A specific tryptophan in the I-II linker is a key determinant of beta-subunit binding and modulation in Ca(V)2.3 calcium channels
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The importance of occupancy rather than affinity of CaV(beta) subunits for the calcium channel I-II linker in relation to calcium channel functionThe ß subunit of voltage-gated Ca2+ channelsFunctional dissection of the intramolecular Src homology 3-guanylate kinase domain coupling in voltage-gated Ca2+ channel beta-subunits.Determinants of the voltage dependence of G protein modulation within calcium channel beta subunits.Functional modularity of the beta-subunit of voltage-gated Ca2+ channels.Negatively charged residues in the N-terminal of the AID helix confer slow voltage dependent inactivation gating to CaV1.2.Beta-subunits promote the expression of Ca(V)2.2 channels by reducing their proteasomal degradation.Outer pore topology of the ECaC-TRPV5 channel by cysteine scan mutagenesis.Double mutant cycle analysis identified a critical leucine residue in the IIS4S5 linker for the activation of the Ca(V)2.3 calcium channel.Identification of Glycosylation Sites Essential for Surface Expression of the CaVα2δ1 Subunit and Modulation of the Cardiac CaV1.2 Channel Activity.The guanylate kinase domain of the beta-subunit of voltage-gated calcium channels suffices to modulate gating.Structure and function of the β subunit of voltage-gated Ca²⁺ channels.A quartet of leucine residues in the guanylate kinase domain of CaVβ determines the plasma membrane density of the CaV2.3 channel.Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain.Mutations of nonconserved residues within the calcium channel alpha1-interaction domain inhibit beta-subunit potentiation.A short polybasic segment between the two conserved domains of the β2a-subunit modulates the rate of inactivation of R-type calcium channel.Molecular determinants of the CaVbeta-induced plasma membrane targeting of the CaV1.2 channel.The C-terminal residues in the alpha-interacting domain (AID) helix anchor CaV beta subunit interaction and modulation of CaV2.3 channels.Topology of the selectivity filter of a TRPV channel: rapid accessibility of contiguous residues from the external medium.Roles of molecular regions in determining differences between voltage dependence of activation of CaV3.1 and CaV1.2 calcium channels.The alpha1-beta-subunit interaction that modulates calcium channel activity is reversible and requires a competent alpha-interaction domain.Inherited Ventricular Arrhythmias: The Role of the Multi-Subunit Structure of the L-Type Calcium Channel Complex.
P2860
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P2860
A specific tryptophan in the I-II linker is a key determinant of beta-subunit binding and modulation in Ca(V)2.3 calcium channels
description
2002 nî lūn-bûn
@nan
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
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name
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@ast
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@en
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@nl
type
label
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@ast
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@en
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@nl
prefLabel
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@ast
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@en
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@nl
P2093
P2860
P1433
P1476
A specific tryptophan in the I ...... n in Ca(V)2.3 calcium channels
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(02)73914-3
P407
P577
2002-09-01T00:00:00Z