NMR analysis of KChIP4a reveals structural basis for control of surface expression of Kv4 channel complexes. - Wikidata - awgldk - TriplyDB

NMR analysis of KChIP4a reveals structural basis for control of surface expression of Kv4 channel complexes.

NMR analysis of KChIP4a reveals structural basis for control of surface expression of Kv4 channel complexes.

http://www.wikidata.org/entity/Q39627863

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Structural Insights into KChIP4a Modulation of Kv4.3 Inactivation Solution NMR Structure of the Ca2+-bound N-terminal Domain of CaBP7: A REGULATOR OF GOLGI TRAFFICKING Interdependent roles for accessory KChIP2, KChIP3, and KChIP4 subunits in the generation of Kv4-encoded IA channels in cortical pyramidal neurons KChIP4a regulates Kv4.2 channel trafficking through PKA phosphorylation.Functional rescue of Kv4.3 channel tetramerization mutants by KChIP4a.RNA polymerase III drives alternative splicing of the potassium channel-interacting protein contributing to brain complexity and neurodegeneration Different KChIPs compete for heteromultimeric assembly with pore-forming Kv4 subunits Auxiliary KChIP4a suppresses A-type K+ current through endoplasmic reticulum (ER) retention and promoting closed-state inactivation of Kv4 channels Convergent modulation of Kv4.2 channel alpha subunits by structurally distinct DPPX and KChIP auxiliary subunits.Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies.Modulatory mechanisms and multiple functions of somatodendritic A-type K (+) channel auxiliary subunits Understanding the physiological roles of the neuronal calcium sensor proteins.Multiple Kv channel-interacting proteins contain an N-terminal transmembrane domain that regulates Kv4 channel trafficking and gating.Ca2+ and Mg2+ modulate conformational dynamics and stability of downstream regulatory element antagonist modulator.DJ-1 based peptide, ND-13, promote functional recovery in mouse model of focal ischemic injury.Kv channel-interacting proteins as neuronal and non-neuronal calcium sensors

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P2860

NMR analysis of KChIP4a reveals structural basis for control of surface expression of Kv4 channel complexes.

http://www.wikidata.org/entity/Q39627863

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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NMR analysis of KChIP4a reveal ...... sion of Kv4 channel complexes.

@en

NMR analysis of KChIP4a reveal ...... sion of Kv4 channel complexes.

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type

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NMR analysis of KChIP4a reveal ...... sion of Kv4 channel complexes.

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NMR analysis of KChIP4a reveal ...... sion of Kv4 channel complexes.

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NMR analysis of KChIP4a reveal ...... sion of Kv4 channel complexes.

@en

NMR analysis of KChIP4a reveal ...... sion of Kv4 channel complexes.

@nl

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Journal of Biological Chemistry

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NMR analysis of KChIP4a reveal ...... ssion of Kv4 channel complexes

@en

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Bernd Fakler

http://www.w3.org/2001/XMLSchema#string

Detlef Bentrop

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Gerd Zolles

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Hubert Kalbacher

http://www.w3.org/2001/XMLSchema#string

Isabel Neubauer

http://www.w3.org/2001/XMLSchema#string

Manuel Covarrubias

http://www.w3.org/2001/XMLSchema#string

Nikolaos G Kandias

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P2860

Modulation of A-type potassium channels by a family of calcium sensors

Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating

Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4

Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase 10 (DPP10)

Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits

Elimination of fast inactivation in Kv4 A-type potassium channels by an auxiliary subunit domain

Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

SWISS-MODEL: An automated protein homology-modeling server

Traffic of Kv4 K+ channels mediated by KChIP1 is via a novel post-ER vesicular pathway

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18937-18946

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scholarly article

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10.1074/JBC.M800976200

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27

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283

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2008-05-05T00:00:00Z

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18458082

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2441559

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