Recovery of Ca2+ current, charge movements, and Ca2+ transients in myotubes deficient in dihydropyridine receptor beta 1 subunit transfected with beta 1 cDNA.
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Functional analysis of a frame-shift mutant of the dihydropyridine receptor pore subunit (alpha1S) expressing two complementary protein fragmentsModulation of L-type Ca2+ current but not activation of Ca2+ release by the gamma1 subunit of the dihydropyridine receptor of skeletal muscleA component of excitation-contraction coupling triggered in the absence of the T671-L690 and L720-Q765 regions of the II-III loop of the dihydropyridine receptor alpha(1s) pore subunit.Ca2+ sparks in embryonic mouse skeletal muscle selectively deficient in dihydropyridine receptor alpha1S or beta1a subunits.Mutations of calcium channel beta subunit genes in miceFunctional expression of transgenic 1sDHPR channels in adult mammalian skeletal muscle fibres.Molecular origin of the L-type Ca2+ current of skeletal muscle myotubes selectively deficient in dihydropyridine receptor beta1a subunitDifferential regulation of skeletal muscle L-type Ca2+ current and excitation-contraction coupling by the dihydropyridine receptor beta subunit.Involvement of the carboxy-terminus region of the dihydropyridine receptor beta1a subunit in excitation-contraction coupling of skeletal muscleTruncation of the carboxyl terminus of the dihydropyridine receptor beta1a subunit promotes Ca2+ dependent excitation-contraction coupling in skeletal myotubes.Ca2+ current and charge movements in skeletal myotubes promoted by the beta-subunit of the dihydropyridine receptor in the absence of ryanodine receptor type 1.RyR1/RyR3 chimeras reveal that multiple domains of RyR1 are involved in skeletal-type E-C couplingCardiac-type EC-coupling in dysgenic myotubes restored with Ca2+ channel subunit isoforms alpha1C and alpha1D does not correlate with current densityCa2+-dependent excitation-contraction coupling triggered by the heterologous cardiac/brain DHPR beta2a-subunit in skeletal myotubesInvolvement of a heptad repeat in the carboxyl terminus of the dihydropyridine receptor beta1a subunit in the mechanism of excitation-contraction coupling in skeletal muscleInteraction between the dihydropyridine receptor Ca2+ channel beta-subunit and ryanodine receptor type 1 strengthens excitation-contraction couplingMultiple loops of the dihydropyridine receptor pore subunit are required for full-scale excitation-contraction coupling in skeletal muscle.Short-term regulation of excitation-contraction coupling by the beta1a subunit in adult mouse skeletal muscle.Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interactionAmino acid residues 489-503 of dihydropyridine receptor (DHPR) β1a subunit are critical for structural communication between the skeletal muscle DHPR complex and type 1 ryanodine receptorTroponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle.Intramolecular ex vivo Fluorescence Resonance Energy Transfer (FRET) of Dihydropyridine Receptor (DHPR) β1a Subunit Reveals Conformational Change Induced by RYR1 in Mouse Skeletal MyotubesAssociation of calcium channel alpha1S and beta1a subunits is required for the targeting of beta1a but not of alpha1S into skeletal muscle triads.Intramembrane charge movements and excitation- contraction coupling expressed by two-domain fragments of the Ca2+ channel.Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channelAlpha2delta1 dihydropyridine receptor subunit is a critical element for excitation-coupled calcium entry but not for formation of tetrads in skeletal myotubesFluorescence Resonance Energy Transfer-based Structural Analysis of the Dihydropyridine Receptor α1S Subunit Reveals Conformational Differences Induced by Binding of the β1a Subunit.Increased CaVbeta1A expression with aging contributes to skeletal muscle weaknessElectrical inhomogeneity in left ventricular hypertrophy.Neuromuscular synaptic patterning requires the function of skeletal muscle dihydropyridine receptors.Voltage-controlled Ca2+ release and entry flux in isolated adult muscle fibres of the mouse.Voltage-dependent Ca2+ fluxes in skeletal myotubes determined using a removal model analysis.Proper restoration of excitation-contraction coupling in the dihydropyridine receptor beta1-null zebrafish relaxed is an exclusive function of the beta1a subunit.The triad targeting signal of the skeletal muscle calcium channel is localized in the COOH terminus of the alpha(1S) subunitThe beta1a subunit regulates the functional properties of adult frog and mouse L-type Ca2+ channels of skeletal muscle.Membrane targeting of L-type calcium channels. Role of palmitoylation in the subcellular localization of the beta2a subunit.
P2860
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P2860
Recovery of Ca2+ current, charge movements, and Ca2+ transients in myotubes deficient in dihydropyridine receptor beta 1 subunit transfected with beta 1 cDNA.
description
1997 nî lūn-bûn
@nan
1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Recovery of Ca2+ current, char ...... transfected with beta 1 cDNA.
@ast
Recovery of Ca2+ current, char ...... transfected with beta 1 cDNA.
@en
type
label
Recovery of Ca2+ current, char ...... transfected with beta 1 cDNA.
@ast
Recovery of Ca2+ current, char ...... transfected with beta 1 cDNA.
@en
prefLabel
Recovery of Ca2+ current, char ...... transfected with beta 1 cDNA.
@ast
Recovery of Ca2+ current, char ...... transfected with beta 1 cDNA.
@en
P2093
P2860
P1433
P1476
Recovery of Ca2+ current, char ...... transfected with beta 1 cDNA.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(97)78113-X
P407
P577
1997-08-01T00:00:00Z