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Volumn 6, Issue , 2015, Pages

The desensitization gate of inhibitory Cys-loop receptors

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID; 4 AMINOBUTYRIC ACID A RECEPTOR; 4 AMINOBUTYRIC ACID A RECEPTOR ALPHA1BETA2; CYSTEINE LOOP LIGAND GATED ION CHANNEL RECEPTOR; GLYCINE RECEPTOR; ION CHANNEL; PICROTOXIN; UNCLASSIFIED DRUG; PROTEIN SUBUNIT; RECOMBINANT PROTEIN;

EID: 84928143338     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms7829     Document Type: Article
Times cited : (112)

References (56)
  • 1
    • 84965075853 scopus 로고
    • A study of the desensitization produced by acetylcholine at the motor end-plate
    • Katz, B. & Thesleff, S. A study of the desensitization produced by acetylcholine at the motor end-plate. J. Physiol. 138, 63-80 (1957).
    • (1957) J. Physiol. , vol.138 , pp. 63-80
    • Katz, B.1    Thesleff, S.2
  • 2
    • 79953141061 scopus 로고    scopus 로고
    • Desensitization of neurotransmitter-gated ion channels during high-frequency stimulation: A comparative study of cys-loop ampa and purinergic receptors
    • Papke, D., Gonzalez-Gutierrez, G. & Grosman, C. Desensitization of neurotransmitter-gated ion channels during high-frequency stimulation: a comparative study of Cys-loop, AMPA and purinergic receptors. J. Physiol. 589, 1571-1585 (2011).
    • (2011) J. Physiol. , vol.589 , pp. 1571-1585
    • Papke, D.1    Gonzalez-Gutierrez, G.2    Grosman, C.3
  • 3
    • 0036794311 scopus 로고    scopus 로고
    • Slow phases of gabaa receptor desensitization: Structural determinants and possible relevance for synaptic function
    • Bianchi, M. T. & MacDonald, R. L. Slow phases of GABAA receptor desensitization: structural determinants and possible relevance for synaptic function. J. Physiol. 544, 3-18 (2002).
    • (2002) J. Physiol. , vol.544 , pp. 3-18
    • Bianchi, M.T.1    Macdonald, R.L.2
  • 4
    • 42049089558 scopus 로고    scopus 로고
    • Surface mobility of postsynaptic ampars tunes synaptic transmission
    • Heine, M. et al. Surface mobility of postsynaptic AMPARs tunes synaptic transmission. Science 320, 201-205 (2008).
    • (2008) Science , vol.320 , pp. 201-205
    • Heine, M.1
  • 5
    • 0030025395 scopus 로고    scopus 로고
    • The impact of receptor desensitization on fast synaptic transmission
    • Jones, M. V. & Westbrook, G. L. The impact of receptor desensitization on fast synaptic transmission. Trends Neurosci. 19, 96-101 (1996).
    • (1996) Trends Neurosci. , vol.19 , pp. 96-101
    • Jones, M.V.1    Westbrook, G.L.2
  • 6
    • 0034331246 scopus 로고    scopus 로고
    • Slow desensitization regulates the availability of synaptic gabaa receptors
    • Overstreet, L. S., Jones, M. V. &Westbrook, G. L. Slow desensitization regulates the availability of synaptic GABAA receptors. J. Neurosci. 20, 7914-7921 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 7914-7921
    • Overstreet, L.S.1    Jones, M.V.2    Westbrook, G.L.3
  • 7
    • 84928104432 scopus 로고    scopus 로고
    • (eds Sheng M. Sabatini B. L. & Sudhof T. C.) (Cold Spring Harbor Laboratory Press
    • Smart, T. G. & Paoletti, P. in The Synapse. (eds Sheng, M., Sabatini, B. L. & Sudhof, T. C.) 191-216 (Cold Spring Harbor Laboratory Press, 2012).
    • (2012) The Synapse , pp. 191-216
    • Smart, T.G.1    Paoletti, P.2
  • 8
    • 33645321641 scopus 로고    scopus 로고
    • Glutamate receptors at atomic resolution
    • Mayer, M. L. Glutamate receptors at atomic resolution. Nature 440, 456-462 (2006).
    • (2006) Nature , vol.440 , pp. 456-462
    • Mayer, M.L.1
  • 9
    • 33847769253 scopus 로고    scopus 로고
    • Structure and mechanism of kainate receptor modulation by anions
    • Plested, A. J. R. & Mayer, M. L. Structure and mechanism of kainate receptor modulation by anions. Neuron 53, 829-841 (2007).
    • (2007) Neuron , vol.53 , pp. 829-841
    • Plested, A.J.R.1    Mayer, M.L.2
  • 10
    • 84906282398 scopus 로고    scopus 로고
    • Structural mechanism of glutamate receptor activation and desensitization
    • Meyerson, J. R. et al. Structural mechanism of glutamate receptor activation and desensitization. Nature 514, 328-334 (2014).
    • (2014) Nature , vol.514 , pp. 328-334
    • Meyerson, J.R.1
  • 11
    • 0037118049 scopus 로고    scopus 로고
    • Mechanism of glutamate receptor desensitization
    • Sun, Y. et al. Mechanism of glutamate receptor desensitization. Nature 417, 245-253 (2002).
    • (2002) Nature , vol.417 , pp. 245-253
    • Sun, Y.1
  • 12
    • 84861963413 scopus 로고    scopus 로고
    • Structure and pharmacology of pentameric receptor channels: From bacteria to brain
    • Corringer, P. J. et al. Structure and pharmacology of pentameric receptor channels: from bacteria to brain. Structure 20, 941-956 (2012).
    • (2012) Structure , vol.20 , pp. 941-956
    • Corringer, P.J.1
  • 13
    • 0034724090 scopus 로고    scopus 로고
    • Gabar1/gabaaa1 receptor chimeras to study receptor desensitization
    • Martinez-Torres, A., Demuro, A. & Miledi, R. GABAr1/GABAAa1 receptor chimeras to study receptor desensitization. Proc. Natl Acad. Sci. USA 97, 3562-3566 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3562-3566
    • Martinez-Torres, A.1    Demuro, A.2    Miledi, R.3
  • 14
    • 79957953215 scopus 로고    scopus 로고
    • Principles of activation and permeation in an anion-selective cys-loop receptor
    • Hibbs, R. E. & Gouaux, E. Principles of activation and permeation in an anion-selective Cys-loop receptor. Nature 474, 54-60 (2011).
    • (2011) Nature , vol.474 , pp. 54-60
    • Hibbs, R.E.1    Gouaux, E.2
  • 15
    • 0029174650 scopus 로고
    • Structure and pharmacology of vertebrate gabaa receptor subtypes
    • Whiting, P. J., McKernan, R. M. & Wafford, K. A. Structure and pharmacology of vertebrate GABAA receptor subtypes. Int. Rev. Neurobiol. 38, 95-138 (1995).
    • (1995) Int. Rev. Neurobiol. , vol.38 , pp. 95-138
    • Whiting, P.J.1    McKernan, R.M.2    Wafford, K.A.3
  • 16
    • 84860195444 scopus 로고    scopus 로고
    • Benzodiazepines modulate gabaa receptors by regulating the preactivation step after gaba binding
    • Gielen, M. C., Lumb, M. J. & Smart, T. G. Benzodiazepines modulate GABAA receptors by regulating the preactivation step after GABA binding. J. Neurosci. 32, 5707-5715 (2012).
    • (2012) J. Neurosci. , vol.32 , pp. 5707-5715
    • Gielen, M.C.1    Lumb, M.J.2    Smart, T.G.3
  • 17
    • 5444265600 scopus 로고    scopus 로고
    • Molecular dynamics simulation links conformation of a pore-flanking region to hyperekplexia-related dysfunction of the inhibitory glycine receptor
    • Breitinger, H. G. et al. Molecular dynamics simulation links conformation of a pore-flanking region to hyperekplexia-related dysfunction of the inhibitory glycine receptor. Chem. Biol. 11, 1339-1350 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 1339-1350
    • Breitinger, H.G.1
  • 18
    • 58149267953 scopus 로고    scopus 로고
    • X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation
    • Bocquet, N. et al. X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation. Nature 457, 111-114 (2009).
    • (2009) Nature , vol.457 , pp. 111-114
    • Bocquet, N.1
  • 19
    • 41149168686 scopus 로고    scopus 로고
    • X-ray structure of a prokaryotic pentameric ligand-gated ion channel
    • Hilf, R. J. C. & Dutzler, R. X-ray structure of a prokaryotic pentameric ligand-gated ion channel. Nature 452, 375-379 (2008).
    • (2008) Nature , vol.452 , pp. 375-379
    • Hilf, R.J.C.1    Dutzler, R.2
  • 20
    • 58149242730 scopus 로고    scopus 로고
    • Structure of a potentially open state of a proton-Activated pentameric ligand-gated ion channel
    • Hilf, R. J. C. & Dutzler, R. Structure of a potentially open state of a proton-Activated pentameric ligand-gated ion channel. Nature 457, 115-118 (2009).
    • (2009) Nature , vol.457 , pp. 115-118
    • Hilf, R.J.C.1    Dutzler, R.2
  • 21
    • 0031870973 scopus 로고    scopus 로고
    • Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism
    • Auerbach, A. & Akk, G. Desensitization of mouse nicotinic acetylcholine receptor channels. A two-gate mechanism. J. Gen. Physiol. 112, 181-197 (1998).
    • (1998) J. Gen. Physiol. , vol.112 , pp. 181-197
    • Auerbach, A.1    Akk, G.2
  • 22
    • 33744477329 scopus 로고    scopus 로고
    • Block of muscle nicotinic receptors by choline suggests that the activation and desensitization gates act as distinct molecular entities
    • Purohit, Y. & Grosman, C. Block of muscle nicotinic receptors by choline suggests that the activation and desensitization gates act as distinct molecular entities. J. Gen. Physiol. 127, 703-717 (2006).
    • (2006) J. Gen. Physiol. , vol.127 , pp. 703-717
    • Purohit, Y.1    Grosman, C.2
  • 23
    • 33846592870 scopus 로고    scopus 로고
    • The location of a closed channel gate in the gabaa receptor channel
    • Bali, M. & Akabas, M. H. The location of a closed channel gate in the GABAA receptor channel. J. Gen. Physiol. 129, 145-159 (2007).
    • (2007) J. Gen. Physiol. , vol.129 , pp. 145-159
    • Bali, M.1    Akabas, M.H.2
  • 24
    • 0029018726 scopus 로고
    • Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, picrotoxin, into an allosteric potentiator
    • Lynch, J. W., Rajendra, S., Barry, P. H. & Schofield, P. R. Mutations affecting the glycine receptor agonist transduction mechanism convert the competitive antagonist, Picrotoxin, into an allosteric potentiator. J. Biol. Chem. 270, 13799-13806 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 13799-13806
    • Lynch, J.W.1    Rajendra, S.2    Barry, P.H.3    Schofield, P.R.4
  • 25
    • 34447524895 scopus 로고    scopus 로고
    • Mechanisms for picrotoxinin and picrotin blocks of a2 homomeric glycine receptors
    • Wang, D. S. et al. Mechanisms for picrotoxinin and picrotin blocks of a2 homomeric glycine receptors. J. Biol. Chem. 282, 16016-16035 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 16016-16035
    • Wang, D.S.1
  • 26
    • 39449096028 scopus 로고    scopus 로고
    • Aromatic residues at position 55 of rat alpha7 nicotinic acetylcholine receptors are critical for maintaining rapid desensitization
    • Gay, E. A., Giniatullin, R., Skorinkin, A. & Yakel, J. L. Aromatic residues at position 55 of rat alpha7 nicotinic acetylcholine receptors are critical for maintaining rapid desensitization. J. Physiol. 586, 1105-1115 (2008).
    • (2008) J. Physiol. , vol.586 , pp. 1105-1115
    • Gay, E.A.1    Giniatullin, R.2    Skorinkin, A.3    Yakel, J.L.4
  • 27
    • 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
    • Bouzat, C., Bartos, M., Corradi, J. & Sine, S. M. The interface between extracellular and transmembrane domains of homomeric cys-loop receptors governs open-channel lifetime and rate of desensitization. J. Neurosci. 28, 7808-7819 (2008).
    • (2008) J. Neurosci. , vol.28 , pp. 7808-7819
    • Bouzat, C.1    Bartos, M.2    Corradi, J.3    Sine, S.M.4
  • 28
    • 80055074583 scopus 로고    scopus 로고
    • Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor
    • Wang, Q. & Lynch, J. W. Activation and desensitization induce distinct conformational changes at the extracellular-transmembrane domain interface of the glycine receptor. J. Biol. Chem. 286, 38814-38824 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 38814-38824
    • Wang, Q.1    Lynch, J.W.2
  • 29
    • 77950494200 scopus 로고    scopus 로고
    • Binding activation and modulation of cys-loop receptors
    • Miller, P. S. & Smart, T. G. Binding, activation and modulation of Cys-loop receptors. Trends Pharmacol. Sci. 31, 161-174 (2010).
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 161-174
    • Miller, P.S.1    Smart, T.G.2
  • 30
    • 84868258417 scopus 로고    scopus 로고
    • Conformational transitions underlying pore opening and desensitization in membrane-embedded gloeobacter violaceus ligand-gated ion channel (glic)
    • Velisetty, P., Chalamalasetti, S. V. & Chakrapani, S. Conformational transitions underlying pore opening and desensitization in membrane-embedded gloeobacter violaceus ligand-gated ion channel (GLIC). J. Biol. Chem. 287, 36864-36872 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 36864-36872
    • Velisetty, P.1    Chalamalasetti, S.V.2    Chakrapani, S.3
  • 31
    • 0032985839 scopus 로고    scopus 로고
    • Nitroxide spin-spin interactions: Applications to protein structure and dynamics
    • Hustedt, E. J. & Beth, A. H. Nitroxide spin-spin interactions: applications to protein structure and dynamics. Annu. Rev. Biophys. Biomol. Struct. 28, 129-153 (1999).
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 129-153
    • Hustedt, E.J.1    Beth, A.H.2
  • 32
    • 84906568725 scopus 로고    scopus 로고
    • X-ray structures of glucl in apo states reveal a gating mechanism of cys-loop receptors
    • Althoff, T., Hibbs, R. E., Banerjee, S. & Gouaux, E. X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors. Nature 512, 333-337 (2014).
    • (2014) Nature , vol.512 , pp. 333-337
    • Althoff, T.1    Hibbs, R.E.2    Banerjee, S.3    Gouaux, E.4
  • 33
    • 33645302360 scopus 로고    scopus 로고
    • Recent advances in cys-loop receptor structure and function
    • Sine, S. M. & Engel, A. G. Recent advances in Cys-loop receptor structure and function. Nature 440, 448-455 (2006).
    • (2006) Nature , vol.440 , pp. 448-455
    • Sine, S.M.1    Engel, A.G.2
  • 35
    • 77954485089 scopus 로고    scopus 로고
    • Structural mechanism of c-type inactivation in k+ channels
    • Cuello, L. G., Jogini, V., Cortes, D. M. & Perozo, E. Structural mechanism of C-type inactivation in K+ channels. Nature 466, 203-208 (2010).
    • (2010) Nature , vol.466 , pp. 203-208
    • Cuello, L.G.1    Jogini, V.2    Cortes, D.M.3    Perozo, E.4
  • 36
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh, J., Gamal El-Din, T. M., Scheuer, T., Zheng, N. & Catterall, W. A. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature 486, 135-139 (2012).
    • (2012) Nature , vol.486 , pp. 135-139
    • Payandeh, J.1    Gamal El-Din, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 37
    • 84861952634 scopus 로고    scopus 로고
    • Crystal structure of an orthologue of the nachbac voltagegated sodium channel
    • Zhang, X. et al. Crystal structure of an orthologue of the NaChBac voltagegated sodium channel. Nature 486, 130-134 (2012).
    • (2012) Nature , vol.486 , pp. 130-134
    • Zhang, X.1
  • 38
    • 33745216690 scopus 로고    scopus 로고
    • A structural interpretation of voltage-gated potassium channel inactivation
    • Kurata, H. T. & Fedida, D. A structural interpretation of voltage-gated potassium channel inactivation. Prog. Biophys. Mol. Biol. 92, 185-208 (2006).
    • (2006) Prog. Biophys. Mol. Biol. , vol.92 , pp. 185-208
    • Kurata, H.T.1    Fedida, D.2
  • 39
    • 0027828292 scopus 로고
    • Effects of external cations and mutations in the pore region on c-type inactivation of shaker potassium channels
    • Lopez-Barneo, J., Hoshi, T., Heinemann, S. H. & Aldrich, R. W. Effects of external cations and mutations in the pore region on C-type inactivation of Shaker potassium channels. Receptors Channels 1, 61-71 (1993).
    • (1993) Receptors Channels , vol.1 , pp. 61-71
    • Lopez-Barneo, J.1    Hoshi, T.2    Heinemann, S.H.3    Aldrich, R.W.4
  • 40
    • 0026079907 scopus 로고
    • Tetraethylammonium blockade distinguishes two inactivation mechanisms in voltage-Activated k+ channels
    • Choi, K. L., Aldrich, R. W. & Yellen, G. Tetraethylammonium blockade distinguishes two inactivation mechanisms in voltage-Activated K+ channels. Proc. Natl Acad. Sci. USA 88, 5092-5095 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 5092-5095
    • Choi, K.L.1    Aldrich, R.W.2    Yellen, G.3
  • 41
    • 0031452203 scopus 로고    scopus 로고
    • Pharmacological and physiological characterization of murine homomeric b3 gabaa receptors
    • Wooltorton, J. R., Moss, S. J. & Smart, T. G. Pharmacological and physiological characterization of murine homomeric b3 GABAA receptors. Eur. J. Neurosci. 9, 2225-2235 (1997).
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 2225-2235
    • Wooltorton, J.R.1    Moss, S.J.2    Smart, T.G.3
  • 42
    • 84905669878 scopus 로고    scopus 로고
    • Crystal structure of a human gaba receptor
    • Miller, P. S. & Aricescu, A. R. Crystal structure of a human GABA receptor. Nature 512, 270-275 (2014).
    • (2014) Nature , vol.512 , pp. 270-275
    • Miller, P.S.1    Aricescu, A.R.2
  • 43
    • 80053244433 scopus 로고    scopus 로고
    • Single-channel and structural foundations of neuronal a7 acetylcholine receptor potentiation
    • daCosta, C. J., Free, C. R., Corradi, J., Bouzat, C. & Sine, S. M. Single-channel and structural foundations of neuronal a7 acetylcholine receptor potentiation. J. Neurosci. 31, 13870-13879 (2011).
    • (2011) J. Neurosci. , vol.31 , pp. 13870-13879
    • Dacosta, C.J.1    Free, C.2    Corradi, J.3    Bouzat, C.4    Sine, S.M.5
  • 44
    • 79955008177 scopus 로고    scopus 로고
    • Agonist activation of a7 nicotinic acetylcholine receptors via an allosteric transmembrane site
    • Gill, J. K. et al. Agonist activation of a7 nicotinic acetylcholine receptors via an allosteric transmembrane site. Proc. Natl Acad. Sci. USA 108, 5867-5872 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 5867-5872
    • Gill, J.K.1
  • 45
    • 81555222819 scopus 로고    scopus 로고
    • Investigation of the molecular mechanism of the a7 nicotinic acetylcholine receptor positive allosteric modulator pnu-120596 provides evidence for two distinct desensitized states
    • Williams, D. K., Wang, J. & Papke, R. L. Investigation of the molecular mechanism of the a7 nicotinic acetylcholine receptor positive allosteric modulator PNU-120596 provides evidence for two distinct desensitized states. Mol. Pharmacol. 80, 1013-1032 (2011).
    • (2011) Mol. Pharmacol. , vol.80 , pp. 1013-1032
    • Williams, D.K.1    Wang, J.2    Papke, R.L.3
  • 46
    • 77952692954 scopus 로고    scopus 로고
    • Nicotine addiction and nicotinic receptors: Lessons from genetically modified mice
    • Changeux, J. P. Nicotine addiction and nicotinic receptors: lessons from genetically modified mice. Nat. Rev. Neurosci. 11, 389-401 (2010).
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 389-401
    • Changeux, J.P.1
  • 47
    • 77955578706 scopus 로고    scopus 로고
    • Mutations affecting gabaergic signaling in seizures and epilepsy
    • Galanopoulou, A. Mutations affecting GABAergic signaling in seizures and epilepsy. Pflügers Arch. 460, 505-523 (2010).
    • (2010) Pflügers Arch. , vol.460 , pp. 505-523
    • Galanopoulou, A.1
  • 48
    • 80054090004 scopus 로고    scopus 로고
    • The gaba system in anxiety and depression and its therapeutic potential
    • Mohler, H. The GABA system in anxiety and depression and its therapeutic potential. Neuropharmacology 62, 42-53 (2012).
    • (2012) Neuropharmacology , vol.62 , pp. 42-53
    • Mohler, H.1
  • 49
    • 27844445687 scopus 로고    scopus 로고
    • Molecular basis for zinc potentiation at strychnine-sensitive glycine receptors
    • Miller, P. S., Da Silva, H. M. & Smart, T. G. Molecular basis for zinc potentiation at strychnine-sensitive glycine receptors. J. Biol. Chem. 280, 37877-37884 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37877-37884
    • Miller, P.S.1    Da Silva, H.M.2    Smart, T.G.3
  • 50
    • 84855499675 scopus 로고    scopus 로고
    • Clconcentration changes and desensitization of gabaa and glycine receptors
    • Karlsson, U., Druzin, M. & Johansson, S. Cl concentration changes and desensitization of GABAA and glycine receptors. J. Gen. Physiol. 138, 609-626 (2011).
    • (2011) J. Gen. Physiol. , vol.138 , pp. 609-626
    • Karlsson, U.1    Druzin, M.2    Johansson, S.3
  • 51
    • 77952909252 scopus 로고    scopus 로고
    • Distinct activities of gaba agonists at synaptic-And extrasynaptic-type gabaa receptors
    • Mortensen, M., Ebert, B., Wafford, K. & Smart, T. G. Distinct activities of GABA agonists at synaptic-And extrasynaptic-type GABAA receptors. J. Physiol. 588, 1251-1268 (2010).
    • (2010) J. Physiol. , vol.588 , pp. 1251-1268
    • Mortensen, M.1    Ebert, B.2    Wafford, K.3    Smart, T.G.4
  • 54
    • 35748972048 scopus 로고    scopus 로고
    • Mole a voronoi diagram-based explorer of molecular channels, pores, and tunnels
    • Petrek, M., Kosinova, P., Koca, J. & Otyepka, M. MOLE: a Voronoi diagram-based explorer of molecular channels, pores, and tunnels. Structure 15, 1357-1363 (2007).
    • (2007) Structure , vol.15 , pp. 1357-1363
    • Petrek, M.1    Kosinova, P.2    Koca, J.3    Otyepka, M.4
  • 55
    • 49649102025 scopus 로고    scopus 로고
    • On the nature of partial agonism in the nicotinic receptor superfamily
    • Lape, R., Colquhoun, D. & Sivilotti, L. G. On the nature of partial agonism in the nicotinic receptor superfamily. Nature 454, 722-727 (2008).
    • (2008) Nature , vol.454 , pp. 722-727
    • Lape, R.1    Colquhoun, D.2    Sivilotti, L.G.3
  • 56
    • 0030329985 scopus 로고    scopus 로고
    • A functional comparison of the antagonists bicuculline and picrotoxin at recombinant gabaa receptors
    • Krishek, B. J., Moss, S. J. & Smart, T. G. A functional comparison of the antagonists bicuculline and picrotoxin at recombinant GABAA receptors. Neuropharmacol. 35, 1289-1298 (1996).
    • (1996) Neuropharmacol. , vol.35 , pp. 1289-1298
    • Krishek, B.J.1    Moss, S.J.2    Smart, T.G.3


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