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Hiroshi Hasegawa

Researcher at University of Toronto

Publications -  14
Citations -  2547

Hiroshi Hasegawa is an academic researcher from University of Toronto. The author has contributed to research in topics: APH-1 & Presenilin. The author has an hindex of 12, co-authored 14 publications receiving 2447 citations. Previous affiliations of Hiroshi Hasegawa include Shiga University of Medical Science & Toronto Western Hospital.

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The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease

TL;DR: It is reported here that inherited variants in the SORL1 neuronal sorting receptor are associated with late-onset Alzheimer disease, and it is shown that SOR l1 directs trafficking of APP into recycling pathways and that when SORl1 is underexpressed, APP is sorted into Aβ-generating compartments.
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Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations.

TL;DR: Results suggest that PINK1 reduces the basal neuronal pro-apoptotic activity and protects neurons from staurosporine-induced apoptosis, and loss of this protective function may underlie the degeneration of nigral dopaminergic neurons in patients with Pink1 mutations.
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APH-1 interacts with mature and immature forms of presenilins and nicastrin and may play a role in maturation of presenilin.nicastrin complexes.

TL;DR: It is reported here that endogenous forms of APH-1 are predominantly expressed in intracellular membrane compartments, including the endoplasmic reticulum andcis-Golgi, and thatAPH-11 in particular may have a role in the initial assembly and maturation of presenilin·nicastrin complexes.
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Mature glycosylation and trafficking of nicastrin modulate its binding to presenilins.

TL;DR: It is reported here that nicastrin is most probably a type 1 transmembrane glycoprotein that is expressed at moderate levels in the brain and in cultured neurons and that presenilin-1 interacts preferentially with mature Nicastrin, suggesting that correct trafficking and co-localization of the presenILin complex components are essential for activity.