Taisuke Tomita

The University of Tokyo, Bunkyō-ku, Tōkyō-to, Japan 
Alzheimer's disease
"Taisuke Tomita"
Mean distance: 18.14 (cluster 31)
Cross-listing: Alzheimer's Tree

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Futai E, Kawasaki H, Sato S, et al. (2023) A Metalloproteinase Cocktail from the Venom of Cleaves Amyloid Beta Peptides at the α-Cleavage Site. Toxins. 15
Tomizawa I, Chiu YW, Hori Y, et al. (2023) [Identification of novel regulators involved in AD pathogenesis using the CRISPR-Cas9 system]. Nihon Yakurigaku Zasshi. Folia Pharmacologica Japonica. 158: 21-25
Kaneshiro N, Komai M, Imaoka R, et al. (2022) Lipid flippase dysfunction as a therapeutic target for endosomal anomalies in Alzheimer's disease. Iscience. 25: 103869
Islam S, Sun Y, Gao Y, et al. (2022) Presenilin is essential for ApoE secretion, a novel role of presenilin involved in Alzheimer's disease pathogenesis. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience
Cai T, Tomita T. (2021) Sequential conformational changes in transmembrane domains of presenilin 1 in Aβ42 downregulation. Journal of Biochemistry
Chiu YW, Hori Y, Ebinuma I, et al. (2020) Identification of calcium and integrin-binding protein 1 as a novel regulator of production of amyloid β peptide using CRISPR/Cas9-based screening system. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology
Cai T, Tomita T. (2020) Structure-activity relationship of presenilin in γ-secretase-mediated intramembrane cleavage. Seminars in Cell & Developmental Biology
Cai T, Hatano A, Kanatsu K, et al. (2019) Histidine 131 in presenilin 1 is the pH-sensitive residue that causes the increase in Aβ42 level in acidic pH. Journal of Biochemistry
Cai T, Morishima K, Takagi-Niidome S, et al. (2019) Conformational dynamics of transmembrane domain 3 of presenilin 1 is associated with the trimming activity of γ-secretase. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience
Furusawa K, Takasugi T, Chiu YW, et al. (2019) CD2-associated protein (CD2AP) overexpression accelerates amyloid precursor protein (APP) transfer from early endosomes to the lysosomal degradation pathway. The Journal of Biological Chemistry
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