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Volumn 14, Issue 3, 2016, Pages

Erratum: Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels (Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels (PLoS Biology (2016) 14:3 (e1002393) DOI: 10.1371/journal.pbio.1002393);Signal Transduction at the Domain Interface of Prokaryotic Pentameric Ligand-Gated Ion Channels

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; ALANINE; ASPARTIC ACID; HISTIDINE; LIGAND GATED ION CHANNEL; PHENYLALANINE; PROLINE;

EID: 84962164539     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1002490     Document Type: Erratum
Times cited : (38)

References (71)
  • 1
    • 69949159308 scopus 로고    scopus 로고
    • Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system
    • 19721446, .;():–.
    • Taly A, Corringer PJ, Guedin D, Lestage P, Changeux JP, Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system. Nat Rev Drug Discov. 2009;8(9):733–50. 19721446. doi: 10.1038/nrd2927
    • (2009) Nat Rev Drug Discov , vol.8 , Issue.9 , pp. 733-750
    • Taly, A.1    Corringer, P.J.2    Guedin, D.3    Lestage, P.4    Changeux, J.P.5
  • 2
    • 33645302360 scopus 로고    scopus 로고
    • Recent advances in Cys-loop receptor structure and function
    • 16554804, .;():–.
    • Sine SM, Engel AG, Recent advances in Cys-loop receptor structure and function. Nature. 2006;440(7083):448–55. 16554804.
    • (2006) Nature , vol.440 , Issue.7083 , pp. 448-455
    • Sine, S.M.1    Engel, A.G.2
  • 3
    • 0014115893 scopus 로고
    • On the application of "a plausible model" of allosteric proteins to the receptor for acetylcholine
    • 6048545, .;():–.
    • Karlin A, On the application of "a plausible model" of allosteric proteins to the receptor for acetylcholine. J Theor Biol. 1967;16(2):306–20. 6048545.
    • (1967) J Theor Biol , vol.16 , Issue.2 , pp. 306-320
    • Karlin, A.1
  • 4
    • 0031745831 scopus 로고    scopus 로고
    • Allosteric transitions of the acetylcholine receptor
    • 9615170, .;:–.
    • Edelstein SJ, Changeux JP, Allosteric transitions of the acetylcholine receptor. Adv Protein Chem. 1998;51:121–84. 9615170.
    • (1998) Adv Protein Chem , vol.51 , pp. 121-184
    • Edelstein, S.J.1    Changeux, J.P.2
  • 5
    • 84855175213 scopus 로고    scopus 로고
    • Thinking in cycles: MWC is a good model for acetylcholine receptor-channels
    • 21807612, .;():–.
    • Auerbach A, Thinking in cycles: MWC is a good model for acetylcholine receptor-channels. J Physiol. 2012;590(Pt 1):93–8. doi: 10.1113/jphysiol.2011.21468421807612.
    • (2012) J Physiol , vol.590 , pp. 93-98
    • Auerbach, A.1
  • 6
    • 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
    • 15642096, .;():.
    • Tasneem A, Iyer LM, Jakobsson E, Aravind L, Identification of the prokaryotic ligand-gated ion channels and their implications for the mechanisms and origins of animal Cys-loop ion channels. Genome Biol. 2005;6(1):R4. 15642096.
    • (2005) Genome Biol , vol.6 , Issue.1 , pp. R4
    • Tasneem, A.1    Iyer, L.M.2    Jakobsson, E.3    Aravind, L.4
  • 8
    • 33846106078 scopus 로고    scopus 로고
    • A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family
    • 17167423, ..;():–.
    • Bocquet N, Prado de Carvalho L, Cartaud J, Neyton J, Le Poupon C, Taly A, et al. A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family. Nature. 2007;445(7123):116–9. 17167423.
    • (2007) Nature , vol.445 , Issue.7123 , pp. 116-119
    • Bocquet, N.1    Prado de Carvalho, L.2    Cartaud, J.3    Neyton, J.4    Le Poupon, C.5    Taly, A.6
  • 9
    • 79959775185 scopus 로고    scopus 로고
    • Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC
    • 21713033, .;():. Epub 2011/06/30.
    • Zimmermann I, Dutzler R, Ligand activation of the prokaryotic pentameric ligand-gated ion channel ELIC. PLoS Biol. 2011;9(6):e1001101. Epub 2011/06/30. doi: 10.1371/journal.pbio.100110121713033.
    • (2011) PLoS Biol , vol.9 , Issue.6 , pp. e1001101
    • Zimmermann, I.1    Dutzler, R.2
  • 10
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4A resolution
    • 15701510, .;():–.
    • Unwin N, Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J Mol Biol. 2005;346(4):967–89. 15701510.
    • (2005) J Mol Biol , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 11
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • 12827192, .;():–.
    • Miyazawa A, Fujiyoshi Y, Unwin N, Structure and gating mechanism of the acetylcholine receptor pore. Nature. 2003;423(6943):949–55. 12827192.
    • (2003) Nature , vol.423 , Issue.6943 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 12
    • 84944273234 scopus 로고    scopus 로고
    • Glycine receptor mechanism elucidated by electron cryo-microscopy
    • 26344198, .;():–.
    • Du J, Lu W, Wu S, Cheng Y, Gouaux E, Glycine receptor mechanism elucidated by electron cryo-microscopy. Nature. 2015;526(7572):224–9. doi: 10.1038/nature1485326344198.
    • (2015) Nature , vol.526 , Issue.7572 , pp. 224-229
    • Du, J.1    Lu, W.2    Wu, S.3    Cheng, Y.4    Gouaux, E.5
  • 13
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • 18322461, .;():–.
    • Hilf RJ, Dutzler R, X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature. 2008;452(7185):375–9. 18322461. doi: 10.1038/nature06717
    • (2008) Nature , vol.452 , Issue.7185 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 14
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • 18987630, .;():–.
    • Hilf RJ, Dutzler R, Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel. Nature. 2009;457(7225):115–8. 18987630. doi: 10.1038/nature07461
    • (2009) Nature , vol.457 , Issue.7225 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 15
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • 18987633, ..;():–.
    • Bocquet N, Nury H, Baaden M, Le Poupon C, Changeux JP, Delarue M, et al. X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature. 2009;457(7225):111–4. 18987633. doi: 10.1038/nature07462
    • (2009) Nature , vol.457 , Issue.7225 , pp. 111-114
    • Bocquet, N.1    Nury, H.2    Baaden, M.3    Le Poupon, C.4    Changeux, J.P.5    Delarue, M.6
  • 16
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective Cys-loop receptor
    • 21572436, .;():–.
    • Hibbs RE, Gouaux E, Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature. 2011;474(7349):54–60. 21572436. doi: 10.1038/nature10139
    • (2011) Nature , vol.474 , Issue.7349 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 17
    • 84905669878 scopus 로고    scopus 로고
    • Crystal structure of a human GABAA receptor
    • 24909990, .;():–.
    • Miller PS, Aricescu AR, Crystal structure of a human GABAA receptor. Nature. 2014;512(7514):270–5. doi: 10.1038/nature1329324909990.
    • (2014) Nature , vol.512 , Issue.7514 , pp. 270-275
    • Miller, P.S.1    Aricescu, A.R.2
  • 18
    • 84906545550 scopus 로고    scopus 로고
    • X-ray structure of the mouse serotonin 5-HT3 receptor
    • 25119048, ..;():–.
    • Hassaine G, Deluz C, Grasso L, Wyss R, Tol MB, Hovius R, et al. X-ray structure of the mouse serotonin 5-HT3 receptor. Nature. 2014;512(7514):276–81. doi: 10.1038/nature1355225119048.
    • (2014) Nature , vol.512 , Issue.7514 , pp. 276-281
    • Hassaine, G.1    Deluz, C.2    Grasso, L.3    Wyss, R.4    Tol, M.B.5    Hovius, R.6
  • 19
    • 84906568725 scopus 로고    scopus 로고
    • X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors
    • 25143115, .;():–.
    • Althoff T, Hibbs RE, Banerjee S, Gouaux E, X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors. Nature. 2014;512(7514):333–7. doi: 10.1038/nature1366925143115.
    • (2014) Nature , vol.512 , Issue.7514 , pp. 333-337
    • Althoff, T.1    Hibbs, R.E.2    Banerjee, S.3    Gouaux, E.4
  • 20
    • 84892910277 scopus 로고    scopus 로고
    • Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation
    • 24367074, ..;():–.
    • Sauguet L, Shahsavar A, Poitevin F, Huon C, Menny A, Nemecz A, et al. Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation. Proc Natl Acad Sci U S A. 2014;111(3):966–71. doi: 10.1073/pnas.131499711124367074.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , Issue.3 , pp. 966-971
    • Sauguet, L.1    Shahsavar, A.2    Poitevin, F.3    Huon, C.4    Menny, A.5    Nemecz, A.6
  • 21
    • 84944052478 scopus 로고    scopus 로고
    • Crystal structure of human glycine receptor-alpha3 bound to antagonist strychnine
    • 26416729, .;():–.
    • Huang X, Chen H, Michelsen K, Schneider S, Shaffer PL, Crystal structure of human glycine receptor-alpha3 bound to antagonist strychnine. Nature. 2015;526(7572):277–80. doi: 10.1038/nature1497226416729.
    • (2015) Nature , vol.526 , Issue.7572 , pp. 277-280
    • Huang, X.1    Chen, H.2    Michelsen, K.3    Schneider, S.4    Shaffer, P.L.5
  • 22
    • 84881437750 scopus 로고    scopus 로고
    • Gating of pentameric ligand-gated ion channels: structural insights and ambiguities
    • 23931140, .;():–.
    • daCosta CJ, Baenziger JE, Gating of pentameric ligand-gated ion channels: structural insights and ambiguities. Structure. 2013;21(8):1271–83. doi: 10.1016/j.str.2013.06.01923931140.
    • (2013) Structure , vol.21 , Issue.8 , pp. 1271-1283
    • daCosta, C.J.1    Baenziger, J.E.2
  • 23
    • 73649096172 scopus 로고    scopus 로고
    • Crystal Structure of the Extracellular Domain of a Bacterial Ligand-Gated Ion Channel
    • 19917292, ...
    • Nury H, Bocquet N, Le Poupon C, Raynal B, Haouz A, Corringer PJ, et al. Crystal Structure of the Extracellular Domain of a Bacterial Ligand-Gated Ion Channel. J Mol Biol. 2009. 19917292.
    • (2009) J Mol Biol
    • Nury, H.1    Bocquet, N.2    Le Poupon, C.3    Raynal, B.4    Haouz, A.5    Corringer, P.J.6
  • 24
    • 34547520128 scopus 로고    scopus 로고
    • Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution
    • 17643119, .;():–.
    • Dellisanti CD, Yao Y, Stroud JC, Wang ZZ, Chen L, Crystal structure of the extracellular domain of nAChR alpha1 bound to alpha-bungarotoxin at 1.94 A resolution. Nat Neurosci. 2007;10(8):953–62. 17643119.
    • (2007) Nat Neurosci , vol.10 , Issue.8 , pp. 953-962
    • Dellisanti, C.D.1    Yao, Y.2    Stroud, J.C.3    Wang, Z.Z.4    Chen, L.5
  • 25
    • 77953709862 scopus 로고    scopus 로고
    • NMR structure of the transmembrane domain of the n-acetylcholine receptor beta2 subunit
    • 20441771, .;():–.
    • Bondarenko V, Tillman T, Xu Y, Tang P, NMR structure of the transmembrane domain of the n-acetylcholine receptor beta2 subunit. Biochim Biophys Acta. 2010;1798(8):1608–14. doi: 10.1016/j.bbamem.2010.04.01420441771.
    • (2010) Biochim Biophys Acta , vol.1798 , Issue.8 , pp. 1608-1614
    • Bondarenko, V.1    Tillman, T.2    Xu, Y.3    Tang, P.4
  • 26
    • 0041352143 scopus 로고    scopus 로고
    • Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels
    • 12695308, .;:–.
    • Sixma TK, Smit AB, Acetylcholine binding protein (AChBP): a secreted glial protein that provides a high-resolution model for the extracellular domain of pentameric ligand-gated ion channels. Annu Rev Biophys Biomol Struct. 2003;32:311–34. 12695308.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 311-334
    • Sixma, T.K.1    Smit, A.B.2
  • 27
    • 4344616080 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel
    • 15318223, ..;():–.
    • Bouzat C, Gumilar F, Spitzmaul G, Wang HL, Rayes D, Hansen SB, et al. Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel. Nature. 2004;430(7002):896–900. 15318223.
    • (2004) Nature , vol.430 , Issue.7002 , pp. 896-900
    • Bouzat, C.1    Gumilar, F.2    Spitzmaul, G.3    Wang, H.L.4    Rayes, D.5    Hansen, S.B.6
  • 28
    • 69249088472 scopus 로고    scopus 로고
    • A prokaryotic perspective on pentameric ligand-gated ion channel structure
    • 19646860, .;():–.
    • Hilf RJ, Dutzler R, A prokaryotic perspective on pentameric ligand-gated ion channel structure. Curr Opin Struct Biol. 2009;19(4):418–24. 19646860. doi: 10.1016/j.sbi.2009.07.006
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.4 , pp. 418-424
    • Hilf, R.J.1    Dutzler, R.2
  • 29
    • 84920385268 scopus 로고    scopus 로고
    • Mechanism of activation of the prokaryotic channel ELIC by propylamine: a single-channel study
    • 25548135, .;():–.
    • Marabelli A, Lape R, Sivilotti L, Mechanism of activation of the prokaryotic channel ELIC by propylamine: a single-channel study. J Gen Physiol. 2015;145(1):23–45. doi: 10.1085/jgp.20141123425548135.
    • (2015) J Gen Physiol , vol.145 , Issue.1 , pp. 23-45
    • Marabelli, A.1    Lape, R.2    Sivilotti, L.3
  • 30
    • 84870266525 scopus 로고    scopus 로고
    • Inhibition of the prokaryotic pentameric ligand-gated ion channel ELIC by divalent cations
    • 23185134, .;():.
    • Zimmermann I, Marabelli A, Bertozzi C, Sivilotti LG, Dutzler R, Inhibition of the prokaryotic pentameric ligand-gated ion channel ELIC by divalent cations. PLoS Biol. 2012;10(11):e1001429. doi: 10.1371/journal.pbio.100142923185134.
    • (2012) PLoS Biol , vol.10 , Issue.11 , pp. e1001429
    • Zimmermann, I.1    Marabelli, A.2    Bertozzi, C.3    Sivilotti, L.G.4    Dutzler, R.5
  • 31
    • 78549271990 scopus 로고    scopus 로고
    • Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel
    • 21037567, .;():–.
    • Hilf RJ, Bertozzi C, Zimmermann I, Reiter A, Trauner D, Dutzler R, Structural basis of open channel block in a prokaryotic pentameric ligand-gated ion channel. Nat Struct Mol Biol. 2010;17(11):1330–6. 21037567. doi: 10.1038/nsmb.1933
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.11 , pp. 1330-1336
    • Hilf, R.J.1    Bertozzi, C.2    Zimmermann, I.3    Reiter, A.4    Trauner, D.5    Dutzler, R.6
  • 32
    • 84859173541 scopus 로고    scopus 로고
    • Structure of the pentameric ligand-gated ion channel ELIC cocrystallized with its competitive antagonist acetylcholine
    • 22395605, ..;:. Epub 2012/03/08.
    • Pan J, Chen Q, Willenbring D, Yoshida K, Tillman T, Kashlan OB, et al. Structure of the pentameric ligand-gated ion channel ELIC cocrystallized with its competitive antagonist acetylcholine. Nat Commun. 2012;3:714. Epub 2012/03/08. doi: 10.1038/ncomms170322395605.
    • (2012) Nat Commun , vol.3 , pp. 714
    • Pan, J.1    Chen, Q.2    Willenbring, D.3    Yoshida, K.4    Tillman, T.5    Kashlan, O.B.6
  • 33
    • 84861856196 scopus 로고    scopus 로고
    • A locally closed conformation of a bacterial pentameric proton-gated ion channel
    • 22580559, ..;():–.
    • Prevost MS, Sauguet L, Nury H, Van Renterghem C, Huon C, Poitevin F, et al. A locally closed conformation of a bacterial pentameric proton-gated ion channel. Nat Struct Mol Biol. 2012;19(6):642–9. doi: 10.1038/nsmb.230722580559.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.6 , pp. 642-649
    • Prevost, M.S.1    Sauguet, L.2    Nury, H.3    Van Renterghem, C.4    Huon, C.5    Poitevin, F.6
  • 34
    • 84887444038 scopus 로고    scopus 로고
    • Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography
    • 24167270, .;():–.
    • Gonzalez-Gutierrez G, Cuello LG, Nair SK, Grosman C, Gating of the proton-gated ion channel from Gloeobacter violaceus at pH 4 as revealed by X-ray crystallography. Proc Natl Acad Sci U S A. 2013;110(46):18716–21. doi: 10.1073/pnas.131315611024167270.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.46 , pp. 18716-18721
    • Gonzalez-Gutierrez, G.1    Cuello, L.G.2    Nair, S.K.3    Grosman, C.4
  • 35
    • 84863116433 scopus 로고    scopus 로고
    • Intramembrane proton binding site linked to activation of bacterial pentameric ion channel
    • 22084238, .;():–.
    • Wang HL, Cheng X, Sine SM, Intramembrane proton binding site linked to activation of bacterial pentameric ion channel. J Biol Chem. 2012;287(9):6482–9. doi: 10.1074/jbc.M111.30583922084238.
    • (2012) J Biol Chem , vol.287 , Issue.9 , pp. 6482-6489
    • Wang, H.L.1    Cheng, X.2    Sine, S.M.3
  • 36
    • 84919924163 scopus 로고    scopus 로고
    • Structural requirements in the transmembrane domain of GLIC revealed by incorporation of noncanonical histidine analogs
    • 25525989, .;():–.
    • Rienzo M, Lummis SC, Dougherty DA, Structural requirements in the transmembrane domain of GLIC revealed by incorporation of noncanonical histidine analogs. Chem Biol. 2014;21(12):1700–6. doi: 10.1016/j.chembiol.2014.10.01925525989.
    • (2014) Chem Biol , vol.21 , Issue.12 , pp. 1700-1706
    • Rienzo, M.1    Lummis, S.C.2    Dougherty, D.A.3
  • 37
    • 84859963646 scopus 로고    scopus 로고
    • Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals
    • 22474383, .. Epub 2012/04/05.
    • Gonzalez-Gutierrez G, Lukk T, Agarwal V, Papke D, Nair SK, Grosman C, Mutations that stabilize the open state of the Erwinia chrisanthemi ligand-gated ion channel fail to change the conformation of the pore domain in crystals. Proc Natl Acad Sci U S A. 2012. Epub 2012/04/05. doi: 10.1073/pnas.111926810922474383.
    • (2012) Proc Natl Acad Sci U S A
    • Gonzalez-Gutierrez, G.1    Lukk, T.2    Agarwal, V.3    Papke, D.4    Nair, S.K.5    Grosman, C.6
  • 38
    • 84889038866 scopus 로고    scopus 로고
    • Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions
    • 24260024, ..;():.
    • Dellisanti CD, Ghosh B, Hanson SM, Raspanti JM, Grant VA, Diarra GM, et al. Site-directed spin labeling reveals pentameric ligand-gated ion channel gating motions. PLoS Biol. 2013;11(11):e1001714. doi: 10.1371/journal.pbio.100171424260024.
    • (2013) PLoS Biol , vol.11 , Issue.11 , pp. e1001714
    • Dellisanti, C.D.1    Ghosh, B.2    Hanson, S.M.3    Raspanti, J.M.4    Grant, V.A.5    Diarra, G.M.6
  • 40
    • 70849100535 scopus 로고    scopus 로고
    • Structural basis of activation of cys-loop receptors: the extracellular-transmembrane interface as a coupling region
    • 19859835, .;():–.
    • Bartos M, Corradi J, Bouzat C, Structural basis of activation of cys-loop receptors: the extracellular-transmembrane interface as a coupling region. Mol Neurobiol. 2009;40(3):236–52. doi: 10.1007/s12035-009-8084-x19859835.
    • (2009) Mol Neurobiol , vol.40 , Issue.3 , pp. 236-252
    • Bartos, M.1    Corradi, J.2    Bouzat, C.3
  • 41
    • 0037448581 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in the GABA(A) receptor
    • 12529644, .;():–.
    • Kash TL, Jenkins A, Kelley JC, Trudell JR, Harrison NL, Coupling of agonist binding to channel gating in the GABA(A) receptor. Nature. 2003;421(6920):272–5. 12529644.
    • (2003) Nature , vol.421 , Issue.6920 , pp. 272-275
    • Kash, T.L.1    Jenkins, A.2    Kelley, J.C.3    Trudell, J.R.4    Harrison, N.L.5
  • 42
    • 0037329589 scopus 로고    scopus 로고
    • Mutation causing severe myasthenia reveals functional asymmetry of AChR signature cystine loops in agonist binding and gating
    • 12588888, ..;():–.
    • Shen XM, Ohno K, Tsujino A, Brengman JM, Gingold M, Sine SM, et al. Mutation causing severe myasthenia reveals functional asymmetry of AChR signature cystine loops in agonist binding and gating. J Clin Invest. 2003;111(4):497–505. 12588888.
    • (2003) J Clin Invest , vol.111 , Issue.4 , pp. 497-505
    • Shen, X.M.1    Ohno, K.2    Tsujino, A.3    Brengman, J.M.4    Gingold, M.5    Sine, S.M.6
  • 43
    • 1842686239 scopus 로고    scopus 로고
    • Gating dynamics of the acetylcholine receptor extracellular domain
    • 15051806, .;():–.
    • Chakrapani S, Bailey TD, Auerbach A, Gating dynamics of the acetylcholine receptor extracellular domain. J Gen Physiol. 2004;123(4):341–56. doi: 10.1085/jgp.20030900415051806.
    • (2004) J Gen Physiol , vol.123 , Issue.4 , pp. 341-356
    • Chakrapani, S.1    Bailey, T.D.2    Auerbach, A.3
  • 44
    • 0029954238 scopus 로고    scopus 로고
    • A single residue in the M2-M3 loop is a major determinant of coupling between binding and gating in neuronal nicotinic receptors
    • 8650229, .;():–.
    • Campos-Caro A, Sala S, Ballesta JJ, Vicente-Agullo F, Criado M, Sala F, A single residue in the M2-M3 loop is a major determinant of coupling between binding and gating in neuronal nicotinic receptors. Proc Natl Acad Sci U S A. 1996;93(12):6118–23. 8650229.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.12 , pp. 6118-6123
    • Campos-Caro, A.1    Sala, S.2    Ballesta, J.J.3    Vicente-Agullo, F.4    Criado, M.5    Sala, F.6
  • 45
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
    • 9009272, .;():–.
    • Lynch JW, Rajendra S, Pierce KD, Handford CA, Barry PH, Schofield PR, Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel. EMBO J. 1997;16(1):110–20. doi: 10.1093/emboj/16.1.1109009272.
    • (1997) EMBO J , vol.16 , Issue.1 , pp. 110-120
    • Lynch, J.W.1    Rajendra, S.2    Pierce, K.D.3    Handford, C.A.4    Barry, P.H.5    Schofield, P.R.6
  • 46
    • 0033811476 scopus 로고    scopus 로고
    • The extracellular linker of muscle acetylcholine receptor channels is a gating control element
    • 10962011, .;():–.
    • Grosman C, Salamone FN, Sine SM, Auerbach A, The extracellular linker of muscle acetylcholine receptor channels is a gating control element. J Gen Physiol. 2000;116(3):327–40. 10962011.
    • (2000) J Gen Physiol , vol.116 , Issue.3 , pp. 327-340
    • Grosman, C.1    Salamone, F.N.2    Sine, S.M.3    Auerbach, A.4
  • 47
    • 36549043834 scopus 로고    scopus 로고
    • Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker
    • 18040057, .;():–.
    • Jha A, Cadugan DJ, Purohit P, Auerbach A, Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker. J Gen Physiol. 2007;130(6):547–58. 18040057.
    • (2007) J Gen Physiol , vol.130 , Issue.6 , pp. 547-558
    • Jha, A.1    Cadugan, D.J.2    Purohit, P.3    Auerbach, A.4
  • 48
    • 49649099967 scopus 로고    scopus 로고
    • Gating at the mouth of the acetylcholine receptor channel: energetic consequences of mutations in the alphaM2-cap
    • 18575616, .;():.
    • Bafna PA, Purohit PG, Auerbach A, Gating at the mouth of the acetylcholine receptor channel: energetic consequences of mutations in the alphaM2-cap. PLoS One. 2008;3(6):e2515. doi: 10.1371/journal.pone.000251518575616.
    • (2008) PLoS One , vol.3 , Issue.6 , pp. e2515
    • Bafna, P.A.1    Purohit, P.G.2    Auerbach, A.3
  • 49
    • 84894149129 scopus 로고    scopus 로고
    • Macroscopic kinetics of pentameric ligand gated ion channels: comparisons between two prokaryotic channels and one eukaryotic channel
    • 24260369, .;():.
    • Laha KT, Ghosh B, Czajkowski C, Macroscopic kinetics of pentameric ligand gated ion channels: comparisons between two prokaryotic channels and one eukaryotic channel. PLoS ONE. 2013;8(11):e80322. doi: 10.1371/journal.pone.008032224260369.
    • (2013) PLoS ONE , vol.8 , Issue.11 , pp. e80322
    • Laha, K.T.1    Ghosh, B.2    Czajkowski, C.3
  • 50
    • 0032520102 scopus 로고    scopus 로고
    • Properties of human glycine receptors containing the hyperekplexia mutation alpha1(K276E), expressed in Xenopus oocytes
    • 9490812, .;():–.
    • Lewis TM, Sivilotti LG, Colquhoun D, Gardiner RM, Schoepfer R, Rees M, Properties of human glycine receptors containing the hyperekplexia mutation alpha1(K276E), expressed in Xenopus oocytes. J Physiol. 1998;507 (Pt 1):25–40. 9490812.
    • (1998) J Physiol , vol.507 , pp. 25-40
    • Lewis, T.M.1    Sivilotti, L.G.2    Colquhoun, D.3    Gardiner, R.M.4    Schoepfer, R.5    Rees, M.6
  • 51
    • 50349093448 scopus 로고    scopus 로고
    • The interface between extracellular and transmembrane domains of homomeric Cys-loop receptors governs open-channel lifetime and rate of desensitization
    • 18667613, .;():–.
    • Bouzat C, Bartos M, Corradi J, Sine SM, The interface between extracellular and transmembrane domains of homomeric Cys-loop receptors governs open-channel lifetime and rate of desensitization. J Neurosci. 2008;28(31):7808–19. doi: 10.1523/JNEUROSCI.0448-08.200818667613.
    • (2008) J Neurosci , vol.28 , Issue.31 , pp. 7808-7819
    • Bouzat, C.1    Bartos, M.2    Corradi, J.3    Sine, S.M.4
  • 52
    • 3543083927 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis in the signature disulfide loop of the glycine receptor alpha 1 subunit: critical residues for activation and modulation
    • 15287733, .;():–.
    • Schofield CM, Trudell JR, Harrison NL, Alanine-scanning mutagenesis in the signature disulfide loop of the glycine receptor alpha 1 subunit: critical residues for activation and modulation. Biochemistry. 2004;43(31):10058–63. 15287733.
    • (2004) Biochemistry , vol.43 , Issue.31 , pp. 10058-10063
    • Schofield, C.M.1    Trudell, J.R.2    Harrison, N.L.3
  • 54
    • 63849179080 scopus 로고    scopus 로고
    • Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2-M3 regions
    • 19279256, .;():–.
    • Lee WY, Free CR, Sine SM, Binding to gating transduction in nicotinic receptors: Cys-loop energetically couples to pre-M1 and M2-M3 regions. J Neurosci. 2009;29(10):3189–99. doi: 10.1523/JNEUROSCI.6185-08.200919279256.
    • (2009) J Neurosci , vol.29 , Issue.10 , pp. 3189-3199
    • Lee, W.Y.1    Free, C.R.2    Sine, S.M.3
  • 55
    • 29244442919 scopus 로고    scopus 로고
    • A unified view of the role of electrostatic interactions in modulating the gating of Cys loop receptors
    • 16216879, .;():–.
    • Xiu X, Hanek AP, Wang J, Lester HA, Dougherty DA, A unified view of the role of electrostatic interactions in modulating the gating of Cys loop receptors. J Biol Chem. 2005;280(50):41655–66. doi: 10.1074/jbc.M50863520016216879.
    • (2005) J Biol Chem , vol.280 , Issue.50 , pp. 41655-41666
    • Xiu, X.1    Hanek, A.P.2    Wang, J.3    Lester, H.A.4    Dougherty, D.A.5
  • 56
    • 34548485996 scopus 로고    scopus 로고
    • Transducing agonist binding to channel gating involves different interactions in 5-HT3 and GABAC receptors
    • 17606617, .;():–.
    • Price KL, Millen KS, Lummis SC, Transducing agonist binding to channel gating involves different interactions in 5-HT3 and GABAC receptors. J Biol Chem. 2007;282(35):25623–30. doi: 10.1074/jbc.M70252420017606617.
    • (2007) J Biol Chem , vol.282 , Issue.35 , pp. 25623-25630
    • Price, K.L.1    Millen, K.S.2    Lummis, S.C.3
  • 57
    • 0347379903 scopus 로고    scopus 로고
    • Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor
    • 14525990, .;():–.
    • Absalom NL, Lewis TM, Kaplan W, Pierce KD, Schofield PR, Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor. J Biol Chem. 2003;278(50):50151–7. doi: 10.1074/jbc.M30535720014525990.
    • (2003) J Biol Chem , vol.278 , Issue.50 , pp. 50151-50157
    • Absalom, N.L.1    Lewis, T.M.2    Kaplan, W.3    Pierce, K.D.4    Schofield, P.R.5
  • 58
    • 36549039473 scopus 로고    scopus 로고
    • Acetylcholine receptor gating at extracellular transmembrane domain interface: the "pre-M1" linker
    • 18040058, .;():–.
    • Purohit P, Auerbach A, Acetylcholine receptor gating at extracellular transmembrane domain interface: the "pre-M1" linker. J Gen Physiol. 2007;130(6):559–68. 18040058.
    • (2007) J Gen Physiol , vol.130 , Issue.6 , pp. 559-568
    • Purohit, P.1    Auerbach, A.2
  • 59
    • 27744438169 scopus 로고    scopus 로고
    • Principal pathway coupling agonist binding to channel gating in nicotinic receptors
    • 16281039, .;():–.
    • Lee WY, Sine SM, Principal pathway coupling agonist binding to channel gating in nicotinic receptors. Nature. 2005;438(7065):243–7. 16281039.
    • (2005) Nature , vol.438 , Issue.7065 , pp. 243-247
    • Lee, W.Y.1    Sine, S.M.2
  • 60
    • 84893466183 scopus 로고    scopus 로고
    • Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC)
    • 24338475, .;():–.
    • Velisetty P, Chalamalasetti SV, Chakrapani S, Structural basis for allosteric coupling at the membrane-protein interface in Gloeobacter violaceus ligand-gated ion channel (GLIC). J Biol Chem. 2014;289(5):3013–25. doi: 10.1074/jbc.M113.52305024338475.
    • (2014) J Biol Chem , vol.289 , Issue.5 , pp. 3013-3025
    • Velisetty, P.1    Chalamalasetti, S.V.2    Chakrapani, S.3
  • 61
    • 79953845449 scopus 로고    scopus 로고
    • A versatile and efficient high-throughput cloning tool for structural biology
    • 21410291, .;():–.
    • Geertsma ER, Dutzler R, A versatile and efficient high-throughput cloning tool for structural biology. Biochemistry. 2011;50(15):3272–8. doi: 10.1021/bi200178z21410291.
    • (2011) Biochemistry , vol.50 , Issue.15 , pp. 3272-3278
    • Geertsma, E.R.1    Dutzler, R.2
  • 62
    • 0029843417 scopus 로고    scopus 로고
    • Heteromultimeric CLC chloride channels with novel properties
    • 8917596, .;():–.
    • Lorenz C, Pusch M, Jentsch TJ, Heteromultimeric CLC chloride channels with novel properties. Proc Natl Acad Sci U S A. 1996;93(23):13362–6. 8917596.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.23 , pp. 13362-13366
    • Lorenz, C.1    Pusch, M.2    Jentsch, T.J.3
  • 63
    • 0033103174 scopus 로고    scopus 로고
    • A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels
    • 10197533, .;():–.
    • Zerangue N, Schwappach B, Jan YN, Jan LY, A new ER trafficking signal regulates the subunit stoichiometry of plasma membrane K(ATP) channels. Neuron. 1999;22(3):537–48. 10197533.
    • (1999) Neuron , vol.22 , Issue.3 , pp. 537-548
    • Zerangue, N.1    Schwappach, B.2    Jan, Y.N.3    Jan, L.Y.4
  • 64
    • 0037196236 scopus 로고    scopus 로고
    • Achieving optimal expression for single channel recording: a plasmid ratio approach to the expression of alpha 1 glycine receptors in HEK293 cells
    • 11772442, .;():–.
    • Groot-Kormelink PJ, Beato M, Finotti C, Harvey RJ, Sivilotti LG, Achieving optimal expression for single channel recording: a plasmid ratio approach to the expression of alpha 1 glycine receptors in HEK293 cells. J Neurosci Methods. 2002;113(2):207–14. 11772442.
    • (2002) J Neurosci Methods , vol.113 , Issue.2 , pp. 207-214
    • Groot-Kormelink, P.J.1    Beato, M.2    Finotti, C.3    Harvey, R.J.4    Sivilotti, L.G.5
  • 65
    • 0027879008 scopus 로고
    • Automatic Processing of Rotation Diffraction Data from Crystals of Initially Unknown Symmetry and Cell Constants
    • .;():–.
    • Kabsch W, Automatic Processing of Rotation Diffraction Data from Crystals of Initially Unknown Symmetry and Cell Constants. J Appl Cryst. 1993;26(6):795–800.
    • (1993) J Appl Cryst , vol.26 , Issue.6 , pp. 795-800
    • Kabsch, W.1
  • 66
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for X-ray crystallography
    • 15299374, .;:–.
    • CCP4Collaborative Computational Project Nr. 4The CCP4 Suite: Programs for X-ray crystallography. Acta Crystallogr D. 1994;50:760–3. 15299374
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 70
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: a program for the analysis of the pore dimensions of ion channel structural models
    • 9195488, .;():–, 76.
    • Smart OS, Neduvelil JG, Wang X, Wallace BA, Sansom MS, HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J Mol Graph. 1996;14(6):354–60, 76. 9195488.
    • (1996) J Mol Graph , vol.14 , Issue.6 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5
  • 71
    • 84861840835 scopus 로고    scopus 로고
    • High-precision isothermal titration calorimetry with automated peak-shape analysis
    • 22530732, .;():–.
    • Keller S, Vargas C, Zhao H, Piszczek G, Brautigam CA, Schuck P, High-precision isothermal titration calorimetry with automated peak-shape analysis. Anal Chem. 2012;84(11):5066–73. doi: 10.1021/ac300752222530732.
    • (2012) Anal Chem , vol.84 , Issue.11 , pp. 5066-5073
    • Keller, S.1    Vargas, C.2    Zhao, H.3    Piszczek, G.4    Brautigam, C.A.5    Schuck, P.6


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