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|Title:||A mutation in the α tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy|
|Other Titles:||A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy|
|Citation:||Nature Genetics, 1995; 9(1):75-79|
|Publisher:||Nature America, Inc.|
|Nigel G. Laing, Stephen D. Wilton, Patrick A. Akkari, Shellie Dorosz, Karyn Boundy, Chris Kneebone, Peter Blumbergs, Sue White, Hugh Watkins, Donald R. Love and Eric Haan|
|Abstract:||Nemaline myopathies are diseases characterized by the presence in muscle fibres of pathognomonic rod bodies. These are composed largely of −actinin and actin. We have identified a missense mutation in the −tropomyosin gene, TPM3, which segregates completely with the disease in a family whose autosomal dominant nemaline myopathy we had previously localized to chromosome 1p13−q25. The mutation substitutes an arginine residue for a highly conserved methionine in a putative actin−binding site near the N terminus of the −tropomyosin. The mutation may strengthen tropomyosin − actin binding, leading to rod body formation, by adding a further basic residue to the postulated actin−binding motif.|
|Keywords:||Chromosomes, Human, Pair 1; Humans; Myopathies, Nemaline; Tropomyosin; DNA; DNA Primers; Pedigree; DNA Mutational Analysis; Amino Acid Sequence; Base Sequence; Genes, Dominant; Point Mutation; Polymorphism, Genetic; Exons; Molecular Sequence Data; Female; Male; Genetic Linkage|
|Rights:||Copyright ©1995 Nature Publishing Group|
|Appears in Collections:||Paediatrics publications|
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