Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating (Q27649689)

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English	Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating	scientific article

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Europe PubMed Central

PMC publication ID

6670991

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title

Structural and single-channel results indicate that the rates of ligand binding domain closing and opening directly impact AMPA receptor gating (English)

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Europe PubMed Central

PMC publication ID

6670991

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main subject

ligand binding

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author

Elias Lolis

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3

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PMC publication ID

6670991

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author name string

Wei Zhang

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1

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Europe PubMed Central

PMC publication ID

6670991

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Yoonsang Cho

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2

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PMC publication ID

6670991

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James R Howe

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4

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PMC publication ID

6670991

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language of work or name

English

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publication date

1 January 2008

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PMC publication ID

6670991

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1 January 2020

published in

Journal of Neuroscience

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PMC publication ID

6670991

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volume

28

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PMC publication ID

6670991

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issue

4

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PMC publication ID

6670991

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page(s)

932-943

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6670991

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The glutamate receptor ion channels

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PubMed

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Ca2+/calmodulin-kinase II enhances channel conductance of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate type glutamate receptors

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Control of GluR1 AMPA receptor function by cAMP-dependent protein kinase

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Heterogeneous conductance levels of native AMPA receptors

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Agonist-induced isomerization in a glutamate receptor ligand-binding domain. A kinetic and mutagenetic analysis.

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Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core

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Heteromeric AMPA receptors assemble with a preferred subunit stoichiometry and spatial arrangement

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Mechanism of glutamate receptor desensitization

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Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core

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The TB structural genomics consortium crystallization facility: towards automation from protein to electron density

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Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate

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How AMPA receptor desensitization depends on receptor occupancy.

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Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes

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Structural basis for partial agonist action at ionotropic glutamate receptors

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Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling

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Reaction mechanism determines NMDA receptor response to repetitive stimulation

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Single-channel behavior of heteromeric alpha1beta glycine receptors: an attempt to detect a conformational change before the channel opens

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Microsecond-to-millisecond conformational dynamics demarcate the GluR2 glutamate receptor bound to agonists glutamate, quisqualate, and AMPA.

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Likelihood-enhanced fast translation functions

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AMPA receptor binding cleft mutations that alter affinity, efficacy, and recovery from desensitization.

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Stargazin modulates AMPA receptor gating and trafficking by distinct domains

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Mechanism of partial agonism at NMDA receptors for a conformationally restricted glutamate analog.

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Mechanism of positive allosteric modulators acting on AMPA receptors

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Influence of agonist concentration on AMPA and kainate channels in CA1 pyramidal cells in rat hippocampal slices

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Glutamate receptors at atomic resolution

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The relationship between agonist potency and AMPA receptor kinetics

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Interdomain interactions in AMPA and kainate receptors regulate affinity for glutamate.

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https://pubmed.ncbi.nlm.nih.gov/18216201

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12 December 2020

based on heuristic

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Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor

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12 December 2020

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Disruption of interdomain interactions in the glutamate binding pocket affects differentially agonist affinity and efficacy of N-methyl-D-aspartate receptor activation

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Currents through single glutamate receptor channels in outside-out patches from rat cerebellar granule cells

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Single-channel study of the spasmodic mutation alpha1A52S in recombinant rat glycine receptors

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Dynamics of the S1S2 glutamate binding domain of GluR2 measured using 19F NMR spectroscopy

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Structural aspects of AMPA receptor activation, desensitization and deactivation

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A stepwise mechanism for acetylcholine receptor channel gating

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Quisqualate activates a rapidly inactivating high conductance ionic channel in hippocampal neurons

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A reinterpretation of mammalian sodium channel gating based on single channel recording

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LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions

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Single channel properties of cloned NMDA receptors in a human cell line: comparison with results from Xenopus oocytes

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based on heuristic

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Satisfying hydrogen bonding potential in proteins

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based on heuristic

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Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events

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based on heuristic

inferred from PubMed ID database lookup

Single-channel properties of recombinant AMPA receptors depend on RNA editing, splice variation, and subunit composition.

1 reference

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based on heuristic

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The tetrameric structure of a glutamate receptor channel

1 reference

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based on heuristic

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Structure of a glutamate-receptor ligand-binding core in complex with kainate

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Identifiers

DOI

10.1523/JNEUROSCI.3309-07.2008

1 reference

stated in

Europe PubMed Central

PMC publication ID

6670991

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18216201%20AND%20SRC:MED&resulttype=core&format=json

retrieved

1 January 2020

PMC publication ID

6670991

1 reference

stated in

Europe PubMed Central

PMC publication ID

6670991

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18216201%20AND%20SRC:MED&resulttype=core&format=json

retrieved

1 January 2020

PubMed publication ID

18216201

1 reference

stated in

Europe PubMed Central

PMC publication ID

6670991

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18216201%20AND%20SRC:MED&resulttype=core&format=json

retrieved

1 January 2020

 

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