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Devin M. Wolfe

Researcher at Nathan Kline Institute for Psychiatric Research

Publications -  11
Citations -  1993

Devin M. Wolfe is an academic researcher from Nathan Kline Institute for Psychiatric Research. The author has contributed to research in topics: Autophagy & Lysosome. The author has an hindex of 8, co-authored 11 publications receiving 1770 citations. Previous affiliations of Devin M. Wolfe include University of Rochester.

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Journal ArticleDOI

Lysosomal Proteolysis and Autophagy Require Presenilin 1 and Are Disrupted by Alzheimer-Related PS1 Mutations

TL;DR: It is shown that macroautophagy requires the Alzheimer's disease-related protein presenilin-1 (PS1) for v-ATPase targeting to lysosomes, lysOSome acidification, and proteolysis during autophagy, which represents a basis for pathogenic protein accumulations and neuronal cell death in AD.
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Autophagy failure in Alzheimer's disease and the role of defective lysosomal acidification.

TL;DR: The most commonly used pH probes for sensitivity and localisation are evaluated, and LysoSensor yellow/blue‐dextran, among currently used probes, are identified as having the optimal profile of properties for measuring lysosomal pH.
Journal ArticleDOI

Presenilin 1 Maintains Lysosomal Ca2+ Homeostasis via TRPML1 by Regulating vATPase-Mediated Lysosome Acidification

TL;DR: The results indicate that vATPase deficiency in PS1 loss-of-function states causes lysosomal/autophagy deficits and contributes to abnormal cellular Ca(2+) homeostasis, thus linking two AD-related pathogenic processes through a common molecular mechanism.

TECHNICAL SPOTLIGHT Autophagy failure in Alzheimer's disease and the role of defective lysosomal acidification

TL;DR: In this article, the authors evaluated the most commonly used pH probes for sensitivity and localisation, and identified LysoSensor yellow/blue-dextran, among currently used probes, as having the optimal profile of properties for measuring lysosomal pH.
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Cd2+, Mn2+, Ni2+ and Se2+ toxicity to Saccharomyces cerevisiae lacking YPK9p the orthologue of human ATP13A2.

TL;DR: The Saccharomyces cerevisiae gene YPK9p encodes a putative integral membrane protein which is 58% similar and 38% identical in amino acid sequence to the human lysosomal P(5B) ATPase ATP13A2 as discussed by the authors.