메뉴 건너뛰기




Volumn 6, Issue NOV, 2013, Pages

Two open states of P2X receptor channels

Author keywords

ATP; Gating; NMDG; Pore dilation; Pore opening; Purinergic receptor channels; YO PRO 1

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; GAP JUNCTION PROTEIN; MACROGOL; MEGLUMINE; PANNEXIN 1; PURINERGIC P2X RECEPTOR; PURINERGIC P2X2 RECEPTOR; PURINERGIC P2X4 RECEPTOR; PURINERGIC P2X7 RECEPTOR; SODIUM ION; UNCLASSIFIED DRUG;

EID: 84888189345     PISSN: 16625102     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncel.2013.00215     Document Type: Article
Times cited : (28)

References (74)
  • 2
    • 54449091027 scopus 로고    scopus 로고
    • The P2X7 carboxyl tail is a regulatorymodule ofP2X7 receptor channel activity
    • doi: 10.1074/jbc.m803855200
    • Becker, D., Woltersdorf, R., Boldt, W., Schmitz, S., Braam, U., Schmalzing, G., et al. (2008). The P2X7 carboxyl tail is a regulatorymodule ofP2X7 receptor channel activity. J.Biol Chem. 283,25725-25734. doi: 10.1074/jbc.m803855200
    • (2008) J.Biol Chem , vol.283 , pp. 25725-25734
    • Becker, D.1    Woltersdorf, R.2    Boldt, W.3    Schmitz, S.4    Braam, U.5    Schmalzing, G.6
  • 3
    • 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
  • 4
    • 0242476118 scopus 로고    scopus 로고
    • Desensitization ofthe (P2X2) receptor controlled by alternative splicing
    • doi: 10.1016/S0014-5793(97)00128-2
    • Brandle, U., Spielmanns, P., Osteroth, R., Sim, J., Surprenant, A., Buell, G., et al. (1997). Desensitization ofthe (P2X2) receptor controlled by alternative splicing. FEBSLett. 404, 294-298. doi: 10.1016/S0014-5793(97)00128-2
    • (1997) FEBSLett , vol.404 , pp. 294-298
    • Brandle, U.1    Spielmanns, P.2    Osteroth, R.3    Sim, J.4    Surprenant, A.5    Buell, G.6
  • 5
    • 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
  • 6
    • 9144269934 scopus 로고    scopus 로고
    • Cellular distribution and functions of P2 receptor subtypes in different systems
    • doi: 10. 1016/s0074-7696(04)40002-3
    • Burnstock, G., and Knight, G. E. (2004). Cellular distribution and functions of P2 receptor subtypes in different systems. Int. Rev. Cytol. 240, 31-304. doi: 10. 1016/s0074-7696(04)40002-3
    • (2004) Int. Rev. Cytol , vol.240 , pp. 31-304
    • Burnstock, G.1    Knight, G.E.2
  • 7
    • 50149118145 scopus 로고    scopus 로고
    • Patch-clamp coordinated spectroscopy shows P2X2 receptor permeability dynamics require cytosolic domain rearrangements but not Panx-1 channels
    • doi: 10.1073/pnas.0803008105
    • Chaumont, S., and Khakh, B. S. (2008). Patch-clamp coordinated spectroscopy shows P2X2 receptor permeability dynamics require cytosolic domain rearrangements but not Panx-1 channels. Proc. Natl. Acad. Sci. USA 105, 12063-12068. doi: 10.1073/pnas.0803008105
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12063-12068
    • Chaumont, S.1    Khakh, B.S.2
  • 8
    • 0034841875 scopus 로고    scopus 로고
    • Dynamics of P2X7 receptor pore dilation: Pharmacological and functional consequences
    • doi: 10.1002/ddr.1171
    • Chessell, I. P., Grahames, C. B. A., Michel, A. D., and Humphrey, P. P. (2001). Dynamics of P2X7 receptor pore dilation: pharmacological and functional consequences. Drug. Dev. Res. 53, 60-65. doi: 10.1002/ddr.1171
    • (2001) Drug. Dev. Res , vol.53 , pp. 60-65
    • Chessell, I.P.1    Grahames, C.B.A.2    Michel, A.D.3    Humphrey, P.P.4
  • 9
    • 0035211065 scopus 로고    scopus 로고
    • P2X receptors and nociception
    • Chizh, B. A., and Illes, P. (2001). P2X receptors and nociception. Pharmacol. Rev. 53,553-568.
    • (2001) Pharmacol. Rev , vol.53 , pp. 553-568
    • Chizh, B.A.1    Illes, P.2
  • 10
    • 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
  • 11
    • 0018353476 scopus 로고
    • ATP induces nucleotide permeabilityin rat mast cells
    • doi: 10.1038/279541a0
    • Cockcroft, S., and Gomperts, B. D. (1979). ATP induces nucleotide permeabilityin rat mast cells. Nature 279, 541-542. doi: 10.1038/279541a0
    • (1979) Nature , vol.279 , pp. 541-542
    • Cockcroft, S.1    Gomperts, B.D.2
  • 13
    • 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
  • 14
    • 84858408591 scopus 로고    scopus 로고
    • P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties
    • doi: 10. 1523/JNEUR0SCI.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/JNEUR0SCI.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
  • 15
    • 0032732474 scopus 로고    scopus 로고
    • Ion permeation and block of P2X(2) purinocep-tors: Single channel recordings
    • doi: 10. 1007/s002329900598
    • Ding, S., and Sachs, F. (1999). Ion permeation and block of P2X(2) purinocep-tors: 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
  • 16
    • 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
  • 17
    • 33745753599 scopus 로고    scopus 로고
    • Biophysics ofP2X receptors
    • doi: 10.1007/s00424-006-0078-1
    • Egan, T. M., Samways, D. S., and Li, Z. (2006). Biophysics ofP2X 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
  • 18
    • 0036023394 scopus 로고    scopus 로고
    • Control of P2X2 channel permeability by the cytosolic domain
    • doi: 10.1085/jgp.20028535
    • Eickhorst, A. N., Berson, A., Cockayne, D., Lester, H. A., and Khakh, B. S. (2002). Control of P2X2 channel permeability by the cytosolic domain. J. Gen. Physiol. 120, 119-131. doi: 10.1085/jgp.20028535
    • (2002) J. Gen. Physiol , vol.120 , pp. 119-131
    • Eickhorst, A.N.1    Berson, A.2    Cockayne, D.3    Lester, H.A.4    Khakh, B.S.5
  • 19
    • 0034703055 scopus 로고    scopus 로고
    • The role of positivelycharged amino acids in ATP recognition by human P2X1 receptors
    • doi: 10.1074/jbc.m003637200
    • Ennion, S., Hagan, S., and Evans, R. J. (2000). The role of positivelycharged amino acids in ATP recognition by human P2X1 receptors. J. Biol. Chem. 275, 29361-29367. doi: 10.1074/jbc.m003637200
    • (2000) J. Biol. Chem , vol.275 , pp. 29361-29367
    • Ennion, S.1    Hagan, S.2    Evans, R.J.3
  • 20
    • 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
  • 21
    • 0022629214 scopus 로고
    • Extracellular ATP: Effects, sources and fate
    • Gordon, J. L. (1986). Extracellular ATP: effects, sources and fate. Biochem. J. 233, 309-319.
    • (1986) Biochem. J , vol.233 , pp. 309-319
    • Gordon, J.L.1
  • 22
    • 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
  • 23
    • 35348901397 scopus 로고    scopus 로고
    • Functional expression of ionotropic purinergic receptors on mouse taste bud cells
    • doi: 10. 1113/jphysiol.2007.138370
    • Hayato, R., Ohtubo, Y., and Yoshii, K. (2007). Functional expression of ionotropic purinergic receptors on mouse taste bud cells. J. Physiol. 584, 473-488. doi: 10. 1113/jphysiol.2007.138370
    • (2007) J. Physiol , vol.584 , pp. 473-488
    • Hayato, R.1    Ohtubo, Y.2    Yoshii, K.3
  • 24
    • 0034021380 scopus 로고    scopus 로고
    • Apparent species differences in the kinetic properties of P2X7 receptors
    • doi: 10.1038/sj.bjp.0703302
    • Hibell, A. D., Kidd, E. J., Chessell, I. P., Humphrey, P. P., and Michel, A. D. (2000). Apparent species differences in the kinetic properties of P2X7 receptors. Br. J. Pharmacol. 130, 167-173. doi: 10.1038/sj.bjp.0703302
    • (2000) Br. J. Pharmacol , vol.130 , pp. 167-173
    • Hibell, A.D.1    Kidd, E.J.2    Chessell, I.P.3    Humphrey, P.P.4    Michel, A.D.5
  • 25
    • 34247631845 scopus 로고    scopus 로고
    • The role of pannexin 1 hemichannels in ATP release and cell-cell communication in mouse taste buds
    • doi: 10.1073/pnas.0611280104
    • Huang, Y. J., Maruyama, Y., Dvoryanchikov, G., Pereira, E., Chaudhari, N., and Roper, S. D. (2007). The role of pannexin 1 hemichannels in ATP release and cell-cell communication in mouse taste buds. Proc. Natl. Acad. Sci. USA 104, 6436-6441. doi: 10.1073/pnas.0611280104
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6436-6441
    • Huang, Y.J.1    Maruyama, Y.2    Dvoryanchikov, G.3    Pereira, E.4    Chaudhari, N.5    Roper, S.D.6
  • 26
    • 66149173401 scopus 로고    scopus 로고
    • Pannexin 1: The molecular substrate of astrocyte hemichannels
    • doi: 10.1523/jneurosci.6062-08.2009
    • Iglesias, R., Dahl, G., Qiu, F., Spray, D. C., and Scemes, E. (2009). Pannexin 1: the molecular substrate of astrocyte hemichannels. J. Neurosci. 29, 7092-7097. doi: 10.1523/jneurosci.6062-08.2009
    • (2009) J. Neurosci , vol.29 , pp. 7092-7097
    • Iglesias, R.1    Dahl, G.2    Qiu, F.3    Spray, D.C.4    Scemes, E.5
  • 27
    • 26844570488 scopus 로고    scopus 로고
    • N-methyl-D-glucamine and propidium dyes utilize different permeation pathways at rat P2X7 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 P2X7 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    Mackenzie, A.3    Zhang, Y.H.4    Surprenant, A.5    North, R.A.6
  • 28
    • 0034602169 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor
    • doi: 10.1074/jbc.m005481200
    • Jiang, L. H., Rassendren, F., Surprenant, A., and North, R. A. (2000). Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor. J. Biol. Chem. 275, 34190-34196. doi: 10.1074/jbc.m005481200
    • (2000) J. Biol. Chem , vol.275 , pp. 34190-34196
    • Jiang, L.H.1    Rassendren, F.2    Surprenant, A.3    North, R.A.4
  • 30
    • 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. PurinergicSignal. 8, 375-417. doi: 10.1007/s11302-012-9314-7
    • (2012) PurinergicSignal , vol.8 , pp. 375-417
    • Kaczmarek-Hajek, K.1    Lorinczi, E.2    Hausmann, R.3    Nicke, A.4
  • 31
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X4 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 P2X4 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
  • 32
    • 84879216741 scopus 로고    scopus 로고
    • Dual gating mechanism and function of P2X7 receptor channels
    • doi: 10.1016/j.bpj.2013.05.006
    • Khadra, A., Tomic, M., Yan, Z., Zemkova, H., Sherman, A., and Stojilkovic, S. S. (2013). Dual gating mechanism and function of P2X7 receptor channels. Biophys.J. 104,2612-2621. doi: 10.1016/j.bpj.2013.05.006
    • (2013) Biophys.J , vol.104 , pp. 2612-2621
    • Khadra, A.1    Tomic, M.2    Yan, Z.3    Zemkova, H.4    Sherman, A.5    Stojilkovic, S.S.6
  • 33
    • 84861125237 scopus 로고    scopus 로고
    • Gating properties of the P2X2a and P2X2b receptor channels: Experiments and mathematical modeling
    • doi: 10. 1085/jgp.201110716
    • Khadra, A., Yan, Z., Coddou, C., Tomic, M., Sherman, A., and Stojilkovic, S. S. (2012). Gating properties of the P2X2a and P2X2b receptor channels: experiments and mathematical modeling. J. Gen. Physiol. 139, 333-348. doi: 10. 1085/jgp.201110716
    • (2012) J. Gen. Physiol , vol.139 , pp. 333-348
    • Khadra, A.1    Yan, Z.2    Coddou, C.3    Tomic, M.4    Sherman, A.5    Stojilkovic, S.S.6
  • 34
    • 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. (1999). 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
  • 35
    • 14044274324 scopus 로고    scopus 로고
    • Contribution of transmembrane regions to ATP-gated P2X2 channelpermeabilitydynamics
    • doi: 10.1074/jbc.m411324200
    • Khakh, B. S., and Egan, T. M. (2005). Contribution of transmembrane regions to ATP-gated P2X2 channelpermeabilitydynamics. 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
  • 36
    • 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
  • 37
    • 84867132775 scopus 로고    scopus 로고
    • Neuromodulation byextracellular ATP and P2Xreceptors inthe CNS
    • doi: 10.1016/j.neuron.2012.09.024
    • Khakh, B. S., and North, R. A. (2012). Neuromodulation byextracellular ATP and P2Xreceptors inthe CNS. Neuron 76, 51-69. doi: 10.1016/j.neuron.2012.09.024
    • (2012) Neuron , vol.76 , pp. 51-69
    • Khakh, B.S.1    North, R.A.2
  • 38
    • 0035396167 scopus 로고    scopus 로고
    • Functional evidence of distinct ATP activation sites at the human P2X7 receptor
    • doi: 10.1111/j.1469-7793.2001.00025.x
    • Klapperstuck, M., Buttner, C., Schmalzing, G., and Markwardt, F. (2001). Functional evidence of distinct ATP activation sites at the human P2X7 receptor. J. Physiol. 534, 25-35. doi: 10.1111/j.1469-7793.2001.00025.x
    • (2001) J. Physiol , vol.534 , pp. 25-35
    • Klapperstuck, M.1    Buttner, C.2    Schmalzing, G.3    Markwardt, F.4
  • 39
    • 0032230275 scopus 로고    scopus 로고
    • Functional role of alternative splicing in pituitary P2X2 receptor-channel activation and desensitization
    • doi: 10.1210/me.12.7. 901
    • Koshimizu, T., Tomic, M., Van Goor, F., and Stojilkovic, S. S. (1998). Functional role of alternative splicing in pituitary P2X2 receptor-channel activation and desensitization. Mol. Endocrinol. 12, 901-913. doi: 10.1210/me.12.7. 901
    • (1998) Mol. Endocrinol , vol.12 , pp. 901-913
    • Koshimizu, T.1    Tomic, M.2    van Goor, F.3    Stojilkovic, S.S.4
  • 40
    • 79956336722 scopus 로고    scopus 로고
    • Expression and roles of pannexins in ATP release in the pituitary gland
    • doi: 10.1210/en.2010-1216
    • Li, S., Bjelobaba, I., Yan, Z., Kucka, M., Tomic, M., and Stojilkovic, S. S. (2011a). Expression and roles of pannexins in ATP release in the pituitary gland. Endocrinology 152, 2342-2352. doi: 10.1210/en.2010-1216
    • (2011) Endocrinology , vol.152 , pp. 2342-2352
    • Li, S.1    Bjelobaba, I.2    Yan, Z.3    Kucka, M.4    Tomic, M.5    Stojilkovic, S.S.6
  • 41
    • 80054112857 scopus 로고    scopus 로고
    • Characterization of novel Pannexin 1 isoforms from rat pituitary cells and their association with ATP-gated P2X channels
    • doi: 10.1016/j.ygcen.2011.08. 019
    • Li, S., Tomic, M., and Stojilkovic, S. S. (2011b). Characterization of novel Pannexin 1 isoforms from rat pituitary cells and their association with ATP-gated P2X channels. Gen. Comp. Endocrinol. 174, 202-210. doi: 10.1016/j.ygcen.2011.08. 019
    • (2011) Gen. Comp. Endocrinol , vol.174 , pp. 202-210
    • Li, S.1    Tomic, M.2    Stojilkovic, S.S.3
  • 42
    • 33646748700 scopus 로고    scopus 로고
    • Pannexin 1 in erythrocytes: Function without a gap
    • doi: 10.1073/pnas. 0601037103
    • Locovei, S., Bao, L., and Dahl, G. (2006). Pannexin 1 in erythrocytes: function without a gap. Proc. Natl. Acad. Sci. USA 103, 7655-7659. doi: 10.1073/pnas. 0601037103
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7655-7659
    • Locovei, S.1    Bao, L.2    Dahl, G.3
  • 43
    • 82755165079 scopus 로고    scopus 로고
    • Corneal epithelium expresses a variant of P2X7 receptor in health and disease
    • doi: 10.1371/journal.pone.0028541
    • Mankus, C., Rich, C., Minns, M., and Trinkaus-Randall, V. (2011). Corneal epithelium expresses a variant of P2X7 receptor in health and disease. PLoS One 6:e28541. doi: 10.1371/journal.pone.0028541
    • (2011) PLoS One , vol.6
    • Mankus, C.1    Rich, C.2    Minns, M.3    Trinkaus-Randall, V.4
  • 44
    • 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
  • 45
    • 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
  • 46
    • 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
  • 47
    • 79958034097 scopus 로고    scopus 로고
    • Pannexin-1 is required for ATP release during apoptosis but not for inflammasome activation
    • doi: 10.4049/jimmunol. 1100478
    • Qu, Y., Misaghi, S., Newton, K., Gilmour, L. L., Louie, S., Cupp, J. E., et al. (2011). Pannexin-1 is required for ATP release during apoptosis but not for inflammasome activation. J. Immunol. 186, 6553-6561. doi: 10.4049/jimmunol. 1100478
    • (2011) J. Immunol , vol.186 , pp. 6553-6561
    • Qu, Y.1    Misaghi, S.2    Newton, K.3    Gilmour, L.L.4    Louie, S.5    Cupp, J.E.6
  • 48
    • 0031052095 scopus 로고    scopus 로고
    • The permeabilizing ATP receptor, P2X7. Cloning and expression of a human cDNA
    • doi: 10.1074/jbc.272.9. 5482
    • Rassendren, F., Buell, G. N., Virginio, C., Collo, G., North, R. A., and Surprenant, A. (1997). The permeabilizing ATP receptor, P2X7. Cloning and expression of a human cDNA. J. Biol. Chem. 272, 5482-5486. doi: 10.1074/jbc.272.9. 5482
    • (1997) J. Biol. Chem , vol.272 , pp. 5482-5486
    • Rassendren, F.1    Buell, G.N.2    Virginio, C.3    Collo, G.4    North, R.A.5    Surprenant, A.6
  • 49
    • 34047233727 scopus 로고    scopus 로고
    • Kinetics ofP2X7 receptor-operated single channels currents
    • doi: 10. 1529/biophysj.106.091413
    • Riedel, T., Lozinsky, I., Schmalzing, G., and Markwardt, F. (2007a). Kinetics ofP2X7 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
  • 50
    • 34547824501 scopus 로고    scopus 로고
    • Influence of extracellular monovalent cations on pore and gating properties of P2X7 receptor-operated single-channel currents
    • doi: 10.1529/biophysj.106. 103614
    • Riedel, T., Schmalzing, G., and Markwardt, F. (2007b). Influence of extracellular monovalent cations on pore and gating properties of P2X7 receptor-operated single-channel currents. Biophys. J. 93, 846-858. doi: 10.1529/biophysj.106. 103614
    • (2007) Biophys. J , vol.93 , pp. 846-858
    • Riedel, T.1    Schmalzing, G.2    Markwardt, F.3
  • 51
    • 33645099729 scopus 로고    scopus 로고
    • Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP
    • doi: 10.1111/j.1471-4159. 2005.03593.x
    • Roberts, J. A., and Evans, R. J. (2006). Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP. J. Neurochem. 96, 843-852. doi: 10.1111/j.1471-4159. 2005.03593.x
    • (2006) J. Neurochem , vol.96 , pp. 843-852
    • Roberts, J.A.1    Evans, R.J.2
  • 52
    • 46749144924 scopus 로고    scopus 로고
    • Facilitation of P2X7 receptor currents and membrane blebbing via constitutive and dynamic calmodulin binding
    • doi: 10.1523/jneurosci.0696-08. 2008
    • Roger, S., Pelegrin, P., and Surprenant, A. (2008). Facilitation of P2X7 receptor currents and membrane blebbing via constitutive and dynamic calmodulin binding. J. Neurosci. 28, 6393-6401. doi: 10.1523/jneurosci.0696-08. 2008
    • (2008) J. Neurosci , vol.28 , pp. 6393-6401
    • Roger, S.1    Pelegrin, P.2    Surprenant, A.3
  • 53
    • 66249107019 scopus 로고    scopus 로고
    • Direct observation of ATP-induced conformational changes in single P2X4 receptors
    • doi: 10.1371/journal.pbio.1000103
    • Shinozaki, Y., Sumitomo, K., Tsuda, M., Koizumi, S., Inoue, K., and Torimitsu, K.(2009). Direct observation of ATP-induced conformational changes in single P2X4 receptors. PLoS Biol. 7:e103. doi: 10.1371/journal.pbio.1000103
    • (2009) PLoS Biol , vol.7
    • Shinozaki, Y.1    Sumitomo, K.2    Tsuda, M.3    Koizumi, S.4    Inoue, K.5    Torimitsu, K.6
  • 54
    • 0037424417 scopus 로고    scopus 로고
    • P2X7 receptor cell surface expression and cytolytic pore formation are regulated by a distal C-terminal region
    • doi: 10. 1074/jbc.m211094200
    • Smart, M. L., Gu, B., Panchal, R. G., Wiley, J., Cromer, B., Williams, D. A., et al. (2003). P2X7 receptor cell surface expression and cytolytic pore formation are regulated by a distal C-terminal region. J. Biol. Chem. 278, 8853-8860. doi: 10. 1074/jbc.m211094200
    • (2003) J. Biol. Chem , vol.278 , pp. 8853-8860
    • Smart, M.L.1    Gu, B.2    Panchal, R.G.3    Wiley, J.4    Cromer, B.5    Williams, D.A.6
  • 56
    • 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
  • 57
    • 72049129143 scopus 로고    scopus 로고
    • Purinergic regulation of hypothalamopituitary functions
    • doi: 10.1016/j.tem.2009.05.005
    • Stojilkovic, S. S. (2009). Purinergic regulation of hypothalamopituitary functions. TrendsEndocrinol. Metab. 20, 460-468. doi: 10.1016/j.tem.2009.05.005
    • (2009) TrendsEndocrinol. Metab , vol.20 , pp. 460-468
    • Stojilkovic, S.S.1
  • 58
    • 77955776526 scopus 로고    scopus 로고
    • Two haplotypes of the P2X7 receptor containing the Ala-348 to Thr polymorphism exhibit a gain-of-function effect and enhanced interleukin-1beta secretion
    • doi: 10.1096/fj.09-150862
    • Stokes, L., Fuller, S. J., Sluyter, R., Skarratt, K. K., Gu, B. J., and Wiley, J. S. (2010). Two haplotypes of the P2X7 receptor containing the Ala-348 to Thr polymorphism exhibit a gain-of-function effect and enhanced interleukin-1beta secretion. FASEB J. 24, 2916-2927. doi: 10.1096/fj.09-150862
    • (2010) FASEB J , vol.24 , pp. 2916-2927
    • Stokes, L.1    Fuller, S.J.2    Sluyter, R.3    Skarratt, K.K.4    Gu, B.J.5    Wiley, J.S.6
  • 59
    • 77950461030 scopus 로고    scopus 로고
    • Identification and characterization of a novel variant of the human P2X7 receptor resulting in gain of function
    • doi: 10.1007/s11302-009-9168-9
    • Sun, C., Chu, J., Singh, S., and Salter, R. D. (2010). Identification and characterization of a novel variant of the human P2X7 receptor resulting in gain of function. Purinergic Signal. 6, 31-45. doi: 10.1007/s11302-009-9168-9
    • (2010) Purinergic Signal , vol.6 , pp. 31-45
    • Sun, C.1    Chu, J.2    Singh, S.3    Salter, R.D.4
  • 60
    • 84876223254 scopus 로고    scopus 로고
    • The second transmembrane domain of P2X7 contributes to dilated pore formation
    • doi: 10.1371/journal.pone.0061886
    • Sun, C., Heid, M. E., Keyel, P. A., and Salter, R. D. (2013). The second transmembrane domain of P2X7 contributes to dilated pore formation. PLoS One 8:e61886. doi: 10.1371/journal.pone.0061886
    • (2013) PLoS One , vol.8
    • Sun, C.1    Heid, M.E.2    Keyel, P.A.3    Salter, R.D.4
  • 61
    • 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
  • 62
    • 0025274812 scopus 로고
    • ATP-induced pore formation in the plasma membrane of rat peritoneal mast cells
    • doi: 10. 1085/jgp.95.3.459
    • Tatham, P. E., and Lindau, M. (1990). ATP-induced pore formation in the plasma membrane of rat peritoneal mast cells. J. Gen. Physiol. 95, 459-476. doi: 10. 1085/jgp.95.3.459
    • (1990) J. Gen. Physiol , vol.95 , pp. 459-476
    • Tatham, P.E.1    Lindau, M.2
  • 63
    • 31044446583 scopus 로고    scopus 로고
    • Functional properties of internalization-deficient P2X4 receptors reveal a novel mechanism of ligand-gated channel facilitation by ivermectin
    • doi: 10. 1124/mol.105.018812
    • Toulme, E., Soto, F., Garret, M., and Boue-Grabot, E. (2006). Functional properties of internalization-deficient P2X4 receptors reveal a novel mechanism of ligand-gated channel facilitation by ivermectin. Mol. Pharmacol. 69, 576-587. doi: 10. 1124/mol.105.018812
    • (2006) Mol. Pharmacol , vol.69 , pp. 576-587
    • Toulme, E.1    Soto, F.2    Garret, M.3    Boue-Grabot, E.4
  • 64
    • 77954659706 scopus 로고    scopus 로고
    • Murine epidermal langerhans cells and keratinocytes express functional P2X7 receptors
    • doi: 10.1111/j.1600-0625.2009. 01029.x
    • Tran, J. N., Pupovac, A., Taylor, R. M., Wiley, J. S., Byrne, S. N., and Sluyter, R. (2010). Murine epidermal langerhans cells and keratinocytes express functional P2X7 receptors. Exp. Dermatol. 19, e151-e157. doi: 10.1111/j.1600-0625.2009. 01029.x
    • (2010) Exp. Dermatol , vol.19
    • Tran, J.N.1    Pupovac, A.2    Taylor, R.M.3    Wiley, J.S.4    Byrne, S.N.5    Sluyter, R.6
  • 65
    • 0034744764 scopus 로고    scopus 로고
    • Adenosine 5'-triphosphate: A P2-purinergic agonist in the myocardium
    • Vassort, G. (2001). Adenosine 5'-triphosphate: a P2-purinergic agonist in the myocardium. Physiol. Rev. 81, 767-806.
    • (2001) Physiol. Rev , vol.81 , pp. 767-806
    • Vassort, G.1
  • 66
    • 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. (1999a). 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    Mackenzie, A.2    North, R.A.3    Surprenant, A.4
  • 68
    • 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
  • 69
    • 79959546453 scopus 로고    scopus 로고
    • Role of purinergic receptor polymorphisms in human bone
    • (LandmarkEd.), doi: 10.2741/3873
    • Wesselius, A., Bours, M. J., Agrawal, A., Gartland, A., Dagnelie, P. C., Schwarz, P., et al. (2011). Role of purinergic receptor polymorphisms in human bone. Front. Biosci. (LandmarkEd.) 16, 2572-2585. doi: 10.2741/3873
    • (2011) Front. Biosci. , vol.16 , pp. 2572-2585
    • Wesselius, A.1    Bours, M.J.2    Agrawal, A.3    Gartland, A.4    Dagnelie, P.C.5    Schwarz, P.6
  • 70
    • 77958530854 scopus 로고    scopus 로고
    • Experimental characterization and mathematical modeling of P2X7 receptor channel gating
    • doi: 10.1523/jneurosci.2390-10.2010
    • Yan, Z., Khadra, A., Li, S., Tomic, M., Sherman, A., and Stojilkovic, S. S. (2010). Experimental characterization and mathematical modeling of P2X7 receptor channel gating. J. Neurosci. 30, 14213-14224. doi: 10.1523/jneurosci.2390-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 14213-14224
    • Yan, Z.1    Khadra, A.2    Li, S.3    Tomic, M.4    Sherman, A.5    Stojilkovic, S.S.6
  • 71
    • 80054018926 scopus 로고    scopus 로고
    • Calcium-dependent block of P2X7 receptor channel function is allosteric
    • doi: 10.1085/jgp.201110647
    • Yan, Z., Khadra, A., Sherman, A., and Stojilkovic, S. S. (2011). Calcium-dependent block of P2X7 receptor channel function is allosteric. J. Gen. Physiol. 138, 437-452. doi: 10.1085/jgp.201110647
    • (2011) J. Gen. Physiol , vol.138 , pp. 437-452
    • Yan, Z.1    Khadra, A.2    Sherman, A.3    Stojilkovic, S.S.4
  • 72
    • 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
  • 73
    • 33845940887 scopus 로고    scopus 로고
    • Participation of the Lys313-Ile333 sequence of the purinergic P2X4 receptor in agonist binding and transduction of signals to the channel gate
    • doi: 10.1074/jbc.m512791200
    • Yan, Z., Liang, Z., Obsil, T., and Stojilkovic, S. S. (2006). Participation of the Lys313-Ile333 sequence of the purinergic P2X4 receptor in agonist binding and transduction of signals to the channel gate. J. Biol. Chem. 281, 32649-32659. doi: 10.1074/jbc.m512791200
    • (2006) J. Biol. Chem , vol.281 , pp. 32649-32659
    • Yan, Z.1    Liang, Z.2    Obsil, T.3    Stojilkovic, S.S.4
  • 74
    • 34547423310 scopus 로고    scopus 로고
    • Role of aromatic and charged ectodomain residues in the P2X4 receptor functions
    • doi: 10.1111/j.1471-4159. 2007.04616.x
    • Zemkova, H., Yan, Z., Liang, Z., Jelinkova, I., Tomic, M., and Stojilkovic, S. S. (2007). Role of aromatic and charged ectodomain residues in the P2X4 receptor functions. J. Neurochem. 102, 1139-1150. doi: 10.1111/j.1471-4159. 2007.04616.x
    • (2007) J. Neurochem , vol.102 , pp. 1139-1150
    • Zemkova, H.1    Yan, Z.2    Liang, Z.3    Jelinkova, I.4    Tomic, M.5    Stojilkovic, S.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.