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Nina Raben

Researcher at National Institutes of Health

Publications -  131
Citations -  25755

Nina Raben is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Glycogen storage disease type II & Enzyme replacement therapy. The author has an hindex of 58, co-authored 129 publications receiving 22441 citations.

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Pompe Disease: From Basic Science to Therapy

TL;DR: How past discoveries of glycogen metabolism, the lysosome, and autophagy have guided Pompe research and impacted recent therapeutic developments is discussed.
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Deconstructing Pompe Disease by Analyzing Single Muscle Fibers: “To See a World in a Grain of Sand…”

TL;DR: Analysis of vesicles of the lysosomal-degradative pathway in isolated single muscle fibers from Pompe patients showed abundant autophagosome formation and areas of autophagic buildup of a wide range of sizes, suggesting clearing or preventing autophagy buildup seems a necessary target of Pompe disease therapy.
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Surprises of genetic engineering: a possible model of polyglucosan body disease.

TL;DR: It is shown here that increased level of GSase in the presence of normal glycogen branching enzyme (GBE) activity leads to polyglucosan accumulation, and an imbalance between GSase and GBE activities is proposed as the mechanism involved in the production of polyglUCosan bodies.
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Biochemical and pharmacological characterization of different recombinant acid α-glucosidase preparations evaluated for the treatment of Pompe disease

TL;DR: In a mouse model of Pompe disease, glycogen was more efficiently removed from the heart than from skeletal muscle for all enzymes, and overall, the CHO cell-derived rhGAA reduced glycogen to a greater extent than that observed with the other enzymes.
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A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope.

TL;DR: In this article, a recombinant histidyl-tRNA synthetase was found to be enzymatically active and recognized by human autoantibodies in the baculovirus system, and the peptides from this region (amino acids 1-60 and 1-47) have the predicted high alpha-helical content, but smaller fragments (1-30, 14-45, and 31-60) do not.