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

Toward decrypting the allosteric mechanism of the ryanodine receptor based on coarse-grained structural and dynamic modeling.

Proteins - 1 Dec 2015

Zheng Wenjun

Abstract excerpt

The ryanodine receptors (RyRs) are a family of calcium (Ca) channels that regulate Ca release by undergoing a closed-to-open gating transition in response to action potential or Ca binding. The allosteric mechanism of RyRs gating, which is activated/regulated by ligand/protein binding >200 Å away from the channel gate, remains elusive for the lack of high-resolution structures. Recent solution of the closed-form...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Cryoelectron Microscopy
Share to EF Hand Motifs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutation

Share to Protein Domains

Share to Ryanodine Receptor Calcium Release Channel

Source

Identifiers

PMID: 26492335
DOI: 10.1002/prot.24951

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

Toward decrypting the allosteric mechanism of the ryanodine receptor based on coarse-grained structural and dynamic modeling.PMID 26492335Read ↗

Investigating dual Ca2+ modulation of the ryanodine receptor 1 by molecular dynamics simulation.Semantic proximity Read ↗

Structural Details of the Ryanodine Receptor Calcium Release Channel and Its Gating Mechanism.Semantic proximity Read ↗

Structural basis for the gating mechanism of the type 2 ryanodine receptor RyR2.Semantic proximity Read ↗

Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM.Semantic proximity Read ↗

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

Mapping Ryanodine Binding Sites in the Pore Cavity of Ryanodine Receptors.Semantic proximity Read ↗

Investigating dual Ca <sup>2+</sup> modulation of the ryanodine receptor 1 by molecular dynamics simulationSemantic proximity Read ↗

Molecular basis for gating of cardiac ryanodine receptor explains the mechanisms for gain- and loss-of function mutations.Semantic proximity Read ↗

Probing the Structural Dynamics of the NMDA Receptor Activation by Coarse-Grained Modeling.Semantic proximity Read ↗

Structural mechanism of two gain-of-function cardiac and skeletal RyR mutations at an equivalent site by cryo-EM.Semantic proximity Read ↗

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

Molecular mechanism of the severe MH/CCD mutation Y522S in skeletal ryanodine receptor (RyR1) by cryo-EM.Semantic proximity Read ↗

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