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

Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains.

The Journal of biological chemistry - 21 Jun 2002

Davis Dawn Belt, Doherty Katherine R, Delmonte Anthony J, McNally Elizabeth M

Abstract excerpt

Mutations in dysferlin, a novel membrane protein of unknown function, lead to muscular dystrophy. Myoferlin is highly homologous to dysferlin and like dysferlin is a plasma membrane protein with six C2 domains highly expressed in muscle. C2 domains are found in a variety of membrane-associated pr...

Read the complete abstract on PubMed

Topics

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

Share to Calcium-Binding Proteins
Share to Dysferlin
Share to Lipid Metabolism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Fluorescence

Share to Muscle Proteins

Share to Muscles

Share to Phosphatidylserines

Share to Phospholipids

Source

Identifiers

PMID: 11959863
DOI: 10.1074/jbc.M201858200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11959863-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains.PMID 11959863Read ↗

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

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

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

Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing.Semantic proximity Read ↗

Structural Basis of Lipid Membrane Binding by Human FerlinsSemantic proximity Read ↗

FER-1 regulates Ca2+ -mediated membrane fusion during C. elegans spermatogenesis.Semantic proximity Read ↗

Translational research and therapeutic perspectives in dysferlinopathies.Semantic proximity Read ↗

Dysferlin mediates membrane tubulation and links T-tubule biogenesis to muscular dystrophy.Semantic proximity Read ↗

FerA is a Membrane-Associating Four-Helix Bundle Domain in the Ferlin Family of Membrane-Fusion Proteins.Semantic proximity Read ↗

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

On the role of dysferlin in striated muscle: membrane repair, t‐tubules and Ca2+ handlingSemantic proximity Read ↗

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