Results 211 to 220 of about 56,717 (273)

Dystrophin isoform localisation:humans

Characterisation of dystrophin isoform localisation in different brain regions from normal human ...
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Displaced myonuclei are attributable to both resident myonuclear migration and stem cell fusion during mechanical loading in adult skeletal muscle. [PDF]

Skelet Muscle
Serrano N, Koopmans PJ, Murach KA.
europepmc   +1 more source

Ineffective behavioral rescue despite partial brain Dp427 restoration by AAV9-U7-mediated exon 51 skipping in <i>mdx52</i> mice. [PDF]

Mol Ther Nucleic Acids
Vacca O, Saoudi A, Doisy M, Phongsavanh X, Le Coz O, Nagy C, Kuzniar J, Vaillend C, Goyenvalle A.   +8 more
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Cell therapy for Duchenne muscular dystrophy: promises, challenges, and controversies. [PDF]

Cell Mol Life Sci
Łoboda A, Dulak J.
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Author Correction: Disease exacerbation in human DMD MYOrganoids enables gene therapy evaluation and unveils persistence of fibrotic activity. [PDF]

NPJ Regen Med
Palmieri L, Bimbi G, Ferrand M, Marcello M, Pili L, Hong AV, Jaber A, El-Khoury R, Brochier G, Bigot A, Israeli D, Richard I, Albini S.   +12 more
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Functions of dystrophin and dystrophin associated proteins

Current Opinion in Neurology, 1997
Dystrophin 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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Dystrophin and disease

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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Membrane organization of the dystrophin-glycoprotein complex

Cell, 1991
Kevin P Campbell
exaly   +2 more sources

Actin-dystrophin interface

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, A, Bonet-Kerrache, J J, Leger, D, Mornet   +3 more
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Dynamic restoration of dystrophin to dystrophin-deficient myotubes

Muscle & Nerve, 2001
Dystrophin 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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