ArticleBiotechnology journal2007
Comprehensive survey of p94/calpain 3 substrates by comparative proteomics--possible regulation of protein synthesis by p94.
Article in Biotechnology journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 30 citations in OpenAlex.
- Insertion sequence 1 from calpain-3 is functional in calpain-2 as an internal propeptide.The Journal of biological chemistry · 2018Article
- Predictions of Cleavability of Calpain Proteolysis by Quantitative Structure-Activity Relationship Analysis Using Newly Determined Cleavage Sites and Catalytic Efficiencies of an Oligopeptide Array.Molecular & cellular proteomics : MCP · 2016Article
- Calpain-3 impairs cell proliferation and stimulates oxidative stress-mediated cell death in melanoma cells.PloS one · 2015Article
- The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Non-proteolytic functions of calpain-3 in sarcoplasmic reticulum in skeletal muscles.Journal of molecular biology · 2011Article
- Calpain chronicle--an enzyme family under multidisciplinary characterization.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2011Review
- Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy.The Journal of clinical investigation · 2010Article
- Skeletal muscle-specific calpain is an intracellular Na+-dependent protease.The Journal of biological chemistry · 2010Article
- Calpain3 is expressed in a proteolitically active form in papillomavirus-associated urothelial tumors of the urinary bladder in cattle.PloS one · 2010Article
- Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.Neuromuscular disorders : NMD · 2008Review
- Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calpain represents a family of Ca(2+)-dependent cytosolic cysteine proteases found in almost all eukaryotes and some bacteria, and is involved in a variety of biological phenomena, including brain function. Several substrates of calpain are aggressively proteolyzed under pathological conditions, e.g., in neurodegenerating processes, fodrin is proteolyzed by calpain. Because very small amounts of substrate are proteolyzed by calpain under normal biological conditions, the molecular identities of calpain substrates are largely unknown. In this study, an extensive survey of the substrates of p94/calpain 3 in COS7 cells was executed using iTRAQ(TM) labeling and 2-D LC-MALDI analysis. p94 was used because: (i) several p94 splicing variants are expressed in brain tissue even though p94 itself is a skeletal-muscle-specific calpain, and (ii) it exhibits Ca(2+)-independent activity in COS cells, which makes it useful for evaluating the effects of p94 protease activity on proteins without perturbing the cells. Our approach revealed several novel protein substrates for p94, including the substrates of conventional calpains, components of the protein synthesis system, and enzymes of the glycolytic pathway. The results demonstrate the usefulness and sensitivity of this approach for mining calpain substrates. A combination of this method with other analytical methods would contribute to elucidation of the biological relevance of the calpain family.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.