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Yasuo Ido
Researcher at Boston University
Publications - 76
Citations - 10032
Yasuo Ido is an academic researcher from Boston University. The author has contributed to research in topics: AMPK & AMP-activated protein kinase. The author has an hindex of 43, co-authored 69 publications receiving 9356 citations. Previous affiliations of Yasuo Ido include University of Texas Health Science Center at Houston & Boston Medical Center.
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Journal ArticleDOI
Hyperglycemic Pseudohypoxia and Diabetic Complications
Joseph R. Williamson,Katherine Chang,Myrto Frangos,Khalid S Hasan,Yasuo Ido,Takahiko Kawamura,Jens R. Nyengaard,Maria van Den Enden,Charles Kilo,Ronald G. Tilton +9 more
TL;DR: Several lines of evidence support the likelihood that the increased cytosolic ratio of free NADH/NAD+ caused by hyperglycemia, referred to as pseudohypoxia, is a characteristic feature of poorly controlled diabetes that mimics the effects of true hypoxia on vascular and neural function and plays an important role in the pathogenesis of diabetic complications.
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AMPK and SIRT1: a long-standing partnership?
TL;DR: The evidence that AMPK and SIRT1 both regulate each other and share many common target molecules is examined and the possibility that their dysregulation predisposes to disorders such as type 2 diabetes and atherosclerotic cardiovascular disease is discussed.
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SIRT1 Regulates Hepatocyte Lipid Metabolism through Activating AMP-activated Protein Kinase *
Xiuyun Hou,Shanqin Xu,Karlene A. Maitland-Toolan,Kaori Sato,Bingbing Jiang,Yasuo Ido,Fan Lan,Kenneth Walsh,Michel Wierzbicki,Tony Verbeuren,Richard A. Cohen,Mengwei Zang +11 more
TL;DR: It is shown that polyphenols, including resveratrol and the synthetic polyphenol S17834, increase SIRT1 deacetylase activity, LKB1 phosphorylation at Ser428, and AMPK activity, which suggests that Sirt1 functions as a novel upstream regulator for L KB1/AMPK signaling and plays an essential role in the regulation of hepatocyte lipid metabolism.
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SIRT1 Modulation of the Acetylation Status, Cytosolic Localization, and Activity of LKB1 POSSIBLE ROLE IN AMP-ACTIVATED PROTEIN KINASE ACTIVATION
TL;DR: The results suggest that LKB1 deacetylation is regulated by SIRT1 and that this in turn influences its intracellular localization, association with STRAD, kinase activity, and ability to activate AMPK.
Journal ArticleDOI
Energy metabolism in uncoupling protein 3 gene knockout mice.
Antonio Vidal-Puig,Danica Grujic,Chen-Yu Zhang,Thilo Hagen,Olivier Boss,Yasuo Ido,Alicja Szczepanik,Jennifer Wade,Vamsi K. Mootha,Ronald N. Cortright,Deborah M. Muoio,Bradford B. Lowell +11 more
TL;DR: It is demonstrated that UCP3 has uncoupling activity and that its absence may lead to increased production of ROS, and the consequence of increased mitochondrial coupling in U CP3 KO mice on metabolism and the possible role of yet unidentified compensatory mechanisms, remains to be determined.