T
Takashi Umehara
Researcher at National Presto Industries
Publications - 107
Citations - 3921
Takashi Umehara is an academic researcher from National Presto Industries. The author has contributed to research in topics: Histone & Histone H4. The author has an hindex of 32, co-authored 90 publications receiving 3358 citations. Previous affiliations of Takashi Umehara include Centre for Life & University of Tokyo.
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Chromosomal gradient of histone acetylation established by Sas2p and Sir2p functions as a shield against gene silencing.
TL;DR: There is a gradient of acetylation of histone H4 at lysine 16 (H4–Lys16) along a yeast chromosome; this gradient ranges from a hypoacetylated state in regions near the telomere to a hyperacetylation state in more distant regions.
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Genome-wide expression analysis of mouse liver reveals CLOCK-regulated circadian output genes.
Katsutaka Oishi,Koyomi Miyazaki,Koji Kadota,Reiko Kikuno,Takahiro Nagase,G Atsumi,Naoki Ohkura,Takashi Azama,Miho Mesaki,Shima Yukimasa,Hisato Kobayashi,Chisato Iitaka,Chisato Iitaka,Takashi Umehara,Masami Horikoshi,Takashi Kudo,Yoshihisa Shimizu,Masahiko Yano,Morito Monden,Kazuhiko Machida,Juzo Matsuda,Shuichi Horie,Takeshi Todo,Norio Ishida,Norio Ishida,Norio Ishida +25 more
TL;DR: The results showed that CLOCK and CRY proteins are involved in the transcriptional regulation of many circadian output genes in the mouse liver and appears to be involved in various physiological functions such as cell cycle, lipid metabolism, immune functions, and proteolysis in peripheral tissues.
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Structurally Designed trans-2-Phenylcyclopropylamine Derivatives Potently Inhibit Histone Demethylase LSD1/KDM1,,§
TL;DR: Several candidate compounds to inhibit LSD1 are designed and synthesized, based on the structures of LSD1 and monoamine oxidase B (MAO-B), in complex with an antidepressant tranylcypromine (2-PCPA) derivative, potential pharmaceutical candidates for cancer or latent virus infection.
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FAD-dependent lysine-specific demethylase-1 regulates cellular energy expenditure
Shinjiro Hino,Akihisa Sakamoto,Katsuya Nagaoka,Kotaro Anan,Y. J. Wang,Shinya Mimasu,Takashi Umehara,Shigeyuki Yokoyama,Ken-ichiro Kosai,Mitsuyoshi Nakao +9 more
TL;DR: It is found that the loss of LSD1 function, either by short interfering RNA or by selective inhibitors in adipocytes, induces a number of regulators of energy expenditure and mitochondrial metabolism such as PPARγ coactivator-1α resulting in the activation of mitochondrial respiration.
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Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25 A.
TL;DR: Results imply that the LSD1-tranylcypromine complex is not completely composed of the five-membered adduct, but partially contains an intermediate, such as the N(5) adduct.