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

Lobe-specific calmodulin binding to different ryanodine receptor isoforms.

Biochemistry - 11 Feb 2014

Lau Kelvin, Chan Mandy M Y, Van Petegem Filip

Abstract excerpt

Ryanodine receptors (RyRs) are large ion channels that are responsible for the release of Ca(2+) from the sarcoplasmic/endoplasmic reticulum. Calmodulin (CaM) is a Ca(2+) binding protein that can affect the channel open probability at both high and low Ca(2+) concentrations, shifting the Ca(2+) dependencies of channel opening in an isoform-specific manner. Here we analyze the binding of CaM and its individual...

Read the complete abstract on PubMed

Topics

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

Share to Calmodulin
Share to Malignant Hyperthermia
Share to Myocardium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Myopathy, Central Core

Share to Protein Isoforms

Share to Rabbits

Share to Ryanodine Receptor Calcium Release Channel

Share to Thermodynamics

Source

Identifiers

PMID: 24447242
DOI: 10.1021/bi401502x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Lobe-specific calmodulin binding to different ryanodine receptor isoforms.PMID 24447242Read ↗

Site-specific modification of calmodulin Ca²(+) affinity tunes the skeletal muscle ryanodine receptor activation profile.Semantic proximity Read ↗

Arrhythmia-Associated Calmodulin E105A Mutation Alters the Binding Affinity of CaM to a Ryanodine Receptor 2 CaM-Binding Pocket.Semantic proximity Read ↗

Computational Analysis of Binding Interactions between the Ryanodine Receptor Type 2 and Calmodulin.Semantic proximity Read ↗

Life-threatening arrhythmogenic CaM mutations disrupt CaM binding to a distinct RyR2 CaM-binding pocket.Semantic proximity Read ↗

Molecular basis of calmodulin binding to cardiac muscle Ca(2+) release channel (ryanodine receptor).Semantic proximity Read ↗

Arrhythmogenic calmodulin variants D131E and Q135P disrupt interaction with the L-type voltage-gated Ca2+ channel (Cav1.2) and reduce Ca2+-dependent inactivation.Semantic proximity Read ↗

Calmodulin-binding locations on the skeletal and cardiac ryanodine receptors.Semantic proximity Read ↗

Calmodulin regulates Ca2+-sensing receptor-mediated Ca2+ signaling and its cell surface expression.Semantic proximity Read ↗

Half-calcified calmodulin promotes basal activity and inactivation of the L-type calcium channel CaV1.2.Semantic proximity Read ↗

Different regions in skeletal and cardiac muscle ryanodine receptors are involved in transducing the functional effects of calmodulin.Semantic proximity Read ↗

Human disease-associated calmodulin mutations alter calcineurin function through multiple mechanisms.Semantic proximity Read ↗

Structural determination of the phosphorylation domain of the ryanodine receptor.Semantic proximity Read ↗

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