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Primary aldosteronism complicated by early-onset heart failure in a young male with a coexisting DMD variant: A case report and literature review. [PDF]
Song X +12 more
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Targeting cellular senescence in dystrophin<sup>-/-</sup>/utrophin<sup>-/-</sup>double knockout mice improves musculoskeletal health and increases lifespan. [PDF]
Gao X +11 more
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Functions of dystrophin and dystrophin associated proteins
Current Opinion in Neurology, 1997Dystrophin is a protein product of the X-linked gene mutation that is responsible for Duchenne and Becker muscular dystrophies. The protein binds actin and associates with dystrophin-glycoprotein complex to link the cytoskeleton to the extracellular matrix.
M, Michalak, M, Opas
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Molecular Aspects of Medicine, 1991
Recent advances concerning the genetic and biochemical basis of Duchenne and Becker muscular dystrophies have resulted in a good understanding of the etiology of these common dystrophies. An important secondary consequence of the genetic and biochemical research has been the generation of gene-based and protein-based diagnostic tools which enable a ...
E P, Hoffman, L, Schwartz
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Recent advances concerning the genetic and biochemical basis of Duchenne and Becker muscular dystrophies have resulted in a good understanding of the etiology of these common dystrophies. An important secondary consequence of the genetic and biochemical research has been the generation of gene-based and protein-based diagnostic tools which enable a ...
E P, Hoffman, L, Schwartz
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Biochemistry, 1993
Dystrophin, an elongated cytoskeletal molecule which is deficient in Duchenne muscular disease, contains an actin-binding domain in its N-terminal portion. We show that this part interacted with actin in the native molecule. By molecular biology techniques, four recombinant proteins were expressed in Escherichia coli using the pMAL vector which allowed
E, Fabbrizio +3 more
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Dystrophin, an elongated cytoskeletal molecule which is deficient in Duchenne muscular disease, contains an actin-binding domain in its N-terminal portion. We show that this part interacted with actin in the native molecule. By molecular biology techniques, four recombinant proteins were expressed in Escherichia coli using the pMAL vector which allowed
E, Fabbrizio +3 more
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Dynamic restoration of dystrophin to dystrophin-deficient myotubes
Muscle & Nerve, 2001Dystrophin domains are observed in myoblast transplantation experiments and in muscle fibers after somatic reversion in human Duchenne and mdx mouse muscular dystrophy. However, the formation and evolution of dystrophin-positive domains are not well established.
J, Kong, J E, Anderson
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Neuromuscular Disorders, 1993
The respective localizations of dystrophin and dystrophin-related protein (DRP or utrophin) along the sarcolemmal membrane and at the neuromuscular junctions (NMJs) in normal and dystrophin-deficient skeletal muscles, were determined using confocal laser microscopy. The analysis was prompted by the recent availability of a new anti-utrophin mAb [Bewick
F, Pons +4 more
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The respective localizations of dystrophin and dystrophin-related protein (DRP or utrophin) along the sarcolemmal membrane and at the neuromuscular junctions (NMJs) in normal and dystrophin-deficient skeletal muscles, were determined using confocal laser microscopy. The analysis was prompted by the recent availability of a new anti-utrophin mAb [Bewick
F, Pons +4 more
openaire +2 more sources

