Structure and Assembly Mechanism for Heteromeric Kainate Receptors - Test2 - elhamkhani - TriplyDB

Structure and Assembly Mechanism for Heteromeric Kainate Receptors

Structure and Assembly Mechanism for Heteromeric Kainate Receptors

http://www.wikidata.org/entity/Q27671015

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A structural biology perspective on NMDA receptor pharmacology and function Structure, Dynamics, and Allosteric Potential of Ionotropic Glutamate Receptor N-Terminal Domains Functional insights from glutamate receptor ion channel structures Emerging models of glutamate receptor ion channel structure and function Anions Mediate Ligand Binding in Adineta vaga Glutamate Receptor Ion Channels Activation of NMDA receptors and the mechanism of inhibition by ifenprodil.Structural basis for integration of GluD receptors within synaptic organizer complexes Assembly stoichiometry of the GluK2/GluK5 kainate receptor complex.Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.A hard-wired glutamatergic circuit pools and relays UV signals to mediate spectral preference in Drosophila.Acid-sensing ion channel (ASIC) 1a/2a heteromers have a flexible 2:1/1:2 stoichiometry Structural mechanism of glutamate receptor activation and desensitization.Structure and organization of heteromeric AMPA-type glutamate receptors Tethered ligands reveal glutamate receptor desensitization depends on subunit occupancy.Contributions of different kainate receptor subunits to the properties of recombinant homomeric and heteromeric receptors.Analysis of high affinity self-association by fluorescence optical sedimentation velocity analytical ultracentrifugation of labeled proteins: opportunities and limitations.Trafficking of kainate receptors.Functional reconstitution of Drosophila melanogaster NMJ glutamate receptors Emerging structural insights into the function of ionotropic glutamate receptors.Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.Drosophila Neto is essential for clustering glutamate receptors at the neuromuscular junction.Mapping the binding of GluN2B-selective N-methyl-D-aspartate receptor negative allosteric modulators.Probing Intersubunit Interfaces in AMPA-subtype Ionotropic Glutamate Receptors.Kainate receptor pore-forming and auxiliary subunits regulate channel block by a novel mechanism Homeostatic control of synaptic transmission by distinct glutamate receptors.Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor.Monochromatic multicomponent fluorescence sedimentation velocity for the study of high-affinity protein interactions.Agonist binding to the GluK5 subunit is sufficient for functional surface expression of heteromeric GluK2/GluK5 kainate receptors.GluA1 signal peptide determines the spatial assembly of heteromeric AMPA receptors.Conduits of life's spark: a perspective on ion channel research since the birth of neuron.Structure and function of glutamate receptor amino terminal domains.Glutamate receptor homologs in plants: functions and evolutionary origins.Expression of recombinant glycoproteins in mammalian cells: towards an integrative approach to structural biology.The multifaceted subunit interfaces of ionotropic glutamate receptors.Structure and gating of tetrameric glutamate receptors.Assembly of AMPA receptors: mechanisms and regulation.Neto2 Influences on Kainate Receptor Pharmacology and Function.α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) and N-methyl-D-aspartate (NMDA) receptors adopt different subunit arrangements.Interacting glutamate receptor-like proteins in Phloem regulate lateral root initiation in Arabidopsis.The N-terminal domain modulates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor desensitization.

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Structure and Assembly Mechanism for Heteromeric Kainate Receptors

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2011年の論文

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Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Structure and mechanism of kainate receptor modulation by anions

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

Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers

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