A two-amino acid mutation encountered in Duchenne muscular dystrophy decreases stability of the rod domain 23 (R23) spectrin-like repeat of dystrophin

Journal of Biological Chemistry

Volumn 284, Issue 13, 2009, Pages 8822-8832

  Legardinier, Sébastien ^a   Legrand, Baptiste ^a   Raguénès Nicol, Céline ^a   Bondon, Arnaud ^a   Hardy, Serge ^b   Tascon, Christophe ^a   Le Rumeur, Elisabeth ^a   Hubert, Jean François ^a  

^a CNRS   (France)

^b UNIVERSITÉ DE RENNES 1   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADDITIVE EFFECTS; BIOCHEMICAL PROPERTIES; CIRCULAR DICHROISM; CYTOSKELETON; DOUBLE MUTATION; DYSTROPHIN; MEMBRANE STRESS; MICE MODELS; MUSCULAR DYSTROPHY; PATHOGENIC MUTATION; PROTEIN LEVEL; REFOLDING; SECONDARY AND TERTIARY STRUCTURES; SINGLE MUTATION; SPECTRIN; STOPPED FLOW; THREE-DIMENSIONAL STRUCTURE; TRYPTOPHAN FLUORESCENCE; WILD TYPES;

AMINES; AMINO ACIDS; CIRCULAR DICHROISM SPECTROSCOPY; DICHROISM; MUSCLE; ORGANIC ACIDS; STABILITY; STRESSES;

CHEMICAL STABILITY;

DYSTROPHIN; SPECTRIN;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DUCHENNE MUSCULAR DYSTROPHY; GENE STRUCTURE; GENETIC STABILITY; MISSENSE MUTATION; MOLECULAR MODEL; MUTANT; NUCLEOTIDE REPEAT; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; WILD TYPE;

AMINO ACID SUBSTITUTION; ANIMALS; DYSTROPHIN; HUMANS; MICE; MODELS, MOLECULAR; MUSCULAR DYSTROPHY, DUCHENNE; MUTATION, MISSENSE; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE;

MUS;

EID: 65849498675     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M805846200     Document Type: Article

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