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Volumn 89, Issue , 2015, Pages 561-580

Purinergic P2X receptors: Structural models and analysis of ligand-target interaction

Author keywords

Molecular modelling; Nucleotides; P2X receptor agonists; P2X receptor antagonists; P2X receptors; Purinergic receptors

Indexed keywords

3 [[5 (2,3 DICHLOROPHENYL) 1H TETRAZOL 1 YL]METHYL]PYRIDINE; 5 [[(3 PHENOXYBENZYL)(1,2,3,4 TETRAHYDRO 1 NAPHTHYL)AMINO]CARBONYL]TRIMELLITIC ACID; A 740003; A 804598; A 839977; PURINERGIC P2X RECEPTOR; PURINERGIC P2X4 RECEPTOR; PURINERGIC RECEPTOR BLOCKING AGENT; UNCLASSIFIED DRUG; A-317491; ADENOSINE TRIPHOSPHATE; ANTHRAQUINONE DERIVATIVE; DICYANDIAMIDO; GUANIDINE DERIVATIVE; LIGAND; PHENOL DERIVATIVE; POLYCYCLIC HYDROCARBON; PURINERGIC P2X RECEPTOR AGONIST; PURINERGIC P2X RECEPTOR ANTAGONIST; PYRROLE DERIVATIVE;

EID: 84908518386     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2014.10.071     Document Type: Article
Times cited : (41)

References (106)
  • 1
    • 84865411454 scopus 로고    scopus 로고
    • Discovery of purinergic signalling, the initial resistance and current explosion of interest
    • G. Burnstock Discovery of purinergic signalling, the initial resistance and current explosion of interest Br. J. Pharmacol. 167 2012 238 255
    • (2012) Br. J. Pharmacol. , vol.167 , pp. 238-255
    • Burnstock, G.1
  • 3
    • 67649639047 scopus 로고    scopus 로고
    • North, signaling at purinergic P2X receptors
    • R.A. Surprenant North, signaling at purinergic P2X receptors Annu. Rev. Physiol. 71 2009 333 359
    • (2009) Annu. Rev. Physiol. , vol.71 , pp. 333-359
    • Surprenant, R.A.1
  • 5
    • 33746701380 scopus 로고    scopus 로고
    • P2X receptors as cell-surface ATP sensors in health and disease
    • B.S. Khakh R.A. North P2X receptors as cell-surface ATP sensors in health and disease Nature 442 2006 527 532
    • (2006) Nature , vol.442 , pp. 527-532
    • Khakh, B.S.1    North, R.A.2
  • 6
    • 75749112926 scopus 로고    scopus 로고
    • P2X receptors: dawn of the post-structure era
    • M.T. Young P2X receptors: dawn of the post-structure era Trends Biochem. Sci. 35 2010 83 90
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 83-90
    • Young, M.T.1
  • 8
    • 77958610109 scopus 로고    scopus 로고
    • Structural interpretation of P2X receptor mutagenesis studies on drug action
    • R.J. Evans Structural interpretation of P2X receptor mutagenesis studies on drug action Br. J. Pharmacol. 161 2010 961 971
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 961-971
    • Evans, R.J.1
  • 9
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • R.A. North Molecular physiology of P2X receptors Physiol. Rev. 82 2002 1013 1067
    • (2002) Physiol. Rev. , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 10
    • 15444372454 scopus 로고    scopus 로고
    • Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize
    • N.P. Barrera S.J. Ormond R.M. Henderson R.D. Murrell-Lagnado J.M. Edwardson Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize J. Biol. Chem. 280 2005 10759 10765
    • (2005) J. Biol. Chem. , vol.280 , pp. 10759-10765
    • Barrera, N.P.1    Ormond, S.J.2    Henderson, R.M.3    Murrell-Lagnado, R.D.4    Edwardson, J.M.5
  • 11
    • 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
    • S.J. Ormond N.P. Barrera O.S. Qureshi R.M. Henderson J.M. Edwardson R.D. Murrell-Lagnado An uncharged region within the N terminus of the P2X6 receptor inhibits its assembly and exit from the endoplasmic reticulum Mol. Pharmacol. 69 2006 1692 1700
    • (2006) Mol. Pharmacol. , vol.69 , 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
  • 13
    • 0033366463 scopus 로고    scopus 로고
    • Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds
    • B.S. Khakh X.R. Bao C. Labarca H.A. Lester Neuronal P2X transmitter-gated cation channels change their ion selectivity in seconds Nat. Neurosci. 2 1999 322 330
    • (1999) Nat. Neurosci. , vol.2 , pp. 322-330
    • Khakh, B.S.1    Bao, X.R.2    Labarca, C.3    Lester, H.A.4
  • 16
    • 79955957628 scopus 로고    scopus 로고
    • P2X receptors in health and disease
    • G. Burnstock C. Kennedy P2X receptors in health and disease Adv. Pharmacol. 61 2011 333 372
    • (2011) Adv. Pharmacol. , vol.61 , pp. 333-372
    • Burnstock, G.1    Kennedy, C.2
  • 17
    • 46449134214 scopus 로고    scopus 로고
    • Purinergic signalling and disorders of the central nervous system
    • G. Burnstock Purinergic signalling and disorders of the central nervous system Nat. Rev. Drug Discov. 7 2008 575 590
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 575-590
    • Burnstock, G.1
  • 19
    • 0029088454 scopus 로고
    • Pharmacological characterization of heterologously expressed ATP-gated cation channels (P2x purinoceptors)
    • R.J. Evans C. Lewis G. Buell S. Valera R.A. North A. Surprenant Pharmacological characterization of heterologously expressed ATP-gated cation channels (P2x purinoceptors) Mol. Pharmacol. 48 1995 178 183
    • (1995) Mol. Pharmacol. , vol.48 , pp. 178-183
    • Evans, R.J.1    Lewis, C.2    Buell, G.3    Valera, S.4    North, R.A.5    Surprenant, A.6
  • 21
    • 0031866948 scopus 로고    scopus 로고
    • North, trinitrophenyl-substituted nucleotides are potent antagonists selective for P2X1, P2X3, and heteromeric P2X2/3 receptors
    • G. Virginio A. Robertson R.A. Surprenant North, trinitrophenyl-substituted nucleotides are potent antagonists selective for P2X1, P2X3, and heteromeric P2X2/3 receptors Mol. Pharmacol. 53 1998 969 973
    • (1998) Mol. Pharmacol. , vol.53 , pp. 969-973
    • Virginio, G.1    Robertson, A.2    Surprenant, R.A.3
  • 26
    • 0242585424 scopus 로고    scopus 로고
    • Synthesis and biological activity of N -arylpiperazine-modified analogues of KN-62, a potent antagonist of the purinergic P2X7 receptor
    • P.G. Baraldi M. del Carmen Nunez A. Morelli S. Falzoni F. Di Virgilio R. Romagnoli Synthesis and biological activity of N -arylpiperazine-modified analogues of KN-62, a potent antagonist of the purinergic P2X7 receptor J. Med. Chem. 46 2003 1318 1329
    • (2003) J. Med. Chem. , vol.46 , pp. 1318-1329
    • Baraldi, P.G.1    Del Carmen Nunez, M.2    Morelli, A.3    Falzoni, S.4    Di Virgilio, F.5    Romagnoli, R.6
  • 29
    • 33644902898 scopus 로고    scopus 로고
    • Decavanadate, a P2X receptor antagonist, and its use to study ligand interactions with P2X7 receptors
    • A.D. Michel M. Xing K.M. Thompson C.A. Jones P.P. Humphrey Decavanadate, a P2X receptor antagonist, and its use to study ligand interactions with P2X7 receptors Eur. J. Pharmacol. 534 2006 19 29
    • (2006) Eur. J. Pharmacol. , vol.534 , pp. 19-29
    • Michel, A.D.1    Xing, M.2    Thompson, K.M.3    Jones, C.A.4    Humphrey, P.P.5
  • 34
    • 40749094413 scopus 로고    scopus 로고
    • Synthesis and in vitro activity of 1-(2,3-dichlorophenyl)- N -(pyridin-3-ylmethyl)-1H-1,2,4-triazol-5-amine and 4-(2,3-dichlorophenyl)- N -(pyridin-3-ylmethyl)-4H-1,2,4-triazol-3-amine P2X7 antagonists
    • A.S. Florjancic S. Peddi A. Perez-Medrano B. Li M.T. Namovic G. Grayson D.L. Donnelly-Roberts M.F. Jarvis W.A. Carroll Synthesis and in vitro activity of 1-(2,3-dichlorophenyl)- N -(pyridin-3-ylmethyl)-1H-1,2,4-triazol-5-amine and 4-(2,3-dichlorophenyl)- N -(pyridin-3-ylmethyl)-4H-1,2,4-triazol-3-amine P2X7 antagonists Bioorg. Med. Chem. Lett. 18 2008 2089 2092
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 2089-2092
    • Florjancic, A.S.1    Peddi, S.2    Perez-Medrano, A.3    Li, B.4    Namovic, M.T.5    Grayson, G.6    Donnelly-Roberts, D.L.7    Jarvis, M.F.8    Carroll, W.A.9
  • 39
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X4 ion channel in the closed state
    • T. Kawate J.C. Michel W.T. Birdsong E. Gouaux Crystal structure of the ATP-gated P2X4 ion channel in the closed state Nature 460 2009 592 598
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 40
    • 84860785529 scopus 로고    scopus 로고
    • Molecular mechanism of ATP binding and ion channel activation in P2X receptors
    • M. Hattori E. Gouaux Molecular mechanism of ATP binding and ion channel activation in P2X receptors Nature 485 2012 207 212
    • (2012) Nature , vol.485 , pp. 207-212
    • Hattori, M.1    Gouaux, E.2
  • 42
    • 0034703055 scopus 로고    scopus 로고
    • The role of positively charged amino acids in ATP recognition by human P2X(1) receptors
    • S. Ennion S. Hagan R.J. Evans The role of positively charged amino acids in ATP recognition by human P2X(1) receptors J. Biol. Chem. 275 2000 29361 29367
    • (2000) J. Biol. Chem. , vol.275 , pp. 29361-29367
    • Ennion, S.1    Hagan, S.2    Evans, R.J.3
  • 43
    • 0034602169 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor
    • L.H. Jiang F. Rassendren A. Surprenant R.A. North Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor J. Biol. Chem. 275 2000 34190 34196
    • (2000) J. Biol. Chem. , vol.275 , pp. 34190-34196
    • Jiang, L.H.1    Rassendren, F.2    Surprenant, A.3    North, R.A.4
  • 44
    • 1542275329 scopus 로고    scopus 로고
    • ATP binding at human P2X1 receptors. Contribution of aromatic and basic amino acids revealed using mutagenesis and partial agonists
    • J.A. Roberts R.J. Evans ATP binding at human P2X1 receptors. Contribution of aromatic and basic amino acids revealed using mutagenesis and partial agonists J. Biol. Chem. 279 2004 9043 9055
    • (2004) J. Biol. Chem. , vol.279 , pp. 9043-9055
    • Roberts, J.A.1    Evans, R.J.2
  • 45
    • 15744376891 scopus 로고    scopus 로고
    • Molecular determinants of the agonist binding domain of a P2X receptor channel
    • Z. Yan Z. Liang M. Tomic T. Obsil S.S. Stojilkovic Molecular determinants of the agonist binding domain of a P2X receptor channel Mol. Pharmacol. 67 2005 1078 1088
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1078-1088
    • Yan, Z.1    Liang, Z.2    Tomic, M.3    Obsil, T.4    Stojilkovic, S.S.5
  • 46
  • 47
    • 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
    • J.A. Roberts H.R. Digby M. Kara S. El Ajouz M.J. Sutcliffe R.J. Evans 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. 283 2008 20126 20136
    • (2008) J. Biol. Chem. , vol.283 , pp. 20126-20136
    • Roberts, J.A.1    Digby, H.R.2    Kara, M.3    El Ajouz, S.4    Sutcliffe, M.J.5    Evans, R.J.6
  • 49
    • 80051696222 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gating
    • R.C. Allsopp S. El Ajouz R. Schmid R.J. Evans Cysteine scanning mutagenesis (residues Glu52-Gly96) of the human P2X1 receptor for ATP: mapping agonist binding and channel gating J. Biol. Chem. 286 2011 29207 29217
    • (2011) J. Biol. Chem. , vol.286 , pp. 29207-29217
    • Allsopp, R.C.1    El Ajouz, S.2    Schmid, R.3    Evans, R.J.4
  • 51
    • 33748944331 scopus 로고    scopus 로고
    • Role of ectodomain lysines in the subunits of the heteromeric P2X2/3 receptor
    • W.J. Wilkinson L.H. Jiang A. Surprenant R.A. North Role of ectodomain lysines in the subunits of the heteromeric P2X2/3 receptor Mol. Pharmacol. 70 2006 1159 1163
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1159-1163
    • Wilkinson, W.J.1    Jiang, L.H.2    Surprenant, A.3    North, R.A.4
  • 54
    • 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
    • J.A. Roberts R.J. Evans Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP J. Neurochem. 96 2006 843 852
    • (2006) J. Neurochem. , vol.96 , pp. 843-852
    • Roberts, J.A.1    Evans, R.J.2
  • 55
    • 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
    • J.A. Roberts M. Valente R.C. Allsopp D. Watt R.J. Evans 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. 109 2009 1042 1052
    • (2009) J. Neurochem. , vol.109 , pp. 1042-1052
    • Roberts, J.A.1    Valente, M.2    Allsopp, R.C.3    Watt, D.4    Evans, R.J.5
  • 57
    • 34247120710 scopus 로고    scopus 로고
    • Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors
    • J.A. Roberts R.J. Evans Cysteine substitution mutants give structural insight and identify ATP binding and activation sites at P2X receptors J. Neurosci. 27 2007 4072 4082
    • (2007) J. Neurosci. , vol.27 , pp. 4072-4082
    • Roberts, J.A.1    Evans, R.J.2
  • 59
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • J. Dundas Z. Ouyang J. Tseng A. Binkowski Y. Turpaz J. Liang CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues Nucleic Acids Res. 34 2006 116 118
    • (2006) Nucleic Acids Res. , vol.34 , pp. 116-118
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 62
    • 0014349825 scopus 로고
    • The characterization of amino acid sequences in proteins by statistical methods
    • J.M. Zimmerman N. Eliezer R. Simha The characterization of amino acid sequences in proteins by statistical methods J. Theor. Biol. 21 1968 170 201
    • (1968) J. Theor. Biol. , vol.21 , pp. 170-201
    • Zimmerman, J.M.1    Eliezer, N.2    Simha, R.3
  • 63
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 64
    • 0023465103 scopus 로고
    • Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients
    • D.J. Abraham A.J. Leo Extension of the fragment method to calculate amino acid zwitterion and side chain partition coefficients Proteins 2 1987 130 152
    • (1987) Proteins , vol.2 , pp. 130-152
    • Abraham, D.J.1    Leo, A.J.2
  • 65
    • 0021977590 scopus 로고
    • Amino acid side-chain partition energies and distribution of residues in soluble proteins
    • H.R. Guy Amino acid side-chain partition energies and distribution of residues in soluble proteins Biophys. J. 47 1985 61 70
    • (1985) Biophys. J. , vol.47 , pp. 61-70
    • Guy, H.R.1
  • 66
    • 0025388957 scopus 로고
    • Hydrophobicity indices for amino acid residues as determined by high-performance liquid chromatography
    • R. Cowan R.G. Whittaker Hydrophobicity indices for amino acid residues as determined by high-performance liquid chromatography Pept. Res. 3 1990 75 80
    • (1990) Pept. Res. , vol.3 , pp. 75-80
    • Cowan, R.1    Whittaker, R.G.2
  • 67
    • 0000484499 scopus 로고
    • Hydrophobic parameters pi of amino acid side chains from partitioning of N -acetyl-amino-acid amides
    • J.L. Fauchere V. Pliska Hydrophobic parameters pi of amino acid side chains from partitioning of N -acetyl-amino-acid amides Eur. J. Med. Chem. 18 1983 369 375
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2
  • 71
    • 0343144816 scopus 로고    scopus 로고
    • Molecular characterization and pharmacological properties of the human P2X3 purinoceptor
    • M. Garcia-Guzman W. Stühmer F. Soto Molecular characterization and pharmacological properties of the human P2X3 purinoceptor Mol. Brain Res. 47 1997 59 66
    • (1997) Mol. Brain Res. , vol.47 , pp. 59-66
    • Garcia-Guzman, M.1    Stühmer, W.2    Soto, F.3
  • 73
    • 0029665112 scopus 로고    scopus 로고
    • Buell, the cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7)
    • F. Surprenant E. Rassendren R.A. Kawashima G. North Buell, the cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7) Science 272 1996 735 738
    • (1996) Science , vol.272 , pp. 735-738
    • Surprenant, F.1    Rassendren, E.2    Kawashima, R.A.3    North, G.4
  • 75
    • 0037855835 scopus 로고    scopus 로고
    • Dependence of purinergic P2X receptor activity on ectodomain structure
    • M.L. He H. Zemkova S.S. Stojilkovic Dependence of purinergic P2X receptor activity on ectodomain structure J. Biol. Chem. 278 2003 10182 10188
    • (2003) J. Biol. Chem. , vol.278 , pp. 10182-10188
    • He, M.L.1    Zemkova, H.2    Stojilkovic, S.S.3
  • 76
    • 70350339068 scopus 로고    scopus 로고
    • Mammalian P2X7 receptor pharmacology: comparison of recombinant mouse, rat and human P2X7 receptors
    • D.L. Donnelly-Roberts M.T. Namovic P. Han M.F. Jarvis Mammalian P2X7 receptor pharmacology: comparison of recombinant mouse, rat and human P2X7 receptors Br. J. Pharmacol. 157 2009 1203 1214
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 1203-1214
    • Donnelly-Roberts, D.L.1    Namovic, M.T.2    Han, P.3    Jarvis, M.F.4
  • 77
    • 0027530024 scopus 로고
    • Oxidized ATP. An irreversible inhibitor of the macrophage purinergic P2Z receptor
    • M. Murgia S. Hanau P. Pizzo M. Rippa F. Di Virgilio Oxidized ATP. An irreversible inhibitor of the macrophage purinergic P2Z receptor J. Biol. Chem. 268 1993 8199 8203
    • (1993) J. Biol. Chem. , vol.268 , pp. 8199-8203
    • Murgia, M.1    Hanau, S.2    Pizzo, P.3    Rippa, M.4    Di Virgilio, F.5
  • 78
    • 0028182521 scopus 로고
    • The P2Z-purinoceptor of human lymphocytes: actions of nucleotide agonists and irreversible inhibition by oxidized ATP
    • J.S. Wiley J.R. Chen M.B. Snook G.P. Jamieson The P2Z-purinoceptor of human lymphocytes: actions of nucleotide agonists and irreversible inhibition by oxidized ATP Br. J. Pharmacol. 112 1994 946 950
    • (1994) Br. J. Pharmacol. , vol.112 , pp. 946-950
    • Wiley, J.S.1    Chen, J.R.2    Snook, M.B.3    Jamieson, G.P.4
  • 80
    • 0142216130 scopus 로고    scopus 로고
    • Novel data point to a broader mechanism of action of oxidized ATP: the P2X7 receptor is not the only target
    • Di Virgilio Novel data point to a broader mechanism of action of oxidized ATP: the P2X7 receptor is not the only target Br. J. Pharmacol. 140 2003 441 443
    • (2003) Br. J. Pharmacol. , vol.140 , pp. 441-443
    • Virgilio, D.1
  • 82
    • 0020479618 scopus 로고
    • The use of 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate for studies of nucleotide interaction with sarcoplasmic reticulum vesicles
    • T. Watanabe G. Inesi The use of 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate for studies of nucleotide interaction with sarcoplasmic reticulum vesicles J. Biol. Chem. 257 1982 11510 11516
    • (1982) J. Biol. Chem. , vol.257 , pp. 11510-11516
    • Watanabe, T.1    Inesi, G.2
  • 83
    • 0027960512 scopus 로고
    • Fluorescence imaging of extracellular purinergic receptor sites and putative ecto-ATPase sites on isolated cochlear hair cells
    • B.G. Mockett G.D. Housley P.R. Thorne Fluorescence imaging of extracellular purinergic receptor sites and putative ecto-ATPase sites on isolated cochlear hair cells J. Neurosci. 14 1994 6992 7007
    • (1994) J. Neurosci. , vol.14 , pp. 6992-7007
    • Mockett, B.G.1    Housley, G.D.2    Thorne, P.R.3
  • 84
    • 0031877057 scopus 로고    scopus 로고
    • 2',3'-O-(2,4,6- trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP)-a nanomolar affinity antagonist at rat mesenteric artery P2X receptor ion channels
    • C.J. Lewis A. Surprenant R.J. Evans 2',3'-O-(2,4,6- trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP)-a nanomolar affinity antagonist at rat mesenteric artery P2X receptor ion channels Br. J. Pharmacol. 124 1998 1463 1466
    • (1998) Br. J. Pharmacol. , vol.124 , pp. 1463-1466
    • Lewis, C.J.1    Surprenant, A.2    Evans, R.J.3
  • 87
    • 1842557492 scopus 로고    scopus 로고
    • Structure-activity relationships of analogues of NF449 confirm NF449 as the most potent and selective known P2X1 receptor antagonist
    • M.U. Kassack K. Braun M. Ganso H. Ullmann P. Nickel B. Boing G. Muller G. Lambrecht Structure-activity relationships of analogues of NF449 confirm NF449 as the most potent and selective known P2X1 receptor antagonist Eur. J. Med. Chem. 39 2004 345 357
    • (2004) Eur. J. Med. Chem. , vol.39 , pp. 345-357
    • Kassack, M.U.1    Braun, K.2    Ganso, M.3    Ullmann, H.4    Nickel, P.5    Boing, B.6    Muller, G.7    Lambrecht, G.8
  • 88
    • 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
    • J. Rettinger K. Braun H. Hochmann M.U. Kassack H. Ullmann P. Nickel G. Schmalzing G. Lambrecht Profiling at recombinant homomeric and heteromeric rat P2X receptors identifies the suramin analogue NF449 as a highly potent P2X1 receptor antagonist Neuropharmacology 48 2005 461 468
    • (2005) Neuropharmacology , vol.48 , 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
  • 89
    • 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
    • R. Hausmann J. Rettinger Z. Gerevich S. Meis M.U. Kassack P. Illes G. Lambrecht G. Schmalzing 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. 69 2006 2058 2067
    • (2006) Mol. Pharmacol. , vol.69 , 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
  • 90
    • 0033004707 scopus 로고    scopus 로고
    • Antagonistic properties of the suramin analogue NF023 at heterologously expressed P2X receptors
    • Soto G. Lambrecht P. Nickel W. Stuhmer A.E. Busch Antagonistic properties of the suramin analogue NF023 at heterologously expressed P2X receptors Neuropharmacology 38 1999 141 149
    • (1999) Neuropharmacology , vol.38 , pp. 141-149
    • Soto1    Lambrecht, G.2    Nickel, P.3    Stuhmer, W.4    Busch, A.E.5
  • 92
  • 96
    • 0030977216 scopus 로고    scopus 로고
    • The isoquinoline derivative KN-62 a potent antagonist of the P2Z-receptor of human lymphocytes
    • C.E. Gargett J.S. Wiley The isoquinoline derivative KN-62 a potent antagonist of the P2Z-receptor of human lymphocytes Br. J. Pharmacol. 120 1997 1483 1490
    • (1997) Br. J. Pharmacol. , vol.120 , pp. 1483-1490
    • Gargett, C.E.1    Wiley, J.S.2
  • 97
    • 84908527372 scopus 로고    scopus 로고
    • Molecular Operating Environment, C.C.G., Inc., 1255 University St., Suite 1600, Montreal, Quebec, Canada, H3B 3X3.
    • Molecular Operating Environment, C.C.G., Inc., 1255 University St., Suite 1600, Montreal, Quebec, Canada, H3B 3X3.
  • 98
    • 0025390935 scopus 로고
    • MOPAC: a semiempirical molecular orbital program
    • J.J. Stewart MOPAC: a semiempirical molecular orbital program J. Comput. Aided Mol. Des. 4 1990 1 105
    • (1990) J. Comput. Aided Mol. Des. , vol.4 , pp. 1-105
    • Stewart, J.J.1
  • 100
    • 0037571112 scopus 로고    scopus 로고
    • Merck molecular force field. I. basis, form, scope, parameterization, and performance of MMFF94
    • T.A. Halgren Merck molecular force field. I. basis, form, scope, parameterization, and performance of MMFF94 J. Comput. Chem. 17 1996 490 519
    • (1996) J. Comput. Chem. , vol.17 , pp. 490-519
    • Halgren, T.A.1
  • 101
    • 0011134241 scopus 로고    scopus 로고
    • Merck molecular force field. II. MMFF94 van der Waals and electrostatic parameters for intermolecular interactions
    • T.A. Halgren Merck molecular force field. II. MMFF94 van der Waals and electrostatic parameters for intermolecular interactions J. Comput. Chem. 17 1996 520 552
    • (1996) J. Comput. Chem. , vol.17 , pp. 520-552
    • Halgren, T.A.1
  • 102
    • 0011143599 scopus 로고    scopus 로고
    • Merck molecular force field. III. molecular geometries and vibrational frequencies for MMFF94
    • T.A. Halgren Merck molecular force field. III. molecular geometries and vibrational frequencies for MMFF94 J. Comput. Chem. 17 1996 553 586
    • (1996) J. Comput. Chem. , vol.17 , pp. 553-586
    • Halgren, T.A.1
  • 103
    • 0001061464 scopus 로고    scopus 로고
    • Merck molecular force field. IV. conformational energies and geometries for MMFF94
    • T.A. Halgren Merck molecular force field. IV. conformational energies and geometries for MMFF94 J. Comput. Chem. 17 1996 587 615
    • (1996) J. Comput. Chem. , vol.17 , pp. 587-615
    • Halgren, T.A.1
  • 104
    • 5244268272 scopus 로고    scopus 로고
    • Merck molecular force field. V. Extension of MMFF94 using experimental data, additional computational data, and empirical rules
    • T.A. Halgren R. Nachbar Merck molecular force field. V. Extension of MMFF94 using experimental data, additional computational data, and empirical rules J. Comput. Chem. 17 1996 616 641
    • (1996) J. Comput. Chem. , vol.17 , pp. 616-641
    • Halgren, T.A.1    Nachbar, R.2
  • 105
    • 5544242529 scopus 로고    scopus 로고
    • MMFF VI. MMFF94s option for energy minimization studies
    • T.A. Halgren MMFF VI. MMFF94s option for energy minimization studies J. Comput. Chem. 20 1999 720 729
    • (1999) J. Comput. Chem. , vol.20 , pp. 720-729
    • Halgren, T.A.1
  • 106
    • 0001242234 scopus 로고    scopus 로고
    • MMFF VII. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular-interaction energies and geometries
    • T.A. Halgren MMFF VII. Characterization of MMFF94, MMFF94s, and other widely available force fields for conformational energies and for intermolecular-interaction energies and geometries J. Comput. Chem. 20 1999 730 748
    • (1999) J. Comput. Chem. , vol.20 , pp. 730-748
    • Halgren, T.A.1


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