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

Direct Evidence That Mutations within Dysferlin's C2A Domain Inhibit Lipid Clustering.

The journal of physical chemistry. B - 14 Jan 2021

Golbek Thaddeus W, Otto Shauna C, Roeters Steven J, Weidner Tobias, Johnson Colin P, Baio Joe E

Abstract excerpt

Mechanical stress on sarcolemma can create small tears in the muscle cell membrane. Within the sarcolemma resides the multidomain dysferlin protein. Mutations in this protein render it unable to repair the sarcolemma and have been linked to muscular dystrophy. A key step in dysferlin-regulated repair is the binding of the C2A domain to the lipid membrane upon increased intracellular calcium. Mutations mapped to...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Cluster Analysis
Share to Dysferlin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipids

Share to Membrane Proteins

Share to Mutation

Share to Protein Binding

Source

Identifiers

PMID: 33355462
DOI: 10.1021/acs.jpcb.0c07143

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Direct Evidence That Mutations within Dysferlin's C2A Domain Inhibit Lipid Clustering.PMID 33355462Read ↗

Calcium binds and rigidifies the dysferlin C2A domain in a tightly coupled manner.Semantic proximity Read ↗

Calcium Sensitive Allostery Regulates the PI(4,5)P2 Binding Site of the Dysferlin C2A DomainSemantic proximity Read ↗

Quantitation of the calcium and membrane binding properties of the C2 domains of dysferlin.Semantic proximity Read ↗

Pathogenic Mutations in the C2A Domain of Dysferlin form Amyloid that Activates the InflammasomeSemantic proximity Read ↗

Proteomic investigation of the molecular pathophysiology of dysferlinopathy.Semantic proximity Read ↗

Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains.Semantic proximity Read ↗

Crystal structures of the human Dysferlin inner DysF domainSemantic proximity Read ↗

Pathogenic mutation R959W alters recognition dynamics of dysferlin inner DysF domain.Semantic proximity Read ↗

Mutation impact on dysferlin inferred from database analysis and computer-based structural predictions.Semantic proximity Read ↗

Dysferlin-mediated phosphatidylserine sorting engages macrophages in sarcolemma repairSemantic proximity Read ↗

In silico functional and structural characterisation of ferlin proteins by mapping disease-causing mutations and evolutionary information onto three-dimensional models of their C2 domains.Semantic proximity Read ↗

Dysferlin-peptides reallocate mutated dysferlin thereby restoring function.Semantic proximity Read ↗

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