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Austin J. Yang
Researcher at University of Maryland, Baltimore
Publications - 54
Citations - 5894
Austin J. Yang is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Proteomics & Neurodegeneration. The author has an hindex of 28, co-authored 53 publications receiving 5470 citations. Previous affiliations of Austin J. Yang include New York University & University of Maryland Marlene and Stewart Greenebaum Cancer Center.
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Journal ArticleDOI
A specific amyloid-|[beta]| protein assembly in the brain impairs memory
Sylvain Lesné,Ming Teng Koh,Linda Kotilinek,Rakez Kayed,Charles G. Glabe,Austin J. Yang,Michela Gallagher,Karen H. Ashe +7 more
TL;DR: It is found that memory deficits in middle-aged Tg2576 mice are caused by the extracellular accumulation of a 56-kDa soluble amyloid-β assembly, which is proposed to be Aβ*56 (Aβ star 56), which may contribute to cognitive deficits associated with Alzheimer's disease.
Journal ArticleDOI
Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer's disease ameliorates amyloid pathologies and memory deficits.
Dun-Sheng Yang,Dun-Sheng Yang,Philip Stavrides,Panaiyur S. Mohan,Panaiyur S. Mohan,Susmita Kaushik,Asok Kumar,Asok Kumar,Masuo Ohno,Masuo Ohno,Stephen D. Schmidt,Daniel W. Wesson,Daniel W. Wesson,Urmi Bandyopadhyay,Ying Jiang,Ying Jiang,Monika Pawlik,Corrinne M. Peterhoff,Austin J. Yang,Donald A. Wilson,Donald A. Wilson,Peter St George-Hyslop,David Westaway,Paul M. Mathews,Paul M. Mathews,Efrat Levy,Efrat Levy,Ana Maria Cuervo,Ralph A. Nixon,Ralph A. Nixon +29 more
TL;DR: The findings support the pathogenic significance of autophagic-lysosomal dysfunction in Alzheimer's disease and indicate the potential value of restoring normal autophagy as an innovative therapeutic strategy for Alzheimer’s disease.
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Loss of endosomal/lysosomal membrane impermeability is an early event in amyloid Abeta1-42 pathogenesis.
TL;DR: The results suggest that the loss of lysosomal membrane impermeability may be an early event in Aβ pathogenesis, and provide an explanation for the miscompartmentalization of extracellular and cytoplasmic components observed in Alzheimer's disease (AD).
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Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation
TL;DR: It was found that soluble PHF-Tau is ubiquitinated at its microtubule-binding domain at residues Lys-254, Lys-311, and Lys-353, suggesting that ubiquitination of PHF -Tau may be an earlier pathological event than previously thought and that Ubiquitination could play a regulatory role in modulating the integrity of microtubules during the course of AD.
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Complement component C1q modulates the phagocytosis of Abeta by microglia.
Scott D. Webster,Austin J. Yang,Larry Margol,William Garzon-Rodriguez,Charles G. Glabe,Andrea J. Tenner +5 more
TL;DR: Mechanisms which interfere with the binding of C1q to Abeta may be of therapeutic value both through inhibition of the inflammatory events resulting from complement activation and via altered access of Abeta sites necessary for ingestion by microglia.