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

Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM.

Nature communications - 5 Feb 2021

Woll Kellie A, Haji-Ghassemi Omid, Van Petegem Filip

Abstract excerpt

Ryanodine Receptors (RyRs) are massive channels that release Ca2+ from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to malignant hyperthermia (MH), myopathies, and arrhythmias. Here, we explore the first MH mutation identified in humans by providing cryo-EM snapshots of the pig homolog, R615C, showing that it affects an interface between three solenoid regions. We also show the...

Read the complete abstract on PubMed

Topics

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

Share to Apoproteins
Share to Calmodulin
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Transport

Share to Malignant Hyperthermia

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Sarcoplasmic Reticulum

Source

Open in PubMed Open full text

Identifiers

PMID: 33547325
DOI: 10.1038/s41467-021-21141-3
PMCID: PMC7864917

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM.PMID 33547325Read ↗

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

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

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

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

Catching the next wave of recombinant RyR2 cryo-EM structures. Commentary on "Molecular basis for gating of cardiac ryanodine receptor explains the mechanisms for gain- and loss-of function mutations".Semantic proximity Read ↗

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

Crystal structure of type I ryanodine receptor amino-terminal beta-trefoil domain reveals a disease-associated mutation "hot spot" loop.Semantic proximity Read ↗

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

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

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

Dynamics of the β-cardiac myosin auto-inhibited state explain cardiomyopathy pathogenesis.Semantic proximity Read ↗

Structures of the junctophilin/voltage-gated calcium channel interface reveal hot spot for cardiomyopathy mutations.Semantic proximity Read ↗

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