Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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.

American journal of physiology. Cell physiology - 1 Oct 2004

Weiss Regina G, O'Connell Kristen M S, Flucher Bernhard E, Allen Paul D, Grabner Manfred, Dirksen Robert T

Abstract excerpt

Malignant hyperthermia (MH) is an inherited pharmacogenetic disorder caused by mutations in the skeletal muscle ryanodine receptor (RyR1) and the dihydropyridine receptor (DHPR) alpha(1S)-subunit. We characterized the effects of an MH mutation in the DHPR cytoplasmic III-IV loop of alpha(1S) (R1086H) on DHPR-RyR1 coupling after reconstitution in dysgenic (alpha(1S) null) myotubes. Compared with wild-type...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Caffeine
Share to Calcium Channels, L-Type

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Central Nervous System Stimulants

Share to Malignant Hyperthermia

Share to Membrane Potentials

Share to Muscle Fibers, Skeletal

Share to Ryanodine Receptor Calcium Release Channel

Share to Sarcolemma

Source

Identifiers

PMID: 15201141
DOI: 10.1152/ajpcell.00173.2004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

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.PMID 15201141Read ↗

Functional defects in six ryanodine receptor isoform-1 (RyR1) mutations associated with malignant hyperthermia and their impact on skeletal excitation-contraction coupling.Semantic proximity Read ↗

Pathogenic CaV1.1 Variants Cause Hyperpolarizing Shift of Depolarization-Induced Ca2+ Release in Malignant Hyperthermia Susceptibility.Semantic proximity Read ↗

A 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.Semantic proximity Read ↗

Dynamic alterations in myoplasmic Ca2+ in malignant hyperthermia and central core disease.Semantic proximity Read ↗

Malignant hyperthermia and excitation-contraction coupling.Semantic proximity Read ↗

Divergent Activity Profiles of Type 1 Ryanodine Receptor Channels Carrying Malignant Hyperthermia and Central Core Disease Mutations in the Amino-Terminal Region.Semantic proximity Read ↗

Genotype-Phenotype Correlations of Malignant Hyperthermia and Central Core Disease Mutations in the Central Region of the RYR1 Channel.Semantic proximity Read ↗

Malignant hyperthermia: an inherited disorder of skeletal muscle Ca+ regulation.Semantic proximity Read ↗

Functional characterization of RYR1 variants identified in malignant hyperthermia susceptible individuals.Semantic proximity Read ↗

Malignant hyperthermia susceptibility arising from altered resting coupling between the skeletal muscle L-type Ca2+ channel and the type 1 ryanodine receptor.Semantic proximity Read ↗

Beyond Hotspots: Functional Characterization of the Novel p.Asp2730Tyr Mutation in RYR1 Associated With Malignant Hyperthermia.Semantic proximity Read ↗

Elevated resting [Ca(2+)](i) in myotubes expressing malignant hyperthermia RyR1 cDNAs is partially restored by modulation of passive calcium leak from the SR.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.