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Calpains: an elaborate proteolytic system.
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Calpain research for drug discovery: challenges and potential
TLDR
The calpain superfamily and calpain-related disorders are reviewed,Therapeutic strategies targeting malfunctions of calpains have been developed, driven primarily by improvements in the specificity and bioavailability of calpain inhibitors.
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Possible Regulation of the Conventional Calpain System by Skeletal Muscle-specific Calpain, p94/Calpain 3*
TLDR
This study enzymatically characterized one alternatively spliced variant of p94, p94:exons 6–15–16– (p94Δ), which lacks two of the p94-specific insertion sequences and established a semi-quantitative fluorescence resonance energy transfer assay using the calpastatin sequence specifically to measure p94 activity.
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Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis.
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Impact of genetic insights into calpain biology.
TLDR
Gene studies show that a variety of defects in many different organisms, including lethality, muscular dystrophies and gastropathy, actually stem from calpain deficiencies, which form the basis for ongoing and future studies regarding the physiological role of calpains.
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Calpain chronicle—an enzyme family under multidisciplinary characterization
TLDR
The study of calpains focuses especially on recent findings about their structure–function relationships, which have been greatly aided by the development of 3D structural studies and genetic models.
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Regulation and physiological roles of the calpain system in muscular disorders
TLDR
Calpains, a family of Ca2+-dependent cytosolic cysteine proteases, can modulate their substrates' structure and function through limited proteolytic activity, and their functions and regulation are summarized.
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The crystal structure of a virus-like particle from the hyperthermophilic archaeon Pyrococcus furiosus provides insight into the evolution of viruses.
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Expanding members and roles of the calpain superfamily and their genetically modified animals.
TLDR
The unique characteristics of this distinctive protease superfamily are introduced in terms of genetically modified animals, some of which are animal models of calpain deficiency diseases.
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Induction and myofibrillar targeting of CARP, and suppression of the Nkx2.5 pathway in the MDM mouse with impaired titin-based signaling.
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