Myopathy mutations in α-skeletal-muscle actin cause a range of molecular defects

Journal of Cell Science

Volumn 117, Issue 15, 2004, Pages 3367-3377

  Costa, Céline F ^a,e   Rommelaere, Heidi ^b   Waterschoot, Davy ^b   Sethi, Kamaljit K ^a   Nowak, Kristen J ^c,d,f   Laing, Nigel G ^c,d   Ampe, Christophe ^b   Machesky, Laura M ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^c UNIVERSITY OF WESTERN AUSTRALIA   (Australia)

^d PATHWEST LABORATORY MEDICINE   (Australia)

^e UNIVERSITY OF GENEVA   (Switzerland)

^f UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Actin; Actin mutations; Actin polymerization; Myopathy; Nemaline myopathy; Protein folding

Indexed keywords

ACTIN BINDING PROTEIN; ALPHA ACTIN; NUCLEOTIDE BINDING PROTEIN;

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL STRAIN 3T3; CONTROLLED STUDY; DISEASE SEVERITY; FIBROBLAST; GENE EXPRESSION; GENE MUTATION; GENETIC CODE; IMMUNOFLUORESCENCE MICROSCOPY; IN VITRO STUDY; MOUSE; MYOPATHY; NONHUMAN; NUCLEOTIDE BINDING SITE; PHENOTYPE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; SKELETAL MUSCLE;

ACTINS; ALLELES; ANIMALS; FIBROBLASTS; MICE; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; MUSCLE, SKELETAL; MUSCULAR DISEASES; MUTATION; NIH 3T3 CELLS; PHENOTYPE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; TRANSFECTION;

ANIMALIA;

EID: 4344656639     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01172     Document Type: Article

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