Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling.
about
Muscle channelopathies and critical points in functional and genetic studies.3D Structure of the Dihydropyridine Receptor of Skeletal MusclePharmGKB summary: succinylcholine pathway, pharmacokinetics/pharmacodynamicsMalignant hyperthermia: a reviewCa(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channelPharmGKB summary: very important pharmacogene information for RYR1Channelopathies of skeletal muscle excitabilityAnesthetic- and heat-induced sudden death in calsequestrin-1-knockout miceCongenital myopathy results from misregulation of a muscle Ca2+ channel by mutant Stac3.The role of CACNA1S in predisposition to malignant hyperthermiaNon-Ca2+-conducting Ca2+ channels in fish skeletal muscle excitation-contraction coupling.The beta 1a subunit is essential for the assembly of dihydropyridine-receptor arrays in skeletal muscle.Distinct effects on Ca2+ handling caused by malignant hyperthermia and central core disease mutations in RyR1.In vivo expression of G-protein beta1gamma2 dimer in adult mouse skeletal muscle alters L-type calcium current and excitation-contraction coupling.Malignant hyperthermia susceptibility arising from altered resting coupling between the skeletal muscle L-type Ca2+ channel and the type 1 ryanodine receptorIdentification and functional characterization of malignant hyperthermia mutation T1354S in the outer pore of the Cavalpha1S-subunit.Orthograde dihydropyridine receptor signal regulates ryanodine receptor passive leakMalignant hyperthermia: a pharmacogenetic disorder.Special article: Future directions in malignant hyperthermia research and patient careNext-generation Sequencing of RYR1 and CACNA1S in Malignant Hyperthermia and Exertional Heat Illness.Fluorescence resonance energy transfer (FRET) indicates that association with the type I ryanodine receptor (RyR1) causes reorientation of multiple cytoplasmic domains of the dihydropyridine receptor (DHPR) α(1S) subunit.Nonspecific sarcolemmal cation channels are critical for the pathogenesis of malignant hyperthermia.Fluorescence Resonance Energy Transfer-based Structural Analysis of the Dihydropyridine Receptor α1S Subunit Reveals Conformational Differences Induced by Binding of the β1a Subunit.A CaV1.1 Ca2+ channel splice variant with high conductance and voltage-sensitivity alters EC coupling in developing skeletal muscle.Effects of inserting fluorescent proteins into the alpha1S II-III loop: insights into excitation-contraction coupling.Calcium-induced calcium release in skeletal muscle.Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Minimally invasive metabolic testing for malignant hyperthermia susceptibility: a systematic review of the methodology and results.Pharmacogenetics and pathophysiology of CACNA1S mutations in malignant hyperthermia.How is SR calcium release in muscle modulated by PIP(4,5)2?Elevated resting [Ca(2+)](i) in myotubes expressing malignant hyperthermia RyR1 cDNAs is partially restored by modulation of passive calcium leak from the SR.The mammalian skeletal muscle DHPR has larger Ca2+ conductance and is phylogenetically ancient to the early ray-finned fish sterlet (Acipenser ruthenus).The Ca2+ influx through the mammalian skeletal muscle dihydropyridine receptor is irrelevant for muscle performance.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.A probable role of dihydropyridine receptors in repression of Ca2+ sparks demonstrated in cultured mammalian muscle.Endogenous and maximal sarcoplasmic reticulum calcium content and calsequestrin expression in type I and type II human skeletal muscle fibres.Malignant Hyperthermia in the Post-Genomics Era: New Perspectives on an Old Concept.Rhabdomyolysis and fluctuating asymptomatic hyperCKemia associated with CACNA1S variant.Modulation of contractile apparatus Ca2+ sensitivity and disruption of excitation-contraction coupling by S-nitrosoglutathione in rat muscle fibres.[Telephone enquiries on the topic of malignant hyperthermia: Evaluation of the content and subsequent diagnostic results at the MH Center Leipzig].
P2860
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P2860
Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@ast
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@en
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@nl
type
label
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@ast
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@en
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@nl
prefLabel
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@ast
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@en
Functional analysis of the R10 ...... n skeletal muscle EC coupling.
@nl
P2093
P1476
Functional analysis of the R10 ...... on skeletal muscle EC coupling
@en
P2093
Manfred Grabner
Paul D Allen
Regina G Weiss
Robert T Dirksen
P304
P356
10.1152/AJPCELL.00173.2004
P577
2004-06-16T00:00:00Z