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David Schubert

Researcher at Salk Institute for Biological Studies

Publications -  241
Citations -  28753

David Schubert is an academic researcher from Salk Institute for Biological Studies. The author has contributed to research in topics: Cell culture & Amyloid beta. The author has an hindex of 76, co-authored 237 publications receiving 27330 citations. Previous affiliations of David Schubert include University of California, San Diego & Washington University in St. Louis.

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Journal ArticleDOI

Hydrogen peroxide mediates amyloid beta protein toxicity.

TL;DR: The cytotoxic action of A beta on neurons results from free radical damage to susceptible cells, suggesting that A beta activates a member of this class of enzymes.
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3D structure of Alzheimer's amyloid-β(1–42) fibrils

TL;DR: The 3D structure of the fibrils comprising Aβ(1–42), which was obtained by using hydrogen-bonding constraints from quenched hydrogen/deuterium-exchange NMR, side-chain packing constraints from pairwise mutagenesis studies, and parallel, in-register β-sheet arrangement from previous solid-state NMR studies, explains the sequence selectivity, the cooperativity, and the apparent unidirectionality of Aβ fibril growth.
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Generation of reactive oxygen species by the mitochondrial electron transport chain

TL;DR: In this paper, it was shown that the major ROS-generating site in mitochondria is limited to the flavin mononucleotide group (FMN) of complex I through reversed electron transfer, not at the ubiquinone of complex III.
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Mechanism of Cellular 3-(4,5-Dimethylthiazol-2-yl)-2,5-Diphenyltetrazolium Bromide (MTT) Reduction

TL;DR: Results suggest that MTT is taken up by cells through endocytosis and that reduced MTT formazan accumulates in the endosomal/lysosomal compartment and is then transported to the cell surface through exocytotic.
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Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules

TL;DR: It is found that peptide and protein hormones in secretory granules of the endocrine system are stored in an amyloid-like cross–β-sheet–rich conformation, which means functional amyloids in the pituitary and other organs can contribute to normal cell and tissue physiology.