메뉴 건너뛰기




Volumn 38, Issue 1, 2013, Pages 20-29

Moving through the gate in ATP-activated P2X receptors

Author keywords

Gating; Ligand gated ion channels; Neurotransmitter; Purinergic receptor; Structure

Indexed keywords

ADENOSINE TRIPHOSPHATE; PURINERGIC P2X RECEPTOR;

EID: 84871504004     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2012.10.006     Document Type: Review
Times cited : (66)

References (95)
  • 1
    • 0015393308 scopus 로고
    • Purinergic nerves
    • Burnstock G. Purinergic nerves. Pharmacol. Rev. 1972, 24:509-581.
    • (1972) Pharmacol. Rev. , vol.24 , pp. 509-581
    • Burnstock, G.1
  • 2
    • 68349152690 scopus 로고    scopus 로고
    • An evolutionary history of P2X receptors
    • Fountain S.J., Burnstock G. An evolutionary history of P2X receptors. Purinergic Signal. 2009, 5:269-272.
    • (2009) Purinergic Signal. , vol.5 , pp. 269-272
    • Fountain, S.J.1    Burnstock, G.2
  • 3
    • 84861526394 scopus 로고    scopus 로고
    • Molecular and functional properties of P2X receptors-recent progress and persisting challenges
    • Kaczmarek-Hajek K., et al. Molecular and functional properties of P2X receptors-recent progress and persisting challenges. Purinergic Signal. 2012, 8:375-417.
    • (2012) Purinergic Signal. , vol.8 , pp. 375-417
    • Kaczmarek-Hajek, K.1
  • 4
    • 84863829102 scopus 로고    scopus 로고
    • A dual polybasic motif determines phosphoinositide binding and regulation in the P2X channel family
    • Bernier L.P., et al. A dual polybasic motif determines phosphoinositide binding and regulation in the P2X channel family. PLoS ONE 2012, 7:e40595.
    • (2012) PLoS ONE , vol.7
    • Bernier, L.P.1
  • 5
    • 3142669217 scopus 로고    scopus 로고
    • Identification of a trafficking motif involved in the stabilization and polarization of P2X receptors
    • Chaumont S., et al. Identification of a trafficking motif involved in the stabilization and polarization of P2X receptors. J. Biol. Chem. 2004, 279:29628-29638.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29628-29638
    • Chaumont, S.1
  • 6
    • 79955950645 scopus 로고    scopus 로고
    • Activation and regulation of purinergic P2X receptor channels
    • Coddou C., et al. Activation and regulation of purinergic P2X receptor channels. Pharmacol. Rev. 2011, 63:641-683.
    • (2011) Pharmacol. Rev. , vol.63 , pp. 641-683
    • Coddou, C.1
  • 7
    • 84858408591 scopus 로고    scopus 로고
    • P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties
    • Compan V., et al. P2X2 and P2X5 subunits define a new heteromeric receptor with P2X7-like properties. J. Neurosci. 2012, 32:4284-4296.
    • (2012) J. Neurosci. , vol.32 , pp. 4284-4296
    • Compan, V.1
  • 8
    • 84860785529 scopus 로고    scopus 로고
    • Molecular mechanism of ATP binding and ion channel activation in P2X receptors
    • Hattori M., Gouaux E. Molecular mechanism of ATP binding and ion channel activation in P2X receptors. Nature 2012, 485:207-212.
    • (2012) Nature , vol.485 , pp. 207-212
    • Hattori, M.1    Gouaux, E.2
  • 9
    • 0028030797 scopus 로고
    • A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP
    • Valera S., et al. A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP. Nature 1994, 371:516-519.
    • (1994) Nature , vol.371 , pp. 516-519
    • Valera, S.1
  • 10
    • 0028025001 scopus 로고
    • New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor
    • Brake A.J., et al. New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor. Nature 1994, 371:519-523.
    • (1994) Nature , vol.371 , pp. 519-523
    • Brake, A.J.1
  • 11
    • 77952551628 scopus 로고    scopus 로고
    • New structure enlivens interest in P2X receptors
    • Browne L.E., et al. New structure enlivens interest in P2X receptors. Trends Pharmacol. Sci. 2010, 31:229-237.
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 229-237
    • Browne, L.E.1
  • 12
    • 75749112926 scopus 로고    scopus 로고
    • P2X receptors: dawn of the post-structure era
    • Young M.T. P2X receptors: dawn of the post-structure era. Trends Biochem. Sci. 2010, 35:83-90.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 83-90
    • Young, M.T.1
  • 13
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • Kawate T., et al. Crystal structure of the ATP-gated P2X(4) ion channel in the closed state. Nature 2009, 460:592-598.
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1
  • 14
    • 67949092829 scopus 로고    scopus 로고
    • Pore architecture and ion sites in acid-sensing ion channels and P2X receptors
    • Gonzales E.B., et al. Pore architecture and ion sites in acid-sensing ion channels and P2X receptors. Nature 2009, 460:599-604.
    • (2009) Nature , vol.460 , pp. 599-604
    • Gonzales, E.B.1
  • 15
    • 77958610109 scopus 로고    scopus 로고
    • Structural interpretation of P2X receptor mutagenesis studies on drug action
    • Evans R.J. Structural interpretation of P2X receptor mutagenesis studies on drug action. Br. J. Pharmacol. 2010, 161:961-971.
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 961-971
    • Evans, R.J.1
  • 16
    • 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
    • Jiang R., et al. A putative extracellular salt bridge at the subunit interface contributes to the ion channel function of the ATP-gated P2X2 receptor. J. Biol. Chem. 2010, 285:15805-15815.
    • (2010) J. Biol. Chem. , vol.285 , pp. 15805-15815
    • Jiang, R.1
  • 17
    • 84880308941 scopus 로고    scopus 로고
    • Pore-opening mechanism in trimeric P2X receptor channels
    • Li M., et al. Pore-opening mechanism in trimeric P2X receptor channels. Nat. Commun. 2010, 1:44.
    • (2010) Nat. Commun. , vol.1 , pp. 44
    • Li, M.1
  • 18
    • 78650677994 scopus 로고    scopus 로고
    • P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance
    • Browne L.E., et al. P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance. Nat. Neurosci. 2011, 14:17-18.
    • (2011) Nat. Neurosci. , vol.14 , pp. 17-18
    • Browne, L.E.1
  • 19
    • 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)
    • Samways D.S., et al. 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. 2011, 108:13800-13805.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 13800-13805
    • Samways, D.S.1
  • 20
    • 84860540831 scopus 로고    scopus 로고
    • Tightening of the ATP-binding sites induces the opening of P2X receptor channels
    • Jiang R., et al. Tightening of the ATP-binding sites induces the opening of P2X receptor channels. EMBO J. 2012, 31:2134-2143.
    • (2012) EMBO J. , vol.31 , pp. 2134-2143
    • Jiang, R.1
  • 21
    • 79958024000 scopus 로고    scopus 로고
    • Ion access pathway to the transmembrane pore in P2X receptor channels
    • Kawate T., et al. Ion access pathway to the transmembrane pore in P2X receptor channels. J. Gen. Physiol. 2011, 137:579-590.
    • (2011) J. Gen. Physiol. , vol.137 , pp. 579-590
    • Kawate, T.1
  • 22
    • 84858665860 scopus 로고    scopus 로고
    • Agonist binding evokes extensive conformational changes in the extracellular domain of the ATP-gated human P2X1 receptor ion channel
    • Roberts J.A., et al. 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. 2012, 109:4663-4667.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 4663-4667
    • Roberts, J.A.1
  • 23
    • 84863914041 scopus 로고    scopus 로고
    • Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor
    • Lorinczi E., et al. Involvement of the cysteine-rich head domain in activation and desensitization of the P2X1 receptor. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:11396-11401.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 11396-11401
    • Lorinczi, E.1
  • 24
    • 0030447892 scopus 로고    scopus 로고
    • Domains of P2X receptors involved in desensitization
    • Werner P., et al. Domains of P2X receptors involved in desensitization. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:15485-15490.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 15485-15490
    • Werner, P.1
  • 25
    • 84455161674 scopus 로고    scopus 로고
    • The intracellular amino terminus plays a dominant role in desensitization of ATP-gated P2X receptor ion channels
    • Allsopp R.C., Evans R.J. The intracellular amino terminus plays a dominant role in desensitization of ATP-gated P2X receptor ion channels. J. Biol. Chem. 2011, 286:44691-44701.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44691-44701
    • Allsopp, R.C.1    Evans, R.J.2
  • 26
    • 0034602169 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor
    • Jiang L.H., et al. Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor. J. Biol. Chem. 2000, 275:34190-34196.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34190-34196
    • Jiang, L.H.1
  • 27
    • 0034703055 scopus 로고    scopus 로고
    • The role of positively charged amino acids in ATP recognition by human P2X(1) receptors
    • Ennion S., et al. The role of positively charged amino acids in ATP recognition by human P2X(1) receptors. J. Biol. Chem. 2000, 275:29361-29367.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29361-29367
    • Ennion, S.1
  • 28
    • 1542275329 scopus 로고    scopus 로고
    • ATP binding at human P2X1 receptors. Contribution of aromatic and basic amino acids revealed using mutagenesis and partial agonists
    • Roberts J.A., Evans R.J. ATP binding at human P2X1 receptors. Contribution of aromatic and basic amino acids revealed using mutagenesis and partial agonists. J. Biol. Chem. 2004, 279:9043-9055.
    • (2004) J. Biol. Chem. , vol.279 , pp. 9043-9055
    • Roberts, J.A.1    Evans, R.J.2
  • 29
    • 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
    • Roberts J.A., Evans R.J. Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP. J. Neurochem. 2006, 96:843-852.
    • (2006) J. Neurochem. , vol.96 , pp. 843-852
    • Roberts, J.A.1    Evans, R.J.2
  • 30
    • 34247120710 scopus 로고    scopus 로고
    • Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors
    • Roberts J.A., Evans R.J. Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors. J. Neurosci. 2007, 27:4072-4082.
    • (2007) J. Neurosci. , vol.27 , pp. 4072-4082
    • Roberts, J.A.1    Evans, R.J.2
  • 31
    • 33846968794 scopus 로고    scopus 로고
    • Identification of an intersubunit cross-link between substituted cysteine residues located in the putative ATP binding site of the P2X1 receptor
    • Marquez-Klaka B., et al. Identification of an intersubunit cross-link between substituted cysteine residues located in the putative ATP binding site of the P2X1 receptor. J. Neurosci. 2007, 27:1456-1466.
    • (2007) J. Neurosci. , vol.27 , pp. 1456-1466
    • Marquez-Klaka, B.1
  • 32
    • 50649117149 scopus 로고    scopus 로고
    • Cysteine substitution mutagenesis and the effects of methanethiosulfonate reagents at P2X2 and P2X4 receptors support a core common mode of ATP action at P2X receptors
    • Roberts J.A., et al. Cysteine substitution mutagenesis and the effects of methanethiosulfonate reagents at P2X2 and P2X4 receptors support a core common mode of ATP action at P2X receptors. J. Biol. Chem. 2008, 283:20126-20136.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20126-20136
    • Roberts, J.A.1
  • 33
    • 60549095934 scopus 로고    scopus 로고
    • Inter-subunit disulfide cross-linking in homomeric and heteromeric P2X receptors
    • Marquez-Klaka B., et al. Inter-subunit disulfide cross-linking in homomeric and heteromeric P2X receptors. Eur. Biophys. J. 2009, 38:329-338.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 329-338
    • Marquez-Klaka, B.1
  • 34
    • 0032199006 scopus 로고    scopus 로고
    • Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors
    • Colquhoun D. Binding, gating, affinity and efficacy: the interpretation of structure-activity relationships for agonists and of the effects of mutating receptors. Br. J. Pharmacol. 1998, 125:924-947.
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 924-947
    • Colquhoun, D.1
  • 35
    • 0035313222 scopus 로고    scopus 로고
    • Cysteine mutants as chemical sensors for ligand-receptor interactions
    • Foucaud B., et al. Cysteine mutants as chemical sensors for ligand-receptor interactions. Trends Pharmacol. Sci. 2001, 22:170-173.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 170-173
    • Foucaud, B.1
  • 36
    • 79959355099 scopus 로고    scopus 로고
    • Agonist trapped in ATP-binding sites of the P2X2 receptor
    • Jiang R., et al. Agonist trapped in ATP-binding sites of the P2X2 receptor. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:9066-9071.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9066-9071
    • Jiang, R.1
  • 37
    • 78951475438 scopus 로고    scopus 로고
    • Amino acid residues constituting the agonist binding site of the human P2X3 receptor
    • Bodnar M., et al. Amino acid residues constituting the agonist binding site of the human P2X3 receptor. J. Biol. Chem. 2011, 286:2739-2749.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2739-2749
    • Bodnar, M.1
  • 38
    • 36348952111 scopus 로고    scopus 로고
    • Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308
    • Cao L., et al. Thr339-to-serine substitution in rat P2X2 receptor second transmembrane domain causes constitutive opening and indicates a gating role for Lys308. J. Neurosci. 2007, 27:12916-12923.
    • (2007) J. Neurosci. , vol.27 , pp. 12916-12923
    • Cao, L.1
  • 39
    • 40449130117 scopus 로고    scopus 로고
    • ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a covalent ligand to its nucleotide binding site
    • Adriouch S., et al. ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a covalent ligand to its nucleotide binding site. FASEB J. 2008, 22:861-869.
    • (2008) FASEB J. , vol.22 , pp. 861-869
    • Adriouch, S.1
  • 40
    • 80053401515 scopus 로고    scopus 로고
    • Role of the ectodomain serine 275 in shaping the binding pocket of the ATP-gated P2X3 receptor
    • Petrenko N., et al. Role of the ectodomain serine 275 in shaping the binding pocket of the ATP-gated P2X3 receptor. Biochemistry 2011, 50:8427-8436.
    • (2011) Biochemistry , vol.50 , pp. 8427-8436
    • Petrenko, N.1
  • 41
    • 83755220410 scopus 로고    scopus 로고
    • Molecular basis of selective antagonism of the P2X1 receptor for ATP by NF449 and suramin: contribution of basic amino acids in the cysteine-rich loop
    • El-Ajouz S., et al. Molecular basis of selective antagonism of the P2X1 receptor for ATP by NF449 and suramin: contribution of basic amino acids in the cysteine-rich loop. Br. J. Pharmacol. 2012, 165:390-400.
    • (2012) Br. J. Pharmacol. , vol.165 , pp. 390-400
    • El-Ajouz, S.1
  • 42
    • 34447503350 scopus 로고    scopus 로고
    • An intracellular P2X receptor required for osmoregulation in Dictyostelium discoideum
    • Fountain S.J., et al. An intracellular P2X receptor required for osmoregulation in Dictyostelium discoideum. Nature 2007, 448:200-203.
    • (2007) Nature , vol.448 , pp. 200-203
    • Fountain, S.J.1
  • 43
    • 71749101439 scopus 로고    scopus 로고
    • Functional characterization of intracellular Dictyostelium discoideum P2X receptors
    • Ludlow M.J., et al. Functional characterization of intracellular Dictyostelium discoideum P2X receptors. J. Biol. Chem. 2009, 284:35227-35239.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35227-35239
    • Ludlow, M.J.1
  • 44
    • 80052823575 scopus 로고    scopus 로고
    • Expression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA
    • Valente M., et al. Expression, purification, electron microscopy, N-glycosylation mutagenesis and molecular modeling of human P2X4 and Dictyostelium discoideum P2XA. Biochim. Biophys. Acta 2011, 1808:2859-2866.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2859-2866
    • Valente, M.1
  • 45
    • 79953023121 scopus 로고    scopus 로고
    • Molecular determinants of potent P2X2 antagonism identified by functional analysis, mutagenesis, and homology docking
    • Wolf C., et al. Molecular determinants of potent P2X2 antagonism identified by functional analysis, mutagenesis, and homology docking. Mol. Pharmacol. 2011, 79:649-661.
    • (2011) Mol. Pharmacol. , vol.79 , pp. 649-661
    • Wolf, C.1
  • 46
    • 84863249245 scopus 로고    scopus 로고
    • Gating mechanism of a P2X4 receptor developed from normal mode analysis and molecular dynamics simulations
    • Du J., et al. Gating mechanism of a P2X4 receptor developed from normal mode analysis and molecular dynamics simulations. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:4140-4145.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 4140-4145
    • Du, J.1
  • 47
    • 22544478846 scopus 로고    scopus 로고
    • An intersubunit zinc binding site in rat P2X2 receptors
    • Nagaya N., et al. An intersubunit zinc binding site in rat P2X2 receptors. J. Biol. Chem. 2005, 280:25982-25993.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25982-25993
    • Nagaya, N.1
  • 48
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky A.I., et al. X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 2009, 462:745-756.
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1
  • 49
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • Hibbs R.E., Gouaux E. Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 2011, 474:54-60.
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 50
    • 84865253138 scopus 로고    scopus 로고
    • Size matters in activation/inhibition of ligand-gated ion channels
    • Du J., et al. Size matters in activation/inhibition of ligand-gated ion channels. Trends Pharmacol. Sci. 2012, 33:482-493.
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 482-493
    • Du, J.1
  • 51
    • 0141864571 scopus 로고    scopus 로고
    • Subunit arrangement in P2X receptors
    • Jiang L.H., et al. Subunit arrangement in P2X receptors. J. Neurosci. 2003, 23:8903-8910.
    • (2003) J. Neurosci. , vol.23 , pp. 8903-8910
    • Jiang, L.H.1
  • 52
    • 0035805612 scopus 로고    scopus 로고
    • Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X(2) receptor
    • Jiang L.H., et al. Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X(2) receptor. J. Biol. Chem. 2001, 276:14902-14908.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14902-14908
    • Jiang, L.H.1
  • 53
    • 80051696222 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gating
    • Allsopp R.C., et al. Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gating. J. Biol. Chem. 2011, 286:29207-29217.
    • (2011) J. Biol. Chem. , vol.286 , pp. 29207-29217
    • Allsopp, R.C.1
  • 54
    • 84856244292 scopus 로고    scopus 로고
    • Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K+ ion channel
    • Brohawn S.G., et al. Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K+ ion channel. Science 2012, 335:436-441.
    • (2012) Science , vol.335 , pp. 436-441
    • Brohawn, S.G.1
  • 55
    • 50849130216 scopus 로고    scopus 로고
    • Roles of ectodomain and transmembrane regions in ethanol and agonist action in purinergic P2X2 and P2X3 receptors
    • Asatryan L., et al. Roles of ectodomain and transmembrane regions in ethanol and agonist action in purinergic P2X2 and P2X3 receptors. Neuropharmacology 2008, 55:835-843.
    • (2008) Neuropharmacology , vol.55 , pp. 835-843
    • Asatryan, L.1
  • 56
    • 71649102934 scopus 로고    scopus 로고
    • A point mutation in the ectodomain-transmembrane 2 interface eliminates the inhibitory effects of ethanol in P2X4 receptors
    • Popova M., et al. A point mutation in the ectodomain-transmembrane 2 interface eliminates the inhibitory effects of ethanol in P2X4 receptors. J. Neurochem. 2010, 112:307-317.
    • (2010) J. Neurochem. , vol.112 , pp. 307-317
    • Popova, M.1
  • 57
    • 84857718067 scopus 로고    scopus 로고
    • Allosteric modulation of Ca2+ flux in ligand-gated cation channel (P2X4) by actions on lateral portals
    • Samways D.S., et al. Allosteric modulation of Ca2+ flux in ligand-gated cation channel (P2X4) by actions on lateral portals. J. Biol. Chem. 2012, 287:7594-7602.
    • (2012) J. Biol. Chem. , vol.287 , pp. 7594-7602
    • Samways, D.S.1
  • 58
    • 0033198189 scopus 로고    scopus 로고
    • Allosteric control of gating and kinetics at P2X(4) receptor channels
    • Khakh B.S., et al. Allosteric control of gating and kinetics at P2X(4) receptor channels. J. Neurosci. 1999, 19:7289-7299.
    • (1999) J. Neurosci. , vol.19 , pp. 7289-7299
    • Khakh, B.S.1
  • 59
    • 84864723315 scopus 로고    scopus 로고
    • Positive allosteric modulation by ivermectin of human but not murine P2X7 receptors
    • Norenberg W., et al. Positive allosteric modulation by ivermectin of human but not murine P2X7 receptors. Br. J. Pharmacol. 2012, 167:48-66.
    • (2012) Br. J. Pharmacol. , vol.167 , pp. 48-66
    • Norenberg, W.1
  • 60
    • 50149118145 scopus 로고    scopus 로고
    • Patch-clamp coordinated spectroscopy shows P2X2 receptor permeability dynamics require cytosolic domain rearrangements but not Panx-1 channels
    • Chaumont S., Khakh B.S. Patch-clamp coordinated spectroscopy shows P2X2 receptor permeability dynamics require cytosolic domain rearrangements but not Panx-1 channels. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:12063-12068.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 12063-12068
    • Chaumont, S.1    Khakh, B.S.2
  • 61
    • 0035903169 scopus 로고    scopus 로고
    • Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor
    • Migita K., et al. Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor. J. Biol. Chem. 2001, 276:30934-30941.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30934-30941
    • Migita, K.1
  • 62
    • 48149111510 scopus 로고    scopus 로고
    • Gating the pore of P2X receptor channels
    • Li M., et al. Gating the pore of P2X receptor channels. Nat. Neurosci. 2008, 11:883-887.
    • (2008) Nat. Neurosci. , vol.11 , pp. 883-887
    • Li, M.1
  • 63
    • 70449635974 scopus 로고    scopus 로고
    • Polar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectification
    • Cao L., et al. Polar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectification. J. Neurosci. 2009, 29:14257-14264.
    • (2009) J. Neurosci. , vol.29 , pp. 14257-14264
    • Cao, L.1
  • 64
    • 77951213527 scopus 로고    scopus 로고
    • Gated access to the pore of a P2X receptor: structural implications for closed-open transitions
    • Kracun S., et al. Gated access to the pore of a P2X receptor: structural implications for closed-open transitions. J. Biol. Chem. 2010, 285:10110-10121.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10110-10121
    • Kracun, S.1
  • 65
    • 1842558753 scopus 로고    scopus 로고
    • Contribution of calcium ions to P2X channel responses
    • Egan T.M., Khakh B.S. Contribution of calcium ions to P2X channel responses. J. Neurosci. 2004, 24:3413-3420.
    • (2004) J. Neurosci. , vol.24 , pp. 3413-3420
    • Egan, T.M.1    Khakh, B.S.2
  • 66
    • 33748423062 scopus 로고    scopus 로고
    • Identification of P2X4 receptor-specific residues contributing to the ivermectin effects on channel deactivation
    • Jelinkova I., et al. Identification of P2X4 receptor-specific residues contributing to the ivermectin effects on channel deactivation. Biochem. Biophys. Res. Commun. 2006, 349:619-625.
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 619-625
    • Jelinkova, I.1
  • 67
    • 34147179943 scopus 로고    scopus 로고
    • Ivermectin interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels
    • Silberberg S.D., et al. Ivermectin interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels. Neuron 2007, 54:263-274.
    • (2007) Neuron , vol.54 , pp. 263-274
    • Silberberg, S.D.1
  • 68
    • 41949101239 scopus 로고    scopus 로고
    • On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor
    • Samways D.S., et al. On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor. J. Biol. Chem. 2008, 283:5110-5117.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5110-5117
    • Samways, D.S.1
  • 69
    • 33847345548 scopus 로고    scopus 로고
    • Acidic amino acids impart enhanced Ca2+ permeability and flux in two members of the ATP-gated P2X receptor family
    • Samways D.S., Egan T.M. Acidic amino acids impart enhanced Ca2+ permeability and flux in two members of the ATP-gated P2X receptor family. J. Gen. Physiol. 2007, 129:245-256.
    • (2007) J. Gen. Physiol. , vol.129 , pp. 245-256
    • Samways, D.S.1    Egan, T.M.2
  • 70
    • 0030962404 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the pore of a P2X receptor
    • Rassendren F., et al. Identification of amino acid residues contributing to the pore of a P2X receptor. EMBO J. 1997, 16:3446-3454.
    • (1997) EMBO J. , vol.16 , pp. 3446-3454
    • Rassendren, F.1
  • 71
    • 47249090581 scopus 로고    scopus 로고
    • Permeation properties of a P2X receptor in the green algae Ostreococcus tauri
    • Fountain S.J., et al. Permeation properties of a P2X receptor in the green algae Ostreococcus tauri. J. Biol. Chem. 2008, 283:15122-15126.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15122-15126
    • Fountain, S.J.1
  • 72
    • 0032940264 scopus 로고    scopus 로고
    • Single channel properties of P2X2 purinoceptors
    • Ding S., Sachs F. Single channel properties of P2X2 purinoceptors. J. Gen. Physiol. 1999, 113:695-720.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 695-720
    • Ding, S.1    Sachs, F.2
  • 73
    • 33745763591 scopus 로고    scopus 로고
    • Vesicular release of ATP at central synapses
    • Pankratov Y., et al. Vesicular release of ATP at central synapses. Pflugers Arch. 2006, 452:589-597.
    • (2006) Pflugers Arch. , vol.452 , pp. 589-597
    • Pankratov, Y.1
  • 74
    • 46449134214 scopus 로고    scopus 로고
    • Purinergic signalling and disorders of the central nervous system
    • Burnstock G. Purinergic signalling and disorders of the central nervous system. Nat. Rev. Drug Discov. 2008, 7:575-590.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 575-590
    • Burnstock, G.1
  • 75
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North R.A. Molecular physiology of P2X receptors. Physiol. Rev. 2002, 82:1013-1067.
    • (2002) Physiol. Rev. , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 76
    • 84867132775 scopus 로고    scopus 로고
    • Neuromodulation by extracellular ATP and P2X receptors in the CNS
    • Khakh B.S., North R.A. Neuromodulation by extracellular ATP and P2X receptors in the CNS. Neuron 2012, 76:51-69.
    • (2012) Neuron , vol.76 , pp. 51-69
    • Khakh, B.S.1    North, R.A.2
  • 77
    • 0034610742 scopus 로고    scopus 로고
    • Reduced vas deferens contraction and male infertility in mice lacking P2X1 receptors
    • Mulryan K., et al. Reduced vas deferens contraction and male infertility in mice lacking P2X1 receptors. Nature 2000, 403:86-89.
    • (2000) Nature , vol.403 , pp. 86-89
    • Mulryan, K.1
  • 78
    • 78449300659 scopus 로고    scopus 로고
    • Sensing muscle ischemia: coincident detection of acid and ATP via interplay of two ion channels
    • Birdsong W.T., et al. Sensing muscle ischemia: coincident detection of acid and ATP via interplay of two ion channels. Neuron 2010, 68:739-749.
    • (2010) Neuron , vol.68 , pp. 739-749
    • Birdsong, W.T.1
  • 79
    • 79960883074 scopus 로고    scopus 로고
    • Neuronal and microglial mechanisms of neuropathic pain
    • Zhuo M., et al. Neuronal and microglial mechanisms of neuropathic pain. Mol. Brain 2011, 4:31.
    • (2011) Mol. Brain , vol.4 , pp. 31
    • Zhuo, M.1
  • 80
    • 79955623602 scopus 로고    scopus 로고
    • Neuronal CCL21 up-regulates microglia P2X4 expression and initiates neuropathic pain development
    • Biber K., et al. Neuronal CCL21 up-regulates microglia P2X4 expression and initiates neuropathic pain development. EMBO J. 2011, 30:1864-1873.
    • (2011) EMBO J. , vol.30 , pp. 1864-1873
    • Biber, K.1
  • 81
    • 84864487226 scopus 로고    scopus 로고
    • P2X4R+ microglia drive neuropathic pain
    • Beggs S., et al. P2X4R+ microglia drive neuropathic pain. Nat. Neurosci. 2012, 15:1068-1073.
    • (2012) Nat. Neurosci. , vol.15 , pp. 1068-1073
    • Beggs, S.1
  • 82
    • 33646072818 scopus 로고    scopus 로고
    • The P2X7 receptor: a key player in IL-1 processing and release
    • Ferrari D., et al. The P2X7 receptor: a key player in IL-1 processing and release. J. Immunol. 2006, 176:3877-3883.
    • (2006) J. Immunol. , vol.176 , pp. 3877-3883
    • Ferrari, D.1
  • 83
    • 67349102910 scopus 로고    scopus 로고
    • The P2X(7) receptor-pannexin connection to dye uptake and IL-1beta release
    • Pelegrin P., Surprenant A. The P2X(7) receptor-pannexin connection to dye uptake and IL-1beta release. Purinergic Signal. 2009, 5:129-137.
    • (2009) Purinergic Signal. , vol.5 , pp. 129-137
    • Pelegrin, P.1    Surprenant, A.2
  • 84
    • 34548444551 scopus 로고    scopus 로고
    • Liaisons dangereuses: P2X(7) and the inflammasome
    • Di Virgilio F. Liaisons dangereuses: P2X(7) and the inflammasome. Trends Pharmacol. Sci. 2007, 28:465-472.
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 465-472
    • Di Virgilio, F.1
  • 85
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux J.P., Edelstein S.J. Allosteric mechanisms of signal transduction. Science 2005, 308:1424-1428.
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.P.1    Edelstein, S.J.2
  • 86
    • 0033366463 scopus 로고    scopus 로고
    • Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds
    • Khakh B.S., et al. Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds. Nat. Neurosci. 1999, 2:322-330.
    • (1999) Nat. Neurosci. , vol.2 , pp. 322-330
    • Khakh, B.S.1
  • 87
    • 0033360313 scopus 로고    scopus 로고
    • Pore dilation of neuronal P2X receptor channels
    • Virginio C., et al. Pore dilation of neuronal P2X receptor channels. Nat. Neurosci. 1999, 2:315-321.
    • (1999) Nat. Neurosci. , vol.2 , pp. 315-321
    • Virginio, C.1
  • 88
    • 66249107019 scopus 로고    scopus 로고
    • Direct observation of ATP-induced conformational changes in single P2X(4) receptors
    • Shinozaki Y., et al. Direct observation of ATP-induced conformational changes in single P2X(4) receptors. PLoS Biol. 2009, 7:e1000103.
    • (2009) PLoS Biol. , vol.7
    • Shinozaki, Y.1
  • 90
    • 33846438625 scopus 로고    scopus 로고
    • Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex
    • Locovei S., et al. Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex. FEBS Lett. 2007, 581:483-488.
    • (2007) FEBS Lett. , vol.581 , pp. 483-488
    • Locovei, S.1
  • 91
    • 59449086148 scopus 로고    scopus 로고
    • The P2X7 receptor channel pore dilates under physiological ion conditions
    • Yan Z., et al. The P2X7 receptor channel pore dilates under physiological ion conditions. J. Gen. Physiol. 2008, 132:563-573.
    • (2008) J. Gen. Physiol. , vol.132 , pp. 563-573
    • Yan, Z.1
  • 92
    • 34547621940 scopus 로고    scopus 로고
    • Responses of rat P2X2 receptors to ultrashort pulses of ATP provide insights into ATP binding and channel gating
    • Moffatt L., Hume R.I. Responses of rat P2X2 receptors to ultrashort pulses of ATP provide insights into ATP binding and channel gating. J. Gen. Physiol. 2007, 130:183-201.
    • (2007) J. Gen. Physiol. , vol.130 , pp. 183-201
    • Moffatt, L.1    Hume, R.I.2
  • 93
    • 84871485564 scopus 로고    scopus 로고
    • Intermediate closed channel state(s) precede(s) activation in the ATP-gated P2X2 receptor
    • Jiang R., et al. Intermediate closed channel state(s) precede(s) activation in the ATP-gated P2X2 receptor. Channels (Austin) 2012, 6:398-402.
    • (2012) Channels (Austin) , vol.6 , pp. 398-402
    • Jiang, R.1
  • 94
    • 49649102025 scopus 로고    scopus 로고
    • On the nature of partial agonism in the nicotinic receptor superfamily
    • Lape R., et al. On the nature of partial agonism in the nicotinic receptor superfamily. Nature 2008, 454:722-727.
    • (2008) Nature , vol.454 , pp. 722-727
    • Lape, R.1
  • 95
    • 67349279395 scopus 로고    scopus 로고
    • Detection and trapping of intermediate states priming nicotinic receptor channel opening
    • Mukhtasimova N., et al. Detection and trapping of intermediate states priming nicotinic receptor channel opening. Nature 2009, 459:451-454.
    • (2009) Nature , vol.459 , pp. 451-454
    • Mukhtasimova, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.