Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle.
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The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phaseCalpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodelingStructure and physiological function of calpainsSkeletal muscle-specific calpain is an intracellular Na+-dependent proteaseThe second-largest subunit of the mouse DNA polymerase alpha-primase complex facilitates both production and nuclear translocation of the catalytic subunit of DNA polymerase alphaNovel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscleDown-regulation of MyoD by calpain 3 promotes generation of reserve cells in C2C12 myoblastsMolecular architecture of the mouse DNA polymerase alpha-primase complexEndogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent on stretchMdm muscular dystrophy: interactions with calpain 3 and a novel functional role for titin's N2A domain.Def defines a conserved nucleolar pathway that leads p53 to proteasome-independent degradationAge-related cataracts in alpha3Cx46-knockout mice are dependent on a calpain 3 isoform.Identification and optimization of a novel inhibitor of mitochondrial calpain 10Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional eventsAtypical Lipomatous Tumor/Well-Differentiated Liposarcoma Developed in a Patient with Progressive Muscular Dystrophy: A Case Report and Review of the LiteratureA New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review.Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy.Stable expression of calpain 3 from a muscle transgene in vivo: immature muscle in transgenic mice suggests a role for calpain 3 in muscle maturation.Comprehensive survey of p94/calpain 3 substrates by comparative proteomics--possible regulation of protein synthesis by p94.The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation.Pathogenity of some limb girdle muscular dystrophy mutations can result from reduced anchorage to myofibrils and altered stability of calpain 3.Calpain chronicle--an enzyme family under multidisciplinary characterizationFrom proteins to genes: immunoanalysis in the diagnosis of muscular dystrophies.Characterization of monoclonal antibodies to calpain 3 and protein expression in muscle from patients with limb-girdle muscular dystrophy type 2ALoss of calpain-3 autocatalytic activity in LGMD2A patients with normal protein expression.Regulation and physiological roles of the calpain system in muscular disordersLoss of calpain 3 proteolytic activity leads to muscular dystrophy and to apoptosis-associated IkappaBalpha/nuclear factor kappaB pathway perturbation in mice.CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cellsScreening of calpain-3 autolytic activity in LGMD muscle: a functional map of CAPN3 gene mutations.Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.Mutations of CAPN3 in Korean patients with limb-girdle muscular dystrophy.Mutations in calpain 3 associated with limb girdle muscular dystrophy: analysis by molecular modeling and by mutation in m-calpain.Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal componentsBiologically active monomeric and heterodimeric recombinant human calpain I produced using the baculovirus expression systemPLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.Purification of native p94, a muscle-specific calpain, and characterization of its autolysisHomodimerization of calpain 3 penta-EF-hand domain.Disruption of excitation-contraction coupling and titin by endogenous Ca2+-activated proteases in toad muscle fibres.A Gastrointestinal Calpain Complex, G-calpain, Is a Heterodimer of CAPN8 and CAPN9 Calpain Isoforms, Which Play Catalytic and Regulatory Roles, Respectively.
P2860
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P2860
Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Muscle-specific calpain, p94, ...... in disappearance from muscle.
@en
type
label
Muscle-specific calpain, p94, ...... in disappearance from muscle.
@en
prefLabel
Muscle-specific calpain, p94, ...... in disappearance from muscle.
@en
P2093
P1476
Muscle-specific calpain, p94, ...... g in disappearance from muscle
@en
P2093
Kawasaki H
Miyasaka M
Sorimachi H
Toyama-Sorimachi N
P304
10593-10605
P407
P577
1993-05-01T00:00:00Z