mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
about
Targeted proteolysis of plectin isoform 1a accounts for hemidesmosome dysfunction in mice mimicking the dominant skin blistering disease EBS-OgnaTaurine supplementation increases skeletal muscle force production and protects muscle function during and after high-frequency in vitro stimulationEndogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent on stretchDifferential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophyRedox state and mitochondrial respiratory chain function in skeletal muscle of LGMD2A patients.Regulatory mechanisms of skeletal muscle protein turnover during exercise.Mechanisms of excitation-contraction uncoupling relevant to activity-induced muscle fatigue.Increased autolysis of μ-calpain in skeletal muscles of chronic alcohol-fed rats.Activity, abundance and expression of Ca²⁺-activated proteases in skeletal muscle of the aestivating frog, Cyclorana alboguttata.Skeletal muscle atrophy in sedentary Zucker obese rats is not caused by calpain-mediated muscle damage or lipid peroxidation induced by oxidative stress.In situ measurements of calpain activity in isolated muscle fibres from normal and dystrophin-lacking mdx mice.Ca2+-dependent proteolysis of junctophilin-1 and junctophilin-2 in skeletal and cardiac muscle.Acute change of titin at mid-sarcomere remains despite 8 wk of plyometric training.Long-lasting muscle fatigue: partial disruption of excitation-contraction coupling by elevated cytosolic Ca2+ concentration during contractions.Role of calpain in eccentric contraction-induced proteolysis of Ca2+-regulatory proteins and force depression in rat fast-twitch skeletal muscle.A mouse model for monitoring calpain activity under physiological and pathological conditions.Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers.Past injurious exercise attenuates activation of primary calcium-dependent injury pathways in skeletal muscle during subsequent exercise.Single fiber analyses of glycogen-related proteins reveal their differential association with glycogen in rat skeletal muscle
P2860
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P2860
mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
@en
mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
@nl
type
label
mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
@en
mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
@nl
prefLabel
mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
@en
mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans.
@nl
P2860
P1476
mu-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans
@en
P2093
Graham D Lamb
Rodney J Snow
P2860
P304
P356
10.1152/AJPCELL.00291.2005
P577
2005-08-17T00:00:00Z