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Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: potentials for protein-protein interactions

Blake, Derek J., Tinsley, Jonathon M., Davies, Kay E., Knight, Alex E., Winder, Stephen J. and Kendrick-Jones, John 1995. Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: potentials for protein-protein interactions. Trends in Biochemical Sciences 20 (4) , pp. 133-135. 10.1016/S0968-0004(00)88986-0

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Abstract

Dystrophin, the protein product of the DMD gene, is a component of the muscle-membrane cytoskeleton. Mutations in the DMD gene result in the allelic myopathies Duchenne and Becket muscular dystrophy (DMD and BMD). The majority of mutations causing DMD and BMD are large intragenic deletions. The spectrum of these deletions can be used to explain the differences in the clinical severity between DMD and BMD patients. In general, mutations causing BMD, the milder disorder, maintain the translational reading frame of dystrophin and result in near normal amounts of an internally truncated protein. By contrast, deletions causing DMD disrupt the reading frame of dystrophin, often resulting in premature translational termination. Thus, DMD patients often produce little or no detectable dystrophin.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
MRC Centre for Neuropsychiatric Genetics and Genomics (CNGG)
Subjects: R Medicine > R Medicine (General)
Publisher: Elsevier
ISSN: 0968-0004
Last Modified: 04 Jun 2017 05:12
URI: http://orca-mwe.cf.ac.uk/id/eprint/49493

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