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 characterization of mutants in the predicted pore region of the rabbit cardiac muscle Ca(2+) release channel (ryanodine receptor isoform 2).

The Journal of biological chemistry - 24 Aug 2001

Du G G, Guo X, Khanna V K, MacLennan D H

Abstract excerpt

A highly conserved amino acid sequence, GVRAGGGIGD(4831), which may form part of the Ca(2+) release channel pore in RyR2, was subjected to Ala scanning or Ala to Val mutagenesis; function was then measured by expression in HEK-293 cells, followed by Ca(2+) photometry, high affinity [(3)H]ryanodine binding, and single-channel recording. All mutants except I4829A and I4829T (corresponding to the I4897T central core...

Read the complete abstract on PubMed

Topics

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

Share to Caffeine
Share to Fluorescent Dyes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Membrane Potentials

Share to Myocardium

Share to Rabbits

Share to Radioligand Assay

Share to Ryanodine Receptor Calcium Release Channel

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 11427530
DOI: 10.1074/jbc.M102751200

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 characterization of mutants in the predicted pore region of the rabbit cardiac muscle Ca(2+) release channel (ryanodine receptor isoform 2).PMID 11427530Read ↗

Characterization of cardiac disease-associated mutations in RyR2 Ca2+- and caffeine-binding sites.Semantic proximity Read ↗

Ca2+ release in muscle fibers expressing R4892W and G4896V type 1 ryanodine receptor disease mutants.Semantic proximity Read ↗

A mutation in the transmembrane/luminal domain of the ryanodine receptor is associated with abnormal Ca2+ release channel function and severe central core disease.Semantic proximity Read ↗

Functional heterogeneity of ryanodine receptor mutations associated with sudden cardiac deathSemantic proximity Read ↗

Novel RyR2 Mutation (G3118R) Is Associated With Autosomal Recessive Ventricular Fibrillation and Sudden Death: Clinical, Functional, and Computational Analysis.Semantic proximity Read ↗

Probing the role of negatively charged amino acid residues in ion permeation of skeletal muscle ryanodine receptor.Semantic proximity Read ↗

Functional effects of central core disease mutations in the cytoplasmic region of the skeletal muscle ryanodine receptor.Semantic proximity Read ↗

Structure and Function of the Human Ryanodine Receptors and Their Association with Myopathies—Present State, Challenges, and PerspectivesSemantic proximity Read ↗

Loss of luminal Ca <sup>2+</sup> activation in the cardiac ryanodine receptor is associated with ventricular fibrillation and sudden deathSemantic proximity Read ↗

Ryanodine receptor mutations in arrhythmias: advances in understanding the mechanisms of channel dysfunction.Semantic proximity Read ↗

Cardiac and skeletal muscle disorders caused by mutations in the intracellular Ca2+ release channels.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 ↗

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