Calpain-mediated proteolysis of tropomodulin isoforms leads to thin filament elongation in dystrophic skeletal muscle

Molecular Biology of the Cell

Volumn 25, Issue 6, 2014, Pages 852-865

  Gokhin, David S ^a   Tierney, Matthew T ^b   Sui, Zhenhua ^a   Sacco, Alessandra ^b   Fowler, Velia M ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b BURNHAM INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA ACTININ; CALPAIN; CALPAIN 2; CYTOPLASMIC GAMMA ACTIN; CYTOSKELETON PROTEIN; NEBULIN; TMOD1 PROTEIN; TMOD3 PROTEIN; TMOD4 PROTEIN; TROPOMODULIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL MODEL; ARTICLE; CELL ELONGATION; CONTROLLED STUDY; DISEASE SEVERITY; DUCHENNE MUSCULAR DYSTROPHY; EMBRYO; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BLOOD LEVEL; PROTEIN DEGRADATION; PROTEIN DEPLETION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN LOCALIZATION; SARCOMERE LENGTH; SOLEUS MUSCLE; THIN FILAMENT;

ACTIN CYTOSKELETON; ACTININ; ACTINS; ANIMALS; CALPAIN; DISEASE MODELS, ANIMAL; MICE; MICE, INBRED MDX; MUSCLE PROTEINS; MUSCLE, SKELETAL; MUSCULAR DYSTROPHY, DUCHENNE; PROTEIN STRUCTURE, TERTIARY; PROTEOLYSIS; TROPOMODULIN;

EID: 84896306375     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-10-0608     Document Type: Article

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