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Human dystrophin gene transfer: genetic correction of dystrophin deficiency
1993Somatic gene therapy, as generally conceived, involves reconstituting a biological function by adding a normal gene to somatic, i.e. non-germline, cells which are genetically deficient in that gene product (Friedmann, 1989). Single gene or Mendelian disorders which are recessive (autosomal or X-linked) are particularly attractive candidates for such a ...
George Dickson, Matthew G. Dunckley
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Dystrophin is not essential for the integrity of the cytoskeleton
Acta Neuropathologica, 1994Dystrophin is localized, in normal muscle fibers, on the cytoplasmic surface of the sarcolemma. The function of this protein is not known but, according to its structure and intracellular distribution, it seems likely that dystrophin interacts with other cytoskeletal proteins to form a complex linkage between myofibrils, sarcolemma and extracellular ...
MASSA, ROBERTO+4 more
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Dystrophin and dystrophin-related protein expression in Torpedo marmorata electric organ
Neuroscience Letters, 1993The presence of different dystrophin-related protein forms was investigated in electric organ as compared to cardiac, white or red skeletal muscles from Torpedo marmorata. Two strategies were followed. First, we used specific C-terminal dystrophin and dystrophin-related protein monoclonal antibodies which we characterized in the present study.
Jean J. Leger+3 more
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Nature, 1992
The primary sequence of two components of the dystrophin-glycoprotein complex has been established by complementary, DNA cloning. The transmembrane 43K and extracellular 156K dystrophin-associated glycoproteins (DAGs) are encoded by a single messenger RNA and the extracellular 156K DAG binds laminin.
James M. Ervasti+5 more
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The primary sequence of two components of the dystrophin-glycoprotein complex has been established by complementary, DNA cloning. The transmembrane 43K and extracellular 156K dystrophin-associated glycoproteins (DAGs) are encoded by a single messenger RNA and the extracellular 156K DAG binds laminin.
James M. Ervasti+5 more
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Dystrophin: A clinical perspective
Pediatric Neurology, 1990Dystrophin, the protein product of the gene related to Duchenne and Becker muscular dystrophies, is a large cytoskeletal protein associated with the muscle fiber membrane. Recently identified dystrophin-related myopathies affecting animals can serve as experimental models for human disease.
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Hippocampal LTP in dystrophin- and dystrophin isoforms-deficient mice
1997info:eu-repo/semantics ...
Godfraind, J M+2 more
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Dystrophin and Dystrophin-Associated Proteins
2014I. Kleyman, T.H. Brannagan
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Dystrophin and Duchenne dystrophy
Neuromuscular Disorders, 2015Victor Dubowitz, Ronald D. Cohn
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