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

Ca2+ dependency of calpain 3 (p94) activation.

Biochemistry - 21 Mar 2006

García Díaz Beatriz E, Gauthier Sherry, Davies Peter L

Abstract excerpt

Calpain 3, commonly called p94 in the literature, is the abundant skeletal muscle-specific calpain that is genetically linked to limb girdle muscular dystrophy type 2A. Recently, we showed that p94's insertion sequence 1 (IS1) is a propeptide that must be autoproteolytically cleaved to provide access of substrates and inhibitors to the enzyme's active site. Removal of IS1 from the core of p94 by recombinant...

Read the complete abstract on PubMed

Topics

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

Share to Calpain
Share to Coumarins
Share to Dipeptides

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Edetic Acid

Share to Hydrolysis

Share to Magnesium

Share to Potassium

Share to Sodium

Source

Identifiers

PMID: 16533054
DOI: 10.1021/bi051917j

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ca2+ dependency of calpain 3 (p94) activation.PMID 16533054Read ↗

Skeletal muscle-specific calpain is an intracellular Na+-dependent protease.Semantic proximity Read ↗

An eccentric calpain, CAPN3/p94/calpain-3.Semantic proximity Read ↗

The importance of conserved amino acid residues in p94 protease sub-domain IIb and the IS2 region for constitutive autolysis.Semantic proximity Read ↗

Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation.Semantic proximity Read ↗

Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C(2)-like domain.Semantic proximity Read ↗

Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.Semantic proximity Read ↗

Roles of individual EF-hands in the activation of m-calpain by calcium.Semantic proximity Read ↗

CAPN3: A muscle‑specific calpain with an important role in the pathogenesis of diseases (Review)Semantic proximity Read ↗

Autolysis, Ca2+ requirement, and heterodimer stability in m-calpain.Semantic proximity Read ↗

Calpains for dummies: What you need to know about the calpain family.Semantic proximity Read ↗

Strategies for regulating calpain activities in living cells.Semantic proximity Read ↗

Calpain activation by cooperative Ca2+ binding at two non-EF-hand sites.Semantic proximity Read ↗

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