Results 151 to 160 of about 21,009 (196)
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Dystrophin and the membrane skeleton
Current Opinion in Cell Biology, 1993Recent studies have confirmed several predictions concerning the structure and possible function of dystrophin, including a direct interaction with F-actin and an indirect interaction with laminin via linkage through a transmembrane protein complex. The results of the past year support a role for dystrophin in linking the actin cytoskeleton with the ...
J M, Ervasti, K P, Campbell
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The dystrophin connection — ATP?
Medical Hypotheses, 1992Clinical evidence is presented supporting the hypothesis that the metabolic abnormality in the dystrophin-defective muscular dystrophies (DMD and BMD) involves the ATP pathway. Objective laboratory data show corrective trends in the abnormal values of parameters relating to creatine and calcium metabolism (ATP) by use of glucagon-stimulated c-AMP and ...
C A, Bonsett, A, Rudman
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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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A quantitative ELISA for dystrophin
Journal of Immunological Methods, 1993A novel approach to the quantitation of the muscular dystrophy protein, dystrophin, in muscle extracts is described. The two-site ELISA uses two monoclonal antibodies against dystrophin epitopes which lie close together in the rod domain of the dystrophin molecule in order to minimize the effects of dystrophin degradation.
G E, Morris, J M, Ellis, T M, Nguyen
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Dystrophin and related proteins
Current Opinion in Genetics & Development, 1993During the past year significant progress has been made in understanding how dystrophin deficiency leads to muscle cell necrosis in Duchenne muscular dystrophy and Becker muscular dystrophy. Dystrophin interacts with a glycoprotein complex spanning the muscle sarcolemma, effectively linking the actin cytoskeleton to the extracellular matrix.
J M, Tinsley +5 more
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The muscular dystrophies and dystrophin
Current Opinion in Neurology, 1993Recent progress in molecular genetics has resulted in more insight in the molecular biology of muscles and the muscular dystrophies, and has provided more reliable tools for prenatal and presymptomatic diagnosis in several disorders. The state of research is reviewed with emphasis on genetic aspects.
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Expression of Dystrophins and the Dystrophin-Associated-Protein Complex by Pituicytes in Culture
Neurochemical Research, 2011The dystrophin-associated-protein complex (DAPC) has been extensively characterized in the central nervous system where it is localized both in neuronal and glial cells. Few studies have characterized this complex in the neurohypophysis. To further study this complex in pituicytes, the resident astroglia of the neurophypophysis, we used adult pituicyte
Bougrid, Abdelkader +7 more
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Dystrophin and dystrophin-related proteins: A review of protein and RNA studies
Neuromuscular Disorders, 1993The analysis of dystrophin gene expression has led to the identification of multiple transcripts and varying isoforms. The data indicate that transcription of the dystrophin gene occurs from several promoters, which involves developmental and tissue-dependent regulation.
D R, Love +4 more
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[Dystrophin, dystrophin-associated protein and dystrophinopathy].
Nihon shinkei seishin yakurigaku zasshi = Japanese journal of psychopharmacology, 1995Dystrophin is a protein product of the gene responsible for Duchenne muscular dystrophy (DMD), and is a long slender protein localized at the protoplasmic surface of sarcolemma. Dystrophin binds with actin filaments at its amino-terminal region, and with dystrophin-associated proteins (DAPs) at its carboxyl-terminal region.
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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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