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Masato Umeda

Researcher at Kyoto University

Publications -  40
Citations -  3257

Masato Umeda is an academic researcher from Kyoto University. The author has contributed to research in topics: Phosphatidylethanolamine & Cell membrane. The author has an hindex of 24, co-authored 40 publications receiving 2824 citations. Previous affiliations of Masato Umeda include Institute of Medical Science & Duke University.

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The ratio of phosphatidylcholine to phosphatidylethanolamine influences membrane integrity and steatohepatitis.

TL;DR: Manipulation of PC/PE levels suggests that this ratio is a key regulator of cell membrane integrity and plays a role in the progression of steatosis into steatohepatitis and has clinical implications as patients with nonalcoholic steato hepatitis have a decreased ratio of PC to PE compared to control livers.
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Upregulated function of mitochondria‐associated ER membranes in Alzheimer disease

TL;DR: It is proposed that upregulated MAM function at the ER–mitochondrial interface, and increased cross‐talk between these two organelles, may play a hitherto unrecognized role in the pathogenesis of AD.
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An Essential Role for a Membrane Lipid in Cytokinesis: Regulation of Contractile Ring Disassembly by Redistribution of Phosphatidylethanolamine

TL;DR: These findings provide the first evidence that PE is required for completion of cytokinesis in mammalian cells, and suggest that redistribution of PE on the cleavage furrow may contribute to regulation of contractile ring disassembly.
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Failure of the Expression of Phospholipid Hydroperoxide Glutathione Peroxidase in the Spermatozoa of Human Infertile Males

TL;DR: The results suggest that failure of the expression of mitochondrial PHGPx in spermatozoa might be one of the causes of oligoasthenozoospermia in infertile men.
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In vivo and in vitro reconstitution of Atg8 conjugation essential for autophagy.

TL;DR: In vitro Atg8p-PE reconstitution system established will provide a powerful system for further understanding the precise role of lipidation and interaction of two ubiquitin-like systems essential for autophagy.