Functional exofacially tagged N-type calcium channels elucidate the interaction with auxiliary α2δ-1 subunits. - Test2 - elhamkhani - TriplyDB

Functional exofacially tagged N-type calcium channels elucidate the interaction with auxiliary α2δ-1 subunits.

Functional exofacially tagged N-type calcium channels elucidate the interaction with auxiliary α2δ-1 subunits.

http://www.wikidata.org/entity/Q33790000

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Mechanisms of the gabapentinoids and α 2 δ-1 calcium channel subunit in neuropathic pain The Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic Potential Current Status of the New Antiepileptic Drugs in Chronic Pain Functional characterization of CaVα2δ mutations associated with sudden cardiac death Sigma-1 Receptor Plays a Negative Modulation on N-type Calcium Channel.The upregulation of α2δ-1 subunit modulates activity-dependent Ca2+ signals in sensory neurons Exercise-mimetic AICAR transiently benefits brain function.Identification of Glycosylation Sites Essential for Surface Expression of the CaVα2δ1 Subunit and Modulation of the Cardiac CaV1.2 Channel Activity.Effect of knockout of α2δ-1 on action potentials in mouse sensory neurons The α2δ-1 subunit remodels CaV1.2 voltage sensors and allows Ca2+ influx at physiological membrane potentials Voltage-gated calcium channels and their auxiliary subunits: physiology and pathophysiology and pharmacology Proteolytic maturation of α2δ represents a checkpoint for activation and neuronal trafficking of latent calcium channels.Ion channel engineering: perspectives and strategies.The Auxiliary Calcium Channel Subunit α2δ4 Is Required for Axonal Elaboration, Synaptic Transmission, and Wiring of Rod Photoreceptors.CaV2 channel subtype expression in rat sympathetic neurons is selectively regulated by α2δ subunits.Targeting voltage-gated calcium channels in neurological and psychiatric diseases.Modulation of TMEM16A channel activity by the von Willebrand factor type A (VWA) domain of the calcium-activated chloride channel regulator 1 (CLCA1).Injury-induced maladaptation and dysregulation of calcium channel α2 δ subunit proteins and its contribution to neuropathic pain development.Surface dynamics of voltage-gated ion channels The CaVβ Subunit Protects the I-II Loop of the Voltage-gated Calcium Channel CaV2.2 from Proteasomal Degradation but Not Oligoubiquitination.The Anti-Allodynic Gabapentinoids: Myths, Paradoxes, and Acute Effects.Alternative Splicing in Ca(V)2.2 Regulates Neuronal Trafficking via Adaptor Protein Complex-1 Adaptor Protein Motifs.Dynamic association of calcium channel subunits at the cellular membrane.Thrombospondin-4 reduces binding affinity of [(3)H]-gabapentin to calcium-channel α2δ-1-subunit but does not interact with α2δ-1 on the cell-surface when co-expressed.A membrane-delimited N-myristoylated CRMP2 peptide aptamer inhibits CaV2.2 trafficking and reverses inflammatory and postoperative pain behaviors.LRP1 influences trafficking of N-type calcium channels via interaction with the auxiliary α2δ-1 subunit.A CaV2.1 N-terminal fragment relieves the dominant-negative inhibition by an Episodic ataxia 2 mutant.Mapping protein interactions of sodium channel NaV1.7 using epitope-tagged gene-targeted mice.miR-183 cluster scales mechanical pain sensitivity by regulating basal and neuropathic pain genes.The CaV2α1 EF-hand F helix tyrosine, a highly conserved locus for GPCR inhibition of CaV2 channels.Analysis of the long-term actions of gabapentin and pregabalin in dorsal root ganglia and substantia gelatinosa.The α2δ-1-NMDA Receptor Complex Is Critically Involved in Neuropathic Pain Development and Gabapentin Therapeutic Actions.Development of a High-Throughput Flow Cytometry Assay to Monitor Defective Trafficking and Rescue of Long QT2 Mutant hERG Channels.Voltage-gated calcium channels: their discovery, function and importance as drug targets

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Functional exofacially tagged N-type calcium channels elucidate the interaction with auxiliary α2δ-1 subunits.

http://www.wikidata.org/entity/Q33790000

description

2014 nî lūn-bûn

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2014 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2014 թվականի հունիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Functional exofacially tagged ...... with auxiliary α2δ-1 subunits.

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Functional exofacially tagged ...... with auxiliary α2δ-1 subunits.

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Functional exofacially tagged ...... with auxiliary α2δ-1 subunits.

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Functional exofacially tagged ...... with auxiliary α2δ-1 subunits.

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Functional exofacially tagged ...... with auxiliary α2δ-1 subunits.

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Functional exofacially tagged ...... with auxiliary α2δ-1 subunits.

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PNAS.1403731111

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Proceedings of the National Academy of Sciences of the United States of America

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Functional exofacially tagged ...... with auxiliary α2δ-1 subunits.

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John S Cassidy

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Laurent Ferron

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Wendy S Pratt

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P2860

Gabapentin receptor alpha2delta-1 is a neuronal thrombospondin receptor responsible for excitatory CNS synaptogenesis

Pharmacological disruption of calcium channel trafficking by the alpha2delta ligand gabapentin

Fragile X mental retardation protein controls synaptic vesicle exocytosis by modulating N-type calcium channel density

Interaction via a key tryptophan in the I-II linker of N-type calcium channels is required for beta1 but not for palmitoylated beta2, implicating an additional binding site in the regulation of channel voltage-dependent properties

Ducky mouse phenotype of epilepsy and ataxia is associated with mutations in the Cacna2d2 gene and decreased calcium channel current in cerebellar Purkinje cells

Beta-subunits promote the expression of Ca(V)2.2 channels by reducing their proteasomal degradation.

The alpha2delta subunits of voltage-gated calcium channels form GPI-anchored proteins, a posttranslational modification essential for function

The metal-ion-dependent adhesion site in the Von Willebrand factor-A domain of alpha2delta subunits is key to trafficking voltage-gated Ca2+ channels.

The beta subunit increases Ca2+ currents and gating charge movements of human cardiac L-type Ca2+ channels.

Quantitative proteomics of the Cav2 channel nano-environments in the mammalian brain.

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8979-8984

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10.1073/PNAS.1403731111

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Annette Dolphin

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262813348

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24889613

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4066493

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