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Yasuo Okamoto

Researcher at Medical University of South Carolina

Publications -  11
Citations -  1030

Yasuo Okamoto is an academic researcher from Medical University of South Carolina. The author has contributed to research in topics: Saccharomyces cerevisiae & Ceramide. The author has an hindex of 11, co-authored 11 publications receiving 975 citations.

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Inhibition of Tumor Necrosis Factor-induced Cell Death in MCF7 by a Novel Inhibitor of Neutral Sphingomyelinase

TL;DR: GW4869 was able, in a dose-dependent manner, to significantly protect from cell death as measured by nuclear condensation, caspase activation, PARP degradation, and trypan blue uptake, therefore localizing N-SMase activation upstream of mitochondrial dysfunction.
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Identification of ISC1 (YER019w) as Inositol Phosphosphingolipid Phospholipase C inSaccharomyces cerevisiae

TL;DR: This study identifies the first enzyme involved in catabolism of complex sphingolipids in S. cerevisiae by identifyingISC1 (YER019w), which has homology to bacterial neutral sphingomyelinase (SMase), encodes IPS phospholipase C (IPS-PLC).
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Simulation and validation of modelled sphingolipid metabolism in Saccharomyces cerevisiae

TL;DR: Simulations of metabolic fluxes, enzyme deletion and the effects of inositol led to predictions that show significant concordance with experimental results generated post hoc, demonstrating that modelling now allows testable predictions as well as the design and evaluation of hypothetical 'thought experiments' that may generate new metabolomic approaches.
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Yeast sphingolipids: metabolism and biology.

TL;DR: This review focuses on the yeast sphingolipid metabolic pathway and its role in regulation of yeast biology and implications of the insights gained from yeast to mammalian cell regulation are discussed.
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Activation and localization of inositol phosphosphingolipid phospholipase C, Isc1p, to the mitochondria during growth of Saccharomyces cerevisiae.

TL;DR: It is revealed that the activity and localization of Isc1p are regulated in a growth-dependent manner and a novel mechanism for activation of IsC1p through localization to mitochondria is proposed, which suggests a role for Isc 1p-generated ceramides in optimal regulation of growth.