Please use this identifier to cite or link to this item:
Scopus Web of Science® Altmetric
Type: Journal article
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
Author: Laing, N.
Wilton, S.
Akkari, P.
Dorosz, S.
Boundy, K.
Kneebone, C.
Blumbergs, P.
White, S.
Watkins, H.
Love, D.
Haan, E.
Citation: Nature Genetics, 1995; 9(1):75-79
Publisher: Nature America, Inc.
Issue Date: 1995
ISSN: 1061-4036
Statement of
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
Myopathies, Nemaline
DNA Primers
DNA Mutational Analysis
Amino Acid Sequence
Base Sequence
Genes, Dominant
Point Mutation
Polymorphism, Genetic
Molecular Sequence Data
Genetic Linkage
Rights: Copyright ©1995 Nature Publishing Group
DOI: 10.1038/ng0195-75
Published version:
Appears in Collections:Aurora harvest 4
Paediatrics publications

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.