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Volumn 61, Issue 8, 2011, Pages 1306-1313

Competitive binding at a nicotinic receptor transmembrane site of two α7-selective positive allosteric modulators with differing effects on agonist-evoked desensitization

Author keywords

Acetylcholine receptor; Ligand gated ion channel; Nicotinic receptor; Positive allosteric modulator

Indexed keywords

BUNGAROTOXIN RECEPTOR; CHOLINERGIC RECEPTOR AFFECTING AGENT; NS 1738; PNU 120596; UNCLASSIFIED DRUG;

EID: 80053618320     PISSN: 00283908     EISSN: 18737064     Source Type: Journal    
DOI: 10.1016/j.neuropharm.2011.07.035     Document Type: Article
Times cited : (55)

References (41)
  • 1
    • 34548677767 scopus 로고    scopus 로고
    • Allosteric modulation of nicotinic acetylcholine receptors
    • DOI 10.1016/j.bcp.2007.07.011, PII S0006295207004637
    • D. Bertrand, and M. Gopalakrishnan Allosteric modulation of nicotinic acetylcholine receptors Biochem. Pharmacol. 74 2007 1155 1163 (Pubitemid 47417931)
    • (2007) Biochemical Pharmacology , vol.74 , Issue.8 , pp. 1155-1163
    • Bertrand, D.1    Gopalakrishnan, M.2
  • 2
    • 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. Casser, 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    Casser, S.3    Gubbins, E.4    Li, J.5    Gopalakrishnan, M.6
  • 3
    • 33748927492 scopus 로고    scopus 로고
    • Incorporation of the β3 subunit has a dominant-negative effect on the function of recombinant central-type neuronal nicotinic receptors
    • S. Broadbent, P.J. Groot-Kormelink, P.A. Krashia, P.C. Harkness, N.S. Millar, M. Beato, and L.G. Sivilotti Incorporation of the β3 subunit has a dominant-negative effect on the function of recombinant central-type neuronal nicotinic receptors Mol. Pharmacol. 70 2006 1350 1356
    • (2006) Mol. Pharmacol. , vol.70 , pp. 1350-1356
    • Broadbent, S.1    Groot-Kormelink, P.J.2    Krashia, P.A.3    Harkness, P.C.4    Millar, N.S.5    Beato, M.6    Sivilotti, L.G.7
  • 4
    • 28844448877 scopus 로고    scopus 로고
    • Channel opening motion of α7 nicotinic acetylcholine receptor as suggested by normal mode analysis
    • DOI 10.1016/j.jmb.2005.10.039, PII S0022283605012830
    • X. Cheng, L. Benzhuo, B. Grant, R.J. Law, and J.A. McCammon Channel opening motion of α7 nicotinic acetylcholine receptor as suggested by normal mode analysis J. Mol. Biol. 355 2006 310 324 (Pubitemid 41774133)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.2 , pp. 310-324
    • Cheng, X.1    Lu, B.2    Grant, B.3    Law, R.J.4    McCammon, J.A.5
  • 5
    • 35348968348 scopus 로고    scopus 로고
    • Nanosecond-timescale conformational dynamics of the human α7 nicotinic acetylcholine receptor
    • DOI 10.1529/biophysj.107.109843
    • X. Cheng, I. Ivanov, H. Wang, S.M. Sine, and J.A. McCammon Nanosecond-timescale conformational dynamics of the human α7 nicotinic acetylcholine receptor Biophys. J. 93 2007 2622 2634 (Pubitemid 47607800)
    • (2007) Biophysical Journal , vol.93 , Issue.8 , pp. 2622-2634
    • Cheng, X.1    Ivanov, I.2    Wang, H.3    Sine, S.M.4    McCammon, J.A.5
  • 6
    • 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
  • 8
    • 0025605864 scopus 로고
    • A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BTX
    • S. Couturier, D. Bertrand, J.M. Matter, M.C. Hernandez, S. Bertrand, N. Millar, S. Valera, T. Barkas, and M. Ballivet A neuronal nicotinic acetylcholine receptor subunit (α7) is developmentally regulated and forms a homo-oligomeric channel blocked by α-BTX Neuron 5 1990 847 856
    • (1990) Neuron , vol.5 , pp. 847-856
    • Couturier, S.1    Bertrand, D.2    Matter, J.M.3    Hernandez, M.C.4    Bertrand, S.5    Millar, N.6    Valera, S.7    Barkas, T.8    Ballivet, M.9
  • 10
    • 39749152191 scopus 로고    scopus 로고
    • Allosteric modulators of the α7 nicotinic acetylcholine receptor
    • DOI 10.1021/jm070256g
    • R. Faghih, M. Gopalakrishnan, and C.A. Briggs Allosteric modulators of the α7 nicotinic acetylcholine receptor J. Med. Chem. 51 2008 701 712 (Pubitemid 351307795)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.4 , pp. 701-712
    • Faghih, R.1    Gopalakrishnan, M.2    Briggs, C.A.3
  • 11
    • 35148898880 scopus 로고    scopus 로고
    • 3H]benzophenone photolabeling identifies state-dependent changes in nicotinic acetylcholine receptor structure
    • DOI 10.1021/bi7008163
    • 3H]Benzophenone photolabeling identifies state-dependent changes in nicotinic acetylcholine receptor structure Biochemistry 46 2007 10296 10307 (Pubitemid 350067623)
    • (2007) Biochemistry , vol.46 , Issue.36 , pp. 10296-10307
    • Garcia III, G.1    Chiara, D.C.2    Nirthanan, S.3    Hamouda, A.K.4    Stewart, D.S.5    Cohen, J.B.6
  • 12
  • 13
    • 34548301101 scopus 로고    scopus 로고
    • Distinct profiles of α7 nAChR positive allosteric modulation revealed by structurally diverse chemotypes
    • DOI 10.1124/mol.107.035410
    • J.H. Grønlien, M. Hkerud, H. Ween, K. Thorin-Hagene, C.A. Briggs, M. Gopalakrishnan, and J. Malysz Distinct profiles of α7 nAChR positive allosteric modulation revealed by structurally diverse chemotypes Mol. Pharmacol. 72 2007 715 724 (Pubitemid 47347306)
    • (2007) Molecular Pharmacology , vol.72 , Issue.3 , pp. 715-724
    • Gronlien, J.H.1    Hakerud, M.2    Ween, H.3    Thorin-Hagene, K.4    Briggs, C.A.5    Gopalakrishnan, M.6    Malysz, J.7
  • 15
    • 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
    • DOI 10.1016/j.jmb.2007.03.067, PII S0022283607004354
    • 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 (Pubitemid 46754061)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.4 , pp. 895-901
    • Hansen, S.B.1    Taylor, P.2
  • 16
    • 77949422530 scopus 로고    scopus 로고
    • Neuronal nicotinic acetylcholine receptors - Targets for the development of drugs to treat cognitive impairment associated with schizophrenia and Alzheimer's disease
    • S.N. Haydar, and J. Dunlop Neuronal nicotinic acetylcholine receptors - targets for the development of drugs to treat cognitive impairment associated with schizophrenia and Alzheimer's disease Curr. Top. Med. Chem. 10 2010 144 152
    • (2010) Curr. Top. Med. Chem. , vol.10 , pp. 144-152
    • Haydar, S.N.1    Dunlop, J.2
  • 17
    • 32344440995 scopus 로고    scopus 로고
    • Blind docking of drug-sized compounds to proteins with up to a thousand residues
    • DOI 10.1016/j.febslet.2006.01.074, PII S001457930600144X
    • C. Hetényi, and D. van der Spoel Blind docking of drug-sized compounds to proteins with up to a thousand residues FEBS Lett. 580 2006 1447 1450 (Pubitemid 43222013)
    • (2006) FEBS Letters , vol.580 , Issue.5 , pp. 1447-1450
    • Hetenyi, C.1    Van Der Spoel, D.2
  • 18
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • R.E. Hibbs, and E. Gouaux Principles of activation and permeation in an anion-selective Cys-loop receptor Nature 474 2011 54 60
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 19
    • 33751314737 scopus 로고    scopus 로고
    • A receptors through two discrete transmembrane sites
    • DOI 10.1038/nature05324, PII NATURE05324
    • A receptors through two different discrete transmembrane sites Nature 444 2006 486 489 (Pubitemid 44809065)
    • (2006) Nature , vol.444 , Issue.7118 , pp. 486-489
    • Hosie, A.M.1    Wilkins, M.E.2    Da Silva, H.M.A.3    Smart, T.G.4
  • 20
    • 33947716119 scopus 로고    scopus 로고
    • Software news and update a semiempirical free energy force field with charge-based desolvation
    • DOI 10.1002/jcc.20634
    • R. Huey, G.M. Morris, A.J. Olson, and D.S. Goodsell A semiemprical free energy force field with charge-based desolvation J. Comput. Chem. 28 2007 1145 1152 (Pubitemid 46506716)
    • (2007) Journal of Computational Chemistry , vol.28 , Issue.6 , pp. 1145-1152
    • Huey, R.1    Morris, G.M.2    Olson, A.J.3    Goodsell, D.S.4
  • 23
    • 78649640881 scopus 로고    scopus 로고
    • Localization by site-directed mutagenesis of a galantamine binding site on α7 nicotinic acetylcholine receptor extracellular domain
    • J. Ludwig, A. Höffle-Mass, M. Samochocki, E. Luttmann, E.X. Albuquerque, G. Fels, and A. Maelicke Localization by site-directed mutagenesis of a galantamine binding site on α7 nicotinic acetylcholine receptor extracellular domain J. Recep. Signal Trans. 30 2010 469 483
    • (2010) J. Recep. Signal Trans. , vol.30 , pp. 469-483
    • Ludwig, J.1    Höffle-Mass, A.2    Samochocki, M.3    Luttmann, E.4    Albuquerque, E.X.5    Fels, G.6    Maelicke, A.7
  • 26
    • 58049091080 scopus 로고    scopus 로고
    • Diversity of vertebrate nicotinic acetylcholine receptors
    • N.S. Millar, and C. Gotti Diversity of vertebrate nicotinic acetylcholine receptors Neuropharmacology 56 2009 237 246
    • (2009) Neuropharmacology , vol.56 , pp. 237-246
    • Millar, N.S.1    Gotti, C.2
  • 27
    • 0024623211 scopus 로고
    • Genetic manipulation of ion channel: A new approach to structure and mechanism
    • C. Miller Genetic manipulation of ion channel: a new approach to structure and mechanism Neuron 2 1989 1195 1205
    • (1989) Neuron , vol.2 , pp. 1195-1205
    • Miller, C.1
  • 30
    • 0021740393 scopus 로고
    • Nicotinic receptor of acetylcholine: Structure of an oligomeric integral membrane protein
    • J.-L. Popot, and J.-P. Changeux Nicotinic receptor of acetylcholine: structure of an oligomeric integral membrane protein Physiol. Rev. 64 1984 1162 1239 (Pubitemid 15218056)
    • (1984) Physiological Reviews , vol.64 , Issue.4 , pp. 1162-1239
    • Popot, J.-L.1    Changeux, J.-P.2
  • 33
    • 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 neuronal nicotinic acetylcholine receptors J. Neurosci. 29 2009 8734 8742
    • (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
  • 34
    • 0027518923 scopus 로고
    • 7: A nicotinic cation channel highly permeable to calcium
    • P. Séguéla, J. Wadiche, K. Dineley-Miller, J.A. Dani, and J.W. Patrick Molecular cloning, functional properties, and distribution of rat brain α7: a nicotinic cation channel highly permeable to calcium J. Neurosci. 13 1993 596 604 (Pubitemid 23045143)
    • (1993) Journal of Neuroscience , vol.13 , Issue.2 , pp. 596-604
    • Seguela, P.1    Wadiche, J.2    Dineley-Miller, K.3    Dani, J.A.4    Patrick, J.W.5
  • 35
    • 69949159308 scopus 로고    scopus 로고
    • Nicotinic receptors: Allosteric transitions and therapeutic targets in the nervous system
    • A. Taly, P.-J. Corringer, D. Guedin, P. Lestage, and J.-P. Changeux Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system Nat. Rev. Drug Discov. 8 2009 733 750
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 733-750
    • Taly, A.1    Corringer, P.-J.2    Guedin, D.3    Lestage, P.4    Changeux, J.-P.5
  • 37
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 à resolution
    • DOI 10.1016/j.jmb.2004.12.031
    • N. Unwin Refined structure of the nicotinic acetylcholine receptor at 4 resolution J. Mol. Biol. 346 2005 967 989 (Pubitemid 40215523)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 39
    • 33846433512 scopus 로고    scopus 로고
    • Species selectivity of a nicotinic acetylcholine receptor agonist is conferred by two adjacent extracellular β4 amino acids that are implicated in the coupling of binding to channel gating
    • DOI 10.1124/mol.106.030809
    • G.T. Young, L.M. Broad, R. Zwart, P.C. Astles, M. Bodkin, E. Sher, and N.S. Millar Species selectivity of a nicotinic acetylcholine receptor agonist is conferred by two adjacent extracellular β4 amino acids that are implicated in the coupling of binding to channel gating Mol. Pharmacol. 71 2007 389 397 (Pubitemid 46147905)
    • (2007) Molecular Pharmacology , vol.71 , Issue.2 , pp. 389-397
    • Young, G.T.1    Broad, L.M.2    Zwart, R.3    Astles, P.C.4    Bodkin, M.5    Sher, E.6    Millar, N.S.7
  • 40
    • 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. U S A 105 2008 14686 14691
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , pp. 14686-14691
    • Young, G.T.1    Zwart, R.2    Walker, A.S.3    Sher, E.4    Millar, N.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.