The calpain system.

By D. E. Goll, V. F. Thompson, Hongqi Li, Wei Wei, J. Cong. Physiological Reviews, 2003

2,966 citations recorded by the source corpus.

Subfields: Cell Biology, Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/46a9bb4ac93e36a639dd2797e3fcbf2bb1bc70f4

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. S. Lecker
2. M. Jackson
3. S. Powers
4. W. Mitch
5. W. Zong
6. A. Goldberg
7. Craig B. Thompson

In Cellular and Molecular Neuroscience

1. A. Goldberg
2. S. Lecker
3. M. Sandri
4. D. Glass

In Molecular Biology

1. S. Lecker
2. W. Zong
3. A. Goldberg
4. Craig B. Thompson
5. W. Mitch
6. L. Valente
7. R. Neira
8. J. Fernandes

Citations in the corpus

• Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production (2008, background): “In vivo calpain activity is regulated by multiple factors including cytosolic free calcium levels and the concentration of the endogenous calpain inhibitor calpastatin (127).”
• Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (2006, background): “These proteases seem to be activated when cells are injured and cytosolic Ca(2) rises, so they may play an important role in tissue injury, necrosis, and autolysis (6).”
• Mechanisms of water-holding capacity of meat: The role of postmortem biochemical and structural changes. (2005, background): “The calpain system is composed of several isoforms of calcium-dependent cysteine proteases (calpains), and their specific competitive inhibitor, calpastatin (Goll, Thompson, Li, Wei, & Cong, 2003).”
• Necrotic death as a cell fate. (2006, background): “There are at least 14 members that can be categorized into two subfamilies: µ-calpains and m-calpains, which are named to reflect their requirements for Ca2+. µ-Calpains are activated by micromolar and m-calpains by millimolar concentrations of Ca2+ (Suzuki and Sorimachi 1998; Goll et al. 2003).”
• What determines growth potential and juvenile quality of farmed fish species (2013, background): “Calpains are a superfamily of Ca regulated proteases involved in numerous physiological processes including cell death and apoptosis, cell motility, signal transduction, myoblast fusion and myofibrillargenesis (Goll et al. 2003).”
• Skeletal muscle fatigue: cellular mechanisms. (2008, background): “Skeletal muscle contains the ubiquitous calcium-dependent neutral proteases -calpain and m-calpain, as well as a muscle-specific isoform, calpain-3 (186).”
• Zebrafish as a model organism for nutrition and growth: towards comparative studies of nutritional genomics applied to aquacultured fishes (2011, background): “This system is important because it regulates a wide range of physiological processes including protein turnover and growth, cell cycle progression, and myoblast differentiation (Goll et al. 2003).”
• Biochemistry of postmortem muscle - lessons on mechanisms of meat tenderization. (2010, neutral): “In one proposed model (Goll et al., 2003; Neti, Novak, Thompson, & Goll, 2009) calpains catalyze the release of myofilaments from the myofibril and are made available to the proteasome and lysosomes for complete degradation to amino acids.”
• Protein Oxidation: Basic Principles and Implications for Meat Quality (2013, background): “Three members of the calpain system are the proteases m- and μ-calpain and their inhibitor calpastatin (Goll et al., 2003).”
• Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. (2006, background): “For more detailed information regarding the calpain system, the reader is referred to the extensive review by Goll et al. (2003).”