Title |
Assessment of the structural and functional impact of in-frame mutations of the DMD gene, using the tools included in the eDystrophin online database
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Published in |
Orphanet Journal of Rare Diseases, July 2012
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DOI | 10.1186/1750-1172-7-45 |
Pubmed ID | |
Authors |
Aurélie Nicolas, Céline Lucchetti-Miganeh, Rabah Ben Yaou, Jean-Claude Kaplan, Jamel Chelly, France Leturcq, Frédérique Barloy-Hubler, Elisabeth Le Rumeur |
Abstract |
Dystrophin is a large essential protein of skeletal and heart muscle. It is a filamentous scaffolding protein with numerous binding domains. Mutations in the DMD gene, which encodes dystrophin, mostly result in the deletion of one or several exons and cause Duchenne (DMD) and Becker (BMD) muscular dystrophies. The most common DMD mutations are frameshift mutations resulting in an absence of dystrophin from tissues. In-frame DMD mutations are less frequent and result in a protein with partial wild-type dystrophin function. The aim of this study was to highlight structural and functional modifications of dystrophin caused by in-frame mutations. |
X Demographics
Geographical breakdown
Country | Count | As % |
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Unknown | 2 | 100% |
Demographic breakdown
Type | Count | As % |
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Members of the public | 1 | 50% |
Scientists | 1 | 50% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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United Kingdom | 1 | 1% |
France | 1 | 1% |
Unknown | 81 | 98% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 16 | 19% |
Researcher | 14 | 17% |
Student > Bachelor | 11 | 13% |
Student > Master | 8 | 10% |
Other | 6 | 7% |
Other | 13 | 16% |
Unknown | 15 | 18% |
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Agricultural and Biological Sciences | 22 | 27% |
Biochemistry, Genetics and Molecular Biology | 21 | 25% |
Medicine and Dentistry | 10 | 12% |
Neuroscience | 3 | 4% |
Nursing and Health Professions | 2 | 2% |
Other | 8 | 10% |
Unknown | 17 | 20% |