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

Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle.

The Journal of cell biology - 23 Feb 1998

Protasi F, Franzini-Armstrong C, Allen P D

Abstract excerpt

In muscle cells, excitation-contraction (e-c) coupling is mediated by "calcium release units," junctions between the sarcoplasmic reticulum (SR) and exterior membranes. Two proteins, which face each other, are known to functionally interact in those structures: the ryanodine receptors (RyRs), or SR calcium release channels, and the dihydropyridine receptors (DHPRs), or L-type calcium channels of exterior...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Cell Line
Share to DNA, Complementary

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Immunohistochemistry

Share to Microscopy, Electron

Share to Mutation

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 9472035
DOI: 10.1083/jcb.140.4.831
PMCID: PMC2141739

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of ryanodine receptors in the assembly of calcium release units in skeletal muscle.PMID 9472035Read ↗

Congenital myopathy associated with the triadin knockout syndrome.Semantic proximity Read ↗

Ryanodine receptors: structure and function.Semantic proximity Read ↗

Muscle fibers from dysgenic mouse in vivo lack a surface component of peripheral couplingsSemantic proximity Read ↗

Massive reduction of RyR1 in muscle spindles of mice carrying recessive Ryr1 mutations alters proprioception and causes scoliosis.Semantic proximity Read ↗

Ryanodine receptor RyR1-mediated elevation of Ca2+ concentration is required for the late stage of myogenic differentiation and fusionSemantic proximity Read ↗

RyR1-related myopathy mutations in ATP and calcium binding sites impair channel regulation.Semantic proximity Read ↗

RyR1 deficiency in congenital myopathies disrupts excitation-contraction coupling.Semantic proximity Read ↗

Massive reduction of RyR1 in muscle spindles of mice carrying recessive <i>Ryr1</i> mutations alters proprioception and causes scoliosisSemantic proximity Read ↗

Abnormal distribution of calcium-handling proteins: a novel distinctive marker in core myopathies.Semantic proximity Read ↗

A reconstituted depolarization-induced Ca2+ release platform for validation of skeletal muscle disease mutations and drug discovery.Semantic proximity Read ↗

The amino-terminal disease hotspot of ryanodine receptors forms a cytoplasmic vestibule.Semantic proximity Read ↗

Reconstituted depolarization-induced Ca <sup>2+</sup> release platform for skeletal muscle disease mutation validation and drug discoverySemantic proximity Read ↗

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