The Ca2+ channel alpha2delta-1 subunit determines Ca2+ current kinetics in skeletal muscle but not targeting of alpha1S or excitation-contraction coupling
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The Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic PotentialCa(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channelStac3 has a direct role in skeletal muscle-type excitation-contraction coupling that is disrupted by a myopathy-causing mutation.Emerging evidence for specific neuronal functions of auxiliary calcium channel α₂δ subunits.Non-Ca2+-conducting Ca2+ channels in fish skeletal muscle excitation-contraction coupling.Activity and calcium regulate nuclear targeting of the calcium channel beta4b subunit in nerve and muscle cellsFunctional expression of transgenic 1sDHPR channels in adult mammalian skeletal muscle fibres.The beta 1a subunit is essential for the assembly of dihydropyridine-receptor arrays in skeletal muscle.Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond.Identification and functional characterization of malignant hyperthermia mutation T1354S in the outer pore of the Cavalpha1S-subunit.The alpha1 subunit EGL-19, the alpha2/delta subunit UNC-36, and the beta subunit CCB-1 underlie voltage-dependent calcium currents in Caenorhabditis elegans striated muscle.Pore stability and gating in voltage-activated calcium channelsComputer modeling of siRNA knockdown effects indicates an essential role of the Ca2+ channel alpha2delta-1 subunit in cardiac excitation-contraction coupling.Alpha2delta1 dihydropyridine receptor subunit is a critical element for excitation-coupled calcium entry but not for formation of tetrads in skeletal myotubesThe skeletal L-type Ca(2+) current is a major contributor to excitation-coupled Ca(2+) entry.Does the voltage-gated calcium channel alpha2delta-1 subunit play a dual function in skeletal muscle?A CaV1.1 Ca2+ channel splice variant with high conductance and voltage-sensitivity alters EC coupling in developing skeletal muscle.Targeted disruption of the voltage-dependent calcium channel alpha2/delta-1-subunit.Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.β1a490-508, a 19-residue peptide from C-terminal tail of Cav1.1 β1a subunit, potentiates voltage-dependent calcium release in adult skeletal muscle fibers.How and why are calcium currents curtailed in the skeletal muscle voltage-gated calcium channels?Trafficking and stability of voltage-gated calcium channels.The role of auxiliary subunits for the functional diversity of voltage-gated calcium channels.Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Dynamic association of calcium channel subunits at the cellular membrane.The calcium channel alpha2/delta1 subunit is involved in extracellular signalling.Proteolytic cleavage of the voltage-gated Ca2+ channel alpha2delta subunit: structural and functional features.The Ca2+ influx through the mammalian skeletal muscle dihydropyridine receptor is irrelevant for muscle performance.Proper restoration of excitation-contraction coupling in the dihydropyridine receptor beta1-null zebrafish relaxed is an exclusive function of the beta1a subunit.The alpha(1S) III-IV loop influences 1,4-dihydropyridine receptor gating but is not directly involved in excitation-contraction coupling interactions with the type 1 ryanodine receptor.Divergent biophysical properties, gating mechanisms, and possible functions of the two skeletal muscle Ca(V)1.1 calcium channel splice variantsSpecific contributions of the four voltage-sensing domains in L-type calcium channels to gating and modulation.Smooth muscle cell alpha2delta-1 subunits are essential for vasoregulation by CaV1.2 channels.Two distinct voltage-sensing domains control voltage sensitivity and kinetics of current activation in CaV1.1 calcium channels.Stable incorporation versus dynamic exchange of β subunits in a native Ca2+ channel complex.The evolution of the four subunits of voltage-gated calcium channels: ancient roots, increasing complexity, and multiple losses.Aerobic exercise training improves Ca2+ handling and redox status of skeletal muscle in mice.The calcium channel α2/δ1 subunit interacts with ATP5b in the plasma membrane of developing muscle cells.Muscle-specific overexpression of IGF-I improves E-C coupling in skeletal muscle fibers from dystrophic mdx mice.De novo reconstitution reveals the proteins required for skeletal muscle voltage-induced Ca2+ release.
P2860
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P2860
The Ca2+ channel alpha2delta-1 subunit determines Ca2+ current kinetics in skeletal muscle but not targeting of alpha1S or excitation-contraction coupling
description
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2005
@ast
im Januar 2005 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2005/01/21)
@sk
vědecký článek publikovaný v roce 2005
@cs
wetenschappelijk artikel (gepubliceerd op 2005/01/21)
@nl
наукова стаття, опублікована в січні 2005
@uk
name
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@ast
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@en
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@nl
type
label
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@ast
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@en
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@nl
prefLabel
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@ast
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@en
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@nl
P2093
P2860
P50
P921
P3181
P356
P1476
The Ca2+ channel alpha2delta-1 ...... xcitation-contraction coupling
@en
P2093
Gerlinde Kugler
Manfred Grabner
Sabine Baumgartner
P2860
P304
P3181
P356
10.1074/JBC.M411501200
P407
P577
2004-11-09T00:00:00Z