메뉴 건너뛰기




Volumn 80, Issue C, 2010, Pages 153-203

Positive and negative modulation of nicotinic receptors

Author keywords

[No Author keywords available]

Indexed keywords


EID: 78649884825     PISSN: 18761623     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381264-3.00005-9     Document Type: Chapter
Times cited : (68)

References (184)
  • 1
    • 14244255827 scopus 로고    scopus 로고
    • Galantamine activates muscle-type nicotinic acetylcholine receptors without binding to the acetylcholine-binding site
    • G. Akk, and J.H. Steinbach Galantamine activates muscle-type nicotinic acetylcholine receptors without binding to the acetylcholine-binding site J. Neurosci. 25 2005 1992 2001
    • (2005) J. Neurosci. , vol.25 , pp. 1992-2001
    • Akk, G.1    Steinbach, J.H.2
  • 2
    • 58249113980 scopus 로고    scopus 로고
    • Mammalian nicotinic acetylcholine receptors: From structure to function
    • E.X. Albuquerque, E.F. Pereira, M. Alkondon, and S.W. Rogers Mammalian nicotinic acetylcholine receptors: from structure to function Physiol. Rev. 89 2009 73 120
    • (2009) Physiol. Rev. , vol.89 , pp. 73-120
    • Albuquerque, E.X.1    Pereira, E.F.2    Alkondon, M.3    Rogers, S.W.4
  • 3
    • 33745271061 scopus 로고    scopus 로고
    • Subtype-specific inhibition of nicotinic acetylcholine receptors by choline: A regulatory pathway
    • M. Alkondon, and E.X. Albuquerque Subtype-specific inhibition of nicotinic acetylcholine receptors by choline: a regulatory pathway J. Pharmacol. Exp. Ther. 318 2006 268 275
    • (2006) J. Pharmacol. Exp. Ther. , vol.318 , pp. 268-275
    • Alkondon, M.1    Albuquerque, E.X.2
  • 4
    • 0031410384 scopus 로고    scopus 로고
    • Choline is a selective agonist of α7 nicotinic acetylcholine receptors in rat brain neurons
    • M. Alkondon, E.F. Pereira, W.S. Cortes, A. Maelicke, and E.X. Albuquerque Choline is a selective agonist of α7 nicotinic acetylcholine receptors in rat brain neurons Eur. J. Neurosci. 9 1997 2734 2742
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 2734-2742
    • Alkondon, M.1    Pereira, E.F.2    Cortes, W.S.3    Maelicke, A.4    Albuquerque, E.X.5
  • 6
    • 68349133470 scopus 로고    scopus 로고
    • Stimulation of dopamine release by nicotinic acetylcholine receptor ligands in rat brain slices correlates with the profile of high, but not low, sensitivity α4β2 subunit combination
    • D.J. Anderson, J. Malysz, J.H. Grønlien, R. El Kouhen, M. Hkerud, and C. Wetterstrand Stimulation of dopamine release by nicotinic acetylcholine receptor ligands in rat brain slices correlates with the profile of high, but not low, sensitivity α4β2 subunit combination Biochem. Pharmacol. 78 2009 844 851
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 844-851
    • Anderson, D.J.1    Malysz, J.2    Grønlien, J.H.3    El Kouhen, R.4    Hkerud, M.5    Wetterstrand, C.6
  • 7
    • 77952669652 scopus 로고    scopus 로고
    • Associated proteins: The universal toolbox controlling ligand gated ion channel function
    • T. Araud, S. Wonnacott, and D. Bertrand Associated proteins: the universal toolbox controlling ligand gated ion channel function Biochem. Pharmacol. 80 2010 160 169
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 160-169
    • Araud, T.1    Wonnacott, S.2    Bertrand, D.3
  • 9
    • 70349267544 scopus 로고    scopus 로고
    • Is the inhibition of nicotinic acetylcholine receptors by bupropion involved in its clinical actions?
    • H.R. Arias Is the inhibition of nicotinic acetylcholine receptors by bupropion involved in its clinical actions? Int. J. Biochem. Cell Biol. 41 2009 2098 2108
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 2098-2108
    • Arias, H.R.1
  • 10
    • 77649200248 scopus 로고    scopus 로고
    • Interaction of lipids and ligands with nicotinic acetylcholine receptor vesicles assessed by electron paramagnetic resonance spectroscopy
    • H.R. Arias Interaction of lipids and ligands with nicotinic acetylcholine receptor vesicles assessed by electron paramagnetic resonance spectroscopy V. Veissig, Liposomes, Methods in Molecular Biology Vol. 606 2010 The Humana Press Inc. USA 291 318
    • (2010) Liposomes, Methods in Molecular Biology , vol.606 , pp. 291-318
    • Arias, H.R.1
  • 11
    • 78649807228 scopus 로고    scopus 로고
    • Molecular interaction of bupropion with nicotine acetylcholine receptors
    • H.R. Arias Molecular interaction of bupropion with nicotine acetylcholine receptors J. Pediatr. Biochem. 1 2010 185 - 197
    • (2010) J. Pediatr. Biochem. , vol.1
    • Arias, H.R.1
  • 12
    • 26844569439 scopus 로고    scopus 로고
    • Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors
    • H.R. Arias, and P. Bhumireddy Anesthetics as chemical tools to study the structure and function of nicotinic acetylcholine receptors Curr. Protein Pept. Sci. 6 2005 451 472
    • (2005) Curr. Protein Pept. Sci. , vol.6 , pp. 451-472
    • Arias, H.R.1    Bhumireddy, P.2
  • 14
    • 78649866226 scopus 로고    scopus 로고
    • Activation and modulation of the nicotine receptor
    • H.R. Arias, and C.B. Bouzat Activation and modulation of the nicotine receptor J. Pediatr. Biochem. 1 2010 53 - 73
    • (2010) J. Pediatr. Biochem. , vol.1
    • Arias, H.R.1    Bouzat, C.B.2
  • 15
    • 33646177253 scopus 로고    scopus 로고
    • Molecular mechanisms and binding site locations for noncompetitive antagonists of nicotinic acetylcholine receptors
    • H.R. Arias, P. Bhumireddy, and C. Bouzat Molecular mechanisms and binding site locations for noncompetitive antagonists of nicotinic acetylcholine receptors Int. J. Biochem. Cell Biol. 38 2006 1254 1276
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 1254-1276
    • Arias, H.R.1    Bhumireddy, P.2    Bouzat, C.3
  • 16
    • 66349094243 scopus 로고    scopus 로고
    • Interaction of bupropion with muscle-type nicotinic acetylcholine receptors in different conformational states
    • H.R. Arias, F. Gumilar, A. Rosenberg, K.M. Targowska-Duda, D. Feuerbach, and K. Jozwiak Interaction of bupropion with muscle-type nicotinic acetylcholine receptors in different conformational states Biochemistry 48 2009 4506 4518
    • (2009) Biochemistry , vol.48 , pp. 4506-4518
    • Arias, H.R.1    Gumilar, F.2    Rosenberg, A.3    Targowska-Duda, K.M.4    Feuerbach, D.5    Jozwiak, K.6
  • 18
    • 77649181290 scopus 로고    scopus 로고
    • Inhibitory mechanisms and binding site locations for serotonin selective reuptake inhibitors on nicotinic acetylcholine receptors
    • H.R. Arias, D. Feuerbach, P. Bhumireddy, and M. Ortells Inhibitory mechanisms and binding site locations for serotonin selective reuptake inhibitors on nicotinic acetylcholine receptors Int. J. Biochem. Cell Biol. 42 2010 712 724
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 712-724
    • Arias, H.R.1    Feuerbach, D.2    Bhumireddy, P.3    Ortells, M.4
  • 19
    • 77952386905 scopus 로고    scopus 로고
    • Different interaction between the agonist JN403 and the competitive antagonist methyllycaconitine with the human α7 nicotinic receptor
    • H.R. Arias, H. Gu, D. Feuerbach, and D.Q. Wei Different interaction between the agonist JN403 and the competitive antagonist methyllycaconitine with the human α7 nicotinic receptor Biochemistry 49 2010 4169 4180
    • (2010) Biochemistry , vol.49 , pp. 4169-4180
    • Arias, H.R.1    Gu, H.2    Feuerbach, D.3    Wei, D.Q.4
  • 21
    • 77249089718 scopus 로고    scopus 로고
    • Different interaction between tricyclic antidepressants and mecamylamine with the human α3β4 nicotinic acetylcholine receptor
    • H.R. Arias, K.M. Targowska-Duda, C.J. Sullivan, D. Feuerbach, R. Maciejewski, and K. Jozwiak Different interaction between tricyclic antidepressants and mecamylamine with the human α3β4 nicotinic acetylcholine receptor Int. Neurochem. 56 2010 642 649
    • (2010) Int. Neurochem. , vol.56 , pp. 642-649
    • Arias, H.R.1    Targowska-Duda, K.M.2    Sullivan, C.J.3    Feuerbach, D.4    MacIejewski, R.5    Jozwiak, K.6
  • 22
    • 41149127406 scopus 로고    scopus 로고
    • Allosteric modulation of α7 nicotinic receptors selectively depolarizes hippocampal interneurons, enhancing spontaneous GABAergic transmission
    • J.J. Arnaiz-Cot, J.C. Gonzlez, M. Sobrado, P. Baldelli, E. Carbone, and L. Ganda Allosteric modulation of α7 nicotinic receptors selectively depolarizes hippocampal interneurons, enhancing spontaneous GABAergic transmission Eur. J. Neurosci. 27 2008 1097 1110
    • (2008) Eur. J. Neurosci. , vol.27 , pp. 1097-1110
    • Arnaiz-Cot, J.J.1    Gonzlez, J.C.2    Sobrado, M.3    Baldelli, P.4    Carbone, E.5    Ganda, L.6
  • 24
    • 36549084005 scopus 로고    scopus 로고
    • How to turn the reaction coordinate into time
    • A. Auerbach How to turn the reaction coordinate into time J. Gen. Physiol. 130 2007 543 546
    • (2007) J. Gen. Physiol. , vol.130 , pp. 543-546
    • Auerbach, A.1
  • 25
    • 72949084363 scopus 로고    scopus 로고
    • Mecamylaminea nicotinic acetylcholine receptor antagonist with potential for the treatment of neuropsychiatric disorders
    • I. Bacher, B. Wu, D.R. Shytle, and T.P. George Mecamylaminea nicotinic acetylcholine receptor antagonist with potential for the treatment of neuropsychiatric disorders Expert Opin. Pharmacother. 10 2009 2709 2721
    • (2009) Expert Opin. Pharmacother. , vol.10 , pp. 2709-2721
    • Bacher, I.1    Wu, B.2    Shytle, D.R.3    George, T.P.4
  • 26
    • 49649099967 scopus 로고    scopus 로고
    • Gating at the mouth of the acetylcholine receptor channel: Energetic consequences of mutations in the αm2-cap
    • P.A. Bafna, P.G. Purohit, and A. Auerbach Gating at the mouth of the acetylcholine receptor channel: energetic consequences of mutations in the αM2-cap PLoS ONE 3 2008 e2515
    • (2008) PLoS ONE , vol.3 , pp. 2515
    • Bafna, P.A.1    Purohit, P.G.2    Auerbach, A.3
  • 27
    • 67650799171 scopus 로고    scopus 로고
    • An allosteric modulator of α7 nicotinic receptors, N-(5-chloro-2, 4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea (PNU-120596), causes conformational changes in the extracellular ligand binding domain similar to those caused by acetylcholine
    • S.C. Barron, J.T. McLaughlin, J.A. See, V.L. Richards, and R.L. Rosenberg An allosteric modulator of α7 nicotinic receptors, N-(5-chloro-2, 4-dimethoxyphenyl)-N'-(5-methyl-3-isoxazolyl)-urea (PNU-120596), causes conformational changes in the extracellular ligand binding domain similar to those caused by acetylcholine Mol. Pharmacol. 76 2009 253 263
    • (2009) Mol. Pharmacol. , vol.76 , pp. 253-263
    • Barron, S.C.1    McLaughlin, J.T.2    See, J.A.3    Richards, V.L.4    Rosenberg, R.L.5
  • 28
    • 70849100535 scopus 로고    scopus 로고
    • Structural basis of activation of Cys-loop receptors: The extracellular - Transmembrane interface as a coupling region
    • M. Bartos, J. Corradi, and C. Bouzat Structural basis of activation of Cys-loop receptors: the extracellular - transmembrane interface as a coupling region Mol. Neurobiol. 40 2009 236 252
    • (2009) Mol. Neurobiol. , vol.40 , pp. 236-252
    • Bartos, M.1    Corradi, J.2    Bouzat, C.3
  • 29
    • 69249109185 scopus 로고    scopus 로고
    • Glutamine 57 at the complementary binding site face is a key determinant of morantel selectivity for α7 nicotinic receptors
    • M. Bartos, K.L. Price, S.C. Lummis, and C. Bouzat Glutamine 57 at the complementary binding site face is a key determinant of morantel selectivity for α7 nicotinic receptors J. Biol. Chem. 284 2009 21478 21487
    • (2009) J. Biol. Chem. , vol.284 , pp. 21478-21487
    • Bartos, M.1    Price, K.L.2    Lummis, S.C.3    Bouzat, C.4
  • 30
    • 33745907550 scopus 로고    scopus 로고
    • A hydrophobic gate in an ion channel: The closed state of the nicotinic acetylcholine receptor
    • O. Beckstein, and M.S. Sansom A hydrophobic gate in an ion channel: the closed state of the nicotinic acetylcholine receptor Phys. Biol. 3 2006 147 159
    • (2006) Phys. Biol. , vol.3 , pp. 147-159
    • Beckstein, O.1    Sansom, M.S.2
  • 31
    • 34548677767 scopus 로고    scopus 로고
    • Allosteric modulation of α7 and α4β2 nicotinic acetylcholine receptors
    • D. Bertrand, and M. Gopalakrishnan Allosteric modulation of α7 and α4β2 nicotinic acetylcholine receptors Biochem. Pharmacol. 74 2007 1155 1163
    • (2007) Biochem. Pharmacol. , vol.74 , pp. 1155-1163
    • Bertrand, D.1    Gopalakrishnan, M.2
  • 32
    • 54349102284 scopus 로고    scopus 로고
    • Positive allosteric modulation of the α7 nicotinic acetylcholine receptor: Ligand interactions with distinct binding sites and evidence for a prominent role of the M2 - M3 segment
    • D. Bertrand, S. Bertrand, S. Cassar, E. Gubbins, J. Li, and M. Gopalakrishnan Positive allosteric modulation of the α7 nicotinic acetylcholine receptor: ligand interactions with distinct binding sites and evidence for a prominent role of the M2 - M3 segment Mol. Pharmacol. 74 2008 1407 1416
    • (2008) Mol. Pharmacol. , vol.74 , pp. 1407-1416
    • Bertrand, D.1    Bertrand, S.2    Cassar, S.3    Gubbins, E.4    Li, J.5    Gopalakrishnan, M.6
  • 33
    • 33846106078 scopus 로고    scopus 로고
    • A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family
    • N. Bocquet, L. Prado de Carvalho, J. Cartaud, J. Neyton, C. Le Poupon, and A. Taly A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family Nature 445 2007 116 119
    • (2007) Nature , vol.445 , pp. 116-119
    • Bocquet, N.1    Prado De Carvalho, L.2    Cartaud, J.3    Neyton, J.4    Le Poupon, C.5    Taly, A.6
  • 34
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • N. Bocquet, H. Nury, M. Baaden, C. Le Poupon, J. -P. Changeux, and M. Delarue X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation Nature 457 2009 111 114
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1    Nury, H.2    Baaden, M.3    Le Poupon, C.4    Changeux, J.-P.5    Delarue, M.6
  • 35
    • 62849094251 scopus 로고    scopus 로고
    • Upregulation of α7 nicotinic receptors by acetylcholinesterase C-terminal peptides
    • C.E. Bond, M. Zimmermann, and S.A. Greenfield Upregulation of α7 nicotinic receptors by acetylcholinesterase C-terminal peptides PLoS ONE 4 2009 e4846
    • (2009) PLoS ONE , vol.4 , pp. 4846
    • Bond, C.E.1    Zimmermann, M.2    Greenfield, S.A.3
  • 36
    • 0028600111 scopus 로고
    • Structural basis of the different gating kinetics of fetal and adult nicotinic acetylcholine receptors
    • C. Bouzat, N. Bren, and S.M. Sine Structural basis of the different gating kinetics of fetal and adult nicotinic acetylcholine receptors Neuron 13 1994 1395 1402
    • (1994) Neuron , vol.13 , pp. 1395-1402
    • Bouzat, C.1    Bren, N.2    Sine, S.M.3
  • 37
    • 0036221142 scopus 로고    scopus 로고
    • Subunit-selective contribution to channel gating of the M4 domain of the nicotinic receptor
    • C. Bouzat, F. Gumilar, M. Esandi, C. del, and S.M. Sine Subunit-selective contribution to channel gating of the M4 domain of the nicotinic receptor Biophys. J. 82 2002 1920 1929 (Pubitemid 34280807)
    • (2002) Biophysical Journal , vol.82 , Issue.4 , pp. 1920-1929
    • Bouzat, C.1    Gumilar, F.2    Del Carmen Esandi, M.3    Sine, S.M.4
  • 38
    • 4344616080 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in an ACh-binding protein linked to ion channel
    • C. Bouzat, F. Gumilar, G. Spitzmaul, H.L. Wang, D. Rayes, and S.B. Hansen Coupling of agonist binding to channel gating in an ACh-binding protein linked to ion channel Nature 430 2004 896 900
    • (2004) Nature , vol.430 , pp. 896-900
    • Bouzat, C.1    Gumilar, F.2    Spitzmaul, G.3    Wang, H.L.4    Rayes, D.5    Hansen, S.B.6
  • 40
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • K. Brejc, W.J. van Dijk, R.V. Klaassen, M. Schuurmans, J. van Der Oost, and A.B. Smit Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors Nature 411 2001 269 276
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    Van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    Van Der Oost, J.5    Smit, A.B.6
  • 41
    • 33747597579 scopus 로고    scopus 로고
    • Identification and pharmacological profile of a new class of selective nicotinic acetylcholine receptor potentiators
    • L.M. Broad, R. Zwart, K.H. Pearson, M. Lee, L. Wallace, and G.I. McPhie Identification and pharmacological profile of a new class of selective nicotinic acetylcholine receptor potentiators J. Pharmacol. Exp. Ther. 318 2006 1108 1117
    • (2006) J. Pharmacol. Exp. Ther. , vol.318 , pp. 1108-1117
    • Broad, L.M.1    Zwart, R.2    Pearson, K.H.3    Lee, M.4    Wallace, L.5    McPhie, G.I.6
  • 42
    • 34248195657 scopus 로고    scopus 로고
    • The dynamics of the rapsyn scaffolding protein at individual acetylcholine receptor clusters
    • E. Bruneau, and M. Akaaboune The dynamics of the rapsyn scaffolding protein at individual acetylcholine receptor clusters J. Biol. Chem. 282 2007 9932 9940
    • (2007) J. Biol. Chem. , vol.282 , pp. 9932-9940
    • Bruneau, E.1    Akaaboune, M.2
  • 44
    • 22144466847 scopus 로고    scopus 로고
    • Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors
    • P.H. Celie, R.V. Klaassen, S.E. van Rossum-Fikkert, R. van Elk, P. van Nierop, and A.B. Smit Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors J. Biol. Chem. 280 2005 26457 26466
    • (2005) J. Biol. Chem. , vol.280 , pp. 26457-26466
    • Celie, P.H.1    Klaassen, R.V.2    Van Rossum-Fikkert, S.E.3    Van Elk, R.4    Van Nierop, P.5    Smit, A.B.6
  • 45
    • 67549125013 scopus 로고    scopus 로고
    • Allosteric activation mechanism of the cys-loop receptors
    • Y. -C. Chang, W. Wu, J. -L. Zhang, and Y. Huang Allosteric activation mechanism of the cys-loop receptors Acta Pharmacol. Sin. 30 2009 663 672
    • (2009) Acta Pharmacol. Sin. , vol.30 , pp. 663-672
    • Chang, Y.-C.1    Wu, W.2    Zhang, J.-L.3    Huang, Y.4
  • 46
    • 40649084279 scopus 로고    scopus 로고
    • Nicotinic receptors, allosteric proteins and medicine
    • J.-P. Changeux, and A. Taly Nicotinic receptors, allosteric proteins and medicine Trends Mol. Med. 14 2008 93 102
    • (2008) Trends Mol. Med. , vol.14 , pp. 93-102
    • Changeux, J.-P.1    Taly, A.2
  • 47
    • 27344437870 scopus 로고    scopus 로고
    • α7 Neuronal nicotinic acetylcholine receptors are negatively regulated by tyrosine phosphorylation and Src-family kinases
    • E. Charpantier, A. Wiesner, K.H. Huh, R. Ogier, J.C. Hoda, and G. Allaman α7 Neuronal nicotinic acetylcholine receptors are negatively regulated by tyrosine phosphorylation and Src-family kinases J. Neurosci. 25 2005 9836 9849
    • (2005) J. Neurosci. , vol.25 , pp. 9836-9849
    • Charpantier, E.1    Wiesner, A.2    Huh, K.H.3    Ogier, R.4    Hoda, J.C.5    Allaman, G.6
  • 48
    • 0344443178 scopus 로고    scopus 로고
    • Identification of SLURP-1 as an epidermal neuromodulator explains the clinical phenotype of Mal de Meleda
    • F. Chimienti, R.C. Hogg, L. Plantard, C. Lehmann, N. Brakch, and J. Fischer Identification of SLURP-1 as an epidermal neuromodulator explains the clinical phenotype of Mal de Meleda Hum. Mol. Genet. 12 2003 3017 3024
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3017-3024
    • Chimienti, F.1    Hogg, R.C.2    Plantard, L.3    Lehmann, C.4    Brakch, N.5    Fischer, J.6
  • 49
    • 17044426320 scopus 로고    scopus 로고
    • Rapid upregulation of α7 nicotinic acetylcholine receptors by tyrosine dephosphorylation
    • C.H. Cho, W. Song, K. Leitzell, E. Teo, A.D. Meleth, and M.W. Quick Rapid upregulation of α7 nicotinic acetylcholine receptors by tyrosine dephosphorylation J. Neurosci. 25 2005 3712 3723
    • (2005) J. Neurosci. , vol.25 , pp. 3712-3723
    • Cho, C.H.1    Song, W.2    Leitzell, K.3    Teo, E.4    Meleth, A.D.5    Quick, M.W.6
  • 50
    • 77954926628 scopus 로고    scopus 로고
    • Nicotinic acetylcholine receptor transmembrane mutations convert ivermectin from a positive to a negative allosteric modulator
    • T. Collins, and N.S. Millar Nicotinic acetylcholine receptor transmembrane mutations convert ivermectin from a positive to a negative allosteric modulator Mol. Pharmacol. 78 2010 198 204
    • (2010) Mol. Pharmacol. , vol.78 , pp. 198-204
    • Collins, T.1    Millar, N.S.2
  • 51
    • 0037289748 scopus 로고    scopus 로고
    • Potentiation of α7-containing nicotinic acetylcholine receptors by select albumins
    • W.G. Conroy, Q.S. Liu, Q. Nai, J.F. Margiotta, and D.K. Berg Potentiation of α7-containing nicotinic acetylcholine receptors by select albumins Mol. Pharmacol. 63 2003 419 428
    • (2003) Mol. Pharmacol. , vol.63 , pp. 419-428
    • Conroy, W.G.1    Liu, Q.S.2    Nai, Q.3    Margiotta, J.F.4    Berg, D.K.5
  • 52
    • 77949538692 scopus 로고    scopus 로고
    • Atomic structure and dynamics of pentameric ligand-gated ion channels: New insight from bacterial homologues
    • P.J. Corringer, M. Baaden, N. Bocquet, M. Delarue, V. Dufresne, and H. Nury Atomic structure and dynamics of pentameric ligand-gated ion channels: new insight from bacterial homologues J. Physiol. 588 Pt 4 2010 565 572
    • (2010) J. Physiol. , vol.588 , Issue.PART 4 , pp. 565-572
    • Corringer, P.J.1    Baaden, M.2    Bocquet, N.3    Delarue, M.4    Dufresne, V.5    Nury, H.6
  • 53
    • 0344441288 scopus 로고    scopus 로고
    • A structural model of agonist binding to the α3β4 neuronal nicotinic receptor
    • V. Costa, A. Nistri, A. Cavalli, and P. Carloni A structural model of agonist binding to the α3β4 neuronal nicotinic receptor Br. J. Pharmacol. 140 2003 921 931
    • (2003) Br. J. Pharmacol. , vol.140 , pp. 921-931
    • Costa, V.1    Nistri, A.2    Cavalli, A.3    Carloni, P.4
  • 54
    • 27844490551 scopus 로고    scopus 로고
    • Mutations of a conserved lysine residue in the N-terminal domain of α7 nicotinic receptors affect gating and binding of nicotinic agonists
    • M. Criado, J. Mulet, J.A. Bernal, S. Gerber, S. Sala, and F. Sala Mutations of a conserved lysine residue in the N-terminal domain of α7 nicotinic receptors affect gating and binding of nicotinic agonists Mol. Pharmacol. 68 2005 1669 1677
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1669-1677
    • Criado, M.1    Mulet, J.2    Bernal, J.A.3    Gerber, S.4    Sala, S.5    Sala, F.6
  • 56
    • 41649119572 scopus 로고    scopus 로고
    • Pore-opening mechanism of the nicotinic acetylcholine receptor evinced by proton transfer
    • G.D. Cymes, and C. Grosman Pore-opening mechanism of the nicotinic acetylcholine receptor evinced by proton transfer Nat. Struct. Mol. Biol. 15 2008 389 396
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 389-396
    • Cymes, G.D.1    Grosman, C.2
  • 57
    • 30744470883 scopus 로고    scopus 로고
    • Probing ion-channel pores one proton at a time
    • G.D. Cymes, Y. Ni, and C. Grosman Probing ion-channel pores one proton at a time Nature 438 2005 975 980
    • (2005) Nature , vol.438 , pp. 975-980
    • Cymes, G.D.1    Ni, Y.2    Grosman, C.3
  • 59
    • 34547520128 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of nAChR α1 bound to α-bungarotoxin at 1.94 resolution
    • C.D. Dellisanti, Y. Yao, J.C. Stroud, Z.Z. Wang, and L. Chen Crystal structure of the extracellular domain of nAChR α1 bound to α-bungarotoxin at 1.94 resolution Nat. Neurosci. 10 2007 953 962
    • (2007) Nat. Neurosci. , vol.10 , pp. 953-962
    • Dellisanti, C.D.1    Yao, Y.2    Stroud, J.C.3    Wang, Z.Z.4    Chen, L.5
  • 60
    • 0036142564 scopus 로고    scopus 로고
    • A novel class of peptides with facilitating action on neuronal nicotinic receptors of rat chromaffin cells in vitro: Functional and molecular dynamics studies
    • S. Di Angelantonio, V. Costa, P. Carloni, L. Messori, and A. Nistri A novel class of peptides with facilitating action on neuronal nicotinic receptors of rat chromaffin cells in vitro: functional and molecular dynamics studies Mol. Pharmacol. 61 2002 43 54
    • (2002) Mol. Pharmacol. , vol.61 , pp. 43-54
    • Di Angelantonio, S.1    Costa, V.2    Carloni, P.3    Messori, L.4    Nistri, A.5
  • 61
    • 0042669974 scopus 로고    scopus 로고
    • Modulation of neuronal nicotinic receptor function by the neuropeptides CGRP and substance P on autonomic nerve cells
    • S. Di Angelantonio, R. Giniatullin, V. Costa, E. Sokolova, and A. Nistri Modulation of neuronal nicotinic receptor function by the neuropeptides CGRP and substance P on autonomic nerve cells Br. J. Pharmacol. 139 2003 1061 1073
    • (2003) Br. J. Pharmacol. , vol.139 , pp. 1061-1073
    • Di Angelantonio, S.1    Giniatullin, R.2    Costa, V.3    Sokolova, E.4    Nistri, A.5
  • 62
    • 62449113374 scopus 로고    scopus 로고
    • Old and new pharmacology: Positive allosteric modulation of the α7 nicotinic acetylcholine receptor by the 5-hydroxytryptamine2B/C receptor antagonist SB-206553 (3, 5-dihydro-5-methyl-N-3-pyridinylbenzo[1, 2-b:4, 5-b′]dipyrrole-1(2H)-carboxamide)
    • J. Dunlop, T. Lock, B. Jow, F. Sitzia, S. Grauer, and F. Jow Old and new pharmacology: positive allosteric modulation of the α7 nicotinic acetylcholine receptor by the 5-hydroxytryptamine2B/C receptor antagonist SB-206553 (3, 5-dihydro-5-methyl-N-3-pyridinylbenzo[1, 2-b:4, 5-b′]dipyrrole-1(2H)-carboxamide) J. Pharmacol. Exp. Ther. 328 2009 766 776
    • (2009) J. Pharmacol. Exp. Ther. , vol.328 , pp. 766-776
    • Dunlop, J.1    Lock, T.2    Jow, B.3    Sitzia, F.4    Grauer, S.5    Jow, F.6
  • 64
    • 66349096318 scopus 로고    scopus 로고
    • Discovery of 4-(5-(4-chlorophenyl)-2-methyl-3-propionyl-1H-pyrrol-1-yl) benzenesulfonamide (A-867744) as a novel positive allosteric modulator of the α7 nicotinic acetylcholine receptor
    • R. Faghih, S.M. Gopalakrishnan, J.H. Gronlien, J. Malysz, C.A. Briggs, and C. Wetterstrand Discovery of 4-(5-(4-chlorophenyl)-2-methyl-3-propionyl-1H- pyrrol-1-yl)benzenesulfonamide (A-867744) as a novel positive allosteric modulator of the α7 nicotinic acetylcholine receptor J. Med. Chem. 52 2009 3377 3384
    • (2009) J. Med. Chem. , vol.52 , pp. 3377-3384
    • Faghih, R.1    Gopalakrishnan, S.M.2    Gronlien, J.H.3    Malysz, J.4    Briggs, C.A.5    Wetterstrand, C.6
  • 66
    • 59649125049 scopus 로고    scopus 로고
    • Differential pharmacologies of mecamylamine enantiomers: Positive allosteric modulation of noncompetitive inhibition
    • N.B. Fedorov, L.C. Benson, J. Graef, and P.M. Lippiello Differential pharmacologies of mecamylamine enantiomers: positive allosteric modulation of noncompetitive inhibition J. Pharmacol. Exp. Ther. 328 2009 525 532
    • (2009) J. Pharmacol. Exp. Ther. , vol.328 , pp. 525-532
    • Fedorov, N.B.1    Benson, L.C.2    Graef, J.3    Lippiello, P.M.4
  • 67
    • 0035312614 scopus 로고    scopus 로고
    • Tobacco cembranoids block behavioral sensitization to nicotine and inhibit neuronal acetylcholine receptor function
    • P.A. Ferchmin, R.J. Lukas, R.M. Hann, J.D. Fryer, J.B. Eaton, and O.R. Pagn Tobacco cembranoids block behavioral sensitization to nicotine and inhibit neuronal acetylcholine receptor function J. Neurosci. Res. 64 2001 18 25
    • (2001) J. Neurosci. Res. , vol.64 , pp. 18-25
    • Ferchmin, P.A.1    Lukas, R.J.2    Hann, R.M.3    Fryer, J.D.4    Eaton, J.B.5    Pagn, O.R.6
  • 68
    • 28444432014 scopus 로고    scopus 로고
    • Tobacco cembranoids protect the function of acute hippocampal slices against NMDA by a mechanism mediated by α4β2 nicotinic receptors
    • P.A. Ferchmin, J. Hao, D. Perez, M. Penzo, H.M. Maldonado, and M.T. Gonzalez Tobacco cembranoids protect the function of acute hippocampal slices against NMDA by a mechanism mediated by α4β2 nicotinic receptors J. Neurosci. Res. 82 2005 631 641
    • (2005) J. Neurosci. Res. , vol.82 , pp. 631-641
    • Ferchmin, P.A.1    Hao, J.2    Perez, D.3    Penzo, M.4    Maldonado, H.M.5    Gonzalez, M.T.6
  • 70
    • 0035931126 scopus 로고    scopus 로고
    • Modulation of α2β4 neuronal nicotinic acetylcholine receptors by zinc
    • J. Garca-Colunga, M. Gonzlez-Herrera, and R. Miledi Modulation of α2β4 neuronal nicotinic acetylcholine receptors by zinc NeuroReport 12 2001 147 150 (Pubitemid 32099045)
    • (2001) NeuroReport , vol.12 , Issue.1 , pp. 147-150
    • Garcia-Colunga, J.1    Gonzalez-Herrera, M.2    Miledi, R.3
  • 71
    • 10044244799 scopus 로고    scopus 로고
    • Combined actions of zinc and fluoxetine on nicotinic acetylcholine receptors
    • J. Garca-Colunga, E. Vzquez-Gmez, and R. Miledi Combined actions of zinc and fluoxetine on nicotinic acetylcholine receptors Pharmacogenomics J. 4 2004 388 393
    • (2004) Pharmacogenomics J. , vol.4 , pp. 388-393
    • Garca-Colunga, J.1    Vzquez-Gmez, E.2    Miledi, R.3
  • 72
    • 51449084722 scopus 로고    scopus 로고
    • Nicotinic antagonist augmentation of selective serotonin reuptake inhibitor-refractory major depressive disorder: A preliminary study
    • T.P. George, K.A. Sacco, J.C. Vessicchio, A.H. Weinberger, and R.D. Shytle Nicotinic antagonist augmentation of selective serotonin reuptake inhibitor-refractory major depressive disorder: a preliminary study J. Clin. Psychopharmacol. 28 2008 340 344
    • (2008) J. Clin. Psychopharmacol. , vol.28 , pp. 340-344
    • George, T.P.1    Sacco, K.A.2    Vessicchio, J.C.3    Weinberger, A.H.4    Shytle, R.D.5
  • 73
    • 20744449198 scopus 로고    scopus 로고
    • Desensitization of nicotinic ACh receptors: Shaping cholinergic signaling
    • R. Giniatullin, A. Nistri, and J.L. Yakel Desensitization of nicotinic ACh receptors: shaping cholinergic signaling Trends Neurosci. 28 2005 371 378
    • (2005) Trends Neurosci. , vol.28 , pp. 371-378
    • Giniatullin, R.1    Nistri, A.2    Yakel, J.L.3
  • 74
    • 59649093446 scopus 로고    scopus 로고
    • Effect of novel negative allosteric modulators of nicotinic receptors on cells expressing native and recombinant nicotinic receptors: Implications for drug discovery
    • T.F. Gonzlez-Cestari, B.J. Henderson, R.E. Pavlovicz, S.B. McKay, R.A. El-Hajj, and A.B. Pulipaka Effect of novel negative allosteric modulators of nicotinic receptors on cells expressing native and recombinant nicotinic receptors: implications for drug discovery J. Pharmacol. Exp. Ther. 328 2009 504 515
    • (2009) J. Pharmacol. Exp. Ther. , vol.328 , pp. 504-515
    • Gonzlez-Cestari, T.F.1    Henderson, B.J.2    Pavlovicz, R.E.3    McKay, S.B.4    El-Hajj, R.A.5    Pulipaka, A.B.6
  • 75
    • 75049083418 scopus 로고    scopus 로고
    • Mouse striatal dopamine nerve terminals express α4α5β2 and two stoichiometric forms of α4β2*-nicotinic acetylcholine receptors
    • S.R. Grady, O. Salminen, J.M. McIntosh, M.J. Marks, and A.C. Collins Mouse striatal dopamine nerve terminals express α4α5β2 and two stoichiometric forms of α4β2*-nicotinic acetylcholine receptors J. Mol. Neurosci. 40 2010 91 95
    • (2010) J. Mol. Neurosci. , vol.40 , pp. 91-95
    • Grady, S.R.1    Salminen, O.2    McIntosh, J.M.3    Marks, M.J.4    Collins, A.C.5
  • 76
    • 40549109577 scopus 로고    scopus 로고
    • Basic and clinical aspects of non-neuronal acetylcholine: Biological and clinical significance of non-canonical ligands of epithelial nicotinic acetylcholine receptors
    • S.A. Grando Basic and clinical aspects of non-neuronal acetylcholine: biological and clinical significance of non-canonical ligands of epithelial nicotinic acetylcholine receptors J. Pharmacol. Sci. 106 2008 174 179
    • (2008) J. Pharmacol. Sci. , vol.106 , pp. 174-179
    • Grando, S.A.1
  • 77
    • 3142660247 scopus 로고    scopus 로고
    • A novel peptide modulates α7 nicotinic receptor responses: Implications for a possible trophic - Toxic mechanism within the brain
    • S.A. Greenfield, T. Day, E.O. Mann, and I. Bermudez A novel peptide modulates α7 nicotinic receptor responses: implications for a possible trophic - toxic mechanism within the brain J. Neurochem. 90 2004 325 331
    • (2004) J. Neurochem. , vol.90 , pp. 325-331
    • Greenfield, S.A.1    Day, T.2    Mann, E.O.3    Bermudez, I.4
  • 78
    • 34548301101 scopus 로고    scopus 로고
    • Distinct profiles of α7 nAChR positive allosteric modulation revealed by structurally diverse chemotypes
    • J.H. Grønlien, M. Hkerud, H. Ween, K. Thorin-Hagene, C.A. Briggs, and M. Gopalakrishnan Distinct profiles of α7 nAChR positive allosteric modulation revealed by structurally diverse chemotypes Mol. Pharmacol. 72 2007 715 724
    • (2007) Mol. Pharmacol. , vol.72 , pp. 715-724
    • Grønlien, J.H.1    Hkerud, M.2    Ween, H.3    Thorin-Hagene, K.4    Briggs, C.A.5    Gopalakrishnan, M.6
  • 79
    • 0037544107 scopus 로고    scopus 로고
    • An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors
    • T. Grutter, L. Prado de Carvalho, N. Le Novre, P. -J. Corringer, S. Edelstein, and J. -P. Changeux An H-bond between two residues from different loops of the acetylcholine binding site contributes to the activation mechanism of nicotinic receptors EMBO J. 22 2003 1990 2003
    • (2003) EMBO J. , vol.22 , pp. 1990-2003
    • Grutter, T.1    Prado De Carvalho, L.2    Le Novre, N.3    Corringer, P.-J.4    Edelstein, S.5    Changeux, J.-P.6
  • 80
    • 0142090758 scopus 로고    scopus 로고
    • Molecular mechanism of inhibition of nicotinic acetylcholine receptors by tricyclic antidepressants
    • F. Gumilar, H.R. Arias, G. Spitzmaul, and C. Bouzat Molecular mechanism of inhibition of nicotinic acetylcholine receptors by tricyclic antidepressants Neuropharmacology 45 2003 964 976
    • (2003) Neuropharmacology , vol.45 , pp. 964-976
    • Gumilar, F.1    Arias, H.R.2    Spitzmaul, G.3    Bouzat, C.4
  • 81
    • 0036283791 scopus 로고    scopus 로고
    • Expression of nicotinic receptors in the skin of patients with palmoplantar pustulosis
    • E. Hagforsen, M. Edvinsson, K. Nordlind, and G. Michalsson Expression of nicotinic receptors in the skin of patients with palmoplantar pustulosis Br. J. Dermatol. 146 2002 383 391
    • (2002) Br. J. Dermatol. , vol.146 , pp. 383-391
    • Hagforsen, E.1    Edvinsson, M.2    Nordlind, K.3    Michalsson, G.4
  • 82
    • 34248598024 scopus 로고    scopus 로고
    • Galanthamine and non-competitive inhibitor binding to ACh-binding protein: Evidence for a binding site on non-α-subunit interfaces of heteromeric neuronal nicotinic receptors
    • S.B. Hansen, and P. Taylor Galanthamine and non-competitive inhibitor binding to ACh-binding protein: evidence for a binding site on non-α-subunit interfaces of heteromeric neuronal nicotinic receptors J. Mol. Biol. 369 2007 895 901
    • (2007) J. Mol. Biol. , vol.369 , pp. 895-901
    • Hansen, S.B.1    Taylor, P.2
  • 83
    • 27144473613 scopus 로고    scopus 로고
    • Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations
    • S.B. Hansen, G. Sulzenbacher, T. Huxford, P. Marchot, P. Taylor, and Y. Bourne Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations EMBO J. 24 2005 3635 3646
    • (2005) EMBO J. , vol.24 , pp. 3635-3646
    • Hansen, S.B.1    Sulzenbacher, G.2    Huxford, T.3    Marchot, P.4    Taylor, P.5    Bourne, Y.6
  • 85
    • 23844439286 scopus 로고    scopus 로고
    • α7 Nicotinic receptor agonists as potential therapeutic drugs for schizophrenia
    • K. Hashimoto, K. Koike, E. Shimizu, and M. Iyo α7 Nicotinic receptor agonists as potential therapeutic drugs for schizophrenia Curr. Med. Chem.CNS Agents 5 2005 171 184
    • (2005) Curr. Med. Chem.CNS Agents , vol.5 , pp. 171-184
    • Hashimoto, K.1    Koike, K.2    Shimizu, E.3    Iyo, M.4
  • 87
    • 33845994767 scopus 로고    scopus 로고
    • Influence of agonists and antagonists on the segmental motion of residues near the agonist binding pocket of the acetylcholine-binding protein
    • R.E. Hibbs, Z. Radic, P. Taylor, and D.A. Johnson Influence of agonists and antagonists on the segmental motion of residues near the agonist binding pocket of the acetylcholine-binding protein J. Biol. Chem. 281 2006 39708 39718
    • (2006) J. Biol. Chem. , vol.281 , pp. 39708-39718
    • Hibbs, R.E.1    Radic, Z.2    Taylor, P.3    Johnson, D.A.4
  • 88
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • R.J. Hilf, and R. Dutzler X-ray structure of a prokaryotic pentameric ligand-gated ion channel Nature 452 2008 375 379
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 89
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • R.J. Hilf, and R. Dutzler Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel Nature 457 2009 115 118
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 90
    • 77649274491 scopus 로고    scopus 로고
    • Manipulating neuronal circuits with endogenous and recombinant cell-surface tethered modulators
    • M. Holford, S. Auer, M. Laqua, and I. Ibaez-Tallon Manipulating neuronal circuits with endogenous and recombinant cell-surface tethered modulators Front. Mol. Neurosci. 2 2009 1 10
    • (2009) Front. Mol. Neurosci. , vol.2 , pp. 1-10
    • Holford, M.1    Auer, S.2    Laqua, M.3    Ibaez-Tallon, I.4
  • 91
    • 72449189587 scopus 로고    scopus 로고
    • Prostate stem cell antigen is an endogenous lynx1-like prototoxin that antagonizes α7-containing nicotinic receptors and prevents programmed cell death of parasympathetic neurons
    • M. Hruska, J. Keefe, D. Wert, A.B. Tekinay, J.J. Hulce, and I. Ibaez-Tallon Prostate stem cell antigen is an endogenous lynx1-like prototoxin that antagonizes α7-containing nicotinic receptors and prevents programmed cell death of parasympathetic neurons J. Neurosci. 29 2009 14847 14854
    • (2009) J. Neurosci. , vol.29 , pp. 14847-14854
    • Hruska, M.1    Keefe, J.2    Wert, D.3    Tekinay, A.B.4    Hulce, J.J.5    Ibaez-Tallon, I.6
  • 92
    • 0035869550 scopus 로고    scopus 로고
    • Subunit-dependent modulation of neuronal nicotinic receptors by zinc
    • B. Hsiao, D. Dweck, and C.W. Luetje Subunit-dependent modulation of neuronal nicotinic receptors by zinc J. Neurosci. 21 2001 1848 1856
    • (2001) J. Neurosci. , vol.21 , pp. 1848-1856
    • Hsiao, B.1    Dweck, D.2    Luetje, C.W.3
  • 94
    • 39149142227 scopus 로고    scopus 로고
    • Zinc potentiates neuronal nicotinic receptors by increasing burst duration
    • B. Hsiao, K.B. Mihalak, K.L. Magleby, and C.W. Luetje Zinc potentiates neuronal nicotinic receptors by increasing burst duration J. Neurophysiol. 99 2008 999 1007
    • (2008) J. Neurophysiol. , vol.99 , pp. 999-1007
    • Hsiao, B.1    Mihalak, K.B.2    Magleby, K.L.3    Luetje, C.W.4
  • 95
    • 71649112438 scopus 로고    scopus 로고
    • Positive allosteric modulation of α7 neuronal nicotinic acetylcholine receptors: Lack of cytotoxicity in PC12 cells and rat primary cortical neurons
    • M. Hu, M. Gopalakrishnan, and J. Li Positive allosteric modulation of α7 neuronal nicotinic acetylcholine receptors: lack of cytotoxicity in PC12 cells and rat primary cortical neurons Br. J. Pharmacol. 158 2009 1857 1864
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 1857-1864
    • Hu, M.1    Gopalakrishnan, M.2    Li, J.3
  • 96
    • 20944441082 scopus 로고    scopus 로고
    • A novel positive allosteric modulator of the α7 neuronal nicotinic acetylcholine receptor: In vitro and in vivo characterization
    • R.S. Hurst, M. Hajs, M. Raggenbass, T.M. Wall, N.R. Higdon, and J.A. Lawson A novel positive allosteric modulator of the α7 neuronal nicotinic acetylcholine receptor: in vitro and in vivo characterization J. Neurosci. 25 2005 4396 4405
    • (2005) J. Neurosci. , vol.25 , pp. 4396-4405
    • Hurst, R.S.1    Hajs, M.2    Raggenbass, M.3    Wall, T.M.4    Higdon, N.R.5    Lawson, J.A.6
  • 97
    • 0037075542 scopus 로고    scopus 로고
    • Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynx1
    • I. Ibaez-Tallon, J.M. Miwa, H. -L. Wang, N.C. Adams, G.W. Crabtree, and S.M. Sine Novel modulation of neuronal nicotinic acetylcholine receptors by association with the endogenous prototoxin lynx1 Neuron 33 2002 893 903
    • (2002) Neuron , vol.33 , pp. 893-903
    • Ibaez-Tallon, I.1    Miwa, J.M.2    Wang, H.-L.3    Adams, N.C.4    Crabtree, G.W.5    Sine, S.M.6
  • 98
    • 33644783933 scopus 로고    scopus 로고
    • Acetylcholine nicotinic receptors: Finding the putative binding site of allosteric modulators using the "blind docking" approach
    • B. Iorga, D. Herlem, E. Barr, and C. Guillou Acetylcholine nicotinic receptors: finding the putative binding site of allosteric modulators using the "blind docking" approach J. Mol. Model. 12 2006 366 372
    • (2006) J. Mol. Model. , vol.12 , pp. 366-372
    • Iorga, B.1    Herlem, D.2    Barr, E.3    Guillou, C.4
  • 99
    • 34447131659 scopus 로고    scopus 로고
    • Barriers to ion translocation in cationic and anionic receptors from the Cys-loop family
    • I. Ivanov, X. Cheng, S.M. Sine, and J.A. McCammon Barriers to ion translocation in cationic and anionic receptors from the Cys-loop family J. Am. Chem. Soc. 129 2007 8217 8224
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 8217-8224
    • Ivanov, I.1    Cheng, X.2    Sine, S.M.3    McCammon, J.A.4
  • 100
    • 36549043834 scopus 로고    scopus 로고
    • Acetylcholine receptor gating at extracellular transmembrane domain interface: The Cys-Loop and M2-M3 linker
    • DOI 10.1085/jgp.200709856
    • A. Jha, D.J. Cadugan, P. Purohit, and A. Auerbach Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2 - M3 linker J. Gen. Physiol. 130 2007 547 558 (Pubitemid 350179573)
    • (2007) Journal of General Physiology , vol.130 , Issue.6 , pp. 547-558
    • Jha, A.1    Cadugan, D.J.2    Purohit, P.3    Auerbach, A.4
  • 101
    • 0024278441 scopus 로고
    • Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor
    • O.T. Jones, and M.G. McNamee Annular and nonannular binding sites for cholesterol associated with the nicotinic acetylcholine receptor Biochemistry 27 1988 2364 2374
    • (1988) Biochemistry , vol.27 , pp. 2364-2374
    • Jones, O.T.1    McNamee, M.G.2
  • 102
  • 104
    • 18744363916 scopus 로고    scopus 로고
    • A gating mechanism proposed from a simulation of a human α7 nicotinic acetylcholine receptor
    • R.J. Law, R.H. Henchman, and J.A. McCammon A gating mechanism proposed from a simulation of a human α7 nicotinic acetylcholine receptor Proc. Natl Acad. Sci. USA 102 2005 6813 6818
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 6813-6818
    • Law, R.J.1    Henchman, R.H.2    McCammon, J.A.3
  • 105
    • 0036891522 scopus 로고    scopus 로고
    • The diversity of subunit composition in nAChRs: Evolutionary origins, physiologic and pharmacologic consequences
    • N. Le Novre, P.J. Corringer, and J. -P. Changeux The diversity of subunit composition in nAChRs: evolutionary origins, physiologic and pharmacologic consequences J. Neurobiol. 53 2002 447 456
    • (2002) J. Neurobiol. , vol.53 , pp. 447-456
    • Le Novre, N.1    Corringer, P.J.2    Changeux, J.-P.3
  • 106
    • 27744438169 scopus 로고    scopus 로고
    • Principal pathway coupling agonist binding to channel gating in nicotinic receptors
    • W.Y. Lee, and S.M. Sine Principal pathway coupling agonist binding to channel gating in nicotinic receptors Nature 438 2005 243 247
    • (2005) Nature , vol.438 , pp. 243-247
    • Lee, W.Y.1    Sine, S.M.2
  • 107
    • 48649097534 scopus 로고    scopus 로고
    • Nicotinic receptor interloop proline anchors β1 - β2 and Cys loops in coupling agonist binding to channel gating
    • W.Y. Lee, C.R. Free, and S.M. Sine Nicotinic receptor interloop proline anchors β1 - β2 and Cys loops in coupling agonist binding to channel gating J. Gen. Physiol. 132 2008 265 728
    • (2008) J. Gen. Physiol. , vol.132 , pp. 265-728
    • Lee, W.Y.1    Free, C.R.2    Sine, S.M.3
  • 108
    • 63849179080 scopus 로고    scopus 로고
    • Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2 - M3 regions
    • W.Y. Lee, C.R. Free, and S.M. Sine Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2 - M3 regions J. Neurosci. 29 2009 3189 3199
    • (2009) J. Neurosci. , vol.29 , pp. 3189-3199
    • Lee, W.Y.1    Free, C.R.2    Sine, S.M.3
  • 110
    • 33646847343 scopus 로고    scopus 로고
    • Low doses of mecamylamine improve learning on the radial-arm maze repeated acquisition task
    • E.D. Levin, and D.P. Caldwell Low doses of mecamylamine improve learning on the radial-arm maze repeated acquisition task Neurobiol. Learn. Mem. 86 2006 117 122
    • (2006) Neurobiol. Learn. Mem. , vol.86 , pp. 117-122
    • Levin, E.D.1    Caldwell, D.P.2
  • 111
    • 0031928549 scopus 로고    scopus 로고
    • Nicotinic acetylcholine involvement in cognitive function in animals
    • E.D. Levin, and B.B. Simon Nicotinic acetylcholine involvement in cognitive function in animals Psychopharmacology (Berl.) 138 1998 217 230
    • (1998) Psychopharmacology (Berl.) , vol.138 , pp. 217-230
    • Levin, E.D.1    Simon, B.B.2
  • 112
    • 41249094915 scopus 로고    scopus 로고
    • α7 Nicotinic acetylcholine receptor agonists and positive allosteric modulators
    • A.P. Lightfoot, J.N.C. Kew, and J. Skidmore α7 Nicotinic acetylcholine receptor agonists and positive allosteric modulators Prog. Med. Chem. 46 2008 131 171
    • (2008) Prog. Med. Chem. , vol.46 , pp. 131-171
    • Lightfoot, A.P.1    Kew, J.N.C.2    Skidmore, J.3
  • 114
    • 34250716453 scopus 로고    scopus 로고
    • Competitive antagonism between the nicotinic allosteric potentiating ligand galantamine and kynurenic acid at α7* nicotinic receptors
    • C. Lopes, E.F. Pereira, H.Q. Wu, P. Purushottamachar, V. Njar, and R. Schwarcz Competitive antagonism between the nicotinic allosteric potentiating ligand galantamine and kynurenic acid at α7* nicotinic receptors J. Pharmacol. Exp. Ther. 322 2007 48 58
    • (2007) J. Pharmacol. Exp. Ther. , vol.322 , pp. 48-58
    • Lopes, C.1    Pereira, E.F.2    Wu, H.Q.3    Purushottamachar, P.4    Njar, V.5    Schwarcz, R.6
  • 115
    • 60149087435 scopus 로고    scopus 로고
    • Positive modulation of α7 nAChR responses in rat hippocampal interneurons to full agonists and the α7-selective partial agonists, 4OH-GTS-21 and S 24795
    • G.Y. Lpez-Hernndez, J.S. Thinschmidt, P. Morain, C. Trocme-Thibierge, W.R. Kem, and F. Soti Positive modulation of α7 nAChR responses in rat hippocampal interneurons to full agonists and the α7-selective partial agonists, 4OH-GTS-21 and S 24795 Neuropharmacology 56 2009 821 830
    • (2009) Neuropharmacology , vol.56 , pp. 821-830
    • Lpez-Hernndez, G.Y.1    Thinschmidt, J.S.2    Morain, P.3    Trocme-Thibierge, C.4    Kem, W.R.5    Soti, F.6
  • 116
    • 73449130190 scopus 로고    scopus 로고
    • Structural model for the binding sites of allosterically potentiating ligands on nicotinic acetylcholine receptors
    • E. Luttmann, J. Ludwig, A. Hffle-Maas, M. Samochocki, A. Maelicke, and G. Fels Structural model for the binding sites of allosterically potentiating ligands on nicotinic acetylcholine receptors ChemMedChem 4 2009 1874 1882
    • (2009) ChemMedChem , vol.4 , pp. 1874-1882
    • Luttmann, E.1    Ludwig, J.2    Hffle-Maas, A.3    Samochocki, M.4    Maelicke, A.5    Fels, G.6
  • 117
    • 0042355340 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in the extracellular domain of α7 nicotinic acetylcholine receptors
    • L.K. Lyford, A.D. Sproul, D. Eddins, J.T. McLaughlin, and R.L. Rosenberg Agonist-induced conformational changes in the extracellular domain of α7 nicotinic acetylcholine receptors Mol. Pharmacol. 64 2003 650 658
    • (2003) Mol. Pharmacol. , vol.64 , pp. 650-658
    • Lyford, L.K.1    Sproul, A.D.2    Eddins, D.3    McLaughlin, J.T.4    Rosenberg, R.L.5
  • 118
    • 0033845742 scopus 로고    scopus 로고
    • Allosterically potentiating ligands of nicotinic receptors as a treatment strategy for Alzheimer's disease
    • DOI 10.1016/S0166-4328(00)00214-X, PII S016643280000214X
    • A. Maelicke, A. Schrattenholz, M. Samochocki, M. Radina, and E.X. Albuquerque Allosterically potentiating ligands of nicotinic receptors as a treatment strategy for Alzheimer's disease Behav. Brain Res. 113 2000 199 206 (Pubitemid 30645557)
    • (2000) Behavioural Brain Research , vol.113 , Issue.1-2 , pp. 199-206
    • Maelicke, A.1    Schrattenholz, A.2    Samochocki, M.3    Radina, M.4    Albuquerque, E.X.5
  • 119
    • 75049085050 scopus 로고    scopus 로고
    • Memogain is a galantamine pro-drug having dramatically reduced adverse effects and enhanced efficacy
    • A. Maelicke, A. Hoeffle-Maas, J. Ludwig, A. Maus, M. Samochocki, and U. Jordis Memogain is a galantamine pro-drug having dramatically reduced adverse effects and enhanced efficacy J. Mol. Neurosci. 40 2010 135 137
    • (2010) J. Mol. Neurosci. , vol.40 , pp. 135-137
    • Maelicke, A.1    Hoeffle-Maas, A.2    Ludwig, J.3    Maus, A.4    Samochocki, M.5    Jordis, U.6
  • 120
    • 78649815741 scopus 로고    scopus 로고
    • In vitro pharmacological profile of a novel α4β2 positive allosteric modulator NS9283 (A-969933)
    • J. Malysz, T. Dyhring, P.K. Ahring, G.M. Olsen, D. Peters, and J.H. Grønlien In vitro pharmacological profile of a novel α4β2 positive allosteric modulator NS9283 (A-969933) Biochem. Pharmacol. 78 2009 919 920
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 919-920
    • Malysz, J.1    Dyhring, T.2    Ahring, P.K.3    Olsen, G.M.4    Peters, D.5    Grønlien, J.H.6
  • 121
    • 67649840644 scopus 로고    scopus 로고
    • In vitro pharmacological characterization of a novel allosteric modulator of α7 neuronal acetylcholine receptor, 4-(5-(4-chlorophenyl)-2-methyl-3- propionyl-1H-pyrrol-1-yl)benzenesulfonamide (A-867744), exhibiting unique pharmacological profile
    • J. Malysz, J.H. Grønlien, D.J. Anderson, M. Hkerud, K. Thorin-Hagene, and H. Ween In vitro pharmacological characterization of a novel allosteric modulator of α7 neuronal acetylcholine receptor, 4-(5-(4-chlorophenyl)-2-methyl-3-propionyl-1H-pyrrol-1-yl)benzenesulfonamide (A-867744), exhibiting unique pharmacological profile J. Pharmacol. Exp. Ther. 330 2009 257 267
    • (2009) J. Pharmacol. Exp. Ther. , vol.330 , pp. 257-267
    • Malysz, J.1    Grønlien, J.H.2    Anderson, D.J.3    Hkerud, M.4    Thorin-Hagene, K.5    Ween, H.6
  • 122
    • 9144244224 scopus 로고    scopus 로고
    • ARS Component B: Structural characterization, tissue expression and regulation of the gene and protein (SLURP-1) associated with Mal de Meleda
    • R. Mastrangeli, S. Donini, C.A. Kelton, C. He, A. Bressan, and F. Milazzo ARS Component B: structural characterization, tissue expression and regulation of the gene and protein (SLURP-1) associated with Mal de Meleda Eur. J. Dermatol. 13 2003 560 570
    • (2003) Eur. J. Dermatol. , vol.13 , pp. 560-570
    • Mastrangeli, R.1    Donini, S.2    Kelton, C.A.3    He, C.4    Bressan, A.5    Milazzo, F.6
  • 123
    • 47849085623 scopus 로고    scopus 로고
    • 2 nicotinic receptor expression and functional toxicity in paraoxon-treated rats
    • 2 nicotinic receptor expression and functional toxicity in paraoxon-treated rats Environ. Toxicol. Pharmacol. 26 2008 247 254
    • (2008) Environ. Toxicol. Pharmacol. , vol.26 , pp. 247-254
    • Mehrani, H.1    Asadi, B.2    Golmanesh, L.3
  • 124
    • 50449100769 scopus 로고    scopus 로고
    • Activation and block of the adult muscle-type nicotinic receptor by physostigmine: Single-channel studies
    • J. Militante, B.W. Ma, G. Akk, and J.H. Steinbach Activation and block of the adult muscle-type nicotinic receptor by physostigmine: single-channel studies Mol. Pharmacol. 74 2008 764 776
    • (2008) Mol. Pharmacol. , vol.74 , pp. 764-776
    • Militante, J.1    Ma, B.W.2    Akk, G.3    Steinbach, J.H.4
  • 125
    • 4644289077 scopus 로고    scopus 로고
    • Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating
    • DOI 10.1016/j.str.2004.08.004, PII S0969212604003089
    • A. Mitra, T.D. Bailey, and A. Auerbach Structural dynamics of the M4 transmembrane segment during acetylcholine receptor gating Structure 12 2004 1909 1918 (Pubitemid 39298974)
    • (2004) Structure , vol.12 , Issue.10 , pp. 1909-1918
    • Mitra, A.1    Bailey, T.D.2    Auerbach, A.L.3
  • 126
    • 0033136270 scopus 로고    scopus 로고
    • Lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS
    • J.M. Miwa, I. Ibanez-Tallon, G.W. Crabtree, R. Snchez, A. Sali, and L.W. Role Lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS Neuron 23 1999 105 114
    • (1999) Neuron , vol.23 , pp. 105-114
    • Miwa, J.M.1    Ibanez-Tallon, I.2    Crabtree, G.W.3    Snchez, R.4    Sali, A.5    Role, L.W.6
  • 127
    • 33748081791 scopus 로고    scopus 로고
    • The prototoxin lynx1 acts on nicotinic acetylcholine receptors to balance neuronal activity and survival in vivo
    • J.M. Miwa, T.R. Stevens, S.L. King, B.J. Caldarone, I. Ibanez-Tallon, and C. Xiao The prototoxin lynx1 acts on nicotinic acetylcholine receptors to balance neuronal activity and survival in vivo Neuron 51 2006 587 600
    • (2006) Neuron , vol.51 , pp. 587-600
    • Miwa, J.M.1    Stevens, T.R.2    King, S.L.3    Caldarone, B.J.4    Ibanez-Tallon, I.5    Xiao, C.6
  • 128
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • A. Miyazawa, Y. Fujiyoshi, and N. Unwin Structure and gating mechanism of the acetylcholine receptor pore Nature 423 2003 949 955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 129
    • 34249333064 scopus 로고    scopus 로고
    • Immune system expression of SLURP-1 and SLURP-2, two endogenous nicotinic acetylcholine receptor ligands
    • Y. Moriwaki, K. Yoshikawa, H. Fukuda, Y.X. Fujii, H. Misawa, and K. Kawashima Immune system expression of SLURP-1 and SLURP-2, two endogenous nicotinic acetylcholine receptor ligands Life Sci. 80 2007 2365 2368
    • (2007) Life Sci. , vol.80 , pp. 2365-2368
    • Moriwaki, Y.1    Yoshikawa, K.2    Fukuda, H.3    Fujii, Y.X.4    Misawa, H.5    Kawashima, K.6
  • 130
    • 67349193646 scopus 로고    scopus 로고
    • Primary sensory neuronal expression of SLURP-1, an endogenous nicotinic acetylcholine receptor ligand
    • Y. Moriwaki, Y. Watanabe, T. Shinagawa, M. Kai, M. Miyazawa, and T. Okuda Primary sensory neuronal expression of SLURP-1, an endogenous nicotinic acetylcholine receptor ligand Neurosci. Res. 64 2009 403 412
    • (2009) Neurosci. Res. , vol.64 , pp. 403-412
    • Moriwaki, Y.1    Watanabe, Y.2    Shinagawa, T.3    Kai, M.4    Miyazawa, M.5    Okuda, T.6
  • 131
    • 33746238089 scopus 로고    scopus 로고
    • α4β2 nicotinic receptors with high and low acetylcholine sensitivity: Pharmacology, stoichiometry, and sensitivity to long-term exposure to nicotine
    • M. Moroni, R. Zwart, E. Sher, B.K. Cassels, and I. Bermudez α4β2 nicotinic receptors with high and low acetylcholine sensitivity: pharmacology, stoichiometry, and sensitivity to long-term exposure to nicotine Mol. Pharmacol. 70 2006 755 768
    • (2006) Mol. Pharmacol. , vol.70 , pp. 755-768
    • Moroni, M.1    Zwart, R.2    Sher, E.3    Cassels, B.K.4    Bermudez, I.5
  • 133
    • 78649877514 scopus 로고    scopus 로고
    • Angiogenesis modulation by nicotine and nicotinic ligands
    • S.A. Mousa, and H.R. Arias Angiogenesis modulation by nicotine and nicotinic ligands J. Pediatr. Biochem. 1 2010, 91 - 104
    • (2010) J. Pediatr. Biochem. , vol.1
    • Mousa, S.A.1    Arias, H.R.2
  • 134
    • 22244478670 scopus 로고    scopus 로고
    • Initial coupling of binding to gating mediated by conserved residues in the muscle nicotinic receptor
    • N. Mukhtasimova, C. Free, and S.M. Sine Initial coupling of binding to gating mediated by conserved residues in the muscle nicotinic receptor J. Gen. Physiol. 126 2005 23 39
    • (2005) J. Gen. Physiol. , vol.126 , pp. 23-39
    • Mukhtasimova, N.1    Free, C.2    Sine, S.M.3
  • 135
    • 67349279395 scopus 로고    scopus 로고
    • Detection and trapping of intermediate states priming nicotinic receptor channel opening
    • N. Mukhtasimova, W.Y. Lee, H.L. Wang, and S.M. Sine Detection and trapping of intermediate states priming nicotinic receptor channel opening Nature 459 2009 451 454
    • (2009) Nature , vol.459 , pp. 451-454
    • Mukhtasimova, N.1    Lee, W.Y.2    Wang, H.L.3    Sine, S.M.4
  • 137
    • 73649096172 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of a bacterial ligand-gated ion channel
    • H. Nury, N. Bocquet, C. Le Poupon, B. Raynal, A. Haouz, and P. -J. Corringer Crystal structure of the extracellular domain of a bacterial ligand-gated ion channel J. Mol. Biol. 395 2010 1114 1127
    • (2010) J. Mol. Biol. , vol.395 , pp. 1114-1127
    • Nury, H.1    Bocquet, N.2    Le Poupon, C.3    Raynal, B.4    Haouz, A.5    Corringer, P.-J.6
  • 140
    • 0035037736 scopus 로고    scopus 로고
    • Analysis of mecamylamine stereoisomers on human nicotinic receptor subtypes
    • R.L. Papke, P.R. Sanberg, and R.D. Shytle Analysis of mecamylamine stereoisomers on human nicotinic receptor subtypes J. Pharmacol. Exp. Ther. 297 2001 646 656
    • (2001) J. Pharmacol. Exp. Ther. , vol.297 , pp. 646-656
    • Papke, R.L.1    Sanberg, P.R.2    Shytle, R.D.3
  • 141
    • 0035449919 scopus 로고    scopus 로고
    • The C terminus of the human nicotinic α4β2 receptor forms a binding site required for potentiation by an estrogenic steroid
    • K. Paradiso, J. Zhang, and J.H. Steinbach The C terminus of the human nicotinic α4β2 receptor forms a binding site required for potentiation by an estrogenic steroid J. Neurosci. 21 2001 6561 6568
    • (2001) J. Neurosci. , vol.21 , pp. 6561-6568
    • Paradiso, K.1    Zhang, J.2    Steinbach, J.H.3
  • 144
    • 33751092270 scopus 로고    scopus 로고
    • The nicotinic antagonist mecamylamine has antidepressant-like effects in wild-type but not β2- or α7-nicotinic acetylcholine receptor subunit knockout mice
    • R.L. Rabenstein, B.J. Caldarone, and M.R. Picciotto The nicotinic antagonist mecamylamine has antidepressant-like effects in wild-type but not β2- or α7-nicotinic acetylcholine receptor subunit knockout mice Psychopharmacology (Berl.) 189 2006 395 401
    • (2006) Psychopharmacology (Berl.) , vol.189 , pp. 395-401
    • Rabenstein, R.L.1    Caldarone, B.J.2    Picciotto, M.R.3
  • 146
    • 65949085351 scopus 로고    scopus 로고
    • Number and locations of agonist binding sites required to activate homomeric Cys-loop receptors
    • D. Rayes, M.J. De Rosa, S.M. Sine, and C. Bouzat Number and locations of agonist binding sites required to activate homomeric Cys-loop receptors J. Neurosci. 29 2009 6022 6032
    • (2009) J. Neurosci. , vol.29 , pp. 6022-6032
    • Rayes, D.1    De Rosa, M.J.2    Sine, S.M.3    Bouzat, C.4
  • 147
    • 33746653795 scopus 로고    scopus 로고
    • A placebo controlled, double-blind study of mecamylamine treatment for cocaine dependence in patients enrolled in an opiate replacement program
    • M.S. Reid, B. Angrist, S.A. Baker, S. O'leary, J. Stone, and M. Schwartz A placebo controlled, double-blind study of mecamylamine treatment for cocaine dependence in patients enrolled in an opiate replacement program Subst. Abus. 26 2005 5 14
    • (2005) Subst. Abus. , vol.26 , pp. 5-14
    • Reid, M.S.1    Angrist, B.2    Baker, S.A.3    O'Leary, S.4    Stone, J.5    Schwartz, M.6
  • 148
    • 9644290891 scopus 로고    scopus 로고
    • Potentiation of human α4β2 neuronal nicotinic receptors by a Flustra foliacea metabolite
    • F. Sala, J. Mulet, K.P. Reddy, J.A. Bernal, P. Wikman, and L.M. Valor Potentiation of human α4β2 neuronal nicotinic receptors by a Flustra foliacea metabolite Neurosci. Lett. 373 2005 144 149
    • (2005) Neurosci. Lett. , vol.373 , pp. 144-149
    • Sala, F.1    Mulet, J.2    Reddy, K.P.3    Bernal, J.A.4    Wikman, P.5    Valor, L.M.6
  • 149
    • 10744232323 scopus 로고    scopus 로고
    • Galantamine is an allosterically potentiating ligand of neuronal nicotinic but not of muscarinic acetylcholine receptors
    • M. Samochocki, A. Hoffle, A. Fehrenbacher, R. Jostock, J. Ludwig, and C. Christner Galantamine is an allosterically potentiating ligand of neuronal nicotinic but not of muscarinic acetylcholine receptors J. Pharmacol. Exp. Ther. 305 2003 1024 1036
    • (2003) J. Pharmacol. Exp. Ther. , vol.305 , pp. 1024-1036
    • Samochocki, M.1    Hoffle, A.2    Fehrenbacher, A.3    Jostock, R.4    Ludwig, J.5    Christner, C.6
  • 150
    • 68349125400 scopus 로고    scopus 로고
    • Comparative pharmacology and computational modelling yield insights into allosteric modulation of human α7 nicotinic acetylcholine receptors
    • D.B. Sattelle, S.D. Buckingham, M. Akamatsu, K. Matsuda, I.S. Pienaar, and A.K. Jones Comparative pharmacology and computational modelling yield insights into allosteric modulation of human α7 nicotinic acetylcholine receptors Biochem. Pharmacol. 78 2009 836 843
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 836-843
    • Sattelle, D.B.1    Buckingham, S.D.2    Akamatsu, M.3    Matsuda, K.4    Pienaar, I.S.5    Jones, A.K.6
  • 152
    • 18844368234 scopus 로고    scopus 로고
    • Expression of lynx1 in developing lung and its modulation by prenatal nicotine exposure
    • H.S. Sekhon, P. Song, Y. Jia, J. Lindstrom, and E.R. Spindel Expression of lynx1 in developing lung and its modulation by prenatal nicotine exposure Cell Tissue Res. 320 2005 287 297
    • (2005) Cell Tissue Res. , vol.320 , pp. 287-297
    • Sekhon, H.S.1    Song, P.2    Jia, Y.3    Lindstrom, J.4    Spindel, E.R.5
  • 153
    • 67650473173 scopus 로고    scopus 로고
    • The positive allosteric modulator morantel binds at noncanonical subunit interfaces of neuronal nicotinic acetylcholine receptors
    • S. Seo, J.T. Henry, A.H. Lewis, N. Wang, and M.M. Levandoski The positive allosteric modulator morantel binds at noncanonical subunit interfaces of
    • (2009) J. Neurosci. , vol.29 , pp. 8734-8742
    • Seo, S.1    Henry, J.T.2    Lewis, A.H.3    Wang, N.4    Levandoski, M.M.5
  • 155
    • 0036431617 scopus 로고    scopus 로고
    • Neuronal nicotinic receptor inhibition for treating mood disorders: Preliminary controlled evidence with mecamylamine
    • R.D. Shytle, A.A. Silver, K.H. Sheehan, D.V. Sheehan, and P.R. Sanberg Neuronal nicotinic receptor inhibition for treating mood disorders: preliminary controlled evidence with mecamylamine Depress. Anxiety 16 2002 89 92
    • (2002) Depress. Anxiety , vol.16 , pp. 89-92
    • Shytle, R.D.1    Silver, A.A.2    Sheehan, K.H.3    Sheehan, D.V.4    Sanberg, P.R.5
  • 156
    • 33645302360 scopus 로고    scopus 로고
    • Recent advances in Cys-loop receptor structure and function
    • S.M. Sine, and A.G. Engel Recent advances in Cys-loop receptor structure and function Nature 440 2006 448 455
    • (2006) Nature , vol.440 , pp. 448-455
    • Sine, S.M.1    Engel, A.G.2
  • 157
    • 69949143152 scopus 로고    scopus 로고
    • Zinc supplementation augments efficacy of imipramine in treatment resistant patients: A double blind, placebo-controlled study
    • M. Siwek, D. Dudek, I.A. Paul, M. Sowa-Kuma, A. Zieba, and P. Popik Zinc supplementation augments efficacy of imipramine in treatment resistant patients: a double blind, placebo-controlled study J. Affect. Disord. 118 2009 187 195
    • (2009) J. Affect. Disord. , vol.118 , pp. 187-195
    • Siwek, M.1    Dudek, D.2    Paul, I.A.3    Sowa-Kuma, M.4    Zieba, A.5    Popik, P.6
  • 160
    • 49649125178 scopus 로고    scopus 로고
    • Activated cholinergic signaling provides a target in squamous cell lung carcinoma
    • P. Song, H.S. Sekhon, X.W. Fu, M. Maier, Y. Jia, and J. Duan Activated cholinergic signaling provides a target in squamous cell lung carcinoma Cancer Res. 68 2008 4693 4700
    • (2008) Cancer Res. , vol.68 , pp. 4693-4700
    • Song, P.1    Sekhon, H.S.2    Fu, X.W.3    Maier, M.4    Jia, Y.5    Duan, J.6
  • 161
    • 0034925442 scopus 로고    scopus 로고
    • The noncompetitive inhibitor quinacrine modifies the desensitization kinetics of muscle acetylcholine receptors
    • G. Spitzmaul, J.P. Dilger, and C. Bouzat The noncompetitive inhibitor quinacrine modifies the desensitization kinetics of muscle acetylcholine receptors Mol. Pharmacol. 60 2001 235 243
    • (2001) Mol. Pharmacol. , vol.60 , pp. 235-243
    • Spitzmaul, G.1    Dilger, J.P.2    Bouzat, C.3
  • 162
    • 70350161799 scopus 로고    scopus 로고
    • The local anaesthetics proadifen and adiphenine inhibit nicotinic receptors by different molecular mechanisms
    • G. Spitzmaul, F. Gumilar, J.P. Dilger, and C. Bouzat The local anaesthetics proadifen and adiphenine inhibit nicotinic receptors by different molecular mechanisms Br. J. Pharmacol. 157 2009 804 817
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 804-817
    • Spitzmaul, G.1    Gumilar, F.2    Dilger, J.P.3    Bouzat, C.4
  • 163
    • 0028984453 scopus 로고
    • Physostigmine, galanthamine and codeine act as 'noncompetitive nicotinic receptor agonists' on clonal rat pheochromocytoma cells
    • A. Storch, A. Schrattenholz, J.C. Cooper, E.M. Abdel Ghani, O. Gutbrod, and K.H. Weber Physostigmine, galanthamine and codeine act as 'noncompetitive nicotinic receptor agonists' on clonal rat pheochromocytoma cells Eur. J. Pharmacol. 290 1995 207 219
    • (1995) Eur. J. Pharmacol. , vol.290 , pp. 207-219
    • Storch, A.1    Schrattenholz, A.2    Cooper, J.C.3    Abdel Ghani, E.M.4    Gutbrod, O.5    Weber, K.H.6
  • 166
    • 26944443142 scopus 로고    scopus 로고
    • Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels
    • A. Tasneem, L.M. Iyer, E. Jakobsson, and L. Aravind Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels Genome Biol. 6 2005 R4
    • (2005) Genome Biol. , vol.6 , pp. 4
    • Tasneem, A.1    Iyer, L.M.2    Jakobsson, E.3    Aravind, L.4
  • 168
    • 0344603807 scopus 로고    scopus 로고
    • Dose-specific improvements in memory-related task performance by rats and aged monkeys administered the nicotinic-cholinergic antagonist mecamylamine
    • A.V. Terry Jr., J.J. Buccafusco, and M.A. Prendergast Dose-specific improvements in memory-related task performance by rats and aged monkeys administered the nicotinic-cholinergic antagonist mecamylamine Drug Dev. Res. 47 1999 127 136
    • (1999) Drug Dev. Res. , vol.47 , pp. 127-136
    • Terry, Jr.A.V.1    Buccafusco, J.J.2    Prendergast, M.A.3
  • 169
    • 34548689531 scopus 로고    scopus 로고
    • An allosteric modulator of the α7 nicotinic acetylcholine receptor possessing cognition-enhancing properties in vivo
    • D.B. Timmermann, J.H. Grønlien, K.L. Kohlhaas, E.Ø. Nielsen, E. Dam, and T.D. Jørgensen An allosteric modulator of the α7 nicotinic acetylcholine receptor possessing cognition-enhancing properties in vivo J. Pharmacol. Exp. Ther. 323 2007 294 307
    • (2007) J. Pharmacol. Exp. Ther. , vol.323 , pp. 294-307
    • Timmermann, D.B.1    Grønlien, J.H.2    Kohlhaas, K.L.3    Nielsen E.Ø4    Dam, E.5    Jørgensen, T.D.6
  • 171
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 resolution
    • N. Unwin Refined structure of the nicotinic acetylcholine receptor at 4 resolution J. Mol. Biol. 346 2005 967 989
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 172
    • 67349087957 scopus 로고    scopus 로고
    • Neuronal nicotinic acetylcholine receptors are modulated by zinc
    • E. Vzquez-Gmez, and J. Garca-Colunga Neuronal nicotinic acetylcholine receptors are modulated by zinc Neuropharmacology 56 2009 1035 1040
    • (2009) Neuropharmacology , vol.56 , pp. 1035-1040
    • Vzquez-Gmez, E.1    Garca-Colunga, J.2
  • 173
    • 0033712121 scopus 로고    scopus 로고
    • The actions of synaptically released zinc in hippocampal mossy fiber synapses
    • K. Vogt, J. Mellor, G. Tong, and R. Nicoll The actions of synaptically released zinc in hippocampal mossy fiber synapses Neuron 26 2000 187 196
    • (2000) Neuron , vol.26 , pp. 187-196
    • Vogt, K.1    Mellor, J.2    Tong, G.3    Nicoll, R.4
  • 174
    • 0032784581 scopus 로고    scopus 로고
    • Antagonist activities of mecamylamine and nicotine show reciprocal dependence on beta subunit sequence in the second transmembrane domain
    • J.C. Webster, M.M. Francis, J.K. Porter, G. Robinson, C. Stokes, and B. Horenstein Antagonist activities of mecamylamine and nicotine show reciprocal dependence on beta subunit sequence in the second transmembrane domain Br. J. Pharmacol. 127 1999 1337 1348
    • (1999) Br. J. Pharmacol. , vol.127 , pp. 1337-1348
    • Webster, J.C.1    Francis, M.M.2    Porter, J.K.3    Robinson, G.4    Stokes, C.5    Horenstein, B.6
  • 175
    • 77956252951 scopus 로고    scopus 로고
    • Pharmacological characterization of the allosteric modulator desformylflustrabromine and its interaction with α4β2 neuronal nicotinic acetylcholine receptor orthosteric ligands
    • M.M. Weltzin, and M.K. Schulte Pharmacological characterization of the allosteric modulator desformylflustrabromine and its interaction with α4β2 neuronal nicotinic acetylcholine receptor orthosteric ligands J. Pharmacol. Exp. Ther. 334 2010 917 926
    • (2010) J. Pharmacol. Exp. Ther. , vol.334 , pp. 917-926
    • Weltzin, M.M.1    Schulte, M.K.2
  • 176
    • 29244442919 scopus 로고    scopus 로고
    • A unified view of the role of electrostatic interactions in modulating the gating of Cys loop receptors
    • X. Xiu, A.P. Hanek, J. Wang, H.A. Lester, and D.A. Dougherty A unified view of the role of electrostatic interactions in modulating the gating of Cys loop receptors J. Biol. Chem. 280 2005 41655 41666
    • (2005) J. Biol. Chem. , vol.280 , pp. 41655-41666
    • Xiu, X.1    Hanek, A.P.2    Wang, J.3    Lester, H.A.4    Dougherty, D.A.5
  • 178
    • 55749111553 scopus 로고    scopus 로고
    • Potentiation of α7 nicotinic acetylcholine receptors via an allosteric transmembrane site
    • G.T. Young, R. Zwart, A.S. Walker, E. Sher, and N.S. Millar Potentiation of α7 nicotinic acetylcholine receptors via an allosteric transmembrane site Proc. Natl. Acad. Sci. USA 105 2008 14686 14691
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14686-14691
    • Young, G.T.1    Zwart, R.2    Walker, A.S.3    Sher, E.4    Millar, N.S.5
  • 179
    • 2342582222 scopus 로고    scopus 로고
    • Bioactivity of a peptide derived from acetylcholinesterase: Involvement of an ivermectin-sensitive site on the α7 nicotinic receptor
    • V. Zbarsky, J. Thomas, and S. Greenfield Bioactivity of a peptide derived from acetylcholinesterase: involvement of an ivermectin-sensitive site on the α7 nicotinic receptor Neurobiol. Dis. 16 2004 283 289
    • (2004) Neurobiol. Dis. , vol.16 , pp. 283-289
    • Zbarsky, V.1    Thomas, J.2    Greenfield, S.3
  • 180
    • 61349196895 scopus 로고    scopus 로고
    • U18666A, a cholesterol-inhibition agent, modulates human neuronal nicotinic acetylcholine receptors heterologously expressed in SH-EP1 cell line
    • C. Zheng, M.Y. Wang, Q. Liu, M. Wakui, P. Whiteaker, and R.J. Lukas U18666A, a cholesterol-inhibition agent, modulates human neuronal nicotinic acetylcholine receptors heterologously expressed in SH-EP1 cell line J. Neurochem. 108 2009 1526 1538
    • (2009) J. Neurochem. , vol.108 , pp. 1526-1538
    • Zheng, C.1    Wang, M.Y.2    Liu, Q.3    Wakui, M.4    Whiteaker, P.5    Lukas, R.J.6
  • 181
    • 0030842275 scopus 로고    scopus 로고
    • Potentiation and inhibition of neuronal nicotinic receptors by atropine: Competitive and noncompetitive effects
    • R. Zwart, and H.P.M. Vijverberg Potentiation and inhibition of neuronal nicotinic receptors by atropine: competitive and noncompetitive effects Mol. Pharmacol. 52 1997 886 895
    • (1997) Mol. Pharmacol. , vol.52 , pp. 886-895
    • Zwart, R.1    Vijverberg, H.P.M.2
  • 182
    • 0034732163 scopus 로고    scopus 로고
    • Potentiation and inhibition of neuronal α4β4 nicotinic acetylcholine receptors by choline
    • R. Zwart, and H.P.M. Vijverberg Potentiation and inhibition of neuronal α4β4 nicotinic acetylcholine receptors by choline Eur. J. Pharmacol. 393 2000 209 214
    • (2000) Eur. J. Pharmacol. , vol.393 , pp. 209-214
    • Zwart, R.1    Vijverberg, H.P.M.2
  • 183
    • 0036711318 scopus 로고    scopus 로고
    • 5-Hydroxyindole potentiates human α7 nicotinic receptor-mediated responses and enhances acetylcholine-induced glutamate release in cerebellar slices
    • R. Zwart, G. De Filippi, L.M. Broad, G.I. McPhie, K.H. Pearson, and T. Baldwinson 5-Hydroxyindole potentiates human α7 nicotinic receptor-mediated responses and enhances acetylcholine-induced glutamate release in cerebellar slices Neuropharmacology 43 2002 374 384
    • (2002) Neuropharmacology , vol.43 , pp. 374-384
    • Zwart, R.1    De Filippi, G.2    Broad, L.M.3    McPhie, G.I.4    Pearson, K.H.5    Baldwinson, T.6
  • 184
    • 33744473099 scopus 로고    scopus 로고
    • 5-I A-85380 and TC-2559 differentially activate heterologously expressed α4β2 nicotinic receptors
    • R. Zwart, L.M. Broad, Q. Xi, M. Lee, M. Moroni, and I. Bermudez 5-I A-85380 and TC-2559 differentially activate heterologously expressed α4β2 nicotinic receptors Eur. J. Pharmacol. 539 2006 10 17
    • (2006) Eur. J. Pharmacol. , vol.539 , pp. 10-17
    • Zwart, R.1    Broad, L.M.2    Xi, Q.3    Lee, M.4    Moroni, M.5    Bermudez, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.