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Volumn 7, Issue DEC, 2013, Pages

Primitive ATP-activated P2X receptors: Discovery, function and pharmacology

Author keywords

3Evolution; Ion channels; Molecular; P2X receptor; Pharmacology; Structure activity relationship

Indexed keywords

ADENOSINE TRIPHOSPHATE; IVERMECTIN; PRAZIQUANTEL; PURINERGIC P2X RECEPTOR; SURAMIN;

EID: 84889803342     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2013.00247     Document Type: Review
Times cited : (34)

References (46)
  • 1
    • 4744370354 scopus 로고    scopus 로고
    • Functional characterization of a P2X receptor from Schistosoma mansoni
    • doi: 10.1074/jbc.M408203200
    • Agboh, K. C., Webb, T. E., Evans, R. J., and Ennion, S. J. (2004). Functional characterization of a P2X receptor from Schistosoma mansoni. J. Biol. Chem. 279, 41650-41657. doi: 10.1074/jbc.M408203200.
    • (2004) J. Biol. Chem , vol.279 , pp. 41650-41657
    • Agboh, K.C.1    Webb, T.E.2    Evans, R.J.3    Ennion, S.J.4
  • 2
    • 84880554080 scopus 로고    scopus 로고
    • Functional properties of five Dictyostelium discoideum P2X receptors
    • doi: 10.1074/jbc.M112.445346
    • Baines, A., Parkinson, K., Sim, J. A., Bragg, L., Thompson, C. R., and North, R. A. (2013). Functional properties of five Dictyostelium discoideum P2X receptors. J. Biol. Chem. 288, 20992-21000. doi: 10.1074/jbc.M112.445346.
    • (2013) J. Biol. Chem , vol.288 , pp. 20992-21000
    • Baines, A.1    Parkinson, K.2    Sim, J.A.3    Bragg, L.4    Thompson, C.R.5    North, R.A.6
  • 3
    • 79952999410 scopus 로고    scopus 로고
    • The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus
    • doi: 10.1124/mol.110.070037
    • Bavan, S., Farmer, L., Singh, S. K., Straub, V. A., Guerrero, F. D., and Ennion, S. J. (2011). The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus. Mol. Pharmacol. 79, 776-785. doi: 10.1124/mol.110.070037.
    • (2011) Mol. Pharmacol , vol.79 , pp. 776-785
    • Bavan, S.1    Farmer, L.2    Singh, S.K.3    Straub, V.A.4    Guerrero, F.D.5    Ennion, S.J.6
  • 4
    • 60049100482 scopus 로고    scopus 로고
    • A P2X receptor from the tardigrade species Hypsibius dujardini with fast kinetics and sensitivity to zinc and copper
    • doi: 10.1186/1471-2148-9-17
    • Bavan, S., Straub, V. A., Blaxter, M. L., and Ennion, S. J. (2009). A P2X receptor from the tardigrade species Hypsibius dujardini with fast kinetics and sensitivity to zinc and copper. BMC Evol. Biol. 9:17. doi: 10.1186/1471-2148-9-17.
    • (2009) BMC Evol. Biol , vol.9 , pp. 17
    • Bavan, S.1    Straub, V.A.2    Blaxter, M.L.3    Ennion, S.J.4
  • 5
    • 84870559546 scopus 로고    scopus 로고
    • Cloning and characterization of a P2X receptor expressed in the central nervous system of Lymnaea stagnalis
    • doi: 10.1371/journal.pone.0050487
    • Bavan, S., Straub, V. A., Webb, T. E., and Ennion, S. J. (2012). Cloning and characterization of a P2X receptor expressed in the central nervous system of Lymnaea stagnalis. PLoS ONE 7:e50487. doi: 10.1371/journal.pone.0050487.
    • (2012) PLoS ONE , vol.7
    • Bavan, S.1    Straub, V.A.2    Webb, T.E.3    Ennion, S.J.4
  • 6
    • 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
  • 7
    • 84865411454 scopus 로고    scopus 로고
    • Discovery of purinergic signalling, the initial resistance and current explosion of interest
    • doi: 10.1111/j.1476-5381.2012.02008.x
    • Burnstock, G. (2012). Discovery of purinergic signalling, the initial resistance and current explosion of interest. Br. J. Pharmacol. 167, 238-255. doi: 10.1111/j.1476-5381.2012.02008.x.
    • (2012) Br. J. Pharmacol , vol.167 , pp. 238-255
    • Burnstock, G.1
  • 8
    • 61849128446 scopus 로고    scopus 로고
    • Evolutionary origins of the purinergic signalling system
    • doi: 10.1111/j.1748-1716.2009.01957.x
    • Burnstock, G., and Verkhratsky, A. (2009). Evolutionary origins of the purinergic signalling system. Acta Physiol. 195, 415-447. doi: 10.1111/j.1748-1716.2009.01957.x.
    • (2009) Acta Physiol , vol.195 , pp. 415-447
    • Burnstock, G.1    Verkhratsky, A.2
  • 9
    • 84857688555 scopus 로고    scopus 로고
    • P2X receptor homologs in basal fungi
    • doi: 10.1007/s11302-011-9261-8
    • Cai, X. (2012). P2X receptor homologs in basal fungi. Purinergic Signal. 8, 11-13. doi: 10.1007/s11302-011-9261-8.
    • (2012) Purinergic Signal , vol.8 , pp. 11-13
    • Cai, X.1
  • 10
    • 84857686131 scopus 로고    scopus 로고
    • Ancestral Ca2+ signaling machinery in early animal and fungal evolution
    • doi: 10.1093/molbev/msr149
    • Cai, X., and Clapham, D. E. (2012). Ancestral Ca2+ signaling machinery in early animal and fungal evolution. Mol. Biol. Evol. 29, 91-100. doi: 10.1093/molbev/msr149.
    • (2012) Mol. Biol. Evol , vol.29 , pp. 91-100
    • Cai, X.1    Clapham, D.E.2
  • 11
    • 3142669217 scopus 로고    scopus 로고
    • Identification of a trafficking motif involved in the stabilization and polarization of P2X receptors
    • doi: 10.1074/jbc.M403940200
    • Chaumont, S., Jiang, L. H., Penna, A., North, R. A., and Rassendren, F. (2004). Identification of a trafficking motif involved in the stabilization and polarization of P2X receptors. J. Biol. Chem. 279, 29628-29638. doi: 10.1074/jbc.M403940200.
    • (2004) J. Biol. Chem , vol.279 , pp. 29628-29638
    • Chaumont, S.1    Jiang, L.H.2    Penna, A.3    North, R.A.4    Rassendren, F.5
  • 12
    • 0038304953 scopus 로고    scopus 로고
    • Neuromodulator role of zinc and copper during prolonged ATP applications to P2X4 purinoceptors
    • doi: 10.1016/S0014-2999(03)01864-8
    • Coddou, C., Morales, B., and Huidobro-Toro, J. P. (2003). Neuromodulator role of zinc and copper during prolonged ATP applications to P2X4 purinoceptors. Eur. J. Pharmacol. 472, 49-56. doi: 10.1016/S0014-2999(03)01864-8.
    • (2003) Eur. J. Pharmacol , vol.472 , pp. 49-56
    • Coddou, C.1    Morales, B.2    Huidobro-Toro, J.P.3
  • 13
    • 0036154216 scopus 로고    scopus 로고
    • Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface
    • doi: 10.1124/mol.61.2.303
    • Ennion, S. J., and Evans, R. J. (2002). Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface. Mol. Pharmacol. 61, 303-311. doi: 10.1124/mol.61.2.303.
    • (2002) Mol. Pharmacol , vol.61 , pp. 303-311
    • Ennion, S.J.1    Evans, R.J.2
  • 14
    • 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
  • 15
    • 0026607210 scopus 로고
    • Vasoconstriction of guinea-pig submucosal arterioles following sympathetic nerve stimulation is mediated by the release of ATP
    • doi: 10.1111/j.1476-5381.1992.tb14323.x
    • Evans, R. J., and Surprenant, A. (1992). Vasoconstriction of guinea-pig submucosal arterioles following sympathetic nerve stimulation is mediated by the release of ATP. Br. J. Pharmacol. 106, 242-249. doi: 10.1111/j.1476-5381.1992.tb14323.x.
    • (1992) Br. J. Pharmacol , vol.106 , pp. 242-249
    • Evans, R.J.1    Surprenant, A.2
  • 16
    • 77951622656 scopus 로고    scopus 로고
    • Neurotransmitter receptor homologues of Dictyostelium discoideum
    • doi: 10.1007/s12031-009-9298-0
    • Fountain, S. J. (2010). Neurotransmitter receptor homologues of Dictyostelium discoideum. J. Mol. Neurosci. 41, 263-266. doi: 10.1007/s12031-009-9298-0.
    • (2010) J. Mol. Neurosci , vol.41 , pp. 263-266
    • Fountain, S.J.1
  • 17
    • 68349152690 scopus 로고    scopus 로고
    • An evolutionary history of P2X receptors
    • doi: 10.1007/s11302-008-9127-x
    • Fountain, S. J., and Burnstock, G. (2009). An evolutionary history of P2X receptors. Purinergic Signal. 5, 269-272. doi: 10.1007/s11302-008-9127-x.
    • (2009) Purinergic Signal , vol.5 , pp. 269-272
    • Fountain, S.J.1    Burnstock, G.2
  • 18
    • 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
  • 19
    • 33744960879 scopus 로고    scopus 로고
    • A C-terminal lysine that controls human P2X4 receptor desensitization
    • doi: 10.1074/jbc.M600442200
    • Fountain, S. J., and North, R. A. (2006). A C-terminal lysine that controls human P2X4 receptor desensitization. J. Biol. Chem. 281, 15044-15049. doi: 10.1074/jbc.M600442200.
    • (2006) J. Biol. Chem , vol.281 , pp. 15044-15049
    • Fountain, S.J.1    North, R.A.2
  • 20
    • 34447503350 scopus 로고    scopus 로고
    • An intracellular P2X receptor required for osmoregulation in Dictyostelium discoideum
    • doi: 10.1038/nature05926
    • Fountain, S. J., Parkinson, K., Young, M. T., Cao, L., Thompson, C. R., and North, R. A. (2007). An intracellular P2X receptor required for osmoregulation in Dictyostelium discoideum. Nature 448, 200-203. doi: 10.1038/nature05926.
    • (2007) Nature , vol.448 , pp. 200-203
    • Fountain, S.J.1    Parkinson, K.2    Young, M.T.3    Cao, L.4    Thompson, C.R.5    North, R.A.6
  • 21
    • 5644227735 scopus 로고    scopus 로고
    • Monitoring real-time release of ATP from the molluscan central nervous system
    • doi: 10.1016/j.jneumeth.2004.03.008
    • Gruenhagen, J. A., Lovell, P., Moroz, L. L., and Yeung, E. S. (2004). Monitoring real-time release of ATP from the molluscan central nervous system. J. Neurosci. Methods139, 145-152. doi: 10.1016/j.jneumeth.2004.03.008.
    • (2004) J. Neurosci. Methods , vol.139 , pp. 145-152
    • Gruenhagen, J.A.1    Lovell, P.2    Moroz, L.L.3    Yeung, E.S.4
  • 22
    • 0027221735 scopus 로고
    • Proton pumps populate the contractile vacuoles of Dictyostelium amoebae
    • doi: 10.1083/jcb.121.6.1311
    • Heuser, J., Zhu, Q., and Clarke, M. (1993). Proton pumps populate the contractile vacuoles of Dictyostelium amoebae. J. Cell Biol. 121, 1311-1327. doi: 10.1083/jcb.121.6.1311.
    • (1993) J. Cell Biol , vol.121 , pp. 1311-1327
    • Heuser, J.1    Zhu, Q.2    Clarke, M.3
  • 23
    • 84862831278 scopus 로고    scopus 로고
    • Conserved ectodomain cysteines are essential for rat P2X7 receptor trafficking
    • doi: 10.1007/s11302-012-9291-x
    • Jindrichova, M., Kuzyk, P., Li, S., Stojilkovic, S. S., and Zemkova, H. (2012). Conserved ectodomain cysteines are essential for rat P2X7 receptor trafficking. Purinergic Signal. 8, 317-325. doi: 10.1007/s11302-012-9291-x.
    • (2012) Purinergic Signal , vol.8 , pp. 317-325
    • Jindrichova, M.1    Kuzyk, P.2    Li, S.3    Stojilkovic, S.S.4    Zemkova, H.5
  • 24
    • 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
  • 25
    • 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
  • 26
    • 0035813213 scopus 로고    scopus 로고
    • Schistosome calcium channel beta subunits. Unusual modulatory effects and potential role in the action of the antischistosomal drug praziquantel
    • doi: 10.1074/jbc.C100273200
    • Kohn, A. B., Anderson, P. A., Roberts-Misterly, J. M., and Greenberg, R. M. (2001). Schistosome calcium channel beta subunits. Unusual modulatory effects and potential role in the action of the antischistosomal drug praziquantel. J. Biol. Chem. 276, 36873-36876. doi: 10.1074/jbc.C100273200.
    • (2001) J. Biol. Chem , vol.276 , pp. 36873-36876
    • Kohn, A.B.1    Anderson, P.A.2    Roberts-Misterly, J.M.3    Greenberg, R.M.4
  • 27
    • 71749101439 scopus 로고    scopus 로고
    • Functional characterization of intracellular Dictyostelium discoideum P2X receptors
    • doi: 10.1074/jbc.M109.045674
    • Ludlow, M. J., Durai, L., and Ennion, S. J. (2009). Functional characterization of intracellular Dictyostelium discoideum P2X receptors. J. Biol. Chem. 284, 35227-35239. doi: 10.1074/jbc.M109.045674.
    • (2009) J. Biol. Chem , vol.284 , pp. 35227-35239
    • Ludlow, M.J.1    Durai, L.2    Ennion, S.J.3
  • 28
    • 55149087708 scopus 로고    scopus 로고
    • Purinergic-mediated Ca2+ influx in Dictyostelium discoideum
    • doi: 10.1016/j.ceca.2008.04.001
    • Ludlow, M. J., Traynor, D., Fisher, P. R., and Ennion, S. J. (2008). Purinergic-mediated Ca2+ influx in Dictyostelium discoideum. Cell Calcium 44, 567-579. doi: 10.1016/j.ceca.2008.04.001.
    • (2008) Cell Calcium , vol.44 , pp. 567-579
    • Ludlow, M.J.1    Traynor, D.2    Fisher, P.R.3    Ennion, S.J.4
  • 29
    • 33746287754 scopus 로고    scopus 로고
    • The contractile vacuole in Ca2+-regulation in Dictyostelium: Its essential function for cAMP-induced Ca2+-influx
    • doi: 10.1186/1471-213X-6-31
    • Malchow, D., Lusche, D. F., Schlatterer, C., De Lozanne, A., and Müller-Taubenberger, A. (2006). The contractile vacuole in Ca2+-regulation in Dictyostelium: its essential function for cAMP-induced Ca2+-influx. BMC Dev. Biol. 6:31. doi: 10.1186/1471-213X-6-31.
    • (2006) BMC Dev. Biol , vol.6 , pp. 31
    • Malchow, D.1    Lusche, D.F.2    Schlatterer, C.3    De Lozanne, A.4    Müller-Taubenberger, A.5
  • 30
    • 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
  • 31
    • 80052275295 scopus 로고    scopus 로고
    • Fusion-activated Ca2+ entry via vesicular P2X4 receptors promotes fusion pore opening and exocytotic content release in pneumocytes
    • doi: 10.1073/pnas.1101039108
    • Miklavc, P., Mair, N., Wittekindt, O. H., Haller, T., Dietl, P., Felder, E., et al. (2011). Fusion-activated Ca2+ entry via vesicular P2X4 receptors promotes fusion pore opening and exocytotic content release in pneumocytes. Proc. Natl. Acad. Sci. U.S.A.108, 14503-14508. doi: 10.1073/pnas.1101039108.
    • (2011) Proc. Natl. Acad. Sci. U.S. A , vol.108 , pp. 14503-14508
    • Miklavc, P.1    Mair, N.2    Wittekindt, O.H.3    Haller, T.4    Dietl, P.5    Felder, E.6
  • 32
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North, R. A. (2002). Molecular physiology of P2X receptors. Physiol. Rev. 82, 1013-1067.
    • (2002) Physiol. Rev , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 33
    • 34250689932 scopus 로고    scopus 로고
    • The tiny eukaryote Ostreococcus provides genomic insights into the paradox of plankton speciation
    • doi: 10.1073/pnas.0611046104
    • Palenik, B., Grimwood, J., Aerts, A., Rouzé, P., Salamov, A., Putnam, N., et al. (2007). The tiny eukaryote Ostreococcus provides genomic insights into the paradox of plankton speciation. Proc. Natl. Acad. Sci. U.S.A. 104, 7705-7710. doi: 10.1073/pnas.0611046104.
    • (2007) Proc. Natl. Acad. Sci. U.S. A , vol.104 , pp. 7705-7710
    • Palenik, B.1    Grimwood, J.2    Aerts, A.3    Rouzé, P.4    Salamov, A.5    Putnam, N.6
  • 34
    • 0019319610 scopus 로고
    • Extracellular ATP, ecto-ATPase and calcium influx in Dictyostelium discoideum cells
    • doi: 10.1016/0014-5793(80)80234-1
    • Parish, R. W., and Weibel, M. (1980). Extracellular ATP, ecto-ATPase and calcium influx in Dictyostelium discoideum cells. FEBS Lett. 118, 263-266. doi: 10.1016/0014-5793(80)80234-1.
    • (1980) FEBS Lett , vol.118 , pp. 263-266
    • Parish, R.W.1    Weibel, M.2
  • 35
    • 1442309855 scopus 로고    scopus 로고
    • Mechanism of ivermectin facilitation of human P2X4 receptor channels
    • doi: 10.1085/jgp.200308986
    • Priel, A., and Silberberg, S. D. (2004). 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
  • 36
    • 36549041874 scopus 로고    scopus 로고
    • Regulation of P2X4 receptors by lysosomal targeting, glycan protection and exocytosis
    • doi: 10.1242/jcs.010348
    • Qureshi, O. S., Paramasivam, A., Yu, J. C., and Murrell-Lagnado, R. D. (2007). Regulation of P2X4 receptors by lysosomal targeting, glycan protection and exocytosis. J. Cell Sci. 120(Pt 21):3838-3849. doi: 10.1242/jcs.010348.
    • (2007) J. Cell Sci , vol.120 , Issue.PART 21 , pp. 3838-3849
    • Qureshi, O.S.1    Paramasivam, A.2    Yu, J.C.3    Murrell-Lagnado, R.D.4
  • 37
    • 78651418254 scopus 로고    scopus 로고
    • Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating
    • Rokic, M. B., Tvrdoňová, V., Vávra, V., Jindřichová, M., Obšil, T., Stojilkovic, S. S., et al. (2010). Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating. Physiol. Res. 59, 927-935.
    • (2010) Physiol. Res , vol.59 , pp. 927-935
    • Rokic, M.B.1    Tvrdoňová, V.2    Vávra, V.3    Jindřichová, M.4    Obšil, T.5    Stojilkovic, S.S.6
  • 38
    • 0032860951 scopus 로고    scopus 로고
    • Cloning, functional characterization and developmental expression of a P2X receptor from chick embryo
    • doi: 10.1016/S0079-6123(08)63547-5
    • Ruppelt, A., Liang, B. T., and Soto, F. (1999). Cloning, functional characterization and developmental expression of a P2X receptor from chick embryo. Prog. Brain Res.120, 81-90. doi: 10.1016/S0079-6123(08)63547-5.
    • (1999) Prog. Brain Res , vol.120 , pp. 81-90
    • Ruppelt, A.1    Liang, B.T.2    Soto, F.3
  • 39
    • 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
  • 40
    • 84865257041 scopus 로고    scopus 로고
    • A mechanism of intracellular P2X receptor activation
    • doi: 10.1074/jbc.M112.372565
    • Sivaramakrishnan, V., and Fountain, S. J. (2012). A mechanism of intracellular P2X receptor activation. J. Biol. Chem. 287, 28315-28326. doi: 10.1074/jbc.M112.372565.
    • (2012) J. Biol. Chem , vol.287 , pp. 28315-28326
    • Sivaramakrishnan, V.1    Fountain, S.J.2
  • 41
    • 84872282572 scopus 로고    scopus 로고
    • Intracellular P2X receptors as novel calcium release channels and modulators of osmoregulation in Dictyostelium: A comparison of two common laboratory strains
    • doi: 10.4161/chan.22737
    • Sivaramakrishnan, V., and Fountain, S. J. (2013). Intracellular P2X receptors as novel calcium release channels and modulators of osmoregulation in Dictyostelium: a comparison of two common laboratory strains. Channels (Austin) 7, 43-46. doi: 10.4161/chan.22737.
    • (2013) Channels (Austin) , vol.7 , pp. 43-46
    • Sivaramakrishnan, V.1    Fountain, S.J.2
  • 43
    • 80052823575 scopus 로고    scopus 로고
    • Expression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA
    • doi: 10.1016/j.bbamem.2011.08.025
    • Valente, M., Watterson, S. J., Parker, M. D., Ford, R. C., and Young, M. T. (2011). Expression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA. Biochim. Biophys. Acta 1808, 2859-2866. doi: 10.1016/j.bbamem.2011.08.025.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2859-2866
    • Valente, M.1    Watterson, S.J.2    Parker, M.D.3    Ford, R.C.4    Young, M.T.5
  • 44
    • 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. Neuropharmacology36, 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
  • 45
    • 54449086943 scopus 로고    scopus 로고
    • Molecular shape, architecture, and size of P2X4 receptors determined using fluorescence resonance energy transfer and electron microscopy
    • doi: 10.1074/jbc.M804458200
    • Young, M. T., Fisher, J. A., Fountain, S. J., Ford, R. C., North, R. A., and Khakh, B. S. (2008). Molecular shape, architecture, and size of P2X4 receptors determined using fluorescence resonance energy transfer and electron microscopy. J. Biol. Chem. 283, 26241-26251. doi: 10.1074/jbc.M804458200.
    • (2008) J. Biol. Chem , vol.283 , pp. 26241-26251
    • Young, M.T.1    Fisher, J.A.2    Fountain, S.J.3    Ford, R.C.4    North, R.A.5    Khakh, B.S.6
  • 46
    • 0037417982 scopus 로고    scopus 로고
    • Photochemical gating of heterologous ion channels: Remote control over genetically designated populations of neurons
    • doi: 10.1073/pnas.242738899
    • Zemelman, B. V., Nesnas, N., Lee, G. A., and Miesenbock, G. (2003). Photochemical gating of heterologous ion channels: remote control over genetically designated populations of neurons. Proc. Natl. Acad. Sci. U.S.A. 100, 1352-1357. doi: 10.1073/pnas.242738899.
    • (2003) Proc. Natl. Acad. Sci. U.S. A , vol.100 , pp. 1352-1357
    • Zemelman, B.V.1    Nesnas, N.2    Lee, G.A.3    Miesenbock, G.4


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