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1
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0024918350
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Explorations of the Nicotinic Acetylcholine Receptor
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(1991)
Harvey Lect
, vol.85
, pp. 71-107
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Karlin1
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2
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0024848780
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The Structure of Ion Channels in Membranes of Excitable Cells
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(1989)
Neuron
, vol.3
, pp. 665-676
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Unwin1
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9
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0025997336
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Primary Structure and Functional Expression of the 5HT3 Receptor, a Serotonin-Gated Ion Channel
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of outstanding interest, This important study not only describes the characterization of a new subtype of serotonin receptor(s) with significant sequence identity to the neuronal nAchR (See Fig. 2), but also adds a new member to the list of excitatory neurotransmitters.
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(1991)
Science
, vol.254
, pp. 432-437
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Maricq1
Peterson2
Brake3
Meyers4
Julius5
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10
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0003443746
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of outstanding interest, 2nd edn., Sinauer, Sunderland, This extremely well written edition surpasses the first in its thorough treatment of ion channels. Chapters 1,6 and 9–17 are highly recommended reading for those who desire to tackle problems of permeation. When ion concentrations are raised sufficiently, all known channels exhibit saturations, competition for binding sites and block by small ions. The Goldman-Hodgkin-Katz (GHK) equation, which assumes independent movement of ions and defines two empirical measures of permeability (relative and absolute), cannot adequately describe these phenomena. Under these conditions, GHK fails to predict absolute permeability whereas the ratios still serve as useful approximations.
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(1992)
Ion Channels of Excitable Membranes
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Hille1
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11
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0025982125
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Strategies for Studying Permeation at Voltage-Gated Ion Channels
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of special interest, This article crystalizes some important concepts in the study of permeation, including the calculation of relative permeability. It also examines some of the approaches used for the voltage-gated cation channels.
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(1991)
Annu Rev Physiol
, vol.53
, pp. 477-496
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Lester1
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12
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0025360229
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Permeation of Calcium through Excitatory Amino Acid Receptor Channels in Cultured Rat Hippocampal Neurons
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(1990)
J Physiol
, vol.424
, pp. 151-165
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Iino1
Ozawa2
Tsuzuki3
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13
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0025828670
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Pentametric Structure and Subunit Stoichiometry of a Neuronal Nicotinic Receptor
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of outstanding interest, Taking advantage of some of the unique properties (conductance states) of the mutant chick neuronal nAchRs, this study proposes a stoichiometru for neuronal nAchRs. Site-directed mutagenesis and single-channel analysis of combinations of mutant and wild-type subunits derived a pentamer structure with two Ach-binding subunits. This structure is also applicable to other species. The chick neuronal nAchRs cloned in the Ballivet laboratory are designated as α and non-α, instead of β, which is used to designate the rat neuronal nAchRs.
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(1991)
Nature
, vol.350
, pp. 235-238
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Cooper1
Couturier2
Baijjvet3
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18
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0026079817
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Mutations in the Channel Domain Alter Desensitization of a Neuronal Nicotinic Receptor
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of outstanding interest, This elegant study combines the best of site-directed mutagenesis and electrophysiology to obtain keen insights into the structure function of the nAchRs. This study has far reaching applications for all nAchRs as well as for the structural basis of desensitization in general.
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(1991)
Nature
, vol.353
, pp. 846-849
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Revah1
Bertrand2
Gaizi3
Devillers-Thiery4
Mulle5
Hussy6
Bertrand7
Ballivet8
Changeux9
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19
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0026586188
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Calcium modulation and High Permeability of Neuronal Nicotinic Acetylcholine Receptors
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2+ in a dose-dependent manner.
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(1992)
Neuron
, vol.8
, pp. 127-134
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Verino1
Amador2
Luetje3
Patrick4
Dani5
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20
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0026580364
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Calcium Influx through Nicotinic Receptor in Rat Central Neurons: Its Relevance to Cellular Regulation
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2+. The physiological significance of these fluxes are discussed.
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(1992)
Neuron
, vol.8
, pp. 135-143
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Mulle1
Choquet2
Korn3
Changeux4
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21
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0023492484
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Permeation and Block of N-Methyl-D-Aspartic Acid Receptor Channels by Divalent Cations in Mouse Cultured Central Neurons
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(1987)
J Physiol
, vol.394
, pp. 501-527
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Mayer1
Westbrook2
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22
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0026716690
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Potentiation of Nicotinic Receptor Response by External Calcium in Rat Central Neurons
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2+ is postulated to play a role in regulating synaptic function.
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(1992)
Neuron
, vol.8
, pp. 937-945
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Mulle1
Lena2
Changeux3
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23
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0025806145
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Permeation of Calcium Ions Through Non-NMDA Glutamate Channels in Retinal Bipolar Cells
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(1991)
Science
, vol.251
, pp. 1613-1615
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Gilbertson1
Scobey2
Wilson3
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24
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0025947845
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Agonist-Activated Cobalt Uptake Identifies Divalent Cation-Permeable Kainate Receptors on Neurons and Glial Cells
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(1991)
Neuron
, vol.7
, pp. 509-518
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Pruss1
Akeson2
Racke3
Wilburn4
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27
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0025923461
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Calcium Permeability of KA-AMPA-gated Ion Channels Depends on Receptor Subunit Composition
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2+ currents in oocytes that express GluR1, Glur3, GluR1 + GluR3 subunits, but not in those that express GluR1 + GluR2 or GluR2 + GluR3. These results suggest that some non-NMDA receptors may also flux significant amounts of calcium into the cell. These results are supported by recent studies of KA/AMPA GluRs in nerve cells [23,24].
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(1991)
Science
, vol.252
, pp. 851-853
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Hollmann1
Hartley2
Heinemann3
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28
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0025784548
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Identification of a Site in Glutamate Receptor Subunits that Controls Calcium Permeability
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− currents endogenous to oocytes. The numbering of the residue at the Q/R site of each subunit begins at the putative translation initiator methionine instead of the amino terminus of the mature protein.
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(1991)
Science
, vol.253
, pp. 1028-1031
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Hume1
Dingledine2
Heinemann3
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29
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0025879427
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Structural Determinants of Ion Flow Through Recombinant Glutamate Receptor Channels
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2+-activated Cl-currents encountered in [28⊎⊎]. The nomenclature used for the GluR subunits is alphabetical instead of numerical (GluR = GluRA, etc.).
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(1991)
Science
, vol.252
, pp. 1715-1717
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Verdoorn1
Burnashev2
Monyer3
Seeburg4
Sakmann5
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30
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0026543243
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Divalent Ion Permeability of AMPA Receptor Channels Is Dominated by the Edited Form of a Single Subunit
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of outstanding interest, A series of mutants at the Q/R site of several GluR subunits was constructed and the I–V relations and divalent cation permeabilities were studied for homomeric and heteromeric channels. These results imply that a single R in a putative pentameric receptor may present a sufficient barrier to drastically affect divalent cation permeability and produce a weak outwardly rectifying channel.
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(1992)
Neuron
, vol.8
, pp. 189-198
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Burnashev1
Monyer2
Seeburg3
Sakmann4
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32
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0026675738
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Structural determinants of Barium Permeation and Rectification in Non-NMDA Glutamate Receptor Channels
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of outstanding interest, This study extends the work done with the AMPA-preferring subunits (GluR1-GluR4 [28⊎⊎]) and the KA-preferring subunits (GluR5–7), where the Q/R site also plays an important role. The authors propose that the Q/R site may reside in TM3, instead of TM2, so that the selectivity filter resides near the cytoplasmic side, similar to the intermediate ring of negative charge in the nAchR channels. Membrane topology studies are needed to test this interesting hypothesis.
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(1992)
J Neuroscience
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Dingledine1
Hume2
Heinemann3
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33
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0026419327
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Molecular Cloning and Characterization of Rat NMDA Receptor
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of outstanding interest, Describes how the first NMDA receptor subunit was obtained by expression cloning. This subunit has approximately 22% sequence identity with other GluR subunits and has an equivalent number of hydrophobic domains, suggesting a similar structure. The NMDA receptor is by far the most interesting and complex of all the GluRs.
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(1991)
Nature
, vol.354
, pp. 31-37
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Moriyoshi1
Masu2
Ishii3
Shigemoto4
Mizuno5
Nakanishi6
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34
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0025995296
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RNA Editing in Brain Controls a Determinant of Ion Flow in Glutamate-Gated Channels
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of outstanding interest, This extremely thorough study proposes that RNA editing of certain GluR transcripts converts a glutamine to argine codon in a hughly conserved region. Although not the first example in eukaryotes, this rare post-transcriptional modification needs further study to determine its mechanism. The ramifications of this Q-to-R conversion range from modifying the channel properties to an important regulatory mechanism in neurons at different times of development.
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(1991)
Cell
, vol.67
, pp. 1-20
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Sommer1
Kohler2
Sprengel3
Seeburg4
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35
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0026005920
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Both NMDA and Non-NMDA Subtypes of Glutamate Receptors Are Concentrated at Synapses on Cerebral Cortical Neurons in Culture
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of special interest, This important study suggests that both NMDA and non-NMDA GluR receptor subtypes are found together beneath synapses in cultured cortical neurons. Organized in post-synaptic densities, these two receptor subtypes may represent a single unit of functional signal transduction. This contrasts with previous studies, which showed that these two subtypes are colocalized in hippocampal neurons in culture, and that the slow kinetics of NMDA receptor activation and inactivation are intrinsic properties of the NMDAR and not a function of glutamate diffusion.
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(1991)
Neuron
, vol.7
, pp. 593-603
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Jones1
Baughman2
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36
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0026560616
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The Aromatic Binding Site for Tetraethylammonium Ion on Potassium Channels
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+ ions through cation-p orbital interactions is also postulated.
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(1992)
Neuron
, vol.8
, pp. 483-491
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Heginbotham1
Mackinnon2
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37
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0025025261
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Progressive Alignment and Phylogenetic Tree Construction of Protein Sequences
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(1990)
Methods Enzymol
, vol.183
, pp. 375-387
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Feng1
Doolittle2
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38
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0025342578
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Nearest Neighbor Procedure for Relating Progressively Aligned Amino Acid Sequences
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(1990)
Methods Enzymol
, vol.183
, pp. 659-669
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Doolittle1
Feng2
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