Distinct RGK GTPases differentially use α1- and auxiliary β-binding-dependent mechanisms to inhibit CaV1.2/CaV2.2 channels.
about
Molecular mechanisms of activity-dependent changes in dendritic morphology: role of RGK proteinsStructure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channelsA loss-of-function analysis reveals that endogenous Rem2 promotes functional glutamatergic synapse formation and restricts dendritic complexityDifferential effects of RGK proteins on L-type channel function in adult mouse skeletal muscleRegulation of high-voltage-activated Ca(2+) channel function, trafficking, and membrane stability by auxiliary subunits.Bio-inspired voltage-dependent calcium channel blockersSolution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel β4 subunit: a low affinity interaction is required for inhibition of Cav2.1 Ca2+ currentsRem uncouples excitation-contraction coupling in adult skeletal muscle fibers.Similar molecular determinants on Rem mediate two distinct modes of inhibition of CaV1.2 channels.Rem2 in the bullfrog (Rana catesbeiana): Patterns of expression within the central nervous system and brain expression at different ontogenetic stagesRegulation of voltage-dependent calcium channels by RGK proteins.Ion channel engineering: perspectives and strategies.RGK regulation of voltage-gated calcium channels.Functional assessment of three Rem residues identified as critical for interactions with Ca(2+) channel β subunits.Localization of rem2 in the central nervous system of the adult rainbow trout (Oncorhynchus mykiss).Rad and Rem are non-canonical G-proteins with respect to the regulatory role of guanine nucleotide binding in Ca(V)1.2 channel regulation.RGK proteins: fashioning muscle with “Rad” new brakes.Defining the MO's of RGK proteins.Molecular mechanisms and physiological relevance of RGK proteins in the heart.
P2860
Q26851882-476559AB-9F35-437F-9501-AF6ABE99016FQ26864613-F7A31EEF-6EEB-417F-9181-49852C20EB2CQ31134091-86271363-A82E-4D05-BAAC-DE9E511919BEQ33595731-2B3F1905-6BA0-4219-B5B1-C7FE2F5AA304Q33763700-F9231097-4E08-406B-8335-E24DC21D5C72Q34308192-2F78D0F4-F177-4927-9C13-1C18B8F06E6CQ35555097-F4EA0440-A215-4307-92FA-3FF4145385DAQ35795789-352BBE24-A8CC-4E1A-80C9-B4DAD2466E99Q37183263-B82D12B2-F251-4967-87EA-23A51763FFBDQ37733140-C4BCCFE9-6B77-494F-942B-D8496279FD22Q38051949-C0ABFD28-ED6B-4678-AF90-68F55097A491Q38247898-34C9D6A5-F0EF-4514-93D2-EBA39CAE8679Q38313471-D016BB18-300C-4CDE-9361-91052C274FD9Q38899941-80219DF3-2F5A-4CF0-B36F-9FFEA8DFEFE4Q39417855-B8E7D35E-C3AF-4F56-9FFD-683FA5A1C0BFQ40478387-29E33818-C289-4A20-AD5F-F4875818A2FBQ40655324-403502AE-22F5-4EDF-A292-A5F97BC4E06EQ41711413-FD425618-2BDA-493B-B8FA-C8F99C85CBFAQ47297180-41F9CEB0-7917-419B-84B1-4F28AFA0FA33
P2860
Distinct RGK GTPases differentially use α1- and auxiliary β-binding-dependent mechanisms to inhibit CaV1.2/CaV2.2 channels.
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@ast
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@en
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@nl
type
label
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@ast
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@en
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@nl
prefLabel
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@ast
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@en
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@nl
P2093
P2860
P1433
P1476
Distinct RGK GTPases different ...... nhibit CaV1.2/CaV2.2 channels.
@en
P2093
Akil Puckerin
Henry M Colecraft
Tingting Yang
P2860
P304
P356
10.1371/JOURNAL.PONE.0037079
P407
P577
2012-05-10T00:00:00Z