메뉴 건너뛰기




Volumn 22, Issue 7, 2014, Pages 799-818

Key sites for P2X receptor function and multimerization: Overview of mutagenesis studies on a structural basis

Author keywords

Mutational P2X receptor analysis; P2X assembly domains; P2X ATP binding pocket; P2X quaternary structure; P2X receptor function

Indexed keywords

ADENOSINE TRIPHOSPHATE; AF 219; AMINO ACID; ANTHRAQUINONE DERIVATIVE; LIGAND GATED ION CHANNEL; PURINERGIC P2X RECEPTOR; PURINERGIC P2X RECEPTOR ANTAGONIST; PURINERGIC P2X1 RECEPTOR; PURINERGIC P2X2 RECEPTOR; PURINERGIC P2X3 RECEPTOR; PURINERGIC P2X4 RECEPTOR; PURINERGIC P2X7 RECEPTOR; PURINERGIC P2Y RECEPTOR; PYRIDOXAL PHOSPHATE 6 AZOPHENYL 2',4' DISULFONIC ACID; SURAMIN; TETRAMER; UNCLASSIFIED DRUG;

EID: 84926305271     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/0929867322666141128163215     Document Type: Article
Times cited : (32)

References (225)
  • 1
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • Kawate, T.; Michel, J.C.; Birdsong, W.T.; Gouaux, E. Crystal structure of the ATP-gated P2X(4) ion channel in the closed state. Nature, 2009, 460(7255), 592-598.
    • (2009) Nature , vol.460 , Issue.7255 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 2
    • 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
  • 4
    • 84860540831 scopus 로고    scopus 로고
    • Tightening of the ATP-binding sites induces the opening of P2X receptor channels
    • Jiang, R.; Taly, A.; Lemoine, D.; Martz, A.; Cunrath, O.; Grutter, T., 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    Taly, A.2    Lemoine, D.3    Martz, A.4    Cunrath, O.5    Grutter, T.6
  • 5
    • 84858665860 scopus 로고    scopus 로고
    • Agonist binding evokes extensive conformational changes in the extracellular domain of the ATPgated human P2X1 receptor ion channel
    • Roberts, J.A.; Allsopp, R.C.; El, A.S.; Vial, C.; Schmid, R.; Young, M.T.; Evans, R.J., Agonist binding evokes extensive conformational changes in the extracellular domain of the ATPgated 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    Allsopp, R.C.2    El, A.S.3    Vial, C.4    Schmid, R.5    Young, M.T.6    Evans, R.J.7
  • 6
    • 84880308941 scopus 로고    scopus 로고
    • Pore-opening mechanism in trimeric P2X receptor channels
    • Li, M.; Kawate, T.; Silberberg, S.D.; Swartz, K.J., Pore-opening mechanism in trimeric P2X receptor channels. Nat. Commun., 2010, 1, 44.
    • (2010) Nat. Commun. , vol.1 , pp. 44
    • Li, M.1    Kawate, T.2    Silberberg, S.D.3    Swartz, K.J.4
  • 7
    • 79958024000 scopus 로고    scopus 로고
    • Ion access pathway to the transmembrane pore in P2X receptor channels
    • Kawate, T.; Robertson, J.L.; Li, M.; Silberberg, S.D.; Swartz, K.J., Ion access pathway to the transmembrane pore in P2X receptor channels. J. Gen. Physiol., 2011, 137(6), 579-590.
    • (2011) J. Gen. Physiol. , vol.137 , Issue.6 , pp. 579-590
    • Kawate, T.1    Robertson, J.L.2    Li, M.3    Silberberg, S.D.4    Swartz, K.J.5
  • 8
    • 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.; Khakh, B.S.; Dutertre, S.; Egan, T.M., 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    Khakh, B.S.2    Dutertre, S.3    Egan, T.M.4
  • 9
    • 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.; Broomhead, H.E.; Young, M.T.; North, R.A., Polar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectification. J. Neurosci., 2009, 29(45), 14257-14264.
    • (2009) J. Neurosci. , vol.29 , Issue.45 , pp. 14257-14264
    • Cao, L.1    Broomhead, H.E.2    Young, M.T.3    North, R.A.4
  • 12
    • 0020695160 scopus 로고
    • Receptor for ATP in the membrane of mammalian sensory neurones
    • Krishtal, O.A.; Marchenko, S.M.; Pidoplichko, V.I., Receptor for ATP in the membrane of mammalian sensory neurones. Neurosci. Lett., 1983, 35(1), 41-45.
    • (1983) Neurosci. Lett. , vol.35 , Issue.1 , pp. 41-45
    • Krishtal, O.A.1    Marchenko, S.M.2    Pidoplichko, V.I.3
  • 13
    • 0020565089 scopus 로고
    • ATP excites a subpopulation of rat dorsal horn neurones
    • Jahr, C.E.; Jessell, T.M., ATP excites a subpopulation of rat dorsal horn neurones. Nature, 1983, 304(5928), 730-733.
    • (1983) Nature , vol.304 , Issue.5928 , pp. 730-733
    • Jahr, C.E.1    Jessell, T.M.2
  • 14
    • 0020637193 scopus 로고
    • Transmitter-like action of ATP on patched membranes of cultured myoblasts and myotubes
    • Kolb, H.A.; Wakelam, M.J., Transmitter-like action of ATP on patched membranes of cultured myoblasts and myotubes. Nature, 1983, 303(5918), 621-623.
    • (1983) Nature , vol.303 , Issue.5918 , pp. 621-623
    • Kolb, H.A.1    Wakelam, M.J.2
  • 15
    • 0022178232 scopus 로고
    • Is there a basis for distinguishing two types of P2-purinoceptor?
    • Burnstock, G.; Kennedy, C., Is there a basis for distinguishing two types of P2-purinoceptor? Gen. Pharmacol., 1985, 16(5), 433-440.
    • (1985) Gen. Pharmacol. , vol.16 , Issue.5 , pp. 433-440
    • Burnstock, G.1    Kennedy, C.2
  • 16
    • 0026612038 scopus 로고
    • Pharmacology and electrophysiology of ATP-activated ion channels
    • Bean, B.P., Pharmacology and electrophysiology of ATP-activated ion channels. Trends Pharmacol. Sci., 1992, 13, 87-90.
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 87-90
    • Bean, B.P.1
  • 19
    • 0028030797 scopus 로고
    • A new class of ligand-gated ion channel defined by P 2x receptor for extracellular ATP
    • Valera, S.; Hussy, N.; Evans, R.J.; Adami, N.; North, R.A.; Surprenant, A.; Buell, G., A new class of ligand-gated ion channel defined by P 2x receptor for extracellular ATP. Nature, 1994, 371, 516-519.
    • (1994) Nature , vol.371 , pp. 516-519
    • Valera, S.1    Hussy, N.2    Evans, R.J.3    Adami, N.4    North, R.A.5    Surprenant, A.6    Buell, G.7
  • 20
    • 0028025001 scopus 로고
    • New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor
    • Brake, A.J.; Wagenbach, M.J.; Julius, D., 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    Wagenbach, M.J.2    Julius, D.3
  • 21
    • 0028982205 scopus 로고
    • Coexpression of P2X 2 and P2X 3 receptor subunits can account for ATP-gated currents in sensory neurons
    • Lewis, C.; Neidhart, S.; Holy, C.; North, R.A.; Buell, G.; Surprenant, A., Coexpression of P2X 2 and P2X 3 receptor subunits can account for ATP-gated currents in sensory neurons. Nature, 1995, 377, 432-435.
    • (1995) Nature , vol.377 , pp. 432-435
    • Lewis, C.1    Neidhart, S.2    Holy, C.3    North, R.A.4    Buell, G.5    Surprenant, A.6
  • 22
    • 0028875979 scopus 로고
    • A P2X purinoceptor cDNA conferring a novel pharmacological profile
    • Bo, X.N.; Zhang, Y.; Nassar, M.; Burnstock, G.; Schoepfer, R., A P2X purinoceptor cDNA conferring a novel pharmacological profile. FEBS Lett., 1995, 375, 129-133.
    • (1995) FEBS Lett. , vol.375 , pp. 129-133
    • Bo, X.N.1    Zhang, Y.2    Nassar, M.3    Burnstock, G.4    Schoepfer, R.5
  • 23
    • 0029671045 scopus 로고    scopus 로고
    • An antagonist-insensitive P2X receptor expressed in epithelia and brain
    • Buell, G.; Lewis, C.; Collo, G.; North, R.A.; Surprenant, A., An antagonist-insensitive P2X receptor expressed in epithelia and brain. EMBO J., 1996, 15, 55-62.
    • (1996) EMBO J. , vol.15 , pp. 55-62
    • Buell, G.1    Lewis, C.2    Collo, G.3    North, R.A.4    Surprenant, A.5
  • 25
    • 0029870327 scopus 로고    scopus 로고
    • Cloning and pharmacological characterization of a fourth P2X receptor subtype widely expressed in brain and peripheral tissues including various endocrine tissues
    • Wang, C.Z.; Namba, N.; Gonoi, T.; Inagaki, N.; Seino, S., Cloning and pharmacological characterization of a fourth P2X receptor subtype widely expressed in brain and peripheral tissues including various endocrine tissues. Biochem. Biophys. Res. Commun., 1996, 220, 196-202.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 196-202
    • Wang, C.Z.1    Namba, N.2    Gonoi, T.3    Inagaki, N.4    Seino, S.5
  • 26
    • 0029670647 scopus 로고    scopus 로고
    • A novel neuronal P 2X ATP receptor ion channel with widespread distribution in the brain
    • Seguela, P.; Haghighi, A.; Soghomonian, J.J.; Cooper, E., A novel neuronal P 2X ATP receptor ion channel with widespread distribution in the brain. J. Neurosci., 1996, 16, 448-455.
    • (1996) J. Neurosci. , vol.16 , pp. 448-455
    • Seguela, P.1    Haghighi, A.2    Soghomonian, J.J.3    Cooper, E.4
  • 27
    • 0029665752 scopus 로고    scopus 로고
    • Cloning of P2X 5 and P2X 6 receptors and the distribution and properties of an extended family of ATP-gated ion channels
    • Collo, G.; North, R.A.; Kawashima, E.; Merlo-Pich, E.; Neidhart, S.; Surprenant, A.; Buell, G., Cloning of P2X 5 and P2X 6 receptors and the distribution and properties of an extended family of ATP-gated ion channels. J. Neurosci., 1996, 16, 2495-2507.
    • (1996) J. Neurosci. , vol.16 , pp. 2495-2507
    • Collo, G.1    North, R.A.2    Kawashima, E.3    Merlo-Pich, E.4    Neidhart, S.5    Surprenant, A.6    Buell, G.7
  • 30
    • 0029665112 scopus 로고    scopus 로고
    • The cytolytic P 2Z receptor for extracellular ATP identified as a P 2X receptor (P2X 7)
    • Surprenant, A.; Rassendren, F.; Kawashima, E.; North, R.A.; Buell, G., The cytolytic P 2Z receptor for extracellular ATP identified as a P 2X receptor (P2X 7). Science, 1996, 272, 735-738.
    • (1996) Science , vol.272 , pp. 735-738
    • Surprenant, A.1    Rassendren, F.2    Kawashima, E.3    North, R.A.4    Buell, G.5
  • 31
    • 0022629214 scopus 로고
    • Extracellular ATP: Effects, sources and fate
    • Gordon, J.L., Extracellular ATP: effects, sources and fate. Biochem. J., 1986, 233, 309-319.
    • (1986) Biochem. J. , vol.233 , pp. 309-319
    • Gordon, J.L.1
  • 32
    • 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(3), 269-272.
    • (2009) Purinergic Signal. , vol.5 , Issue.3 , pp. 269-272
    • Fountain, S.J.1    Burnstock, G.2
  • 33
    • 84861526394 scopus 로고    scopus 로고
    • Molecular and functional properties of P2X receptors-recent progress and persisting challenges
    • Kaczmarek-Hajek, K.; Lorinczi, E.; Hausmann, R.; Nicke, A., Molecular and functional properties of P2X receptors-recent progress and persisting challenges. Purinergic Signal., 2012, 8(3), 375-417.
    • (2012) Purinergic Signal. , vol.8 , Issue.3 , pp. 375-417
    • Kaczmarek-Hajek, K.1    Lorinczi, E.2    Hausmann, R.3    Nicke, A.4
  • 34
    • 34447503350 scopus 로고    scopus 로고
    • An intracellular P2X receptor required for osmoregulation in dictyostelium discoideum
    • Fountain, S.J.; Parkinson, K.; Young, M.T.; Cao, L.; Thompson, C.R.; North, R.A., An intracellular P2X receptor required for osmoregulation in Dictyostelium discoideum. Nature, 2007, 448(7150), 200-203.
    • (2007) Nature , vol.448 , Issue.7150 , 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
  • 35
    • 67649639047 scopus 로고    scopus 로고
    • Signaling at purinergic P2X receptors
    • Surprenant, A.; North, R.A., Signaling at purinergic P2X receptors. Annu. Rev. Physiol., 2009, 71, 333-359.
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 333-359
    • Surprenant, A.1    North, R.A.2
  • 36
    • 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(1), 51-69.
    • (2012) Neuron , vol.76 , Issue.1 , pp. 51-69
    • Khakh, B.S.1    North, R.A.2
  • 37
    • 84869063239 scopus 로고    scopus 로고
    • P2X1 and P2X2 receptors in the central nervous system as possible drug targets
    • Hausmann, R.; Schmalzing, G., P2X1 and P2X2 receptors in the central nervous system as possible drug targets. CNS Neurol. Disord. Drug Targets, 2012, 11(6), 675-686.
    • (2012) CNS Neurol. Disord. Drug Targets , vol.11 , Issue.6 , pp. 675-686
    • Hausmann, R.1    Schmalzing, G.2
  • 38
    • 84875426837 scopus 로고    scopus 로고
    • P2X receptors as drug targets
    • North, R.A.; Jarvis, M.F., P2X receptors as drug targets. Mol. Pharmacol., 2013, 83(4), 759-769.
    • (2013) Mol. Pharmacol. , vol.83 , Issue.4 , pp. 759-769
    • North, R.A.1    Jarvis, M.F.2
  • 39
    • 84856298187 scopus 로고    scopus 로고
    • In pursuit of P2X3 antagonists: Novel therapeutics for chronic pain and afferent sensitization
    • Ford, A.P., In pursuit of P2X3 antagonists: novel therapeutics for chronic pain and afferent sensitization. Purinergic Signal., 2012, 8(Suppl 1), 3-26.
    • (2012) Purinergic Signal. , vol.8 , pp. 3-26
    • Ford, A.P.1
  • 40
    • 84926299764 scopus 로고    scopus 로고
    • Inhibition of ATP-gated P2X3 channels by AF-219: An effective anti-tussive mechanism in chronic cough
    • Abdulqawi, R.; Dockry, R.; Holt, K.; Woodcock, A.; Layton, G.; McCarthy, B.; Ford, A.; Jaclyn, S., Inhibition of ATP-gated P2X3 channels by AF-219: An effective anti-tussive mechanism in chronic cough. Eur. Respir. J., 2013, 42(Suppl.57), 386s.
    • (2013) Eur. Respir. J. , vol.42 , pp. 386s
    • Abdulqawi, R.1    Dockry, R.2    Holt, K.3    Woodcock, A.4    Layton, G.5    McCarthy, B.6    Ford, A.7    Jaclyn, S.8
  • 42
    • 84866105881 scopus 로고    scopus 로고
    • Clinical evaluation of the efficacy of the P2X7 purinergic receptor antagonist AZD9056 on the signs and symptoms of rheumatoid arthritis in patients with active disease despite treatment with methotrexate or sulphasalazine
    • Keystone, E.C.; Wang, M.M.; Layton, M.; Hollis, S.; McInnes, I.B., Clinical evaluation of the efficacy of the P2X7 purinergic receptor antagonist AZD9056 on the signs and symptoms of rheumatoid arthritis in patients with active disease despite treatment with methotrexate or sulphasalazine. Ann. Rheum. Dis., 2012, 71(10), 1630-1635.
    • (2012) Ann. Rheum. Dis. , vol.71 , Issue.10 , pp. 1630-1635
    • Keystone, E.C.1    Wang, M.M.2    Layton, M.3    Hollis, S.4    McInnes, I.B.5
  • 43
    • 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(7), 575-590.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , Issue.7 , pp. 575-590
    • Burnstock, G.1
  • 44
    • 84885103040 scopus 로고    scopus 로고
    • Physiological roles and potential therapeutic applications of the P2X7 receptor in inflammation and pain
    • Alves, L.A.; Bezerra, R.J.; Faria, R.X.; Ferreira, L.G.; da Silva Frutuoso, V., Physiological roles and potential therapeutic applications of the P2X7 receptor in inflammation and pain. Molecules, 2013, 18(9), 10953-10972.
    • (2013) Molecules , vol.18 , Issue.9 , pp. 10953-10972
    • Alves, L.A.1    Bezerra, R.J.2    Faria, R.X.3    Ferreira, L.G.4    Da Silva-Frutuoso, V.5
  • 45
    • 84868248487 scopus 로고    scopus 로고
    • Purines, purinergic receptors, and cancer
    • Di Virgilio, F., Purines, purinergic receptors, and cancer. Cancer Res., 2012, 72(21), 5441-5447.
    • (2012) Cancer Res. , vol.72 , Issue.21 , pp. 5441-5447
    • Di Virgilio, F.1
  • 46
    • 67349094026 scopus 로고    scopus 로고
    • P2X(7): A growthpromoting receptor-implications for cancer
    • Di Virgilio, F.; Ferrari, D.; Adinolfi, E., P2X(7): a growthpromoting receptor-implications for cancer. Purinergic Signal., 2009, 5(2), 251-256.
    • (2009) Purinergic Signal. , vol.5 , Issue.2 , pp. 251-256
    • Di Virgilio, F.1    Ferrari, D.2    Adinolfi, E.3
  • 47
    • 84876509176 scopus 로고    scopus 로고
    • P2X7 receptor function in bone-related cancer
    • Adinolfi, E.; Amoroso, F.; Giuliani, A.L. P2X7 Receptor Function in Bone-Related Cancer. J. Osteoporos., 2012, 2012, 637863.
    • (2012) J. Osteoporos. , vol.2012 , pp. 637863
    • Adinolfi, E.1    Amoroso, F.2    Giuliani, A.L.3
  • 50
    • 0032089620 scopus 로고    scopus 로고
    • P2X 1 and P2X 3 receptors form stable trimers: A novel structural motif of ligand-gated ion channels
    • Nicke, A.; Bäumert, H.G.; Rettinger, J.; Eichele, A.; Lambrecht, G.; Mutschler, E.; Schmalzing, G., P2X 1 and P2X 3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels. EMBO J., 1998, 17, 3016-3028.
    • (1998) EMBO J. , vol.17 , pp. 3016-3028
    • Nicke, A.1    Bäumert, H.G.2    Rettinger, J.3    Eichele, A.4    Lambrecht, G.5    Mutschler, E.6    Schmalzing, G.7
  • 51
    • 0037220541 scopus 로고    scopus 로고
    • Monomeric and dimeric byproducts are the principal functional elements of higher order P2X 1 concatamers
    • Nicke, A.; Rettinger, J.; Schmalzing, G., Monomeric and dimeric byproducts are the principal functional elements of higher order P2X 1 concatamers. Mol. Pharmacol., 2003, 63, 243-252.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 243-252
    • Nicke, A.1    Rettinger, J.2    Schmalzing, G.3
  • 52
    • 4143136452 scopus 로고    scopus 로고
    • Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes
    • Aschrafi, A.; Sadtler, S.; Niculescu, C.; Rettinger, J.; Schmalzing, G. Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes J. Mol. Biol., 2004, 342, 333-343.
    • (2004) J. Mol. Biol. , vol.342 , pp. 333-343
    • Aschrafi, A.1    Sadtler, S.2    Niculescu, C.3    Rettinger, J.4    Schmalzing, G.5
  • 54
    • 0025055702 scopus 로고
    • ATP-activated channels in rat and bullfrog sensory neurons: Concentration dependence and kinetics
    • Bean, B.P., ATP-activated channels in rat and bullfrog sensory neurons: concentration dependence and kinetics. J. Neurosci., 1990, 10(1), 1-10.
    • (1990) J. Neurosci. , vol.10 , Issue.1 , pp. 1-10
    • Bean, B.P.1
  • 55
    • 0030879448 scopus 로고    scopus 로고
    • Baculovirus expression provides direct evidence for heteromeric assembly of P2X 2 and P2X 3 receptors
    • Radford, K.M.; Virginio, C.; Surprenant, A.; North, R.A.; Kawashima, E., Baculovirus expression provides direct evidence for heteromeric assembly of P2X 2 and P2X 3 receptors. J. Neurosci., 1997, 17(17), 6529-6533.
    • (1997) J. Neurosci. , vol.17 , Issue.17 , pp. 6529-6533
    • Radford, K.M.1    Virginio, C.2    Surprenant, A.3    North, R.A.4    Kawashima, E.5
  • 56
    • 0030222204 scopus 로고    scopus 로고
    • Families of ion channels with two hydrophobic segments
    • North, R.A. Families of ion channels with two hydrophobic segments. Curr. Opin. Cell Biol., 1996, 8, 474-483.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 474-483
    • North, R.A.1
  • 57
    • 13344262697 scopus 로고
    • Determination of the subunit stoichiometry of an inwardly rectifying potassium channel
    • Yang, J.; Jan, Y.N.; Jan, L.Y., Determination of the subunit stoichiometry of an inwardly rectifying potassium channel. Neuron, 1995, 15, 1441-1447.
    • (1995) Neuron , vol.15 , pp. 1441-1447
    • Yang, J.1    Jan, Y.N.2    Jan, L.Y.3
  • 58
    • 0032584662 scopus 로고    scopus 로고
    • Tetrameric subunit structure of the native brain inwardly rectifying potassium channel kir 2.2
    • Raab-Graham, K.F.; Vandenberg, C.A. Tetrameric subunit structure of the native brain inwardly rectifying potassium channel Kir 2.2. J. Biol. Chem., 1998, 273(31), 19699-19707.
    • (1998) J. Biol. Chem. , vol.273 , Issue.31 , pp. 19699-19707
    • Raab-Graham, K.F.1    Vandenberg, C.A.2
  • 59
    • 0032518665 scopus 로고    scopus 로고
    • The heterotetrameric architecture of the epithelial sodium channel (ENaC)
    • Firsov, D.; Gautschi, I.; Merillat, A.M.; Rossier, B.C.; Schild, L., The heterotetrameric architecture of the epithelial sodium channel (ENaC). EMBO J., 1998, 17(2), 344-352.
    • (1998) EMBO J. , vol.17 , Issue.2 , pp. 344-352
    • Firsov, D.1    Gautschi, I.2    Merillat, A.M.3    Rossier, B.C.4    Schild, L.5
  • 60
    • 0032478834 scopus 로고    scopus 로고
    • The phe-met-arg-phe-amide-activated sodium channel is a tetramer
    • Coscoy, S.; Lingueglia, E.; Lazdunski, M.; Barbry, P., The Phe-Met-Arg-Phe-amide-activated sodium channel is a tetramer. J. Biol. Chem., 1998, 273(14), 8317-8322.
    • (1998) J. Biol. Chem. , vol.273 , Issue.14 , pp. 8317-8322
    • Coscoy, S.1    Lingueglia, E.2    Lazdunski, M.3    Barbry, P.4
  • 61
    • 0031668776 scopus 로고    scopus 로고
    • ATP binding site of P2X channel proteins: Structural similarities with class II aminoacyl-tRNA synthetases
    • Freist, W.; Verhey, J.F.; Stühmer, W.; Gauss, D.H., ATP binding site of P2X channel proteins: structural similarities with class II aminoacyl-tRNA synthetases. FEBS Lett., 1998, 434(1-2), 61-65.
    • (1998) FEBS Lett. , vol.434 , Issue.1-2 , pp. 61-65
    • Freist, W.1    Verhey, J.F.2    Stühmer, W.3    Gauss, D.H.4
  • 62
    • 0031587406 scopus 로고    scopus 로고
    • Molecular assembly of the extracellular domain of P2X2, an ATP-gated ion channel
    • Kim, M.; Yoo, O.J.; Choe, S., Molecular assembly of the extracellular domain of P2X2, an ATP-gated ion channel. Biochem. Biophys. Res. Commun., 1997, 240(3), 618-622.
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , Issue.3 , pp. 618-622
    • Kim, M.1    Yoo, O.J.2    Choe, S.3
  • 63
    • 0026758059 scopus 로고
    • The adhesion molecule on glia (AMOG/b2) and a1 subunits assemble to functional sodium pumps in xenopus oocytes
    • Schmalzing, G.; Kröner, S.; Schachner, M.; Gloor, S., The adhesion molecule on glia (AMOG/b2) and a1 subunits assemble to functional sodium pumps in Xenopus oocytes. J. Biol. Chem., 1992, 267, 20212-20216.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20212-20216
    • Schmalzing, G.1    Kröner, S.2    Schachner, M.3    Gloor, S.4
  • 64
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H.; von Jagow, G., Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem., 1991, 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 67
    • 0018191759 scopus 로고
    • Effect of pyridoxal phosphate on the DNA binding site of activated hepatic glucocorticoid receptor
    • Cake, M.H.; DiSorbo, D.M.; Litwack, G., Effect of pyridoxal phosphate on the DNA binding site of activated hepatic glucocorticoid receptor. J. Biol. Chem., 1978, 253, 4886-4891.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4886-4891
    • Cake, M.H.1    Disorbo, D.M.2    Litwack, G.3
  • 68
    • 0025646749 scopus 로고
    • Primary structure and functional expression of the alpha-, beta-, gamma-, delta- and epsilon-subunits of the acetylcholine receptor from rat muscle
    • Witzemann, V.; Stein, E.; Barg, B.; Konno, T.; Koenen, M.; Kues, W.; Criado, M.; Hofmann, M.; Sakmann, B., Primary structure and functional expression of the alpha-, beta-, gamma-, delta- and epsilon-subunits of the acetylcholine receptor from rat muscle. Eur. J. Biochem., 1990, 194(2), 437-448.
    • (1990) Eur. J. Biochem. , vol.194 , Issue.2 , pp. 437-448
    • Witzemann, V.1    Stein, E.2    Barg, B.3    Konno, T.4    Koenen, M.5    Kues, W.6    Criado, M.7    Hofmann, M.8    Sakmann, B.9
  • 69
    • 84887007845 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: Insights from torpedo postsynaptic membranes
    • Unwin, N., Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: insights from Torpedo postsynaptic membranes. Q. Rev. Biophys., 2013, 46(4), 283-322.
    • (2013) Q. Rev. Biophys. , vol.46 , Issue.4 , pp. 283-322
    • Unwin, N.1
  • 70
    • 0033041549 scopus 로고    scopus 로고
    • Blue native PAGE as a useful method for the analysis of the assembly of distinct combinations of nicotinic acetylcholine receptor subunits
    • Nicke, A.; Rettinger, J.; Mutschler, E.; Schmalzing, G., Blue native PAGE as a useful method for the analysis of the assembly of distinct combinations of nicotinic acetylcholine receptor subunits. J. Recept. Signal. Transduct. Res., 1999, 19(1-4), 493-507.
    • (1999) J. Recept. Signal. Transduct. Res. , vol.19 , Issue.1-4 , pp. 493-507
    • Nicke, A.1    Rettinger, J.2    Mutschler, E.3    Schmalzing, G.4
  • 74
    • 0344172759 scopus 로고    scopus 로고
    • Molecular determinants of glycine receptor subunit assembly
    • Griffon, N.; Buttner, C.; Nicke, A.; Kuhse, J.; Schmalzing, G.; Betz, H., Molecular determinants of glycine receptor subunit assembly. EMBO J., 1999, 18(17), 4711-4721.
    • (1999) EMBO J. , vol.18 , Issue.17 , pp. 4711-4721
    • Griffon, N.1    Buttner, C.2    Nicke, A.3    Kuhse, J.4    Schmalzing, G.5    Betz, H.6
  • 75
    • 0035900794 scopus 로고    scopus 로고
    • Ubiquitination precedes internalization and proteolytic cleavage of plasma membrane-bound glycine receptors
    • Buttner, C.; Sadtler, S.; Leyendecker, A.; Laube, B.; Griffon, N.; Betz, H.; Schmalzing, G., Ubiquitination precedes internalization and proteolytic cleavage of plasma membrane-bound glycine receptors. J. Biol. Chem., 2001, 276(46), 42978-42985.
    • (2001) J. Biol. Chem. , vol.276 , Issue.46 , pp. 42978-42985
    • Buttner, C.1    Sadtler, S.2    Leyendecker, A.3    Laube, B.4    Griffon, N.5    Betz, H.6    Schmalzing, G.7
  • 76
    • 0037931744 scopus 로고    scopus 로고
    • A basic cluster determines topology of the cytoplasmic M3-M4 loop of the glycine receptor alpha1 subunit
    • Sadtler, S.; Laube, B.; Lashub, A.; Nicke, A.; Betz, H.; Schmalzing, G., A basic cluster determines topology of the cytoplasmic M3-M4 loop of the glycine receptor alpha1 subunit. J. Biol. Chem., 2003, 278(19), 16782-16790.
    • (2003) J. Biol. Chem. , vol.278 , Issue.19 , pp. 16782-16790
    • Sadtler, S.1    Laube, B.2    Lashub, A.3    Nicke, A.4    Betz, H.5    Schmalzing, G.6
  • 77
    • 4544336463 scopus 로고    scopus 로고
    • Assembly of nicotinic alpha7 subunits in xenopus oocytes is partially blocked at the tetramer level
    • Nicke, A.; Thurau, H.; Sadtler, S.; Rettinger, J.; Schmalzing, G., Assembly of nicotinic alpha7 subunits in Xenopus oocytes is partially blocked at the tetramer level. FEBS Lett., 2004, 575(1-3), 52-58.
    • (2004) FEBS Lett. , vol.575 , Issue.1-3 , pp. 52-58
    • Nicke, A.1    Thurau, H.2    Sadtler, S.3    Rettinger, J.4    Schmalzing, G.5
  • 79
    • 34247170892 scopus 로고    scopus 로고
    • Molecular basis of gephyrin clustering at inhibitory synapses: Role of G- and E-domain interactions
    • Saiyed, T.; Paarmann, I.; Schmitt, B.; Haeger, S.; Sola, M.; Schmalzing, G.; Weissenhorn, W.; Betz, H., Molecular basis of gephyrin clustering at inhibitory synapses: role of G- and E-domain interactions. J. Biol. Chem., 2007, 282(8), 5625-5632.
    • (2007) J. Biol. Chem. , vol.282 , Issue.8 , pp. 5625-5632
    • Saiyed, T.1    Paarmann, I.2    Schmitt, B.3    Haeger, S.4    Sola, M.5    Schmalzing, G.6    Weissenhorn, W.7    Betz, H.8
  • 80
    • 0032529842 scopus 로고    scopus 로고
    • Central P2X4 and P2X6 channel subunits coassemble into a novel heteromeric ATP receptor
    • Le, K.T.; Babinski, K.; Seguela, P., Central P2X4 and P2X6 channel subunits coassemble into a novel heteromeric ATP receptor J. Neurosci., 1998, 18(18), 7152-7159.
    • (1998) J. Neurosci. , vol.18 , Issue.18 , pp. 7152-7159
    • Le, K.T.1    Babinski, K.2    Seguela, P.3
  • 81
    • 15444372454 scopus 로고    scopus 로고
    • Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize
    • Barrera, N.P.; Ormond, S.J.; Henderson, R.M.; Murrell-Lagnado, R.D.; Edwardson, J.M., Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize. J. Biol. Chem., 2005, 280(11), 10759-10765.
    • (2005) J. Biol. Chem. , vol.280 , Issue.11 , pp. 10759-10765
    • Barrera, N.P.1    Ormond, S.J.2    Henderson, R.M.3    Murrell-Lagnado, R.D.4    Edwardson, J.M.5
  • 82
    • 33645837836 scopus 로고    scopus 로고
    • An uncharged region within the N terminus of the P2X6 receptor inhibits its assembly and exit from the endoplasmic reticulum
    • Ormond, S.J.; Barrera, N.P.; Qureshi, O.S.; Henderson, R.M.; Edwardson, J.M.; Murrell-Lagnado, R.D., An uncharged region within the N terminus of the P2X6 receptor inhibits its assembly and exit from the endoplasmic reticulum. Mol. Pharmacol., 2006, 69, (5), 1692-1700.
    • (2006) Mol. Pharmacol. , vol.69 , Issue.5 , pp. 1692-1700
    • Ormond, S.J.1    Barrera, N.P.2    Qureshi, O.S.3    Henderson, R.M.4    Edwardson, J.M.5    Murrell-Lagnado, R.D.6
  • 83
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman, I.; Bulleid, N.J., Protein folding and modification in the mammalian endoplasmic reticulum. Annu. Rev. Biochem., 2011, 80, 71-99.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 84
    • 26844438833 scopus 로고    scopus 로고
    • Visualization of the trimeric P2X2 receptor with a crown-capped extracellular domain
    • Mio, K.; Kubo, Y.; Ogura, T.; Yamamoto, T.; Sato, C., Visualization of the trimeric P2X2 receptor with a crown-capped extracellular domain. Biochem. Biophys. Res. Commun., 2005, 337(3), 998-1005.
    • (2005) Biochem. Biophys. Res. Commun. , vol.337 , Issue.3 , pp. 998-1005
    • Mio, K.1    Kubo, Y.2    Ogura, T.3    Yamamoto, T.4    Sato, C.5
  • 85
    • 54449086943 scopus 로고    scopus 로고
    • Molecular shape, architecture, and size of P2X4 receptors determined using fluorescence resonance energy transfer and electron microscopy
    • Young, M.T.; Fisher, J.A.; Fountain, S.J.; Ford, R.C.; North, R.A.; Khakh, B.S., Molecular shape, architecture, and size of P2X4 receptors determined using fluorescence resonance energy transfer and electron microscopy. J. Biol. Chem., 2008, 283(38), 26241-26251.
    • (2008) J. Biol. Chem. , vol.283 , Issue.38 , 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
  • 88
    • 0036451193 scopus 로고    scopus 로고
    • The epithelial sodium channel (ENaC) is intracellularly located as a tetramer
    • Dijkink, L.; Hartog, A.; van Os, C.H.; Bindels, R.J., The epithelial sodium channel (ENaC) is intracellularly located as a tetramer. Pflugers Arch. J., 2002, 444(4), 549-555.
    • (2002) Pflugers Arch. J. , vol.444 , Issue.4 , pp. 549-555
    • Dijkink, L.1    Hartog, A.2    Van Os, C.H.3    Bindels, R.J.4
  • 89
    • 34347218655 scopus 로고    scopus 로고
    • Determination of epithelial Na+ channel subunit stoichiometry from single-channel conductances
    • Anantharam, A.; Palmer, L.G., Determination of epithelial Na+ channel subunit stoichiometry from single-channel conductances. J. Gen. Physiol., 2007, 130(1), 55-70.
    • (2007) J. Gen. Physiol. , vol.130 , Issue.1 , pp. 55-70
    • Anantharam, A.1    Palmer, L.G.2
  • 90
  • 91
    • 80052765537 scopus 로고    scopus 로고
    • Atomic force microscopy reveals the architecture of the epithelial sodium channel (ENaC)
    • Stewart, A.P.; Haerteis, S.; Diakov, A.; Korbmacher, C.; Edwardson, J.M., Atomic force microscopy reveals the architecture of the epithelial sodium channel (ENaC). J. Biol. Chem., 2011, 286(37), 31944-31952.
    • (2011) J. Biol. Chem. , vol.286 , Issue.37 , pp. 31944-31952
    • Stewart, A.P.1    Haerteis, S.2    Diakov, A.3    Korbmacher, C.4    Edwardson, J.M.5
  • 92
    • 34548813656 scopus 로고    scopus 로고
    • Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH
    • Jasti, J.; Furukawa, H.; Gonzales, E.B.; Gouaux, E., Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH. Nature, 2007, 449(7160), 316-323.
    • (2007) Nature , vol.449 , Issue.7160 , pp. 316-323
    • Jasti, J.1    Furukawa, H.2    Gonzales, E.B.3    Gouaux, E.4
  • 93
    • 84878601303 scopus 로고    scopus 로고
    • Unanticipated parallels in architecture and mechanism between ATP-gated P2X receptors and acid sensing ion channels
    • Baconguis, I.; Hattori, M.; Gouaux, E., Unanticipated parallels in architecture and mechanism between ATP-gated P2X receptors and acid sensing ion channels. Curr. Opin. Struct. Biol., 2013, 23(2), 277-284.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , Issue.2 , pp. 277-284
    • Baconguis, I.1    Hattori, M.2    Gouaux, E.3
  • 94
    • 0028224356 scopus 로고
    • A large-conductance mechanosensitive channel in E. Coli encoded by mscL alone
    • Sukharev, S.I.; Blount, P.; Martinac, B.; Blattner, F.R.; Kung, C., A large-conductance mechanosensitive channel in E. coli encoded by mscL alone. Nature, 1994, 368, (6468), 265-268.
    • (1994) Nature , vol.368 , Issue.6468 , pp. 265-268
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Blattner, F.R.4    Kung, C.5
  • 95
    • 0029813032 scopus 로고    scopus 로고
    • Membrane topology and multimeric structure of a mechanosensitive channel protein of escherichia coli
    • Blount, P.; Sukharev, S.I.; Moe, P.C.; Schroeder, M.J.; Guy, H.R.; Kung, C., Membrane topology and multimeric structure of a mechanosensitive channel protein of Escherichia coli EMBO J., 1996, 15(18), 4798-4805.
    • (1996) EMBO J. , vol.15 , Issue.18 , pp. 4798-4805
    • Blount, P.1    Sukharev, S.I.2    Moe, P.C.3    Schroeder, M.J.4    Guy, H.R.5    Kung, C.6
  • 96
    • 0345543722 scopus 로고    scopus 로고
    • A hexameric transmembrane pore revealed by twodimensional crystallization of the large mechanosensitive ion channel (MscL) of escherichia coli
    • Saint, N.; Lacapere, J.J.; Gu, L.Q.; Ghazi, A.; Martinac, B.; Rigaud, J.L., A hexameric transmembrane pore revealed by twodimensional crystallization of the large mechanosensitive ion channel (MscL) of Escherichia coli. J. Biol. Chem., 1998, 273(24), 14667-14670.
    • (1998) J. Biol. Chem. , vol.273 , Issue.24 , pp. 14667-14670
    • Saint, N.1    Lacapere, J.J.2    Gu, L.Q.3    Ghazi, A.4    Martinac, B.5    Rigaud, J.L.6
  • 97
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the mscl homolog from mycobacterium tuberculosis : A gated mechanosensitive ion channel
    • Chang, G.; Spencer, R.H.; Lee, A.T.; Barclay, M.T.; Rees, D.C., Structure of the MscL homolog from Mycobacterium tuberculosis : a gated mechanosensitive ion channel. Science, 1998, 282(5397), 2220-2226.
    • (1998) Science , vol.282 , Issue.5397 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 98
    • 69949160755 scopus 로고    scopus 로고
    • Structure of a tetrameric mscl in an expanded intermediate state
    • Liu, Z.; Gandhi, C.S.; Rees, D.C., Structure of a tetrameric MscL in an expanded intermediate state. Nature, 2009, 461(7260), 120-124.
    • (2009) Nature , vol.461 , Issue.7260 , pp. 120-124
    • Liu, Z.1    Gandhi, C.S.2    Rees, D.C.3
  • 100
    • 0033529694 scopus 로고    scopus 로고
    • Identification of a domain involved in ATP-gated ionotropic receptor subunit assembly
    • Torres, G.E.; Egan, T.M.; Voigt, M.M., Identification of a domain involved in ATP-gated ionotropic receptor subunit assembly. J. Biol. Chem., 1999, 274(32), 22359-22365.
    • (1999) J. Biol. Chem. , vol.274 , Issue.32 , pp. 22359-22365
    • Torres, G.E.1    Egan, T.M.2    Voigt, M.M.3
  • 101
    • 33846021314 scopus 로고    scopus 로고
    • P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate
    • Duckwitz, W.; Hausmann, R.; Aschrafi, A.; Schmalzing, G., P2X5 subunit assembly requires scaffolding by the second transmembrane domain and a conserved aspartate. J. Biol. Chem., 2006, 281(51), 39561-39572.
    • (2006) J. Biol. Chem. , vol.281 , Issue.51 , pp. 39561-39572
    • Duckwitz, W.1    Hausmann, R.2    Aschrafi, A.3    Schmalzing, G.4
  • 102
    • 33845343261 scopus 로고    scopus 로고
    • Membrane-protein topology
    • von Heijne, G., Membrane-protein topology. Nat. Rev. Mol. Cell Biol., 2006, 7(12), 909-918.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , Issue.12 , pp. 909-918
    • Von Heijne, G.1
  • 103
    • 0033525891 scopus 로고    scopus 로고
    • Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners
    • Torres, G.E.; Egan, T.M.; Voigt, M.M., Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners. J. Biol. Chem., 1999, 274(10), 6653-6659.
    • (1999) J. Biol. Chem. , vol.274 , Issue.10 , pp. 6653-6659
    • Torres, G.E.1    Egan, T.M.2    Voigt, M.M.3
  • 104
    • 0030775751 scopus 로고    scopus 로고
    • Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system
    • Le, K.T.; Paquet, M.; Nouel, D.; Babinski, K.; Seguela, P., Primary structure and expression of a naturally truncated human P2X ATP receptor subunit from brain and immune system. FEBS Lett., 1997, 418(1-2), 195-199.
    • (1997) FEBS Lett. , vol.418 , Issue.1-2 , pp. 195-199
    • Le, K.T.1    Paquet, M.2    Nouel, D.3    Babinski, K.4    Seguela, P.5
  • 105
    • 0033983453 scopus 로고    scopus 로고
    • Asparagine-mediated self-association of a model transmembrane helix
    • Choma, C.; Gratkowski, H.; Lear, J.D.; DeGrado, W.F., Asparagine-mediated self-association of a model transmembrane helix. Nat. Struct. Mol. Biol., 2000, 7(2), 161-166.
    • (2000) Nat. Struct. Mol. Biol. , vol.7 , Issue.2 , pp. 161-166
    • Choma, C.1    Gratkowski, H.2    Lear, J.D.3    Degrado, W.F.4
  • 106
    • 0007949690 scopus 로고    scopus 로고
    • Interhelical hydrogen bonding drives strong interactions in membrane proteins
    • Zhou, F.X.; Cocco, M.J.; Russ, W.P.; Brunger, A.T.; Engelman, D.M., Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nat. Struct. Mol. Biol., 2000, 7(2), 154-160.
    • (2000) Nat. Struct. Mol. Biol. , vol.7 , Issue.2 , pp. 154-160
    • Zhou, F.X.1    Cocco, M.J.2    Russ, W.P.3    Brunger, A.T.4    Engelman, D.M.5
  • 107
    • 84877773919 scopus 로고    scopus 로고
    • Influences of membrane mimetic environments on membrane protein structures
    • Zhou, H.X.; Cross, T.A., Influences of membrane mimetic environments on membrane protein structures. Annu. Rev. Biophys., 2013, 42, 361-392.
    • (2013) Annu. Rev. Biophys. , vol.42 , pp. 361-392
    • Zhou, H.X.1    Cross, T.A.2
  • 108
    • 84885767038 scopus 로고    scopus 로고
    • Inter- and intrasubunit interactions between transmembrane helices in the open state of P2X receptor channels
    • Heymann, G.; Dai, J.; Li, M.; Silberberg, S.D.; Zhou, H.X.; Swartz, K.J., Inter- and intrasubunit interactions between transmembrane helices in the open state of P2X receptor channels. Proc. Natl. Acad. Sci. U.S.A., 2013, 110(42), E4045-4054.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , Issue.42 , pp. E4045-4054
    • Heymann, G.1    Dai, J.2    Li, M.3    Silberberg, S.D.4    Zhou, H.X.5    Swartz, K.J.6
  • 109
    • 84881159982 scopus 로고    scopus 로고
    • Functional identification of close proximity amino acid side chains within the transmembrane-spanning helixes of the P2X2 receptor
    • Liang, X.; Xu, H.; Li, C.; Yin, S.; Xu, T.; Liu, J.; Li, Z., Functional identification of close proximity amino acid side chains within the transmembrane-spanning helixes of the P2X2 receptor. PloS One, 2013, 8(8), e70629.
    • (2013) PloS One , vol.8 , Issue.8 , pp. e70629
    • Liang, X.1    Xu, H.2    Li, C.3    Yin, S.4    Xu, T.5    Liu, J.6    Li, Z.7
  • 110
    • 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(5), 961-971.
    • (2010) Br. J. Pharmacol. , vol.161 , Issue.5 , pp. 961-971
    • Evans, R.J.1
  • 111
    • 84871504004 scopus 로고    scopus 로고
    • Moving through the gate in ATPactivated P2X receptors
    • Jiang, R.; Taly, A.; Grutter, T., Moving through the gate in ATPactivated P2X receptors. Trends Biochem. Sci., 2013, 38(1), 20-29.
    • (2013) Trends Biochem. Sci. , vol.38 , Issue.1 , pp. 20-29
    • Jiang, R.1    Taly, A.2    Grutter, T.3
  • 112
    • 77952551628 scopus 로고    scopus 로고
    • New structure enlivens interest in P2X receptors
    • Browne, L.E.; Jiang, L.H.; North, R.A., New structure enlivens interest in P2X receptors. Trends Pharmacol. Sci., 2010, 31(5), 229-237.
    • (2010) Trends Pharmacol. Sci. , vol.31 , Issue.5 , pp. 229-237
    • Browne, L.E.1    Jiang, L.H.2    North, R.A.3
  • 114
    • 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(2), 83-90.
    • (2010) Trends Biochem. Sci. , vol.35 , Issue.2 , pp. 83-90
    • Young, M.T.1
  • 115
    • 60549098817 scopus 로고    scopus 로고
    • Orthosteric and allosteric binding sites of P2X receptors
    • Evans, R.J., Orthosteric and allosteric binding sites of P2X receptors. Eur. Biophys. J., 2009, 38(3), 319-327.
    • (2009) Eur. Biophys. J. , vol.38 , Issue.3 , pp. 319-327
    • Evans, R.J.1
  • 117
    • 0034703055 scopus 로고    scopus 로고
    • The role of positively charged amino acids in ATP recognition by human P2X 1 receptors
    • Ennion, S.; Hagan, S.; Evans, R.J., 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    Hagan, S.2    Evans, R.J.3
  • 118
    • 0034602169 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the ATPbinding site of a purinergic P2X receptor
    • Jiang, L.H.; Rassendren, F.; Surprenant, A.; North, R.A., Identification of amino acid residues contributing to the ATPbinding site of a purinergic P2X receptor. J. Biol. Chem., 2000, 275(44), 34190-34196.
    • (2000) J. Biol. Chem. , vol.275 , Issue.44 , pp. 34190-34196
    • Jiang, L.H.1    Rassendren, F.2    Surprenant, A.3    North, R.A.4
  • 120
    • 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(10), 9043-9055.
    • (2004) J. Biol. Chem. , vol.279 , Issue.10 , pp. 9043-9055
    • Roberts, J.A.1    Evans, R.J.2
  • 121
    • 29144521525 scopus 로고    scopus 로고
    • Contribution of conserved glycine residues to ATP action at human P2X1 receptors: Mutagenesis indicates that the glycine at position 250 is important for channel function
    • Digby, H.R.; Roberts, J.A.; Sutcliffe, M.J.; Evans, R.J., Contribution of conserved glycine residues to ATP action at human P2X1 receptors: mutagenesis indicates that the glycine at position 250 is important for channel function. J. Neurochem., 2005, 95(6), 1746-1754.
    • (2005) J. Neurochem. , vol.95 , Issue.6 , pp. 1746-1754
    • Digby, H.R.1    Roberts, J.A.2    Sutcliffe, M.J.3    Evans, R.J.4
  • 122
    • 15744376891 scopus 로고    scopus 로고
    • Molecular determinants of the agonist binding domain of a P2X receptor channel
    • Yan, Z.; Liang, Z.; Tomic, M.; Obsil, T.; Stojilkovic, S.S., Molecular determinants of the agonist binding domain of a P2X receptor channel. Mol. Pharmacol., 2005, 67(4), 1078-1088.
    • (2005) Mol. Pharmacol. , vol.67 , Issue.4 , pp. 1078-1088
    • Yan, Z.1    Liang, Z.2    Tomic, M.3    Obsil, T.4    Stojilkovic, S.S.5
  • 123
    • 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
    • Yan, Z.; Liang, Z.; Obsil, T.; Stojilkovic, S.S., 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., 2006, 281(43), 32649-32659.
    • (2006) J. Biol. Chem. , vol.281 , Issue.43 , pp. 32649-32659
    • Yan, Z.1    Liang, Z.2    Obsil, T.3    Stojilkovic, S.S.4
  • 124
    • 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(3), 843-852.
    • (2006) J. Neurochem. , vol.96 , Issue.3 , pp. 843-852
    • Roberts, J.A.1    Evans, R.J.2
  • 125
    • 70350339068 scopus 로고    scopus 로고
    • Mammalian P2X7 receptor pharmacology: Comparison of recombinant mouse, rat and human P2X7 receptors
    • Donnelly-Roberts, D.L.; Namovic, M.T.; Han, P.; Jarvis, M.F., Mammalian P2X7 receptor pharmacology: comparison of recombinant mouse, rat and human P2X7 receptors. Br. J. Pharmacol., 2009, 157(7), 1203-1214.
    • (2009) Br. J. Pharmacol. , vol.157 , Issue.7 , pp. 1203-1214
    • Donnelly-Roberts, D.L.1    Namovic, M.T.2    Han, P.3    Jarvis, M.F.4
  • 126
    • 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.; Digby, H.R.; Kara, M.; El, A.S.; Sutcliffe, M.J.; Evans, R.J., 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(29), 20126-20136.
    • (2008) J. Biol. Chem. , vol.283 , Issue.29 , pp. 20126-20136
    • Roberts, J.A.1    Digby, H.R.2    Kara, M.3    El, A.S.4    Sutcliffe, M.J.5    Evans, R.J.6
  • 127
    • 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(15), 4072-4082.
    • (2007) J. Neurosci. , vol.27 , Issue.15 , pp. 4072-4082
    • Roberts, J.A.1    Evans, R.J.2
  • 128
    • 65649133613 scopus 로고    scopus 로고
    • Contribution of the region glu181 to val200 of the extracellular loop of the human P2X1 receptor to agonist binding and gating revealed using cysteine scanning mutagenesis
    • Roberts, J.A.; Valente, M.; Allsopp, R.C.; Watt, D.; Evans, R.J., Contribution of the region Glu181 to Val200 of the extracellular loop of the human P2X1 receptor to agonist binding and gating revealed using cysteine scanning mutagenesis. J. Neurochem., 2009, 109(4), 1042-1052.
    • (2009) J. Neurochem. , vol.109 , Issue.4 , pp. 1042-1052
    • Roberts, J.A.1    Valente, M.2    Allsopp, R.C.3    Watt, D.4    Evans, R.J.5
  • 129
    • 33748944331 scopus 로고    scopus 로고
    • Role of ectodomain lysines in the subunits of the heteromeric P2X2/3 receptor
    • Wilkinson, W.J.; Jiang, L.H.; Surprenant, A.; North, R.A., Role of ectodomain lysines in the subunits of the heteromeric P2X2/3 receptor. Mol. Pharmacol., 2006, 70(4), 1159-1163.
    • (2006) Mol. Pharmacol. , vol.70 , Issue.4 , pp. 1159-1163
    • Wilkinson, W.J.1    Jiang, L.H.2    Surprenant, A.3    North, R.A.4
  • 130
    • 33845891326 scopus 로고    scopus 로고
    • Amino acid residues in the P2X7 receptor that mediate differential sensitivity to ATP and BzATP
    • Young, M.T.; Pelegrin, P.; Surprenant, A., Amino acid residues in the P2X7 receptor that mediate differential sensitivity to ATP and BzATP. Mol. Pharmacol., 2007, 71(1), 92-100.
    • (2007) Mol. Pharmacol. , vol.71 , Issue.1 , pp. 92-100
    • Young, M.T.1    Pelegrin, P.2    Surprenant, A.3
  • 131
    • 35348913169 scopus 로고    scopus 로고
    • Conserved lysin and arginin residues in the extracellular loop of P2X(3) receptors are involved in agonist binding
    • Fischer, W.; Zadori, Z.; Kullnick, Y.; Groger-Arndt, H.; Franke, H.; Wirkner, K.; Illes, P.; Mager, P.P., Conserved lysin and arginin residues in the extracellular loop of P2X(3) receptors are involved in agonist binding. Eur. J. Pharmacol., 2007, 576(1-3), 7-17.
    • (2007) Eur. J. Pharmacol. , vol.576 , Issue.1-3 , pp. 7-17
    • Fischer, W.1    Zadori, Z.2    Kullnick, Y.3    Groger-Arndt, H.4    Franke, H.5    Wirkner, K.6    Illes, P.7    Mager, P.P.8
  • 132
    • 34547423310 scopus 로고    scopus 로고
    • Role of aromatic and charged ectodomain residues in the P2X(4) receptor functions
    • Zemkova, H.; Yan, Z.; Liang, Z.; Jelinkova, I.; Tomic, M.; Stojilkovic, S.S., Role of aromatic and charged ectodomain residues in the P2X(4) receptor functions. J. Neurochem., 2007, 102(4), 1139-1150.
    • (2007) J. Neurochem. , vol.102 , Issue.4 , pp. 1139-1150
    • Zemkova, H.1    Yan, Z.2    Liang, Z.3    Jelinkova, I.4    Tomic, M.5    Stojilkovic, S.S.6
  • 133
    • 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.; Rettinger, J.; Bhargava, Y.; Eisele, T.; Nicke, A., 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(6), 1456-1466.
    • (2007) J. Neurosci. , vol.27 , Issue.6 , pp. 1456-1466
    • Marquez-Klaka, B.1    Rettinger, J.2    Bhargava, Y.3    Eisele, T.4    Nicke, A.5
  • 135
    • 80051696222 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis (residues E52-G96) of the human P2X1 receptor for ATP; mapping agonist binding and channel gating
    • Allsopp, R.C.; El, A.S.; Schmid, R.; Evans, R.J., Cysteine scanning mutagenesis (residues E52-G96) 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    El, A.S.2    Schmid, R.3    Evans, R.J.4
  • 137
    • 84871485564 scopus 로고    scopus 로고
    • Intermediate closed channel state(s) precede(s) activation in the ATP-gated P2X2 receptor
    • Jiang, R.; Taly, A.; Lemoine, D.; Martz, A.; Specht, A.; Grutter, T., Intermediate closed channel state(s) precede(s) activation in the ATP-gated P2X2 receptor. Channels, 2012, 6(5), 398-402.
    • (2012) Channels , vol.6 , Issue.5 , pp. 398-402
    • Jiang, R.1    Taly, A.2    Lemoine, D.3    Martz, A.4    Specht, A.5    Grutter, T.6
  • 138
    • 84882668864 scopus 로고    scopus 로고
    • Validation of alexa-647-ATP as a powerful tool to study P2X receptor ligand binding and desensitization
    • Bhargava, Y.; Nicke, A.; Rettinger, J., Validation of Alexa-647-ATP as a powerful tool to study P2X receptor ligand binding and desensitization. Biochem. Biophys. Res. Commun., 2013, 438(2), 295-300.
    • (2013) Biochem. Biophys. Res. Commun. , vol.438 , Issue.2 , pp. 295-300
    • Bhargava, Y.1    Nicke, A.2    Rettinger, J.3
  • 139
    • 84868124518 scopus 로고    scopus 로고
    • Covalent modification of mutant rat P2X2 receptors with a thiol-reactive fluorophore allows channel activation by zinc or acidic pH without ATP
    • Dellal, S.S.; Hume, R.I., Covalent modification of mutant rat P2X2 receptors with a thiol-reactive fluorophore allows channel activation by zinc or acidic pH without ATP. PloS One, 2012, 7(10), e47147.
    • (2012) PloS One , vol.7 , Issue.10 , pp. e47147
    • Dellal, S.S.1    Hume, R.I.2
  • 140
  • 141
    • 84902355195 scopus 로고    scopus 로고
    • Inherent dynamics of head domain correlates with ATP-recognition of P2X4 receptors: Insights gained from molecular simulations
    • Huang, L.D.; Fan, Y.Z.; Tian, Y.; Yang, Y.; Liu, Y.; Wang, J.; Zhao, W.S.; Zhou, W.C.; Cheng, X.Y.; Cao, P.; Lu, X.Y.; Yu, Y., Inherent dynamics of head domain correlates with ATP-recognition of P2X4 receptors: insights gained from molecular simulations. PloS One, 2014, 9(5), e97528.
    • (2014) PloS One , vol.9 , Issue.5 , pp. e97528
    • Huang, L.D.1    Fan, Y.Z.2    Tian, Y.3    Yang, Y.4    Liu, Y.5    Wang, J.6    Zhao, W.S.7    Zhou, W.C.8    Cheng, X.Y.9    Cao, P.10    Lu, X.Y.11    Yu, Y.12
  • 143
    • 0032940264 scopus 로고    scopus 로고
    • Single channel properties of P2X 2 purinoceptors
    • Ding, S.; Sachs, F., Single channel properties of P2X 2 purinoceptors. J. Gen. Physiol., 1999, 113(5), 695-720.
    • (1999) J. Gen. Physiol. , vol.113 , Issue.5 , pp. 695-720
    • Ding, S.1    Sachs, F.2
  • 144
    • 0030768931 scopus 로고    scopus 로고
    • The hill equation revisited: Uses and misuses
    • Weiss, J.N., The Hill equation revisited: uses and misuses. FASEB J., 1997, 11(11), 835-841.
    • (1997) FASEB J. , vol.11 , Issue.11 , pp. 835-841
    • Weiss, J.N.1
  • 146
    • 84866862218 scopus 로고    scopus 로고
    • Activation of trimeric P2X2 receptors by fewer than three ATP molecules
    • Stelmashenko, O.; Lalo, U.; Yang, Y.; Bragg, L.; North, R.A.; Compan, V., Activation of trimeric P2X2 receptors by fewer than three ATP molecules. Mol. Pharmacol., 2012, 82(4), 760-766.
    • (2012) Mol. Pharmacol. , vol.82 , Issue.4 , pp. 760-766
    • Stelmashenko, O.1    Lalo, U.2    Yang, Y.3    Bragg, L.4    North, R.A.5    Compan, V.6
  • 147
    • 77958530854 scopus 로고    scopus 로고
    • Experimental characterization and mathematical modeling of P2X7 receptor channel gating
    • Yan, Z.; Khadra, A.; Li, S.; Tomic, M.; Sherman, A.; Stojilkovic, S.S., Experimental characterization and mathematical modeling of P2X7 receptor channel gating. J. Neurosci., 2010, 30(42), 14213-14224.
    • (2010) J. Neurosci. , vol.30 , Issue.42 , pp. 14213-14224
    • Yan, Z.1    Khadra, A.2    Li, S.3    Tomic, M.4    Sherman, A.5    Stojilkovic, S.S.6
  • 148
    • 37349124729 scopus 로고    scopus 로고
    • The unusual statedependent affinity of P2X3 receptors can be explained by an allosteric two-open-state model
    • Karoly, R.; Mike, A.; Illes, P.; Gerevich, Z., The unusual statedependent affinity of P2X3 receptors can be explained by an allosteric two-open-state model. Mol. Pharmacol., 2008, 73(1), 224-234.
    • (2008) Mol. Pharmacol. , vol.73 , Issue.1 , pp. 224-234
    • Karoly, R.1    Mike, A.2    Illes, P.3    Gerevich, Z.4
  • 149
    • 84861125237 scopus 로고    scopus 로고
    • Gating properties of the P2X2a and P2X2b receptor channels: Experiments and mathematical modeling
    • Khadra, A.; Yan, Z.; Coddou, C.; Tomic, M.; Sherman, A.; Stojilkovic, S.S., Gating properties of the P2X2a and P2X2b receptor channels: experiments and mathematical modeling. J. Gen. Physiol., 2012, 139(5), 333-348.
    • (2012) J. Gen. Physiol. , vol.139 , Issue.5 , pp. 333-348
    • Khadra, A.1    Yan, Z.2    Coddou, C.3    Tomic, M.4    Sherman, A.5    Stojilkovic, S.S.6
  • 150
    • 84883666686 scopus 로고    scopus 로고
    • P2X receptor intermediate activation states have altered nucleotide selectivity
    • Browne, L.E.; North, R.A., P2X receptor intermediate activation states have altered nucleotide selectivity. J. Neurosci., 2013, 33(37), 14801-14808.
    • (2013) J. Neurosci. , vol.33 , Issue.37 , pp. 14801-14808
    • Browne, L.E.1    North, R.A.2
  • 151
    • 84867763158 scopus 로고    scopus 로고
    • Allosteric nature of P2X receptor activation probed by photoaffinity labelling
    • Bhargava, Y.; Rettinger, J.; Mourot, A., Allosteric nature of P2X receptor activation probed by photoaffinity labelling. Br. J. Pharmacol., 2012, 167(6), 1301-1310.
    • (2012) Br. J. Pharmacol. , vol.167 , Issue.6 , pp. 1301-1310
    • Bhargava, Y.1    Rettinger, J.2    Mourot, A.3
  • 152
    • 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(2), 183-201.
    • (2007) J. Gen. Physiol. , vol.130 , Issue.2 , pp. 183-201
    • Moffatt, L.1    Hume, R.I.2
  • 153
    • 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.; Ray, D.; Allsopp, R.C.; Evans, R.J., 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., 2011, 165, 390-400.
    • (2011) Br. J. Pharmacol. , vol.165 , pp. 390-400
    • El-Ajouz, S.1    Ray, D.2    Allsopp, R.C.3    Evans, R.J.4
  • 154
    • 13844294341 scopus 로고    scopus 로고
    • Profiling at recombinant homomeric and heteromeric rat P2X receptors identifies the suramin analogue NF449 as a highly potent P2X1 receptor antagonist
    • Rettinger, J.; Braun, K.; Hochmann, H.; Kassack, M.U.; Ullmann, H.; Nickel, P.; Schmalzing, G.; Lambrecht, G., Profiling at recombinant homomeric and heteromeric rat P2X receptors identifies the suramin analogue NF449 as a highly potent P2X1 receptor antagonist. Neuropharmacology, 2005, 48(3), 461-468.
    • (2005) Neuropharmacology , vol.48 , Issue.3 , pp. 461-468
    • Rettinger, J.1    Braun, K.2    Hochmann, H.3    Kassack, M.U.4    Ullmann, H.5    Nickel, P.6    Schmalzing, G.7    Lambrecht, G.8
  • 155
    • 33745146902 scopus 로고    scopus 로고
    • The suramin analog 4,4′,4",4"′-(carbonylbis(imino-5,1,3-benzenetriylbis (carbonylimino)))tetra-kis-benzenesulfonic acid (NF110) potently blocks P2X3 receptors: Subtype selectivity is determined by location of sulfonic acid groups
    • Hausmann, R.; Rettinger, J.; Gerevich, Z.; Meis, S.; Kassack, M.U.; Illes, P.; Lambrecht, G.; Schmalzing, G., The suramin analog 4,4′,4",4"′-(carbonylbis(imino-5,1,3-benzenetriylbis (carbonylimino)))tetra-kis-benzenesulfonic acid (NF110) potently blocks P2X3 receptors: subtype selectivity is determined by location of sulfonic acid groups. Mol. Pharmacol., 2006, 69(6), 2058-2067.
    • (2006) Mol. Pharmacol. , vol.69 , Issue.6 , pp. 2058-2067
    • Hausmann, R.1    Rettinger, J.2    Gerevich, Z.3    Meis, S.4    Kassack, M.U.5    Illes, P.6    Lambrecht, G.7    Schmalzing, G.8
  • 157
    • 73949115258 scopus 로고    scopus 로고
    • NF546 [4,4′- (carbonylbis(imino-3,1-phenylene-carbonylimino-3,1-(4-methylphenylene)- car bonylimino))-bis(1,3-xylene-alpha,alpha′- diphosphonic acid) tetrasodium salt] is a non-nucleotide P2Y11 agonist and stimulates release of interleukin-8 from human monocyte-derived dendritic cells
    • Meis, S.; Hamacher, A.; Hongwiset, D.; Marzian, C.; Wiese, M.; Eckstein, N.; Royer, H.D.; Communi, D.; Boeynaems, J.M.; Hausmann, R.; Schmalzing, G.; Kassack, M.U., NF546 [4,4′- (carbonylbis(imino-3,1-phenylene-carbonylimino-3,1-(4-methylphenylene)- car bonylimino))-bis(1,3-xylene-alpha,alpha′- diphosphonic acid) tetrasodium salt] is a non-nucleotide P2Y11 agonist and stimulates release of interleukin-8 from human monocyte-derived dendritic cells. J. Pharmacol. Exp. Ther., 2010, 332(1), 238-247.
    • (2010) J. Pharmacol. Exp. Ther. , vol.332 , Issue.1 , pp. 238-247
    • Meis, S.1    Hamacher, A.2    Hongwiset, D.3    Marzian, C.4    Wiese, M.5    Eckstein, N.6    Royer, H.D.7    Communi, D.8    Boeynaems, J.M.9    Hausmann, R.10    Schmalzing, G.11    Kassack, M.U.12
  • 158
    • 57649178304 scopus 로고    scopus 로고
    • Ectodomain lysines and suramin block of P2X1 receptors
    • Sim, J.A.; Broomhead, H.E.; North, R.A., Ectodomain lysines and suramin block of P2X1 receptors. J. Biol. Chem., 2008, 283(44), 29841-29846.
    • (2008) J. Biol. Chem. , vol.283 , Issue.44 , pp. 29841-29846
    • Sim, J.A.1    Broomhead, H.E.2    North, R.A.3
  • 159
    • 79851471254 scopus 로고    scopus 로고
    • Discovery of potent competitive antagonists and positive modulators of the P2X2 receptor
    • Baqi, Y.; Hausmann, R.; Rosefort, C.; Rettinger, J.; Schmalzing, G.; Muller, C.E., Discovery of potent competitive antagonists and positive modulators of the P2X2 receptor. J. Med. Chem., 2011, 54(3), 817-830.
    • (2011) J. Med. Chem. , vol.54 , Issue.3 , pp. 817-830
    • Baqi, Y.1    Hausmann, R.2    Rosefort, C.3    Rettinger, J.4    Schmalzing, G.5    Muller, C.E.6
  • 161
    • 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.; Young, M.T.; Broomhead, H.E.; Fountain, S.J.; North, R.A., 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(47), 12916-12923.
    • (2007) J. Neurosci. , vol.27 , Issue.47 , pp. 12916-12923
    • Cao, L.1    Young, M.T.2    Broomhead, H.E.3    Fountain, S.J.4    North, R.A.5
  • 162
    • 84862668708 scopus 로고    scopus 로고
    • High potency zinc modulation of human P2X2 receptors and low potency zinc modulation of rat P2X2 receptors share a common molecular mechanism
    • Punthambaker, S.; Blum, J.A.; Hume, R.I., High potency zinc modulation of human P2X2 receptors and low potency zinc modulation of rat P2X2 receptors share a common molecular mechanism. J. Biol. Chem., 2012, 287(26), 22099-22111.
    • (2012) J. Biol. Chem. , vol.287 , Issue.26 , pp. 22099-22111
    • Punthambaker, S.1    Blum, J.A.2    Hume, R.I.3
  • 163
    • 39749177079 scopus 로고    scopus 로고
    • Trace metals in the brain: Allosteric modulators of ligand-gated receptor channels, the case of ATP-gated P2X receptors
    • Huidobro-Toro, J.P.; Lorca, R.A.; Coddou, C., Trace metals in the brain: allosteric modulators of ligand-gated receptor channels, the case of ATP-gated P2X receptors. Eur. Biophys. J., 2008, 37(3), 301-314.
    • (2008) Eur. Biophys. J. , vol.37 , Issue.3 , pp. 301-314
    • Huidobro-Toro, J.P.1    Lorca, R.A.2    Coddou, C.3
  • 164
    • 22544478846 scopus 로고    scopus 로고
    • An intersubunit zinc binding site in rat P2X2 receptors
    • Nagaya, N.; Tittle, R.K.; Saar, N.; Dellal, S.S.; Hume, R.I., An intersubunit zinc binding site in rat P2X2 receptors. J. Biol. Chem., 2005, 280(28), 25982-25993.
    • (2005) J. Biol. Chem. , vol.280 , Issue.28 , pp. 25982-25993
    • Nagaya, N.1    Tittle, R.K.2    Saar, N.3    Dellal, S.S.4    Hume, R.I.5
  • 165
    • 56149101801 scopus 로고    scopus 로고
    • Opposite effects of zinc on human and rat P2X2 receptors
    • Tittle, R.K.; Hume, R.I., Opposite effects of zinc on human and rat P2X2 receptors. J. Neurosci., 2008, 28(44), 11131-11140.
    • (2008) J. Neurosci. , vol.28 , Issue.44 , pp. 11131-11140
    • Tittle, R.K.1    Hume, R.I.2
  • 166
    • 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.; Rassendren, F.; Spelta, V.; Surprenant, A.; North, R.A., Amino acid residues involved in gating identified in the first membrane-spanning domain of the rat P2X(2) receptor. J. Biol. Chem., 2001, 276(18), 14902-14908.
    • (2001) J. Biol. Chem. , vol.276 , Issue.18 , pp. 14902-14908
    • Jiang, L.H.1    Rassendren, F.2    Spelta, V.3    Surprenant, A.4    North, R.A.5
  • 167
    • 60549095934 scopus 로고    scopus 로고
    • Inter-subunit disulfide cross-linking in homomeric and heteromeric P2X receptors
    • Marquez-Klaka, B.; Rettinger, J.; Nicke, A., Inter-subunit disulfide cross-linking in homomeric and heteromeric P2X receptors. Eur. Biophys. J., 2009, 38(3), 329-338.
    • (2009) Eur. Biophys. J. , vol.38 , Issue.3 , pp. 329-338
    • Marquez-Klaka, B.1    Rettinger, J.2    Nicke, A.3
  • 168
    • 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.; Martz, A.; Gonin, S.; Taly, A.; de Carvalho, L.P.; Grutter, T., 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(21), 15805-15815.
    • (2010) J. Biol. Chem. , vol.285 , Issue.21 , pp. 15805-15815
    • Jiang, R.1    Martz, A.2    Gonin, S.3    Taly, A.4    De Carvalho, L.P.5    Grutter, T.6
  • 169
    • 84898063955 scopus 로고    scopus 로고
    • Ectodomain movements of an ATP-gated ion channel (P2X2 receptor) probed by disulfide locking
    • Stelmashenko, O.; Compan, V.; Browne, L.E.; North, R.A., Ectodomain movements of an ATP-gated ion channel (P2X2 receptor) probed by disulfide locking. J. Biol. Chem., 2014, 289(14), 9909-9917.
    • (2014) J. Biol. Chem. , vol.289 , Issue.14 , pp. 9909-9917
    • Stelmashenko, O.1    Compan, V.2    Browne, L.E.3    North, R.A.4
  • 172
    • 84891934512 scopus 로고    scopus 로고
    • Direct gating of ATP-activated ion channels (P2X2 receptors) by lipophilic attachment at the outer end of the second transmembrane domain
    • Rothwell, S.W.; Stansfeld, P.J.; Bragg, L.; Verkhratsky, A.; North, R.A., Direct gating of ATP-activated ion channels (P2X2 receptors) by lipophilic attachment at the outer end of the second transmembrane domain. J. Biol. Chem., 2014, 289(2), 618-626.
    • (2014) J. Biol. Chem. , vol.289 , Issue.2 , pp. 618-626
    • Rothwell, S.W.1    Stansfeld, P.J.2    Bragg, L.3    Verkhratsky, A.4    North, R.A.5
  • 173
    • 0035882361 scopus 로고    scopus 로고
    • On the contribution of the first transmembrane domain to wholecell current through an ATP-gated ionotropic P2X receptor
    • Haines, W.R.; Voigt, M.M.; Migita, K.; Torres, G.E.; Egan, T.M., On the contribution of the first transmembrane domain to wholecell current through an ATP-gated ionotropic P2X receptor. J. Neurosci., 2001, 21(16), 5885-5892.
    • (2001) J. Neurosci. , vol.21 , Issue.16 , pp. 5885-5892
    • Haines, W.R.1    Voigt, M.M.2    Migita, K.3    Torres, G.E.4    Egan, T.M.5
  • 174
    • 7244261780 scopus 로고    scopus 로고
    • Gain and loss of channel function by alanine substitutions in the transmembrane segments of the rat ATP-gated P2X2 receptor
    • Li, Z.; Migita, K.; Samways, D.S.; Voigt, M.M.; Egan, T.M., Gain and loss of channel function by alanine substitutions in the transmembrane segments of the rat ATP-gated P2X2 receptor. J. Neurosci., 2004, 24(33), 7378-7386.
    • (2004) J. Neurosci. , vol.24 , Issue.33 , pp. 7378-7386
    • Li, Z.1    Migita, K.2    Samways, D.S.3    Voigt, M.M.4    Egan, T.M.5
  • 175
    • 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(3), 245-256.
    • (2007) J. Gen. Physiol. , vol.129 , Issue.3 , pp. 245-256
    • Samways, D.S.1    Egan, T.M.2
  • 176
    • 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.; Migita, K.; Li, Z.; Egan, T.M., On the role of the first transmembrane domain in cation permeability and flux of the ATP-gated P2X2 receptor. J. Biol. Chem., 2008, 283(8), 5110-5117.
    • (2008) J. Biol. Chem. , vol.283 , Issue.8 , pp. 5110-5117
    • Samways, D.S.1    Migita, K.2    Li, Z.3    Egan, T.M.4
  • 178
    • 17044400916 scopus 로고    scopus 로고
    • Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels
    • Silberberg, S.D.; Chang, T.H.; Swartz, K.J., Secondary structure and gating rearrangements of transmembrane segments in rat P2X4 receptor channels. J. Gen. Physiol., 2005, 125(4), 347-359.
    • (2005) J. Gen. Physiol. , vol.125 , Issue.4 , pp. 347-359
    • Silberberg, S.D.1    Chang, T.H.2    Swartz, K.J.3
  • 179
    • 0030962404 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the pore of a P2X receptor
    • Rassendren, F.; Buell, G.; Newbolt, A.; North, R.A.; Surprenant, A., 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    Buell, G.2    Newbolt, A.3    North, R.A.4    Surprenant, A.5
  • 180
    • 0032053981 scopus 로고    scopus 로고
    • A domain contributing to the ion channel of ATP-gated P2X 2 receptors identified by the substituted cysteine accessibility method
    • Egan, T.M.; Haines, W.R.; Voigt, M.M., A domain contributing to the ion channel of ATP-gated P2X 2 receptors identified by the substituted cysteine accessibility method. J. Neurosci.,1998, 18(7), 2350-2359.
    • (1998) J. Neurosci. , vol.18 , Issue.7 , pp. 2350-2359
    • Egan, T.M.1    Haines, W.R.2    Voigt, M.M.3
  • 181
    • 0035903169 scopus 로고    scopus 로고
    • Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor
    • Migita, K.; Haines, W.R.; Voigt, M.M.; Egan, T.M., Polar residues of the second transmembrane domain influence cation permeability of the ATP-gated P2X(2) receptor. J. Biol. Chem., 2001, 276(33), 30934-30941.
    • (2001) J. Biol. Chem. , vol.276 , Issue.33 , pp. 30934-30941
    • Migita, K.1    Haines, W.R.2    Voigt, M.M.3    Egan, T.M.4
  • 182
    • 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(13), 3413-3420.
    • (2004) J. Neurosci. , vol.24 , Issue.13 , pp. 3413-3420
    • Egan, T.M.1    Khakh, B.S.2
  • 183
    • 79953157461 scopus 로고    scopus 로고
    • Residues 155 and 348 contribute to the determination of P2X7 receptor function via distinct mechanisms revealed by single-nucleotide polymorphisms
    • Bradley, H.J.; Baldwin, J.M.; Goli, G.R.; Johnson, B.; Zou, J.; Sivaprasadarao, A.; Baldwin, S.A.; Jiang, L.H., Residues 155 and 348 contribute to the determination of P2X7 receptor function via distinct mechanisms revealed by single-nucleotide polymorphisms. J. Biol. Chem., 2011, 286(10), 8176-8187.
    • (2011) J. Biol. Chem. , vol.286 , Issue.10 , pp. 8176-8187
    • Bradley, H.J.1    Baldwin, J.M.2    Goli, G.R.3    Johnson, B.4    Zou, J.5    Sivaprasadarao, A.6    Baldwin, S.A.7    Jiang, L.H.8
  • 184
    • 47249090581 scopus 로고    scopus 로고
    • Permeation properties of a P2X receptor in the green algae ostreococcus tauri
    • Fountain, S.J.; Cao, L.; Young, M.T.; North, R.A., Permeation properties of a P2X receptor in the green algae Ostreococcus tauri. J. Biol. Chem., 2008, 283(22), 15122-15126.
    • (2008) J. Biol. Chem. , vol.283 , Issue.22 , pp. 15122-15126
    • Fountain, S.J.1    Cao, L.2    Young, M.T.3    North, R.A.4
  • 185
    • 84874195644 scopus 로고    scopus 로고
    • P2X7 receptor channels allow direct permeation of nanometer-sized dyes
    • Browne, L.E.; Compan, V.; Bragg, L.; North, R.A., P2X7 receptor channels allow direct permeation of nanometer-sized dyes. J. Neurosci., 2013, 33(8), 3557-3566.
    • (2013) J. Neurosci. , vol.33 , Issue.8 , pp. 3557-3566
    • Browne, L.E.1    Compan, V.2    Bragg, L.3    North, R.A.4
  • 186
    • 77951213527 scopus 로고    scopus 로고
    • Gated access to the pore of a P2X receptor: Structural implications for closedopen transitions
    • Kracun, S.; Chaptal, V.; Abramson, J.; Khakh, B.S., Gated access to the pore of a P2X receptor: Structural implications for closedopen transitions. J. Biol. Chem., 2010, 285, 10110-10121.
    • (2010) J. Biol. Chem. , vol.285 , pp. 10110-10121
    • Kracun, S.1    Chaptal, V.2    Abramson, J.3    Khakh, B.S.4
  • 187
    • 84893635581 scopus 로고    scopus 로고
    • Principles and properties of ion flow in P2X receptors
    • Samways, D.S.; Li, Z.; Egan, T.M., Principles and properties of ion flow in P2X receptors. Front. Cell. Neurosci., 2014, 8, 6.
    • (2014) Front. Cell. Neurosci. , vol.8 , pp. 6
    • Samways, D.S.1    Li, Z.2    Egan, T.M.3
  • 188
    • 78650677994 scopus 로고    scopus 로고
    • P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance
    • Browne, L.E.; Cao, L.; Broomhead, H.E.; Bragg, L.; Wilkinson, W.J.; North, R.A., P2X receptor channels show threefold symmetry in ionic charge selectivity and unitary conductance. Nat. Neurosci., 2011, 14(1), 17-18.
    • (2011) Nat. Neurosci. , vol.14 , Issue.1 , pp. 17-18
    • Browne, L.E.1    Cao, L.2    Broomhead, H.E.3    Bragg, L.4    Wilkinson, W.J.5    North, R.A.6
  • 189
    • 84893192449 scopus 로고    scopus 로고
    • Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating
    • Rokic, M.B.; Stojilkovic, S.S.; Zemkova, H., Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating. Front. Cell. Neurosci., 2014, 8, 3.
    • (2014) Front. Cell. Neurosci. , vol.8 , pp. 3
    • Rokic, M.B.1    Stojilkovic, S.S.2    Zemkova, H.3
  • 190
    • 84857718067 scopus 로고    scopus 로고
    • Allosteric modulation of Ca2+ flux in ligand-gated cation channel (P2X4) by actions on lateral portals
    • Samways, D.S.; Khakh, B.S.; Egan, T.M., Allosteric Modulation of Ca2+ flux in Ligand-gated Cation Channel (P2X4) by Actions on Lateral Portals. J. Biol. Chem., 2012, 287(10), 7594-7602.
    • (2012) J. Biol. Chem. , vol.287 , Issue.10 , pp. 7594-7602
    • Samways, D.S.1    Khakh, B.S.2    Egan, T.M.3
  • 191
    • 84875345806 scopus 로고    scopus 로고
    • Multiple roles of the extracellular vestibule amino acid residues in the function of the rat P2X4 receptor
    • Rokic, M.B.; Stojilkovic, S.S.; Vavra, V.; Kuzyk, P.; Tvrdonova, V.; Zemkova, H., Multiple roles of the extracellular vestibule amino acid residues in the function of the rat P2X4 receptor. PloS One, 2013, 8(3), e59411.
    • (2013) PloS One , vol.8 , Issue.3 , pp. e59411
    • Rokic, M.B.1    Stojilkovic, S.S.2    Vavra, V.3    Kuzyk, P.4    Tvrdonova, V.5    Zemkova, H.6
  • 192
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • North, R.A., Molecular physiology of P2X receptors. Physiol. Rev., 2002, 82(4), 1013-1067.
    • (2002) Physiol. Rev. , vol.82 , Issue.4 , pp. 1013-1067
    • North, R.A.1
  • 196
    • 0033621352 scopus 로고    scopus 로고
    • Contributions of the C-terminal domain to the control of P2X receptor desensitization
    • Koshimizu, T.; Koshimizu, M.; Stojilkovic, S.S., Contributions of the C-terminal domain to the control of P2X receptor desensitization. J. Biol. Chem., 1999, 274(53), 37651-37657.
    • (1999) J. Biol. Chem. , vol.274 , Issue.53 , pp. 37651-37657
    • Koshimizu, T.1    Koshimizu, M.2    Stojilkovic, S.S.3
  • 197
    • 0032557429 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to desensitization of the P2X2 receptor channel
    • Koshimizu, T.; Tomic, M.; Koshimizu, M.; Stojilkovic, S.S., Identification of amino acid residues contributing to desensitization of the P2X2 receptor channel. J. Biol. Chem., 1998, 273(21), 12853-12857.
    • (1998) J. Biol. Chem. , vol.273 , Issue.21 , pp. 12853-12857
    • Koshimizu, T.1    Tomic, M.2    Koshimizu, M.3    Stojilkovic, S.S.4
  • 198
    • 0032230275 scopus 로고    scopus 로고
    • Functional role of alternative splicing in pituitary P2X2 receptorchannel activation and desensitization
    • Koshimizu, T.; Tomic, M.; Van Goor, F.; Stojilkovic, S.S., Functional role of alternative splicing in pituitary P2X2 receptorchannel activation and desensitization. Mol. Endocrinol., 1998, 12(7), 901-913.
    • (1998) Mol. Endocrinol. , vol.12 , Issue.7 , pp. 901-913
    • Koshimizu, T.1    Tomic, M.2    Van Goor, F.3    Stojilkovic, S.S.4
  • 199
    • 33744960879 scopus 로고    scopus 로고
    • A C-terminal lysine that controls human P2X4 receptor desensitization
    • Fountain, S.J.; North, R.A., A C-terminal lysine that controls human P2X4 receptor desensitization. J. Biol. Chem., 2006, 281(22), 15044-15049.
    • (2006) J. Biol. Chem. , vol.281 , Issue.22 , pp. 15044-15049
    • Fountain, S.J.1    North, R.A.2
  • 200
    • 84880552270 scopus 로고    scopus 로고
    • P2X receptor chimeras highlight roles of the amino terminus to partial agonist efficacy, the carboxyl terminus to recovery from desensitization, and independent regulation of channel transitions
    • Allsopp, R.C.; Farmer, L.K.; Fryatt, A.G.; Evans, R.J., P2X receptor chimeras highlight roles of the amino terminus to partial agonist efficacy, the carboxyl terminus to recovery from desensitization, and independent regulation of channel transitions. J. Biol. Chem., 2013, 288(29), 21412-21421.
    • (2013) J. Biol. Chem. , vol.288 , Issue.29 , pp. 21412-21421
    • Allsopp, R.C.1    Farmer, L.K.2    Fryatt, A.G.3    Evans, R.J.4
  • 201
    • 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(52), 44691-44701.
    • (2011) J. Biol. Chem. , vol.286 , Issue.52 , pp. 44691-44701
    • Allsopp, R.C.1    Evans, R.J.2
  • 202
    • 1342282988 scopus 로고    scopus 로고
    • Desensitization masks nanomolar potency of ATP at the P2X1 receptor
    • Rettinger, J.; Schmalzing, G., Desensitization masks nanomolar potency of ATP at the P2X1 receptor. J. Biol. Chem., 2004, 279(8), 6426-6433.
    • (2004) J. Biol. Chem. , vol.279 , Issue.8 , pp. 6426-6433
    • Rettinger, J.1    Schmalzing, G.2
  • 203
    • 0141507009 scopus 로고    scopus 로고
    • 2′, 3′-O (2,4,6, trinitrophenyl)-ATP and A-317491 are competitive antagonists at a slowly desensitizing chimeric human P2X3 receptor
    • Neelands, T.R.; Burgard, E.C.; Uchic, M.E.; McDonald, H.A.; Niforatos, W.; Faltynek, C.R.; Lynch, K.J.; Jarvis, M.F., 2′, 3′-O (2,4,6, trinitrophenyl)-ATP and A-317491 are competitive antagonists at a slowly desensitizing chimeric human P2X3 receptor. Br. J. Pharmacol., 2003, 140(1), 202-210.
    • (2003) Br. J. Pharmacol. , vol.140 , Issue.1 , pp. 202-210
    • Neelands, T.R.1    Burgard, E.C.2    Uchic, M.E.3    McDonald, H.A.4    Niforatos, W.5    Faltynek, C.R.6    Lynch, K.J.7    Jarvis, M.F.8
  • 204
    • 84896711394 scopus 로고    scopus 로고
    • A hydrophobic residue in position 15 of the rP2X3 receptor slows desensitization and reveals properties beneficial for pharmacological analysis and high-throughput screening
    • Hausmann, R.; Bahrenberg, G.; Kuhlmann, D.; Schumacher, M.; Braam, U.; Bieler, D.; Schlusche, I.; Schmalzing, G., A hydrophobic residue in position 15 of the rP2X3 receptor slows desensitization and reveals properties beneficial for pharmacological analysis and high-throughput screening. Neuropharmacology, 2014, 79, 603-615.
    • (2014) Neuropharmacology , vol.79 , pp. 603-615
    • Hausmann, R.1    Bahrenberg, G.2    Kuhlmann, D.3    Schumacher, M.4    Braam, U.5    Bieler, D.6    Schlusche, I.7    Schmalzing, G.8
  • 205
    • 0036840533 scopus 로고    scopus 로고
    • Purinergic P2X(2) receptor desensitization depends on coupling between ectodomain and C-terminal domain
    • He, M.L.; Koshimizu, T.A.; Tomic, M.; Stojilkovic, S.S., Purinergic P2X(2) receptor desensitization depends on coupling between ectodomain and C-terminal domain. Mol. Pharmacol., 2002, 62(5), 1187-1197.
    • (2002) Mol. Pharmacol. , vol.62 , Issue.5 , pp. 1187-1197
    • He, M.L.1    Koshimizu, T.A.2    Tomic, M.3    Stojilkovic, S.S.4
  • 207
    • 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
    • Bavan, S.; Farmer, L.; Singh, S.K.; Straub, V.A.; Guerrero, F.D.; Ennion, S.J., The penultimate arginine of the carboxyl terminus determines slow desensitization in a P2X receptor from the cattle tick Boophilus microplus. Mol. Pharmacol., 2011, 79(4), 776-785.
    • (2011) Mol. Pharmacol. , vol.79 , Issue.4 , 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
  • 209
    • 3843134191 scopus 로고    scopus 로고
    • Identification of ectodomain regions contributing to gating, deactivation, and resensitization of purinergic P2X receptors
    • Zemkova, H.; He, M.L.; Koshimizu, T.A.; Stojilkovic, S.S., Identification of ectodomain regions contributing to gating, deactivation, and resensitization of purinergic P2X receptors. J. Neurosci., 2004, 24(31), 6968-6978.
    • (2004) J. Neurosci. , vol.24 , Issue.31 , pp. 6968-6978
    • Zemkova, H.1    He, M.L.2    Koshimizu, T.A.3    Stojilkovic, S.S.4
  • 210
    • 80054795773 scopus 로고    scopus 로고
    • Highly conserved tyrosine 37 stabilizes desensitized states and restricts calcium permeability of ATP-gated P2X3 receptor
    • Jindrichova, M.; Khafizov, K.; Skorinkin, A.; Fayuk, D.; Bart, G.; Zemkova, H.; Giniatullin, R., Highly conserved tyrosine 37 stabilizes desensitized states and restricts calcium permeability of ATP-gated P2X3 receptor. J. Neurochem., 2011, 119(4), 676-685.
    • (2011) J. Neurochem. , vol.119 , Issue.4 , pp. 676-685
    • Jindrichova, M.1    Khafizov, K.2    Skorinkin, A.3    Fayuk, D.4    Bart, G.5    Zemkova, H.6    Giniatullin, R.7
  • 211
    • 36248936564 scopus 로고    scopus 로고
    • Lack of evidence for direct phosphorylation of recombinantly expressed P2X(2) and P2X (3) receptors by protein kinase C
    • Franklin, C.; Braam, U.; Eisele, T.; Schmalzing, G.; Hausmann, R., Lack of evidence for direct phosphorylation of recombinantly expressed P2X(2) and P2X (3) receptors by protein kinase C. Purinergic Signal., 2007, 3(4), 377-388.
    • (2007) Purinergic Signal. , vol.3 , Issue.4 , pp. 377-388
    • Franklin, C.1    Braam, U.2    Eisele, T.3    Schmalzing, G.4    Hausmann, R.5
  • 212
    • 0040609340 scopus 로고    scopus 로고
    • A protein kinase C site highly conserved in P2X subunits controls the desensitization kinetics of P2X 2 ATP-gated channels
    • Boue-Grabot, E.; Archambault, V.; Seguela, P., A protein kinase C site highly conserved in P2X subunits controls the desensitization kinetics of P2X 2 ATP-gated channels J. Biol. Chem., 2000, 275(14), 10190-10195.
    • (2000) J. Biol. Chem. , vol.275 , Issue.14 , pp. 10190-10195
    • Boue-Grabot, E.1    Archambault, V.2    Seguela, P.3
  • 213
    • 79551588144 scopus 로고    scopus 로고
    • Contribution of the intracellular C terminal domain to regulation of human P2X1 receptors for ATP by phorbol ester and Gq coupled mGlu(1alpha) receptors
    • Wen, H.; Evans, R.J., Contribution of the intracellular C terminal domain to regulation of human P2X1 receptors for ATP by phorbol ester and Gq coupled mGlu(1alpha) receptors. Eur. J. Pharmacol., 2011, 654(2), 155-159.
    • (2011) Eur. J. Pharmacol. , vol.654 , Issue.2 , pp. 155-159
    • Wen, H.1    Evans, R.J.2
  • 214
    • 0036290377 scopus 로고    scopus 로고
    • P2X(1) receptor subunit contribution to gating revealed by a dominant negative PKC mutant
    • Ennion, S.J.; Evans, R.J., P2X(1) receptor subunit contribution to gating revealed by a dominant negative PKC mutant. Biochem. Biophys. Res. Commun., 2002, 291(3), 611-616.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , Issue.3 , pp. 611-616
    • Ennion, S.J.1    Evans, R.J.2
  • 215
    • 33748893444 scopus 로고    scopus 로고
    • Regulation of the desensitization and ion selectivity of ATP-gated P2X2 channels by phosphoinositides
    • Fujiwara, Y.; Kubo, Y., Regulation of the desensitization and ion selectivity of ATP-gated P2X2 channels by phosphoinositides. J. Physiol., 2006, 576(Pt 1), 135-149.
    • (2006) J. Physiol. , vol.576 , pp. 135-149
    • Fujiwara, Y.1    Kubo, Y.2
  • 216
    • 0037095757 scopus 로고    scopus 로고
    • Mutational analysis of the conserved cysteines of the rat P2X2 purinoceptor
    • Clyne, J.D.; Wang, L.F.; Hume, R.I., Mutational analysis of the conserved cysteines of the rat P2X2 purinoceptor. J. Neurosci., 2002, 22(10), 3873-3880.
    • (2002) J. Neurosci. , vol.22 , Issue.10 , pp. 3873-3880
    • Clyne, J.D.1    Wang, L.F.2    Hume, R.I.3
  • 217
    • 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
    • Ennion, S.J.; Evans, R.J., 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., 2002, 61(2), 303-311.
    • (2002) Mol. Pharmacol. , vol.61 , Issue.2 , pp. 303-311
    • Ennion, S.J.1    Evans, R.J.2
  • 218
    • 78651418254 scopus 로고    scopus 로고
    • Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating
    • Rokic, M.B.; Tvrdonova, V.; Vavra, V.; Jindrichova, M.; Obsil, T.; Stojilkovic, S.S.; Zemkova, H., Roles of conserved ectodomain cysteines of the rat P2X4 purinoreceptor in agonist binding and channel gating. Physiol. Res., 2010, 59(6), 927-935.
    • (2010) Physiol. Res. , vol.59 , Issue.6 , pp. 927-935
    • Rokic, M.B.1    Tvrdonova, V.2    Vavra, V.3    Jindrichova, M.4    Obsil, T.5    Stojilkovic, S.S.6    Zemkova, H.7
  • 220
    • 84863724617 scopus 로고    scopus 로고
    • Functional differences between ATP-gated human and rat P2X3 receptors are caused by critical residues of the intracellular cterminal domain
    • Sundukova, M.; Vilotti, S.; Abbate, R.; Fabbretti, E.; Nistri, A., Functional differences between ATP-gated human and rat P2X3 receptors are caused by critical residues of the intracellular Cterminal domain. J. Neurochem., 2012, 122(3), 557-567.
    • (2012) J. Neurochem. , vol.122 , Issue.3 , pp. 557-567
    • Sundukova, M.1    Vilotti, S.2    Abbate, R.3    Fabbretti, E.4    Nistri, A.5
  • 221
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W.L.; Maxwell, D.S.; TiradoRives, J., Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc., 1996, 118(45), 11225-11236.
    • (1996) J. Am. Chem. Soc. , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tiradorives, J.3
  • 222
    • 0001509942 scopus 로고    scopus 로고
    • Prediction of physicochemical parameters by atomic contributions
    • Wildman, S.A.; Crippen, G.M., Prediction of physicochemical parameters by atomic contributions. J. Chem. Inf. Comput. Sci., 1999, 39(5), 868-873.
    • (1999) J. Chem. Inf. Comput. Sci. , vol.39 , Issue.5 , pp. 868-873
    • Wildman, S.A.1    Crippen, G.M.2
  • 223
    • 0027673371 scopus 로고
    • A new approach to analysis and display of local lipophilicity hydrophilicity mapped on molecular-surfaces
    • Heiden, W.; Moeckel, G.; Brickmann, J., A new approach to analysis and display of local lipophilicity hydrophilicity mapped on molecular-surfaces. J. Comput. Aided Mol. Des., 1993, 7(5), 503-514.
    • (1993) J. Comput. Aided Mol. Des. , vol.7 , Issue.5 , pp. 503-514
    • Heiden, W.1    Moeckel, G.2    Brickmann, J.3
  • 225
    • 22244449669 scopus 로고    scopus 로고
    • Do all backbone polar groups in proteins form hydrogen bonds?
    • Fleming, P.J.; Rose, G.D. Do all backbone polar groups in proteins form hydrogen bonds? Protein Sci., 2005, 14(7), 1911-1917.
    • (2005) Protein Sci. , vol.14 , Issue.7 , pp. 1911-1917
    • Fleming, P.J.1    Rose, G.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.