Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors - Test2 - elhamkhani - TriplyDB

Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors

Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors

http://www.wikidata.org/entity/Q27667242

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Structure, Dynamics, and Allosteric Potential of Ionotropic Glutamate Receptor N-Terminal Domains Glutamatergic autoencephalitides: an emerging field Functional insights from glutamate receptor ion channel structures Emerging models of glutamate receptor ion channel structure and function Crystal structure of the glutamate receptor GluA1 N-terminal domain Dynamics and allosteric potential of the AMPA receptor N-terminal domain Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers Structure and Assembly Mechanism for Heteromeric Kainate Receptors Comparative Dynamics of NMDA- and AMPA-Glutamate Receptor N-Terminal Domains Structural Insights into Competitive Antagonism in NMDA Receptors Crystal structure of a heterotetrameric NMDA receptor ion channel Activation of NMDA receptors and the mechanism of inhibition by ifenprodil.An alternating GluN1-2-1-2 subunit arrangement in mature NMDA receptors Amino terminal domains of the NMDA receptor are organized as local heterodimers Genetically encoding a light switch in an ionotropic glutamate receptor reveals subunit-specific interfaces.Single-particle electron microscopy in the study of membrane protein structure Tissue-type plasminogen activator controls neuronal death by raising surface dynamics of extrasynaptic NMDA receptors.Molecular dissection of the interaction between the AMPA receptor and cornichon homolog-3.NR2B-deficient mice are more sensitive to the locomotor stimulant and depressant effects of ethanol ER to synapse trafficking of NMDA receptors Building and breaking interfaces: how a receptor takes shape Arrangement of subunits in functional NMDA receptors.Interaction of the M4 segment with other transmembrane segments is required for surface expression of mammalian α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors.Emerging structural insights into the function of ionotropic glutamate receptors.Mapping the binding of GluN2B-selective N-methyl-D-aspartate receptor negative allosteric modulators.Differences in AMPA and kainate receptor interactomes facilitate identification of AMPA receptor auxiliary subunit GSG1L Key amino acid residues within the third membrane domains of NR1 and NR2 subunits contribute to the regulation of the surface delivery of N-methyl-D-aspartate receptors.Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.Structure and function of glutamate receptor amino terminal domains.Influence of GluN2 subunit identity on NMDA receptor function.Molecular basis of positive allosteric modulation of GluN2B NMDA receptors by polyamines.The σ-1 receptor interacts directly with GluN1 but not GluN2A in the GluN1/GluN2A NMDA receptor.α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.The N-terminal domain modulates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor desensitization.Cysteine residues 87 and 320 in the amino terminal domain of NMDA receptor GluN2A govern its homodimerization but do not influence GluN2A/GluN1 heteromeric assembly A eukaryotic specific transmembrane segment is required for tetramerization in AMPA receptors Visualization of structural changes accompanying activation of N-methyl-D-aspartate (NMDA) receptors using fast-scan atomic force microscopy imaging.Deletion of the N-terminal domain alters the ethanol inhibition of N-methyl-D-aspartate receptors in a subunit-dependent manner.Distinct regions within the GluN2C subunit regulate the surface delivery of NMDA receptors.Engineering defined membrane-embedded elements of AMPA receptor induces opposing gating modulation by cornichon 3 and stargazin.

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Separation of Domain Contacts Is Required for Heterotetrameric Assembly of Functional NMDA Receptors

http://www.wikidata.org/entity/Q27667242

description

2011 nî lūn-bûn

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2011 թվականի մարտին հրատարակված գիտական հոդված

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Separation of Domain Contacts ...... y of Functional NMDA Receptors

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Anthony N Farina

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Katherine Y Blain

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Senyon Choe

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Terunaga Nakagawa

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Tomohiko Maruo

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Witek Kwiatkowski

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P2860

Nucleotide sequence, genomic organization, and chromosomal localization of genes encoding the human NMDA receptor subunits NR3A and NR3B

Negative staining and image classification — powerful tools in modern electron microscopy

Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor

Crystal structure and association behaviour of the GluR2 amino-terminal domain

The N-terminal domain of GluR6-subtype glutamate receptor ion channels

Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors

Structure of the zinc-bound amino-terminal domain of the NMDA receptor NR2B subunit

X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor

Crystal Structures of the Glutamate Receptor Ion Channel GluK3 and GluK5 Amino-Terminal Domains

High-efficiency transformation of mammalian cells by plasmid DNA

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