ArticleBiochimica et biophysica acta. Molecular cell research2021
The C2 domain of calpain 5 contributes to enzyme activation and membrane localization.
Article in Biochimica et biophysica acta. Molecular cell research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Calpains as Potential Regulators of Microtubule-Associated Cytokinesis: A Cross-Eukaryotic Unifying Hypothesis.Life (Basel, Switzerland) · 2026Article
- Article
- The Identification of Proteolytic Substrates of Calpain-5 with N-Terminomics.International journal of molecular sciences · 2025Article
- Genetic Loci Influencing Cue-Reactivity in Heterogeneous Stock Rats.Genes, brain, and behavior · 2025Article
- Proteolysis of mitochondrial calpain-13 in cerebral ischemia-reperfusion injury.Biochemistry and biophysics reports · 2024Article
- Genomic Loci Influencing Cue-Reactivity in Heterogeneous Stock Rats.bioRxiv : the preprint server for biology · 2024Article
- Impaired activity and membrane association of most calpain-5 mutants causal for neovascular inflammatory vitreoretinopathy.Biochimica et biophysica acta. Molecular basis of disease · 2023Article
- Membrane-anchored calpains - hidden regulators of growth and development beyond plants?Frontiers in plant science · 2023Article
- Calpains as mechanistic drivers and therapeutic targets for ocular disease.Trends in molecular medicine · 2022Review
- Calpain-Independent Intracellular Protease Activity Is Elevated in Excitotoxic Cortical Neurons Prior to Delayed Calcium Deregulation and Mitochondrial Dysfunction.Biomolecules · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The enzymatic characteristics of the ubiquitous calpain 5 (CAPN5) remain undescribed despite its high expression in the central nervous system and links to eye development and disease. CAPN5 contains the typical protease core domains but lacks the C terminal penta-EF hand domain of classical calpains, and instead contains a putative C2 domain. This study used the SH-SY5Y neuroblastoma cell line stably transfected with CAPN5-3xFLAG variants to assess the potential roles of the CAPN5 C2 domain in Ca
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