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Weak protein-bicelle binding quantification via surface-based DNA nanolevers. [PDF]
Eur Biophys JCombet S +9 more
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An antisense method for efficient exon skipping and its application to Duchenne muscular dystrophy. [PDF]
Proc Natl Acad Sci U S AFeng P +5 more
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Emerging roles of microRNAs and other non-coding transcriptome in muscular dystrophies. [PDF]
Inflamm RegenAbdelrehim FG +5 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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Progress in Neurobiology, 1997
Dystrophin is a plasma membrane-associated cytoskeletal protein of the spectrin superfamily. The dystrophin cytoskeleton has been first characterized in muscle. Muscular 427 kDa dystrophin binds to subplasmalemmal actin filaments via its amino-terminal domain.
F, Schmitz, D, Drenckhahn
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Dystrophin is a plasma membrane-associated cytoskeletal protein of the spectrin superfamily. The dystrophin cytoskeleton has been first characterized in muscle. Muscular 427 kDa dystrophin binds to subplasmalemmal actin filaments via its amino-terminal domain.
F, Schmitz, D, Drenckhahn
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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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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
J J Leger, L V Nicholson
exaly +3 more sources
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
J J Leger, L V Nicholson
exaly +3 more sources
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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Molecular Extensibility of Mini-dystrophins and a Dystrophin Rod Construct
Journal of Molecular Biology, 2005Muscular dystrophies arise with various mutations in dystrophin, implicating this protein in force transmission in normal muscle. With 24 three-helix, spectrin repeats interspersed with proline-rich hinges, dystrophin's large size is an impediment to gene therapy, prompting the construction of mini-dystrophins.
Nishant, Bhasin +7 more
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