Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
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Multiple regions of RyR1 mediate functional and structural interactions with alpha(1S)-dihydropyridine receptors in skeletal muscleThe Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic PotentialCa(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channelA 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.Upregulation of the CaV 1.1-ryanodine receptor complex in a rat model of critical illness myopathyAn Ryr1I4895T mutation abolishes Ca2+ release channel function and delays development in homozygous offspring of a mutant mouse lineThe Ca2+ channel alpha2delta-1 subunit determines Ca2+ current kinetics in skeletal muscle but not targeting of alpha1S or excitation-contraction couplingStac3 has a direct role in skeletal muscle-type excitation-contraction coupling that is disrupted by a myopathy-causing mutation.The excitation-contraction coupling mechanism in skeletal muscle.A malignant hyperthermia-inducing mutation in RYR1 (R163C): consequent alterations in the functional properties of DHPR channelsRyanodine modification of RyR1 retrogradely affects L-type Ca(2+) channel gating in skeletal muscle.The cardiac alpha(1C) subunit can support excitation-triggered Ca2+ entry in dysgenic and dyspedic myotubesCa2+ current and charge movements in skeletal myotubes promoted by the beta-subunit of the dihydropyridine receptor in the absence of ryanodine receptor type 1.Ca2+-dependent excitation-contraction coupling triggered by the heterologous cardiac/brain DHPR beta2a-subunit in skeletal myotubesDistinct effects on Ca2+ handling caused by malignant hyperthermia and central core disease mutations in RyR1.Interaction between the dihydropyridine receptor Ca2+ channel beta-subunit and ryanodine receptor type 1 strengthens excitation-contraction couplingMalignant hyperthermia and excitation-contraction coupling.Identification and functional characterization of malignant hyperthermia mutation T1354S in the outer pore of the Cavalpha1S-subunit.Muscle weakness in Ryr1I4895T/WT knock-in mice as a result of reduced ryanodine receptor Ca2+ ion permeation and release from the sarcoplasmic reticulum.Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interactionStac adaptor proteins regulate trafficking and function of muscle and neuronal L-type Ca2+ channelsAccelerated activation of SOCE current in myotubes from two mouse models of anesthetic- and heat-induced sudden death.Excitation--contraction uncoupling by a human central core disease mutation in the ryanodine receptor.Bidirectional signaling between calcium channels of skeletal muscle requires multiple direct and indirect interactions.Regions of ryanodine receptors that influence activation by the dihydropyridine receptor β1a subunitTemperature and RyR1 regulate the activation rate of store-operated Ca²+ entry current in myotubesThe pore region of the skeletal muscle ryanodine receptor is a primary locus for excitation-contraction uncoupling in central core diseaseFunctional effects of central core disease mutations in the cytoplasmic region of the skeletal muscle ryanodine receptorCalmodulin binding to the 3614-3643 region of RyR1 is not essential for excitation-contraction coupling in skeletal myotubesCOOH-terminal truncated alpha(1S) subunits conduct current better than full-length dihydropyridine receptors.Effects of dantrolene on steps of excitation-contraction coupling in mammalian skeletal muscle fibers.Rem inhibits skeletal muscle EC coupling by reducing the number of functional L-type Ca2+ channels.Alpha2delta1 dihydropyridine receptor subunit is a critical element for excitation-coupled calcium entry but not for formation of tetrads in skeletal myotubesDistinct Components of Retrograde Ca(V)1.1-RyR1 Coupling Revealed by a Lethal Mutation in RyR1.Dantrolene-induced inhibition of skeletal L-type Ca2+ current requires RyR1 expression.Effect of Electroacupuncture on the Expression of Glycyl-tRNA Synthetase and Ultrastructure Changes in Atrophied Rat Peroneus Longus Muscle Induced by Sciatic Nerve Injection InjuryA truncation in the RYR1 gene associated with central core lesions in skeletal muscle fibres.The skeletal L-type Ca(2+) current is a major contributor to excitation-coupled Ca(2+) entry.A retrograde signal from RyR1 alters DHP receptor inactivation and limits window Ca2+ release in muscle fibers of Y522S RyR1 knock-in mice.A CaV1.1 Ca2+ channel splice variant with high conductance and voltage-sensitivity alters EC coupling in developing skeletal muscle.
P2860
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P2860
Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
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2000 nî lūn-bûn
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name
Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
@ast
Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
@en
type
label
Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
@ast
Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
@en
prefLabel
Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
@ast
Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
@en
P2860
P356
P1476
Functional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channel
@en
P2093
P2860
P304
P356
10.1085/JGP.115.4.467
P577
2000-04-01T00:00:00Z