메뉴 건너뛰기




Volumn 39, Issue 1, 2009, Pages 37-49

Gating mechanisms in Cys-loop receptors

Author keywords

Coupling; Cys loop receptor; Gating; Ligand gated ion channels; Review

Indexed keywords

4 AMINOBUTYRIC ACID A RECEPTOR; CYSTEINE LOOP RECEPTOR; ION CHANNEL; NEUROTRANSMITTER; NICOTINIC RECEPTOR; RECEPTOR; RECEPTOR SUBUNIT; UNCLASSIFIED DRUG;

EID: 70450255330     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-009-0452-y     Document Type: Review
Times cited : (48)

References (71)
  • 1
    • 0347379903 scopus 로고    scopus 로고
    • Role of Charged Residues in Coupling Ligand Binding and Channel Activation in the Extracellular Domain of the Glycine Receptor
    • DOI 10.1074/jbc.M305357200
    • NL Absalom TM Lewis W Kaplan KD Pierce PR Schofield 2003 Role of charged residues in coupling ligand binding and channel activation in the extracellular domain of the glycine receptor J Biol Chem 278 50151 50157 10.1074/jbc. M305357200 10.1074/jbc.M305357200 14525990 (Pubitemid 37548853)
    • (2003) Journal of Biological Chemistry , 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
  • 2
    • 25844431698 scopus 로고    scopus 로고
    • Coarse-grained normal mode analysis in structural biology
    • DOI 10.1016/j.sbi.2005.08.007, PII S0959440X05001557, Carbohydrates and Glycoconjugates/Biophysical Methods
    • I Bahar AJ Rader 2005 Coarse-grained normal mode analysis in structural biology Curr Opin Struct Biol 15 586 592 10.1016/j.sbi.2005.08.007 10.1016/j.sbi.2005.08.007 16143512 (Pubitemid 41393491)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 586-592
    • Bahar, I.1    Rader, A.J.2
  • 4
    • 0037044793 scopus 로고    scopus 로고
    • A receptor M2-M3 loop secondary structure and changes in accessibility during channel gating
    • DOI 10.1074/jbc.M206321200
    • AK Bera M Chatav MH Akabas 2002 GABAA receptor M2-M3 loop secondary structure and changes in accessibility during channel gating J Biol Chem 277 43002 43010 10.1074/jbc.M206321200 10.1074/jbc.M206321200 12226083 (Pubitemid 35285680)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43002-43010
    • Bera, A.K.1    Chatav, M.2    Akabas, M.H.3
  • 5
    • 34547653836 scopus 로고    scopus 로고
    • Normal-mode analysis of the glycine alpha1 receptor by three separate methods
    • DOI 10.1021/ci600566j
    • EJ Bertaccini JR Trudell E Lindahl 2007 Normal-mode analysis of the glycine alpha1 receptor by three separate methods J Chem Inf Model 47 1572 1579 10.1021/ci600566j 10.1021/ci600566j 17602605 (Pubitemid 47210060)
    • (2007) Journal of Chemical Information and Modeling , vol.47 , Issue.4 , pp. 1572-1579
    • Bertaccini, E.J.1    Tradelia, J.R.2    Lindane, E.3
  • 6
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • 10.1038/nature07462 10.1038/nature07462 18987633
    • N Bocquet H Nury M Baaden C Le Poupon JP Changeux M Delarue PJ Corringer 2009 X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation Nature 457 111 114 10.1038/nature07462 10.1038/nature07462 18987633
    • (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    Corringer, P.J.7
  • 7
    • 4344616080 scopus 로고    scopus 로고
    • Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel
    • DOI 10.1038/nature02753
    • C Bouzat F Gumilar G Spitzmaul HL Wang D Rayes SB Hansen P Taylor SM Sine 2004 Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel Nature 430 896 900 10.1038/nature02753 10.1038/nature02753 15318223 (Pubitemid 39119217)
    • (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    Taylor, P.7    Sine, S.M.8
  • 8
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • DOI 10.1038/35077011
    • K Brejc WJ van Dijk RV Klaassen M Schuurmans J Der Oost AB Smit TK Sixma 2001 Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors Nature 411 269 276 10.1038/35077011 10.1038/35077011 11357122 (Pubitemid 32467026)
    • (2001) Nature , vol.411 , Issue.6835 , 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    Sixma, T.K.7
  • 10
    • 59049083491 scopus 로고    scopus 로고
    • Characterization of the effects of charged residues in the intracellular loop on ion permeation in α1 glycine receptor channels
    • 10.1074/jbc.M806618200 10.1074/jbc.M806618200 19049967
    • JE Carland MA Cooper S Sugiharto HJ Jeong TM Lewis PH Barry JA Peters JJ Lambert AJ Moorhouse 2009 Characterization of the effects of charged residues in the intracellular loop on ion permeation in α1 glycine receptor channels J Biol Chem 284 2023 2030 10.1074/jbc.M806618200 10.1074/jbc.M806618200 19049967
    • (2009) J Biol Chem , vol.284 , pp. 2023-2030
    • Carland, J.E.1    Cooper, M.A.2    Sugiharto, S.3    Jeong, H.J.4    Lewis, T.M.5    Barry, P.H.6    Peters, J.A.7    Lambert, J.J.8    Moorhouse, A.J.9
  • 12
    • 29344468233 scopus 로고    scopus 로고
    • 3A receptor upon mutations at the M2-M3 extracellular loop
    • DOI 10.1016/j.febslet.2005.12.010, PII S0014579305014663
    • M Castillo J Mulet JA Bernal M Criado F Sala S Sala 2006 Improved gating of a chimeric α7-5HT3A receptor upon mutations at the M2-M3 extracellular loop FEBS Lett 580 256 260 10.1016/j.febslet.2005.12.010 10.1016/j.febslet.2005. 12.010 16364316 (Pubitemid 43005346)
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 256-260
    • Castillo, M.1    Mulet, J.2    Bernal, J.A.3    Criado, M.4    Sala, F.5    Sala, S.6
  • 13
    • 1842475289 scopus 로고    scopus 로고
    • Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures
    • DOI 10.1016/S0896-6273(04)00115-1, PII S0896627304001151
    • PH Celie SE van Rossum-Fikkert WJ van Dijk K Brejc AB Smit TK Sixma 2004 Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures Neuron 41 907 914 10.1016/S0896-6273(04) 00115-1 10.1016/S0896-6273(04)00115-1 15046723 (Pubitemid 38429734)
    • (2004) Neuron , vol.41 , Issue.6 , pp. 907-914
    • Celie, P.H.N.1    Van Rossum-Fikkert, S.E.2    Van Dijk, W.J.3    Brejc, K.4    Smit, A.B.5    Sixma, T.K.6
  • 14
    • 1842686239 scopus 로고    scopus 로고
    • Gating Dynamics of the Acetylcholine Receptor Extracellular Domain
    • DOI 10.1085/jgp.200309004
    • S Chakrapani TD Bailey A Auerbach 2004 Gating dynamics of the acetylcholine receptor extracellular domain J Gen Physiol 123 341 356 10.1085/jgp.200309004 10.1085/jgp.200309004 15051806 (Pubitemid 38469279)
    • (2004) Journal of General Physiology , vol.123 , Issue.4 , pp. 341-356
    • Chakrapani, S.1    Bailey, T.D.2    Auerbach, A.3
  • 15
    • 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 B Lu B Grant RJ Law JA McCammon 2006 Channel opening motion of α7 nicotinic acetylcholine receptor as suggested by normal mode analysis J Mol Biol 355 310 324 10.1016/j.jmb.2005.10.039 10.1016/j.jmb.2005.10.039 16307758 (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
  • 16
    • 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 SM Sine JA McCammon 2007 Nanosecond-timescale conformational dynamics of the human α7 nicotinic acetylcholine receptor Biophys J 93 2622 2634 10.1529/biophysj.107.109843 10.1529/biophysj.107.109843 17573436 (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
  • 17
    • 55549124541 scopus 로고    scopus 로고
    • Roles for loop 2 residues of α1 glycine receptors in agonist activation
    • 10.1074/jbc.M802384200 10.1074/jbc.M802384200 18658152
    • DK Crawford DI Perkins JR Trudell EJ Bertaccini DL Davies RL Alkana 2008 Roles for loop 2 residues of α1 glycine receptors in agonist activation J Biol Chem 283 27698 27706 10.1074/jbc.M802384200 10.1074/jbc.M802384200 18658152
    • (2008) J Biol Chem , vol.283 , pp. 27698-27706
    • Crawford, D.K.1    Perkins, D.I.2    Trudell, J.R.3    Bertaccini, E.J.4    Davies, D.L.5    Alkana, R.L.6
  • 18
    • 0025719155 scopus 로고
    • Agonist binding site of Torpedo electric tissue nicotinic acetylcholine receptor. A negatively charged region of the δ subunit within 0.9 nm of the α subunit binding site disulfide
    • 1939274
    • C Czajkowski A Karlin 1991 Agonist binding site of Torpedo electric tissue nicotinic acetylcholine receptor. A negatively charged region of the δ subunit within 0.9 nm of the α subunit binding site disulfide J Biol Chem 266 22603 22612 1939274
    • (1991) J Biol Chem , vol.266 , pp. 22603-22612
    • Czajkowski, C.1    Karlin, A.2
  • 20
    • 0029960845 scopus 로고    scopus 로고
    • Analysis of GLRA1 in hereditary and sporadic hyperekplexia: A novel mutation in a family cosegregating for hyperekplexia and spastic paraparesis
    • 10.1136/jmg.33.5.435 10.1136/jmg.33.5.435 8733061
    • FV Elmslie SM Hutchings V Spencer A Curtis T Covanis RM Gardiner M Rees 1996 Analysis of GLRA1 in hereditary and sporadic hyperekplexia: a novel mutation in a family cosegregating for hyperekplexia and spastic paraparesis J Med Genet 33 435 436 10.1136/jmg.33.5.435 10.1136/jmg.33.5.435 8733061
    • (1996) J Med Genet , vol.33 , pp. 435-436
    • Elmslie, F.V.1    Hutchings, S.M.2    Spencer, V.3    Curtis, A.4    Covanis, T.5    Gardiner, R.M.6    Rees, M.7
  • 21
    • 14844300820 scopus 로고    scopus 로고
    • Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence
    • DOI 10.1074/jbc.M412389200
    • F Gao N Bren TP Burghardt S Hansen RH Henchman P Taylor JA McCammon SM Sine 2005 Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence J Biol Chem 280 8443 8451 10.1074/jbc.M412389200 10.1074/jbc.M412389200 15591050 (Pubitemid 40349749)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 8443-8451
    • Gao, F.1    Bren, N.2    Burghardt, T.P.3    Hansen, S.4    Henchman, R.H.5    Taylor, P.6    McCammon, J.A.7    Sine, S.M.8
  • 22
    • 35648953223 scopus 로고    scopus 로고
    • Gating of nicotinic ACh receptors; new insights into structural transitions triggered by agonist binding that induce channel opening
    • DOI 10.1113/jphysiol.2007.142554
    • EA Gay JL Yakel 2007 Gating of nicotinic ACh receptors; new insights into structural transitions triggered by agonist binding that induce channel opening J Physiol 584 727 733 10.1113/jphysiol.2007.142554 10.1113/jphysiol.2007.142554 17823204 (Pubitemid 350031918)
    • (2007) Journal of Physiology , vol.584 , Issue.3 , pp. 727-733
    • Gay, E.A.1    Yakel, J.L.2
  • 24
    • 58149093958 scopus 로고    scopus 로고
    • An intersubunit hydrogen bond in the nicotinic acetylcholine receptor that contributes to channel gating
    • 10.1074/jbc.M807226200 10.1074/jbc.M807226200 18952603
    • KR Gleitsman SM Kedrowski HA Lester DA Dougherty 2008 An intersubunit hydrogen bond in the nicotinic acetylcholine receptor that contributes to channel gating J Biol Chem 283 35638 35643 10.1074/jbc.M807226200 10.1074/jbc.M807226200 18952603
    • (2008) J Biol Chem , vol.283 , pp. 35638-35643
    • Gleitsman, K.R.1    Kedrowski, S.M.2    Lester, H.A.3    Dougherty, D.A.4
  • 25
    • 0033811476 scopus 로고    scopus 로고
    • The extracellular linker of muscle acetylcholine receptor channels is a gating control element
    • DOI 10.1085/jgp.116.3.327
    • C Grosman FN Salamone SM Sine A Auerbach 2000 The extracellular linker of muscle acetylcholine receptor channels is a gating control element J Gen Physiol 116 327 340 10.1085/jgp.116.3.327 10.1085/jgp.116.3.327 10962011 (Pubitemid 30694136)
    • (2000) Journal of General Physiology , vol.116 , Issue.3 , pp. 327-339
    • Grosman, C.1    Salamone, F.N.2    Sine, S.M.3    Auerbach, A.4
  • 26
    • 0034677524 scopus 로고    scopus 로고
    • Mapping the conformational wave of acetylcholine receptor channel gating
    • DOI 10.1038/35001586
    • C Grosman M Zhou A Auerbach 2000 Mapping the conformational wave of acetylcholine receptor channel gating Nature 403 773 776 10.1038/35001586 10.1038/35001586 10693806 (Pubitemid 30111838)
    • (2000) Nature , vol.403 , Issue.6771 , pp. 773-776
    • Grosman, C.1    Zhou, M.2    Auerbach, A.3
  • 28
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • 10.1038/nature06717 10.1038/nature06717 18322461
    • RJ Hilf R Dutzler 2008 X-ray structure of a prokaryotic pentameric ligand-gated ion channel Nature 452 375 379 10.1038/nature06717 10.1038/nature06717 18322461
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.1    Dutzler, R.2
  • 29
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel
    • 10.1038/nature07461 10.1038/nature07461 18987630
    • RJ Hilf R Dutzler 2009 Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel Nature 457 115 118 10.1038/nature07461 10.1038/nature07461 18987630
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.1    Dutzler, R.2
  • 30
  • 31
    • 38749094806 scopus 로고    scopus 로고
    • 3 and GABA ρ1 receptors lacking the large cytoplasmic M3M4 loop
    • DOI 10.1085/jgp.200709896
    • 3 and GABA ρ1 receptors lacking the large cytoplasmic M3M4 loop J Gen Physiol 131 137 146 10.1085/jgp.200709896 10.1085/jgp.200709896 18227272 (Pubitemid 351185795)
    • (2008) Journal of General Physiology , vol.131 , Issue.2 , pp. 137-146
    • Jansen, M.1    Bali, M.2    Akabas, M.H.3
  • 32
    • 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 DJ Cadugan P Purohit A Auerbach 2007 Acetylcholine receptor gating at extracellular transmembrane domain interface: the cys-loop and M2-M3 linker J Gen Physiol 130 547 558 10.1085/jgp.200709856 10.1085/jgp.200709856 18040057 (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
  • 35
    • 7444260900 scopus 로고    scopus 로고
    • A and glycine receptors
    • DOI 10.1016/j.neulet.2004.09.002, PII S0304394004011103
    • A and glycine receptors Neurosci Lett 371 230 234 10.1016/j.neulet.2004.09.002 10.1016/j.neulet.2004.09.002 15519763 (Pubitemid 39440777)
    • (2004) Neuroscience Letters , vol.371 , Issue.2-3 , pp. 230-234
    • Kash, T.L.1    Kim, T.2    Trudell, J.R.3    Harrison, N.L.4
  • 38
    • 27744438169 scopus 로고    scopus 로고
    • Principal pathway coupling agonist binding to channel gating in nicotinic receptors
    • DOI 10.1038/nature04156, PII N04156
    • WY Lee SM Sine 2005 Principal pathway coupling agonist binding to channel gating in nicotinic receptors Nature 438 243 247 10.1038/nature04156 10.1038/nature04156 16281039 (Pubitemid 41599878)
    • (2005) Nature , vol.438 , Issue.7065 , pp. 243-247
    • Lee, W.Y.1    Sine, S.M.2
  • 39
    • 48649097534 scopus 로고    scopus 로고
    • Nicotinic receptor interloop proline anchors β1-β2 and cys loops in coupling agonist binding to channel gating
    • 10.1085/jgp.200810014 10.1085/jgp.200810014 18663134
    • WY Lee CR Free SM Sine 2008 Nicotinic receptor interloop proline anchors β1-β2 and cys loops in coupling agonist binding to channel gating J Gen Physiol 132 265 278 10.1085/jgp.200810014 10.1085/jgp.200810014 18663134
    • (2008) J Gen Physiol , vol.132 , pp. 265-278
    • Lee, W.Y.1    Free, C.R.2    Sine, S.M.3
  • 40
    • 2542432136 scopus 로고    scopus 로고
    • Cys-loop receptors: New twists and turns
    • DOI 10.1016/j.tins.2004.04.002, PII S0166223604001092
    • HA Lester MI Dibas DS Dahan JF Leite DA Dougherty 2004 Cys-loop receptors: new twists and turns Trends Neurosci 27 329 336 10.1016/j.tins.2004. 04.002 10.1016/j.tins.2004.04.002 15165737 (Pubitemid 38692414)
    • (2004) Trends in Neurosciences , vol.27 , Issue.6 , pp. 329-336
    • Lester, H.A.1    Dibas, M.I.2    Dahan, D.S.3    Leite, J.F.4    Dougherty, D.A.5
  • 41
    • 0032520102 scopus 로고    scopus 로고
    • Properties of human glycine receptors containing the hyperekplexia mutation α1 (K276E), expressed in Xenopus oocytes
    • DOI 10.1111/j.1469-7793.1998.025bu.x
    • TM Lewis LG Sivilotti D Colquhoun RM Gardiner R Schoepfer M Rees 1998 Properties of human glycine receptors containing the hyperekplexia mutation α1 (K276E), expressed in Xenopus oocytes J Physiol 507 Pt 1 25 40 10.1111/j.1469-7793.1998.025bu.x 10.1111/j.1469-7793.1998.025bu.x 9490812 (Pubitemid 28102673)
    • (1998) Journal of Physiology , vol.507 , Issue.1 , pp. 25-40
    • Lewis, T.M.1    Sivilotti, L.G.2    Colquhoun, D.3    Gardiner, R.M.4    Schoepfer, R.5    Rees, M.6
  • 42
    • 38949181306 scopus 로고    scopus 로고
    • Mechanics of channel gating of the nicotinic acetylcholine receptor
    • DOI 10.1371/journal.pcbi.0040019
    • X Liu Y Xu H Li X Wang H Jiang FJ Barrantes 2008 Mechanics of channel gating of the nicotinic acetylcholine receptor PLOS Comput Biol 4 e19 10.1371/journal.pcbi.0040019 10.1371/journal.pcbi.0040019 18225945 (Pubitemid 351230859)
    • (2008) PLoS Computational Biology , vol.4 , Issue.1 , pp. 0100-0110
    • Liu, X.1    Xu, Y.2    Li, H.3    Wang, X.4    Jiang, H.5    Barrantes, F.J.6
  • 43
    • 27744608733 scopus 로고    scopus 로고
    • Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel
    • DOI 10.1038/nature04130, PII N04130
    • SC Lummis DL Beene LW Lee HA Lester RW Broadhurst DA Dougherty 2005 Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel Nature 438 248 252 10.1038/nature04130 10.1038/nature04130 16281040 (Pubitemid 41599879)
    • (2005) Nature , vol.438 , Issue.7065 , pp. 248-252
    • Lummis, S.C.R.1    Beene, D.L.2    Lee, L.W.3    Lester, H.A.4    Broadhurst, R.W.5    Dougherty, D.A.6
  • 44
    • 0029018726 scopus 로고
    • Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator
    • 10.1074/jbc.270.23.13799 10.1074/jbc.270.23.13799 7775436
    • JW Lynch S Rajendra PH Barry PR Schofield 1995 Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator J Biol Chem 270 13799 13806 10.1074/jbc.270.23.13799 10.1074/jbc.270.23.13799 7775436
    • (1995) J Biol Chem , vol.270 , pp. 13799-13806
    • Lynch, J.W.1    Rajendra, S.2    Barry, P.H.3    Schofield, P.R.4
  • 45
    • 0031027684 scopus 로고    scopus 로고
    • Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel
    • DOI 10.1093/emboj/16.1.110
    • JW Lynch S Rajendra KD Pierce CA Handford PH Barry PR Schofield 1997 Identification of intracellular and extracellular domains mediating signal transduction in the inhibitory glycine receptor chloride channel EMBO J 16 110 120 10.1093/emboj/16.1.110 10.1093/emboj/16.1.110 9009272 (Pubitemid 27032854)
    • (1997) EMBO Journal , 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
    • 34247536305 scopus 로고    scopus 로고
    • Agonist-driven conformational changes in the inner β-sheet of α7 nicotinic receptors
    • DOI 10.1124/mol.106.033092
    • JT McLaughlin J Fu RL Rosenberg 2007 Agonist-driven conformational changes in the inner β-sheet of α7 nicotinic receptors Mol Pharmacol 71 1312 1318 10.1124/mol.106.033092 10.1124/mol.106.033092 17325129 (Pubitemid 46658684)
    • (2007) Molecular Pharmacology , vol.71 , Issue.5 , pp. 1312-1318
    • McLaughlin, J.T.1    Fu, J.2    Rosenberg, R.L.3
  • 47
    • 33644520967 scopus 로고    scopus 로고
    • A receptor activation
    • DOI 10.1523/JNEUROSCI.4555-05.2006
    • A receptor activation J Neurosci 26 2031 2040 10.1523/JNEUROSCI.4555-05.2006 10.1523/JNEUROSCI.4555-05.2006 16481436 (Pubitemid 43295855)
    • (2006) Journal of Neuroscience , vol.26 , Issue.7 , pp. 2031-2040
    • Mercado, J.1    Czajkowski, C.2
  • 48
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • DOI 10.1038/nature01748
    • A Miyazawa Y Fujiyoshi N Unwin 2003 Structure and gating mechanism of the acetylcholine receptor pore Nature 423 949 955 10.1038/nature01748 10.1038/nature01748 12827192 (Pubitemid 36806903)
    • (2003) Nature , vol.423 , Issue.6943 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 49
    • 34247109679 scopus 로고    scopus 로고
    • An intersubunit trigger of channel gating in the muscle nicotinic receptor
    • DOI 10.1523/JNEUROSCI.0025-07.2007
    • N Mukhtasimova SM Sine 2007 An intersubunit trigger of channel gating in the muscle nicotinic receptor J Neurosci 27 4110 4119 10.1523/JNEUROSCI.0025-07. 2007 10.1523/JNEUROSCI.0025-07.2007 17428989 (Pubitemid 46597150)
    • (2007) Journal of Neuroscience , vol.27 , Issue.15 , pp. 4110-4119
    • Mukhtasimova, N.1    Sine, S.M.2
  • 50
    • 22244478670 scopus 로고    scopus 로고
    • Initial coupling of binding to gating mediated by conserved residues in the muscle nicotinic receptor
    • DOI 10.1085/jgp.200509283
    • N Mukhtasimova C Free SM Sine 2005 Initial coupling of binding to gating mediated by conserved residues in the muscle nicotinic receptor J Gen Physiol 126 23 39 10.1085/jgp.200509283 10.1085/jgp.200509283 15955875 (Pubitemid 40994106)
    • (2005) Journal of General Physiology , vol.126 , Issue.1 , pp. 23-39
    • Mukhtasimova, N.1    Free, C.2    Sine, S.M.3
  • 51
    • 34248212784 scopus 로고    scopus 로고
    • Single-channel study of the spasmodic mutation α1A52S in recombinant rat glycine receptors
    • DOI 10.1113/jphysiol.2006.126920
    • AJ Plested PJ Groot-Kormelink D Colquhoun LG Sivilotti 2007 Single-channel study of the spasmodic mutation α1A52S in recombinant rat glycine receptors J Physiol 581 51 73 10.1113/jphysiol.2006.126920 10.1113/jphysiol.2006.126920 17331994 (Pubitemid 46712027)
    • (2007) Journal of Physiology , vol.581 , Issue.1 , pp. 51-73
    • Plested, A.J.R.1    Groot-kormelink, P.J.2    Colquhoun, D.3    Sivilotti, L.G.4
  • 54
    • 36549039473 scopus 로고    scopus 로고
    • Acetylcholine receptor gating at extracellular transmembrane domain interface: The "pre-M1" linker
    • DOI 10.1085/jgp.200709857
    • P Purohit A Auerbach 2007 Acetylcholine receptor gating at extracellular transmembrane domain interface: the "pre-M1" linker J Gen Physiol 130 559 568 10.1085/jgp.200709857 10.1085/jgp.200709857 18040058 (Pubitemid 350179574)
    • (2007) Journal of General Physiology , vol.130 , Issue.6 , pp. 559-568
    • Purohit, P.1    Auerbach, A.2
  • 55
    • 36549080807 scopus 로고    scopus 로고
    • Acetylcholine receptor gating: Movement in the α-subunit extracellular domain
    • DOI 10.1085/jgp.200709858
    • P Purohit A Auerbach 2007 Acetylcholine receptor gating: movement in the α-subunit extracellular domain J Gen Physiol 130 569 579 10.1085/jgp.200709858 10.1085/jgp.200709858 18040059 (Pubitemid 350179575)
    • (2007) Journal of General Physiology , vol.130 , Issue.6 , pp. 569-579
    • Purohit, P.1    Auerbach, A.2
  • 56
    • 34247375206 scopus 로고    scopus 로고
    • A stepwise mechanism for acetylcholine receptor channel gating
    • DOI 10.1038/nature05721, PII NATURE05721
    • P Purohit A Mitra A Auerbach 2007 A stepwise mechanism for acetylcholine receptor channel gating Nature 446 930 933 10.1038/nature05721 10.1038/nature05721 17443187 (Pubitemid 46633166)
    • (2007) Nature , vol.446 , Issue.7138 , pp. 930-933
    • Purohit, P.1    Mitra, A.2    Auerbach, A.3
  • 57
    • 0028361803 scopus 로고
    • Startle disease mutations reduce the agonist sensitivity of the human inhibitory glycine receptor
    • 7518444
    • S Rajendra JW Lynch KD Pierce CR French PH Barry PR Schofield 1994 Startle disease mutations reduce the agonist sensitivity of the human inhibitory glycine receptor J Biol Chem 269 18739 18742 7518444
    • (1994) J Biol Chem , vol.269 , pp. 18739-18742
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 58
    • 0028831226 scopus 로고
    • Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists
    • 10.1016/0896-6273(95)90251-1 10.1016/0896-6273(95)90251-1 7826634
    • S Rajendra JW Lynch KD Pierce CR French PH Barry PR Schofield 1995 Mutation of an arginine residue in the human glycine receptor transforms β-alanine and taurine from agonists into competitive antagonists Neuron 14 169 175 10.1016/0896-6273(95)90251-1 10.1016/0896-6273(95)90251-1 7826634
    • (1995) Neuron , vol.14 , pp. 169-175
    • Rajendra, S.1    Lynch, J.W.2    Pierce, K.D.3    French, C.R.4    Barry, P.H.5    Schofield, P.R.6
  • 61
    • 41449097191 scopus 로고    scopus 로고
    • Inhibition mechanism of the acetylcholine receptor by α-neurotoxins as revealed by normal-mode dynamics
    • 10.1021/bi702272j 10.1021/bi702272j 18327915
    • AO Samson M Levitt 2008 Inhibition mechanism of the acetylcholine receptor by α-neurotoxins as revealed by normal-mode dynamics Biochemistry 47 4065 4070 10.1021/bi702272j 10.1021/bi702272j 18327915
    • (2008) Biochemistry , vol.47 , pp. 4065-4070
    • Samson, A.O.1    Levitt, M.2
  • 62
    • 0141483292 scopus 로고    scopus 로고
    • A Highly Conserved Aspartic Acid Residue in the Signature Disulfide Loop of the α1 Subunit Is a Determinant of Gating in the Glycine Receptor
    • DOI 10.1074/jbc.M302416200
    • CM Schofield A Jenkins NL Harrison 2003 A highly conserved aspartic acid residue in the signature disulfide loop of the α1 subunit is a determinant of gating in the glycine receptor J Biol Chem 278 34079 34083 10.1074/jbc.M302416200 10.1074/jbc.M302416200 12826676 (Pubitemid 37553246)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.36 , pp. 34079-34083
    • Schofield, C.M.1    Jenkins, A.2    Harrison, N.L.3
  • 63
    • 0027330927 scopus 로고
    • 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia
    • 10.1038/ng1293-351 10.1038/ng1293-351 8298642
    • 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia Nat Genet 5 351 358 10.1038/ng1293-351 10.1038/ng1293-351 8298642
    • (1993) Nat Genet , vol.5 , pp. 351-358
    • Shiang, R.1    Ryan, S.G.2    Zhu, Y.Z.3    Hahn, A.F.4    O'Connell, P.5    Wasmuth, J.J.6
  • 65
    • 22244438519 scopus 로고    scopus 로고
    • Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism
    • DOI 10.1529/biophysj.104.050229
    • A Taly M Delarue T Grutter M Nilges N Le Novere PJ Corringer JP Changeux 2005 Normal mode analysis suggests a quaternary twist model for the nicotinic receptor gating mechanism Biophys J 88 3954 3965 10.1529/biophysj.104.050229 10.1529/biophysj.104.050229 15805177 (Pubitemid 40991108)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 3954-3965
    • Taly, A.1    Delarue, M.2    Grutter, T.3    Nilges, M.4    Le Novere, N.5    Corringer, P.-J.6    Changeux, J.-P.7
  • 66
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 A resolution
    • DOI 10.1016/j.jmb.2004.12.031
    • N Unwin 2005 Refined structure of the nicotinic acetylcholine receptor at 4A resolution J Mol Biol 346 967 989 10.1016/j.jmb.2004.12.031 10.1016/j.jmb.2004.12.031 15701510 (Pubitemid 40215523)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 967-989
    • Unwin, N.1
  • 67
    • 0036304564 scopus 로고    scopus 로고
    • Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the a subunits
    • DOI 10.1016/S0022-2836(02)00381-9
    • N Unwin A Miyazawa J Li Y Fujiyoshi 2002 Activation of the nicotinic acetylcholine receptor involves a switch in conformation of the α subunits J Mol Biol 319 1165 1176 10.1016/S0022-2836(02)00381-9 10.1016/S0022-2836(02) 00381-9 12079355 (Pubitemid 34729426)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.5 , pp. 1165-1176
    • Unwin, N.1    Miyazawa, A.2    Li, J.3    Fujiyoshi, Y.4
  • 68
    • 51649117317 scopus 로고    scopus 로고
    • A receptor function and loop C dynamics
    • 10.1073/pnas.0801854105 10.1073/pnas.0801854105 18757734
    • A receptor function and loop C dynamics Proc Natl Acad Sci USA 105 13604 13609 10.1073/pnas.0801854105 10.1073/pnas.0801854105 18757734
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13604-13609
    • Venkatachalan, S.P.1    Czajkowski, C.2
  • 70
    • 34548831934 scopus 로고    scopus 로고
    • Establishing an ion pair interaction in the homomeric ρ1 γ-aminobutyric acid type A receptor that contributes to the gating pathway
    • DOI 10.1074/jbc.M702314200
    • J Wang HA Lester DA Dougherty 2007 Establishing an ion pair interaction in the homomeric ρ1 γ-aminobutyric acid type A receptor that contributes to the gating pathway J Biol Chem 282 26210 26216 10.1074/jbc.M702314200 10.1074/jbc.M702314200 17606618 (Pubitemid 47443808)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.36 , pp. 26210-26216
    • Wang, J.1    Lester, H.A.2    Dougherty, D.A.3
  • 71
    • 29244442919 scopus 로고    scopus 로고
    • A unified view of the role of electrostatic interactions in modulating the gating of Cys loop receptors
    • DOI 10.1074/jbc.M508635200
    • X Xiu AP Hanek J Wang HA Lester DA Dougherty 2005 A unified view of the role of electrostatic interactions in modulating the gating of Cys loop receptors J Biol Chem 280 41655 41666 10.1074/jbc.M508635200 10.1074/jbc.M508635200 16216879 (Pubitemid 41832228)
    • (2005) Journal of Biological Chemistry , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.