Role of calcium permeation in dihydropyridine receptor function. Insights into channel gating and excitation-contraction coupling.
about
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 muscleCa(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.Excitation-contraction coupling in skeletal muscle of a mouse lacking the dihydropyridine receptor subunit gamma1A malignant hyperthermia-inducing mutation in RYR1 (R163C): alterations in Ca2+ entry, release, and retrograde signaling to the DHPR.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 myotubesTruncation of the carboxyl terminus of the dihydropyridine receptor beta1a subunit promotes Ca2+ dependent excitation-contraction coupling in skeletal myotubes.Ca2+-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 muscleMalignant hyperthermia susceptibility arising from altered resting coupling between the skeletal muscle L-type Ca2+ channel and the type 1 ryanodine receptorMalignant hyperthermia and excitation-contraction coupling.Multiple loops of the dihydropyridine receptor pore subunit are required for full-scale excitation-contraction coupling in skeletal muscle.Reduced gain of excitation-contraction coupling in triadin-null myotubes is mediated by the disruption of FKBP12/RyR1 interactionCa(2+) permeation and/or binding to CaV1.1 fine-tunes skeletal muscle Ca(2+) signaling to sustain muscle function.Properties of Na+ currents conducted by a skeletal muscle L-type Ca2+ channel pore mutant (SkEIIIK).Accessibility of targeted DHPR sites to streptavidin and functional effects of binding on EC coupling.Potentiated L-type Ca2+ channels rectifyFunctional impact of the ryanodine receptor on the skeletal muscle L-type Ca(2+) channelRem inhibits skeletal muscle EC coupling by reducing the number of functional L-type Ca2+ channels.Impaired gating of an L-Type Ca(2+) channel carrying a mutation linked to malignant hyperthermia.The skeletal L-type Ca(2+) current is a major contributor to excitation-coupled Ca(2+) entry.Checking your SOCCs and feet: the molecular mechanisms of Ca2+ entry in skeletal muscle.Conformational activation of Ca2+ entry by depolarization of skeletal myotubes.Muscle weakness in myotonic dystrophy associated with misregulated splicing and altered gating of Ca(V)1.1 calcium channel.Ca2+ Release Channels Join the 'Resolution Revolution'.New factors contributing to dynamic calcium regulation in the skeletal muscle triad-a crowded placeStructural requirements of the dihydropyridine receptor alpha1S II-III loop for skeletal-type excitation-contraction coupling.Enhanced dihydropyridine receptor calcium channel activity restores muscle strength in JP45/CASQ1 double knockout mice.The Ca2+ influx through the mammalian skeletal muscle dihydropyridine receptor is irrelevant for muscle performance.A focus on extracellular Ca2+ entry into skeletal muscle.Ca2+ release through ryanodine receptors regulates skeletal muscle L-type Ca2+ channel expression.Mechanisms by which a CACNA1H mutation in epilepsy patients increases seizure susceptibility.Increases in diastolic [Ca2+] can contribute to positive inotropy in guinea pig ventricular myocytes in the absence of changes in amplitudes of Ca2+ transients.Ryanodine receptor type 1 (RyR1) mutations C4958S and C4961S reveal excitation-coupled calcium entry (ECCE) is independent of sarcoplasmic reticulum store depletion.Junctional trafficking and restoration of retrograde signaling by the cytoplasmic RyR1 domain.A skeletal muscle L-type Ca2+ channel with a mutation in the selectivity filter (CaV1.1 E1014K) conducts K.
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P2860
Role of calcium permeation in dihydropyridine receptor function. Insights into channel gating and excitation-contraction coupling.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Role of calcium permeation in ...... citation-contraction coupling.
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Role of calcium permeation in ...... citation-contraction coupling.
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type
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Role of calcium permeation in ...... citation-contraction coupling.
@ast
Role of calcium permeation in ...... citation-contraction coupling.
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prefLabel
Role of calcium permeation in ...... citation-contraction coupling.
@ast
Role of calcium permeation in ...... citation-contraction coupling.
@en
P2860
P356
P1476
Role of calcium permeation in ...... citation-contraction coupling.
@en
P2093
P2860
P304
P356
10.1085/JGP.114.3.393
P577
1999-09-01T00:00:00Z