers Arch , vol.463 , pp. 585-592
    • Ma, W.1    Compan, V.2    Zheng, W.3    Martin, E.4    North, R.A.5    Verkhratsky, A.6
  • 92
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • doi: 10.1016/S0014-5793(03)01104-9
    • MacKinnon, R. (2003). Potassium channels. FEBS Lett. 555, 62-65. doi: 10.1016/S0014-5793(03)01104-9
    • (2003) FEBS Lett , vol.555 , pp. 62-65
    • McKinnon, R.1
  • 93
    • 0025743521 scopus 로고
    • Conductance and kinetic properties of single nicotinic acetylcholine receptor channels in rat sympathetic neurones
    • Mathie, A., Cull-Candy, S. G., and Colquhoun, D. (1991). Conductance and kinetic properties of single nicotinic acetylcholine receptor channels in rat sympathetic neurones. J. Physiol. 439, 717-750.
    • (1991) J. Physiol , vol.439 , pp. 717-750
    • Mathie, A.1    Cull-Candy, S.G.2    Colquhoun, D.3
  • 94
    • 0035903169 scopus 로고    scopus 로고
    • Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor
    • doi: 10.1074/jbc.M103366200
    • Migita, K., Haines, W. R., Voigt, M. M., and Egan, T. M. (2001). Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor. J. Biol. Chem. 276, 30934-30941. doi: 10.1074/jbc.M103366200
    • (2001) J. Biol. Chem , vol.276 , pp. 30934-30941
    • Migita, K.1    Haines, W.R.2    Voigt, M.M.3    Egan, T.M.4
  • 95
    • 0028784222 scopus 로고
    • The use of fura-2 for estimating Ca buffers and Ca fluxes
    • doi: 10.1016/0028-3908(95)00144-U
    • Neher, E. (1995). The use of fura-2 for estimating Ca buffers and Ca fluxes. Neuropharmacology 34, 1423-1442. doi: 10.1016/0028-3908(95)00144-U
    • (1995) Neuropharmacology , vol.34 , pp. 1423-1442
    • Neher, E.1
  • 96
    • 0032510957 scopus 로고    scopus 로고
    • Membrane topology of an ATP-gated ion channel (P2X receptor)
    • doi: 10.1074/jbc.273.24.15177
    • Newbolt, A., Stoop, R., Virginio, C., Surprenant, A., North, R. A., Buell, G., et al. (1998). Membrane topology of an ATP-gated ion channel (P2X receptor). J. Biol. Chem. 273, 15177-15182. doi: 10.1074/jbc.273.24.15177
    • (1998) J. Biol. Chem , vol.273 , pp. 15177-15182
    • Newbolt, A.1    Stoop, R.2    Virginio, C.3    Surprenant, A.4    North, R.A.5    Buell, G.6
  • 97
    • 0032089620 scopus 로고    scopus 로고
    • P2X1 and P2X3 receptors form stable trimers: A novel structural motif of ligand-gated ion channels
    • doi: 10.1093/emboj/17.11.3016
    • Nicke, A., Baumert, H. G., Rettinger, J., Eichele, A., Lambrecht, G., Mutschler, E., et al. (1998). P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels. Embo J. 17, 3016-3028. doi: 10.1093/emboj/17.11.3016
    • (1998) Embo J , vol.17 , pp. 3016-3028
    • Nicke, A.1    Baumert, H.G.2    Rettinger, J.3    Eichele, A.4    Lambrecht, G.5    Mutschler, E.6
  • 98
    • 70350012258 scopus 로고    scopus 로고
    • A functional P2X7 splice variant with an alternative transmembrane domain 1 escapes gene inactivation in P2X7 knock-out mice
    • doi: 10.1074/jbc.M109.033134
    • Nicke, A., Kuan, Y. H., Masin, M., Rettinger, J., Marquez-Klaka, B., Bender, O., et al. (2009). A functional P2X7 splice variant with an alternative transmembrane domain 1 escapes gene inactivation in P2X7 knock-out mice. J. Biol. Chem. 284, 25813-25822. doi: 10.1074/jbc.M109.033134
    • (2009) J. Biol. Chem , vol.284 , pp. 25813-25822
    • Nicke, A.1    Kuan, Y.H.2    Masin, M.3    Rettinger, J.4    Marquez-Klaka, B.5    Bender, O.6
  • 99
    • 0035961228 scopus 로고    scopus 로고
    • Stimulation of mouse cultured sympathetic neurons by uracil but not adenine
    • doi: 10.1016/S0306-4522(00)00547-9
    • Norenberg, W., Gobel, I., Meyer, A., Cox, S. L., Starke, K., and Trendelenburg, A. U. (2001). Stimulation of mouse cultured sympathetic neurons by uracil but not adenine nucleotides 103, 227-236. doi: 10.1016/S0306-4522(00)00547-9
    • (2001) Nucleotides , vol.103 , pp. 227-236
    • Norenberg, W.1    Gobel, I.2    Meyer, A.3    Cox, S.L.4    Starke, K.5    Trendelenburg, A.U.6
  • 100
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • doi: 10.1152/physrev.00015.2002
    • North, R. A. (2002) Molecular physiology of P2X receptors. Physiol. Rev. 82, 1013-1067. doi: 10.1152/physrev.00015.2002
    • (2002) Physiol. Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 101
    • 84875426837 scopus 로고    scopus 로고
    • P2X receptors as drug targets
    • doi: 10.1124/mol.112.083758
    • North, R. A., and Jarvis, M. F. (2013). P2X receptors as drug targets. Mol. Pharmacol. 83, 759-769. doi: 10.1124/mol.112.083758
    • (2013) Mol. Pharmacol , vol.83 , pp. 759-769
    • North, R.A.1    Jarvis, M.F.2
  • 102
    • 0028303241 scopus 로고
    • Differential activation of cation channels and non-selective pores by macrophage P2z purinergic receptors expressed in xenopus oocytes
    • Nuttle, L. C., and Dubyak, G. R. (1994). Differential activation of cation channels and non-selective pores by macrophage P2z purinergic receptors expressed in xenopus oocytes. J. Biol. Chem. 269, 13988-13996.
    • (1994) J. Biol. Chem , vol.269 , pp. 13988-13996
    • Nuttle, L.C.1    Dubyak, G.R.2
  • 104
    • 79958789017 scopus 로고    scopus 로고
    • Many ways to dilate the P2X7 receptor pore
    • doi: 10.1111/j.1476-5381.2011.01325.x
    • Pelegrin, P. (2011). Many ways to dilate the P2X7 receptor pore. Br. J. Pharmacol. 163, 908-911. doi: 10.1111/j.1476-5381.2011.01325.x
    • (2011) Br. J. Pharmacol , vol.163 , pp. 908-911
    • Pelegrin, P.1
  • 105
    • 33750473352 scopus 로고    scopus 로고
    • Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor
    • doi: 10.1038/sj.emboj.7601378
    • Pelegrin, P., and 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
  • 106
    • 0031567594 scopus 로고    scopus 로고
    • P2X7 purinoceptor expression in Xenopus oocytes is not sufficient to produce a pore-forming P2Z-like phenotype
    • doi: 10.1016/S0014-5793(97)00700-X
    • Petrou, S., Ugur, M., Drummond, R. M., Singer, J. J., and Walsh, J. V. Jr. (1997). P2X7 purinoceptor expression in Xenopus oocytes is not sufficient to produce a pore-forming P2Z-like phenotype. FEBS Lett. 411, 339-345. doi: 10.1016/S0014-5793(97)00700-X
    • (1997) FEBS Lett , vol.411 , pp. 339-345
    • Petrou, S.1    Ugur, M.2    Drummond, R.M.3    Singer, J.J.4    Walsh Jr., J.V.5
  • 107
    • 84859141893 scopus 로고    scopus 로고
    • P2X7 receptor-pannexin 1 hemichannel association: Effect of extracellular calcium on membrane permeabilization
    • doi: 10.1007/s12031-011-9646-8
    • Poornima, V., Madhupriya, M., Kootar, S., Sujatha, G., Kumar, A., and Bera, A. K. (2012). P2X7 receptor-pannexin 1 hemichannel association: effect of extracellular calcium on membrane permeabilization. J. Mol. Neurosci. 46, 585-594. doi: 10.1007/s12031-011-9646-8
    • (2012) J. Mol. Neurosci , vol.46 , pp. 585-594
    • Poornima, V.1    Madhupriya, M.2    Kootar, S.3    Sujatha, G.4    Kumar, A.5    Bera, A.K.6
  • 108
    • 0037112377 scopus 로고    scopus 로고
    • Single-channel properties of native and cloned rat vanilloid receptors
    • doi: 10.1113/jphysiol.2002.016352
    • Premkumar, L. S., Agarwal, S., and Steffen, D. (2002). Single-channel properties of native and cloned rat vanilloid receptors. J. Physiol. 545, 107-117. doi: 10.1113/jphysiol.2002.016352
    • (2002) J. Physiol , vol.545 , pp. 107-117
    • Premkumar, L.S.1    Agarwal, S.2    Steffen, D.3
  • 109
    • 1442309855 scopus 로고    scopus 로고
    • Silberberg, Mechanism of ivermectin facilitation of human P2X4 receptor channels
    • doi: 10.1085/jgp.200308986
    • Priel, A., and Silberberg, S. D. (2004). Silberberg, Mechanism of ivermectin facilitation of human P2X4 receptor channels. J. Gen. Physiol. 123, 281-293. doi: 10.1085/jgp.200308986
    • (2004) J. Gen. Physiol , vol.123 , pp. 281-293
    • Priel, A.1    Silberberg, S.D.2
  • 110
    • 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 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
    • Qiu, F.1    Dahl, G.2
  • 111
    • 0030962404 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the pore of a P2X receptor
    • doi: 10.1093/emboj/16.12.3446
    • Rassendren, F., Buell, G., Newbolt, A., North, R. A., and Surprenant, A. (1997). Identification of amino acid residues contributing to the pore of a P2X receptor. Embo. J. 16, 3446-3454. doi: 10.1093/emboj/16.12.3446
    • (1997) Embo. J , vol.16 , pp. 3446-3454
    • Rassendren, F.1    Buell, G.2    Newbolt, A.3    North, R.A.4    Surprenant, A.5
  • 112
    • 34047233727 scopus 로고    scopus 로고
    • Kinetics of P2X7 receptor-operated single channels currents
    • doi: 10.1529/biophysj.106.091413
    • Riedel, T., Lozinsky, I., Schmalzing, G., and Markwardt, F. (2007). Kinetics of P2X7 receptor-operated single channels currents. Biophys. J. 92, 2377-2391. doi: 10.1529/biophysj.106.091413
    • (2007) Biophys. J , vol.92 , pp. 2377-2391
    • Riedel, T.1    Lozinsky, I.2    Schmalzing, G.3    Markwardt, F.4
  • 113
    • 84858665860 scopus 로고    scopus 로고
    • Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel
    • doi: 10.1073/pnas.1201872109
    • Roberts, J. A., Allsopp, R. C., El Ajouz, S., Vial, C., Schmid, R., Young, M. T., et al. (2012a). Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel. Proc. Natl. Acad. Sci. U.S.A. 109, 4663-4667. doi: 10.1073/pnas.1201872109
    • (2012) Proc. Natl. Acad. Sci. U.S. A , vol.109 , pp. 4663-4667
    • Roberts, J.A.1    Allsopp, R.C.2    El Ajouz, S.3    Vial, C.4    Schmid, R.5    Young, M.T.6
  • 114
    • 84868652948 scopus 로고    scopus 로고
    • Mass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes
    • doi: 10.1111/jnc.12012
    • Roberts, J. A., Bottrill, A. R., Mistry, S., and Evans, R. J. (2012b). Mass spectrometry analysis of human P2X1 receptors; insight into phosphorylation, modelling and conformational changes. J. Neurochem. 123, 725-735. doi: 10.1111/jnc.12012
    • (2012) J. Neurochem , vol.123 , pp. 725-735
    • Roberts, J.A.1    Bottrill, A.R.2    Mistry, S.3    Evans, R.J.4
  • 115
    • 34247120710 scopus 로고    scopus 로고
    • Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors
    • doi: 10.1523/JNEUROSCI.2310-06.2007
    • Roberts, J. A., and Evans, R. J. (2007). Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors. J. Neurosci. 27, 4072-4082. doi: 10.1523/JNEUROSCI.2310-06.2007
    • (2007) J. Neurosci , vol.27 , pp. 4072-4082
    • Roberts, J.A.1    Evans, R.J.2
  • 117
    • 0028814237 scopus 로고
    • Comparison of quantitative calcium flux through NMDA, ATP, and ACh receptor channels
    • doi: 10.1016/S0006-3495(95)80211-0
    • Rogers, M., and Dani, J. A. (1995). Comparison of quantitative calcium flux through NMDA, ATP, and ACh receptor channels. Biophys. J. 68, 501-506. doi: 10.1016/S0006-3495(95)80211-0
    • (1995) Biophys. J , vol.68 , pp. 501-506
    • Rogers, M.1    Dani, J.A.2
  • 118
    • 8844263063 scopus 로고    scopus 로고
    • Activation of ureter nociceptors by exogenous and endogenous ATP in guinea pig
    • doi: 10.1016/j.neuropharm.2004.08.003
    • Rong, W., and Burnstock, G. (2004). Activation of ureter nociceptors by exogenous and endogenous ATP in guinea pig. Neuropharmacology 47, 1093-1101. doi: 10.1016/j.neuropharm.2004.08.003
    • (2004) Neuropharmacology , vol.47 , pp. 1093-1101
    • Rong, W.1    Burnstock, G.2
  • 119
    • 20544431525 scopus 로고    scopus 로고
    • Ion conduction and selectivity in K(+) channels
    • doi: 10.1146/annurev.biophys.34.040204.144655
    • Roux, B. (2005). Ion conduction and selectivity in K(+) channels. Annu. Rev. Biophys. Biomol. Struct. 34, 153-171. doi: 10.1146/annurev.biophys.34.040204.144655
    • (2005) Annu. Rev. Biophys. Biomol. Struct , vol.34 , pp. 153-171
    • Roux, B.1
  • 120
    • 0035007786 scopus 로고    scopus 로고
    • Genomic structure, developmental distribution and functional properties of the chicken P2X(5) receptor
    • doi: 10.1046/j.1471-4159.2001.00348.x
    • Ruppelt, A., Ma, W., Borchardt, K., Silberberg, S. D., and Soto, F. (2001). Genomic structure, developmental distribution and functional properties of the chicken P2X(5) receptor. J. Neurochem. 77, 1256-1265. doi: 10.1046/j.1471-4159.2001.00348.x
    • (2001) J. Neurochem , vol.77 , pp. 1256-1265
    • Ruppelt, A.1    Ma, W.2    Borchardt, K.3    Silberberg, S.D.4    Soto, F.5
  • 121
    • 33847345548 scopus 로고    scopus 로고
    • Acidic amino acids impart enhanced Ca2+ permeability and flux in two members of the ATP-gated P2X receptor family
    • doi: 10.1085/jgp.200609677
    • Samways, D. S., and Egan, T. M. (2007). Acidic amino acids impart enhanced Ca2+ permeability and flux in two members of the ATP-gated P2X receptor family. J. Gen. Physiol. 129, 245-256. doi: 10.1085/jgp.200609677
    • (2007) J. Gen. Physiol , vol.129 , pp. 245-256
    • Samways, D.S.1    Egan, T.M.2
  • 122
    • 80054756055 scopus 로고    scopus 로고
    • Calcium-dependent decrease in the single-channel conductance of TRPV1
    • doi: 10.1007/s00424-011-1013-7
    • Samways, D. S., and Egan, T. M. (2011). Calcium-dependent decrease in the single-channel conductance of TRPV1. Pflugers Arch. 462, 681-691. doi: 10.1007/s00424-011-1013-7
    • (2011) Pflugers Arch , vol.462 , pp. 681-691
    • Samways, D.S.1    Egan, T.M.2
  • 123
    • 80051959810 scopus 로고    scopus 로고
    • Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors)
    • doi: 10.1073/pnas.1017550108
    • Samways, D. S., Khakh, B. S., Dutertre, S., and Egan, T. M. (2011). Preferential use of unobstructed lateral portals as the access route to the pore of human ATP-gated ion channels (P2X receptors). Proc. Natl. Acad. Sci. U.S.A. 108, 13800-13805. doi: 10.1073/pnas.1017550108
    • (2011) Proc. Natl. Acad. Sci. U.S. A , vol.108 , pp. 13800-13805
    • Samways, D.S.1    Khakh, B.S.2    Dutertre, S.3    Egan, T.M.4
  • 124
    • 41949101239 scopus 로고    scopus 로고
    • On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor
    • doi: 10.1074/jbc.M708713200
    • Samways, D. S., Migita, K., Li, Z., and Egan, T. M. (2008a). On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor. J. Biol. Chem. 283, 5110-5117. doi: 10.1074/jbc.M708713200
    • (2008) J. Biol. Chem , vol.283 , pp. 5110-5117
    • Samways, D.S.1    Migita, K.2    Li, Z.3    Egan, T.M.4
  • 125
    • 57649120783 scopus 로고    scopus 로고
    • Tunable calcium current through TRPV1 receptor channels
    • doi: 10.1074/jbc.C800131200
    • Samways, D. S., Khakh, B. S., and Egan, T. M. (2008b). Tunable calcium current through TRPV1 receptor channels. J. Biol. Chem. 283, 31274-31278. doi: 10.1074/jbc.C800131200
    • (2008) J. Biol. Chem , vol.283 , pp. 31274-31278
    • Samways, D.S.1    Khakh, B.S.2    Egan, T.M.3
  • 126
    • 84857718067 scopus 로고    scopus 로고
    • Allosteric modulation of Ca2+ flux in a ligand-gated cation channel (P2X4) by actions on lateral portals
    • doi: 10.1074/jbc.M111.322461
    • Samways, D. S., Khakh, B. S., and Egan, T. M. (2012). Allosteric modulation of Ca2+ flux in a ligand-gated cation channel (P2X4) by actions on lateral portals. J. Biol. Chem. 287, 7594-7602. doi: 10.1074/jbc.M111.322461
    • (2012) J. Biol. Chem , vol.287 , pp. 7594-7602
    • Samways, D.S.1    Khakh, B.S.2    Egan, T.M.3
  • 127
    • 0038170314 scopus 로고    scopus 로고
    • Permeation and selectivity in calcium channels
    • doi: 10.1146/annurev.physiol.65.092101.142345
    • Sather, W. A., and McCleskey, E. W. (2003). Permeation and selectivity in calcium channels. Annu. Rev. Physiol. 65, 133-159. doi: 10.1146/annurev.physiol.65.092101.142345
    • (2003) Annu. Rev. Physiol , vol.65 , pp. 133-159
    • Sather, W.A.1    McCleskey, E.W.2
  • 128
    • 55649094970 scopus 로고    scopus 로고
    • ATP-induced P2X7-associated uptake of large molecules involves distinct mechanisms for cations and anions in macrophages
    • doi: 10.1242/jcs.029991
    • Schachter, J., Motta, A. P., de Souza Zamorano, A., da Silva-Souza, H. A., Guimaraes, M. Z., and Persechini, P. M. (2008). ATP-induced P2X7-associated uptake of large molecules involves distinct mechanisms for cations and anions in macrophages. J. Cell Sci. 121, 3261-3270. doi: 10.1242/jcs.029991
    • (2008) J. Cell Sci , vol.121 , pp. 3261-3270
    • Schachter, J.1    Motta, A.P.2    de Souza Zamorano, A.3    da Silva-Souza, H.A.4    Guimaraes, M.Z.5    Persechini, P.M.6
  • 129
    • 75049085160 scopus 로고    scopus 로고
    • On the origin of ion selectivity in the Cys-loop receptor family
    • doi: 10.1007/s12031-009-9260-1
    • Sine, S. M., Wang, H. L., Hansen, S., and Taylor, P. (2010). On the origin of ion selectivity in the Cys-loop receptor family. J. Mol. Neurosci. 40, 70-76. doi: 10.1007/s12031-009-9260-1
    • (2010) J. Mol. Neurosci , vol.40 , pp. 70-76
    • Sine, S.M.1    Wang, H.L.2    Hansen, S.3    Taylor, P.4
  • 130
    • 4444230523 scopus 로고    scopus 로고
    • Mechanisms underlying postjunctional synergism between responses of the vas deferens to noradrenaline and ATP
    • doi: 10.1016/j.ejphar.2004.07.055
    • Smith, N. C., and Burnstock, G. (2004). Mechanisms underlying postjunctional synergism between responses of the vas deferens to noradrenaline and ATP. Eur. J. Pharmacol. 498, 241-248. doi: 10.1016/j.ejphar.2004.07.055
    • (2004) Eur. J. Pharmacol , vol.498 , pp. 241-248
    • Smith, N.C.1    Burnstock, G.2
  • 131
    • 18344382709 scopus 로고    scopus 로고
    • A strategy for mapping and neutralizing conformational immunogenic sites on protein therapeutics
    • doi: 10.1002/1615-9861(200203)2:3%3C271::AID-PROT271%3E3.0.CO;2-W
    • Spencer, D. I., Robson, L., Purdy, D., Whitelegg, N. R., Michael, N. P., Bhatia, J., et al. (2002). A strategy for mapping and neutralizing conformational immunogenic sites on protein therapeutics. Proteomics 2, 271-279. doi: 10.1002/1615-9861(200203)2:3%3C271::AID-PROT271%3E3.0.CO;2-W
    • (2002) Proteomics , vol.2 , pp. 271-279
    • Spencer, D.I.1    Robson, L.2    Purdy, D.3    Whitelegg, N.R.4    Michael, N.P.5    Bhatia, J.6
  • 132
    • 0023664593 scopus 로고
    • ATP4-permeabilizes the plasma membrane of mouse macrophages to fluorescent dyes
    • Steinberg, T. H., Newman, A. S., Swanson, J. A., and Silverstein, S. C. (1987). ATP4-permeabilizes the plasma membrane of mouse macrophages to fluorescent dyes. J. Biol. Chem. 262, 8884-8888.
    • (1987) J. Biol. Chem , vol.262 , pp. 8884-8888
    • Steinberg, T.H.1    Newman, A.S.2    Swanson, J.A.3    Silverstein, S.C.4
  • 133
    • 0027099647 scopus 로고
    • Single-channel conductances of NMDA receptors expressed from cloned cDNAs: Comparison with native receptors
    • doi: 10.1098/rspb.1992.0159
    • Stern, P., Behe, P., Schoepfer, R., and Colquhoun, D. (1992). Single-channel conductances of NMDA receptors expressed from cloned cDNAs: comparison with native receptors. Proc. Biol. Sci. 250, 271-277. doi: 10.1098/rspb.1992.0159
    • (1992) Proc. Biol. Sci , vol.250 , pp. 271-277
    • Stern, P.1    Behe, P.2    Schoepfer, R.3    Colquhoun, D.4
  • 134
    • 0032705299 scopus 로고    scopus 로고
    • Contribution of individual subunits to the multimeric P2X(2) receptor: Estimates based on methanethiosulfonate block at T336C
    • Stoop, R., Thomas, S., Rassendren, F., Kawashima, E., Buell, G., Surprenant, A., et al. (1999). Contribution of individual subunits to the multimeric P2X(2) receptor: estimates based on methanethiosulfonate block at T336C. Mol. Pharmacol. 56, 973-981.
    • (1999) Mol. Pharmacol , vol.56 , pp. 973-981
    • Stoop, R.1    Thomas, S.2    Rassendren, F.3    Kawashima, E.4    Buell, G.5    Surprenant, A.6
  • 135
    • 0029665112 scopus 로고    scopus 로고
    • The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7)
    • doi: 10.1126/science.272.5262.735
    • Surprenant, A., Rassendren, F., Kawashima, E., North, R. A., and Buell, G. (1996). The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7). Science 272, 735-738. doi: 10.1126/science.272.5262.735
    • (1996) Science , vol.272 , pp. 735-738
    • Surprenant, A.1    Rassendren, F.2    Kawashima, E.3    North, R.A.4    Buell, G.5
  • 136
    • 0033121302 scopus 로고    scopus 로고
    • Ca2+-permeable P2X receptor channels in cultured rat retinal ganglion cells
    • Taschenberger, H., Juttner, R., and Grantyn, R. (1999). Ca2+-permeable P2X receptor channels in cultured rat retinal ganglion cells. J. Neurosci. 19, 3353-3366.
    • (1999) J. Neurosci , vol.19 , pp. 3353-3366
    • Taschenberger, H.1    Juttner, R.2    Grantyn, R.3
  • 137
    • 0023820529 scopus 로고
    • Characterisation of the ATP4-receptor that mediates permeabilisation of rat mast cells
    • doi: 10.1016/0014-2999(88)90628-0
    • Tatham, P. E., Cusack, N. J., and Gomperts, B. D. (1988). Characterisation of the ATP4-receptor that mediates permeabilisation of rat mast cells. Eur. J. Pharmacol. 147, 13-21. doi: 10.1016/0014-2999(88)90628-0
    • (1988) Eur. J. Pharmacol , vol.147 , pp. 13-21
    • Tatham, P.E.1    Cusack, N.J.2    Gomperts, B.D.3
  • 138
    • 0025278255 scopus 로고
    • Permeation of both cations and anions through a single class of ATP-activated ion channels in developing chick skeletal muscle
    • doi: 10.1085/jgp.95.4.569
    • Thomas, S. A., and Hume, R. I. (1990). Permeation of both cations and anions through a single class of ATP-activated ion channels in developing chick skeletal muscle. J. Gen. Physiol. 95, 569-590. doi: 10.1085/jgp.95.4.569
    • (1990) J. Gen. Physiol , vol.95 , pp. 569-590
    • Thomas, S.A.1    Hume, R.I.2
  • 139
    • 0032552895 scopus 로고    scopus 로고
    • N-Linked glycosylation is essential for the functional expression of the recombinant P2X2 receptor
    • doi: 10.1021/bi981209g
    • Torres, G. E., Egan, T. M., and Voigt, M. M. (1998a). N-Linked glycosylation is essential for the functional expression of the recombinant P2X2 receptor. Biochemistry 37, 14845-14851. doi: 10.1021/bi981209g
    • (1998) Biochemistry , vol.37 , pp. 14845-14851
    • Torres, G.E.1    Egan, T.M.2    Voigt, M.M.3
  • 140
    • 0032549559 scopus 로고    scopus 로고
    • Topological analysis of the ATP-gated ionotropic [correction of ionotrophic] P2X2 receptor subunit
    • doi: 10.1016/S0014-5793(98)00179-3
    • Torres, G. E., Egan, T. M., and Voigt, M. M. (1998b). Topological analysis of the ATP-gated ionotropic [correction of ionotrophic] P2X2 receptor subunit. FEBS Lett. 425, 19-23. doi: 10.1016/S0014-5793(98)00179-3
    • (1998) FEBS Lett , vol.425 , pp. 19-23
    • Torres, G.E.1    Egan, T.M.2    Voigt, M.M.3
  • 141
    • 0032217176 scopus 로고    scopus 로고
    • Co-expression of P2X1 and P2X5 receptor subunits reveals a novel ATP-gated ion channel
    • Torres, G. E., Haines, W. R., Egan, T. M., and Voigt, M. M. (1998c). Co-expression of P2X1 and P2X5 receptor subunits reveals a novel ATP-gated ion channel. Mol. Pharmacol. 54, 989-993.
    • (1998) Mol. Pharmacol , vol.54 , pp. 989-993
    • Torres, G.E.1    Haines, W.R.2    Egan, T.M.3    Voigt, M.M.4
  • 142
    • 0033525891 scopus 로고    scopus 로고
    • Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners
    • doi: 10.1074/jbc.274.10.6653
    • Torres, G. E., Egan, T. M., and Voigt, M. M. (1999). Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners. J. Biol. Chem. 274, 6653-6659. doi: 10.1074/jbc.274.10.6653
    • (1999) J. Biol. Chem , vol.274 , pp. 6653-6659
    • Torres, G.E.1    Egan, T.M.2    Voigt, M.M.3
  • 143
    • 77950201361 scopus 로고    scopus 로고
    • P2X4 receptors in activated C8-B4 cells of cerebellar microglial origin
    • doi: 10.1085/jgp.200910336
    • Toulme, E., Garcia, A., Samways, D., Egan, T. M., Carson, M. J., and Khakh, B. S. (2010). P2X4 receptors in activated C8-B4 cells of cerebellar microglial origin. J. Gen. Physiol. 135, 333-353. doi: 10.1085/jgp.200910336
    • (2010) J. Gen. Physiol , vol.135 , pp. 333-353
    • Toulme, E.1    Garcia, A.2    Samways, D.3    Egan, T.M.4    Carson, M.J.5    Khakh, B.S.6
  • 144
    • 77952363301 scopus 로고    scopus 로고
    • Glutamate receptor ion channels: Structure, regulation, and function
    • doi: 10.1124/pr.109.002451
    • Traynelis, S. F., Wollmuth, L. P., McBain, C. J., Menniti, F. S., Vance, K. M., Ogden, K. K., et al. (2010). Glutamate receptor ion channels: structure, regulation, and function. Pharmacol. Rev. 62, 405-496. doi: 10.1124/pr.109.002451
    • (2010) Pharmacol. Rev , vol.62 , pp. 405-496
    • Traynelis, S.F.1    Wollmuth, L.P.2    McBain, C.J.3    Menniti, F.S.4    Vance, K.M.5    Ogden, K.K.6
  • 145
    • 0028030797 scopus 로고
    • A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP
    • doi: 10.1038/371516a0
    • Valera, S., Hussy, N., Evans, R. J., Adami, N., North, R. A., Surprenant, A., et al. (1994). A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP. Nature 371, 516-519. doi: 10.1038/371516a0
    • (1994) Nature , vol.371 , pp. 516-519
    • Valera, S.1    Hussy, N.2    Evans, R.J.3    Adami, N.4    North, R.A.5    Surprenant, A.6
  • 146
    • 0029564426 scopus 로고
    • Characterization and chromosomal localization of a human P2X receptor from the urinary bladder
    • Valera, S., Talabot, F., Evans, R. J., Gos, A., Antonarakis, S. E., Morris, M. A., et al. (1995). Characterization and chromosomal localization of a human P2X receptor from the urinary bladder. Receptors Channels 3, 283-289.
    • (1995) Receptors Channels , vol.3 , pp. 283-289
    • Valera, S.1    Talabot, F.2    Evans, R.J.3    Gos, A.4    Antonarakis, S.E.5    Morris, M.A.6
  • 147
    • 0028945477 scopus 로고
    • Dimensions of the narrow portion of a recombinant NMDA receptor channel
    • doi: 10.1016/S0006-3495(95)80263-8
    • Villarroel, A., Burnashev, N., and Sakmann, B. (1995). Dimensions of the narrow portion of a recombinant NMDA receptor channel. Biophys. J. 68, 866-875. doi: 10.1016/S0006-3495(95)80263-8
    • (1995) Biophys. J , vol.68 , pp. 866-875
    • Villarroel, A.1    Burnashev, N.2    Sakmann, B.3
  • 148
    • 0030661885 scopus 로고    scopus 로고
    • Effects of divalent cations, protons and calmidazolium at the rat P2X7 receptor
    • doi: 10.1016/S0028-3908(97)00141-X
    • Virginio, C., Church, D., North, R. A., and Surprenant, A. (1997). Effects of divalent cations, protons and calmidazolium at the rat P2X7 receptor. Neuropharmacology 36, 1285-1294. doi: 10.1016/S0028-3908(97)00141-X
    • (1997) Neuropharmacology , vol.36 , pp. 1285-1294
    • Virginio, C.1    Church, D.2    North, R.A.3    Surprenant, A.4
  • 150
    • 0033198510 scopus 로고    scopus 로고
    • Kinetics of cell lysis, dye uptake and permeability changes in cells expressing the rat P2X7 receptor
    • doi: 10.1111/j.1469-7793.1999.0335m.x
    • Virginio, C., MacKenzie, A., North, R. A., and Surprenant, A. (1999b). Kinetics of cell lysis, dye uptake and permeability changes in cells expressing the rat P2X7 receptor. J. Physiol. 519(Pt 2), 335-346. doi: 10.1111/j.1469-7793.1999.0335m.x
    • (1999) J. Physiol , vol.519 , Issue.PART 2 , pp. 335-346
    • Virginio, C.1    McKenzie, A.2    North, R.A.3    Surprenant, A.4
  • 151
    • 0032127817 scopus 로고    scopus 로고
    • Calcium permeability and block at homomeric and heteromeric P2X2 and P2X3 receptors, and P2X receptors in rat nodose neurones
    • doi: 10.1111/j.1469-7793.1998.027bz.x
    • Virginio, C., North, R. A., and Surprenant, A. (1998). Calcium permeability and block at homomeric and heteromeric P2X2 and P2X3 receptors, and P2X receptors in rat nodose neurones. J. Physiol. 510(Pt 1), 27-35. doi: 10.1111/j.1469-7793.1998.027bz.x
    • (1998) J. Physiol , vol.510 , Issue.PART 1 , pp. 27-35
    • Virginio, C.1    North, R.A.2    Surprenant, A.3
  • 153
    • 0032976359 scopus 로고    scopus 로고
    • Role of action potentials and calcium influx in ATP-and UDP-induced noradrenaline release from rat cultured sympathetic neurones
    • doi: 10.1007/PL00005362
    • von Kugelgen, I., Norenberg, W., Meyer, A., Illes, P., and Starke, K. (1999). Role of action potentials and calcium influx in ATP-and UDP-induced noradrenaline release from rat cultured sympathetic neurones. Naunyn. Schmiedebergs. Arch. Pharmacol. 359, 360-369. doi: 10.1007/PL00005362
    • (1999) Naunyn. Schmiedebergs. Arch. Pharmacol , vol.359 , pp. 360-369
    • von Kugelgen, I.1    Norenberg, W.2    Meyer, A.3    Illes, P.4    Starke, K.5
  • 154
    • 0027338244 scopus 로고
    • The ATP4-receptor-operated channel (P2Z class) of human lymphocytes allows Ba2+ and ethidium+ uptake: Inhibition of fluxes by suramin
    • doi: 10.1006/abbi.1993.1392
    • Wiley, J. S., Chen, R., and Jamieson, G. P. (1993). The ATP4-receptor-operated channel (P2Z class) of human lymphocytes allows Ba2+ and ethidium+ uptake: inhibition of fluxes by suramin. Arch. Biochem. Biophys. 305, 54-60. doi: 10.1006/abbi.1993.1392
    • (1993) Arch. Biochem. Biophys , vol.305 , pp. 54-60
    • Wiley, J.S.1    Chen, R.2    Jamieson, G.P.3
  • 155
    • 84867112397 scopus 로고    scopus 로고
    • Splice variants of the P2X7 receptor reveal differential agonist dependence and functional coupling with pannexin-1
    • doi: 10.1242/jcs.099374
    • Xu, X. J., Boumechache, M., Robinson, L. E., Marschall, V., Gorecki, D. C., Masin, M., et al. (2012). Splice variants of the P2X7 receptor reveal differential agonist dependence and functional coupling with pannexin-1. J. Cell Sci. 125, 3776-3789. doi: 10.1242/jcs.099374
    • (2012) J. Cell Sci , vol.125 , pp. 3776-3789
    • Xu, X.J.1    Boumechache, M.2    Robinson, L.E.3    Marschall, V.4    Gorecki, D.C.5    Masin, M.6
  • 156
    • 59449086148 scopus 로고    scopus 로고
    • The P2X7 receptor channel pore dilates under physiological ion conditions
    • doi: 10.1085/jgp.200810059
    • Yan, Z., Li, S., Liang, Z., Tomic, M., and Stojilkovic, S. S. (2008). The P2X7 receptor channel pore dilates under physiological ion conditions. J. Gen. Physiol. 132, 563-573. doi: 10.1085/jgp.200810059
    • (2008) J. Gen. Physiol , vol.132 , pp. 563-573
    • Yan, Z.1    Li, S.2    Liang, Z.3    Tomic, M.4    Stojilkovic, S.S.5
  • 157
    • 84877773919 scopus 로고    scopus 로고
    • Influences of membrane mimetic environments on membrane protein structures
    • doi: 10.1146/annurev-biophys-083012-130326
    • Zhou, H. X., and Cross, T. A. (2013). Influences of membrane mimetic environments on membrane protein structures. Annu. Rev. Biophys. 42, 361-392. doi: 10.1146/annurev-biophys-083012-130326
    • (2013) Annu. Rev. Biophys , vol.42 , pp. 361-392
    • Zhou, H.X.1    Cross, T.A.2


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