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Daniel E. Michele

Researcher at University of Michigan

Publications -  72
Citations -  5585

Daniel E. Michele is an academic researcher from University of Michigan. The author has contributed to research in topics: Myocyte & Muscular dystrophy. The author has an hindex of 33, co-authored 67 publications receiving 5168 citations. Previous affiliations of Daniel E. Michele include University of Iowa & Roy J. and Lucille A. Carver College of Medicine.

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Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies

TL;DR: The results suggest that at least three distinct mammalian genes function within a convergent post-translational processing pathway during the biosynthesis of dystroglycan, and that abnormal dystoglycan–ligand interactions underlie the pathogenic mechanism of muscular dystrophy with brain abnormalities.
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Dystrophin-Glycoprotein Complex: Post-translational Processing and Dystroglycan Function

TL;DR: The dystrophin-glycoprotein complex (DGC) is a multimeric transmembrane protein complex first isolated from skeletal muscle membranes and the central protein is dystroglycan, which is thought to contribute to the structural stability of the muscle cell membrane during cycles of contraction and relaxation.
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Dystrophic heart failure blocked by membrane sealant poloxamer

TL;DR: It is shown that intact, isolated dystrophin-deficient cardiac myocytes have reduced compliance and increased susceptibility to stretch-mediated calcium overload, leading to cell contracture and death, and that application of the membrane sealant poloxamer 188 corrects these defects in vitro.
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Disruption of DAG1 in differentiated skeletal muscle reveals a role for dystroglycan in muscle regeneration.

TL;DR: It is found that satellite cells, expressing dystroglycan, support continued efficient regeneration of skeletal muscle along with transient expression of dystrophin-glycoprotein complex in differentiated muscle and in regenerating muscle fibers in a mild form of human muscular dystrophy caused by disruption of posttranslational dystoglycan processing.