Calmodulin activation limits the rate of KCNQ2 K+ channel exit from the endoplasmic reticulum. - Wikidata - awgldk - TriplyDB

Calmodulin activation limits the rate of KCNQ2 K+ channel exit from the endoplasmic reticulum.

Calmodulin activation limits the rate of KCNQ2 K+ channel exit from the endoplasmic reticulum.

http://www.wikidata.org/entity/Q37344005

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Trafficking mechanisms underlying neuronal voltage-gated ion channel localization at the axon initial segment Activation of m1 muscarinic acetylcholine receptor induces surface transport of KCNQ channels through a CRMP-2-mediated pathway.Calmodulation meta-analysis: predicting calmodulin binding via canonical motif clustering.Polarized axonal surface expression of neuronal KCNQ potassium channels is regulated by calmodulin interaction with KCNQ2 subunit.Kv7 channels can function without constitutive calmodulin tethering Surface expression and subunit specific control of steady protein levels by the Kv7.2 helix A-B linker The Role of the Carboxyl Terminus Helix C-D Linker in Regulating KCNQ3 K+ Current Amplitudes by Controlling Channel Trafficking Structural insights into neuronal K+ channel-calmodulin complexes.Mechanisms of Calmodulin Regulation of Different Isoforms of Kv7.4 K+ Channels Conditional deletions of epilepsy-associated KCNQ2 and KCNQ3 channels from cerebral cortex cause differential effects on neuronal excitability Cytoplasmic domains and voltage-dependent potassium channel gating.Structural analysis of calmodulin binding to ion channels demonstrates the role of its plasticity in regulation.Modulation of Kv7 channels and excitability in the brain.Calcium dependent interaction of calmodulin with the GlyT1 C-terminus.Calmodulin regulates KCNQ2 function in epilepsy.Pivoting between calmodulin lobes triggered by calcium in the Kv7.2/calmodulin complex.Regions of KCNQ K(+) channels controlling functional expression Calmodulin confers calcium sensitivity to the stability of the distal intracellular assembly domain of Kv7.2 channels.Dominant-negative effects of KCNQ2 mutations are associated with epileptic encephalopathy.Endoplasmic reticulum retention of KCNQ2 potassium channel mutants following temperature elevation.Lack of correlation between surface expression and currents in epileptogenic AB-calmodulin binding domain Kv7.2 potassium channel mutants

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Calmodulin activation limits the rate of KCNQ2 K+ channel exit from the endoplasmic reticulum.

http://www.wikidata.org/entity/Q37344005

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 03 June 2009

@en

vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Calmodulin activation limits t ...... rom the endoplasmic reticulum.

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Calmodulin activation limits t ...... rom the endoplasmic reticulum.

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type

label

Calmodulin activation limits t ...... rom the endoplasmic reticulum.

@en

Calmodulin activation limits t ...... rom the endoplasmic reticulum.

@nl

prefLabel

Calmodulin activation limits t ...... rom the endoplasmic reticulum.

@en

Calmodulin activation limits t ...... rom the endoplasmic reticulum.

@nl

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JBC.M109.019539

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Journal of Biological Chemistry

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Calmodulin activation limits t ...... from the endoplasmic reticulum

@en

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Ainhoa Etxeberría

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

Alvaro Villarroel

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

Jose Angel Rodriguez-Alfaro

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

Juan Camilo Gómez-Posada

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

Paloma Aivar

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

Pilar Areso

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

P2860

KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel

Surface expression and single channel properties of KCNQ2/KCNQ3, M-type K+ channels involved in epilepsy

The identification and characterization of a noncontinuous calmodulin-binding site in noninactivating voltage-dependent KCNQ potassium channels

Ion channel variation causes epilepsies

Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels

Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy.

Neuronal KCNQ potassium channels: physiology and role in disease.

Calmodulin as an ion channel subunit.

Novel mutations in the KCNQ2 gene link epilepsy to a dysfunction of the KCNQ2-calmodulin interaction.

Calmodulin mediates Ca2+-dependent modulation of M-type K+ channels

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20668-20675

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scholarly article

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10.1074/JBC.M109.019539

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31

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284

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Alessandro Alaimo

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2009-06-03T00:00:00Z

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19494108

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endoplasmic reticulum

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2742831

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