Analysis of high-affinity assembly for AMPA receptor amino-terminal domains. - Test2 - elhamkhani - TriplyDB

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

http://www.wikidata.org/entity/Q35931870

about

Structural basis for the binding specificity of human Recepteur d'Origine Nantais (RON) receptor tyrosine kinase to macrophage-stimulating protein Structure, Dynamics, and Allosteric Potential of Ionotropic Glutamate Receptor N-Terminal Domains Comparative Dynamics of NMDA- and AMPA-Glutamate Receptor N-Terminal Domains Anions Mediate Ligand Binding in Adineta vaga Glutamate Receptor Ion Channels Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.Structural mechanism of glutamate receptor activation and desensitization.Are fluorescence-detected sedimentation velocity data reliable?Accounting for photophysical processes and specific signal intensity changes in fluorescence-detected sedimentation velocity Multi-signal sedimentation velocity analysis with mass conservation for determining the stoichiometry of protein complexes.Tools for the quantitative analysis of sedimentation boundaries detected by fluorescence optical analytical ultracentrifugation Analysis of high affinity self-association by fluorescence optical sedimentation velocity analytical ultracentrifugation of labeled proteins: opportunities and limitations.Variable-Field Analytical Ultracentrifugation: I. Time-Optimized Sedimentation Equilibrium.Mapping the binding of GluN2B-selective N-methyl-D-aspartate receptor negative allosteric modulators.Global multi-method analysis of affinities and cooperativity in complex systems of macromolecular interactions Analysis of high-affinity binding of protein kinase R to double-stranded RNA Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.Analytical Ultracentrifugation as a Tool for Studying Protein Interactions.Monochromatic multicomponent fluorescence sedimentation velocity for the study of high-affinity protein interactions.Improving the thermal, radial, and temporal accuracy of the analytical ultracentrifuge through external references Analysis of protein interactions with picomolar binding affinity by fluorescence-detected sedimentation velocity.Assembly of AMPA receptors: mechanisms and regulation.Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.Mapping the interaction sites between AMPA receptors and TARPs reveals a role for the receptor N-terminal domain in channel gating.Aggregation Limits Surface Expression of Homomeric GluA3 Receptors.Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains.Sedimentation velocity analytical ultracentrifugation for characterization of therapeutic antibodies.Measuring Protein Interactions by Optical Biosensors.

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P2860

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

http://www.wikidata.org/entity/Q35931870

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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2012年论文

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2012年论文

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name

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

@ast

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

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type

label

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

@ast

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

@en

prefLabel

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

@ast

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

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The Journal of General Physiology

P1476

Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.

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P2093

Andrea Balbo

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Anthony J Berger

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Carrie A May

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Ernesto Casillas

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George H Patterson

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Huaying Zhao

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Janesh Kumar

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Mark L Mayer

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Patrick H Brown

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Peter Schuck

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P2860

Mechanism of glutamate receptor desensitization

Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization

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

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

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

Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors

Structure and Assembly Mechanism for Heteromeric Kainate Receptors

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

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371-388

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scholarly article

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10.1085/JGP.201210770

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5

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139

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2012-04-16T00:00:00Z

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22508847

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