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

Contribution of distinct structural elements to activation of calpain by Ca2+ ions.

The Journal of biological chemistry - 7 May 2004

Alexa Anita, Bozóky Zoltán, Farkas Attila, Tompa Peter, Friedrich Peter

Abstract excerpt

The effect of Ca2+ in calpain activation is mediated via several binding sites in the enzyme molecule. To test the contribution of structural elements suspected to be part of this Ca2+ relay system, we made a site-directed mutagenesis study on calpains, measuring consequential changes in Ca2+ binding and Ca2+ sensitivity of enzyme activity. Evidence is provided for earlier suggestions that an acidic loop in...

Read the complete abstract on PubMed

Topics

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

Share to Calpain
Share to Catalysis
Share to DNA Restriction Enzymes

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

Share to Genetic Vectors

Share to Hydrolysis

Share to Liposomes

Share to Phospholipids

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 14976200
DOI: 10.1074/jbc.M311969200

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

Contribution of distinct structural elements to activation of calpain by Ca2+ ions.PMID 14976200Read ↗

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

Ca2+ dependency of calpain 3 (p94) activation.Semantic proximity Read ↗

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

Origins of the difference in Ca2+ requirement for activation of mu- and m-calpain.Semantic proximity Read ↗

Activation of calpain by Ca2+: roles of the large subunit N-terminal and domain III-IV linker peptides.Semantic proximity Read ↗

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

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

Calmodulin regulates Ca2+-sensing receptor-mediated Ca2+ signaling and its cell surface expression.Semantic proximity Read ↗

A tail of multiple calcium-sensing domains.Semantic proximity Read ↗

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

Mutant analysis approaches to understanding calcium signal transduction through calmodulin and calmodulin regulated enzymes.Semantic proximity Read ↗

Mutational effects on the cooperativity of Ca2+ binding in calmodulin.Semantic proximity Read ↗

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