Udagawa O - Search Results

1

Mitochondrial fission factor Drp1 maintains oocyte quality via dynamic rearrangement of multiple organelles.

Udagawa O, Ishihara T, Maeda M, Matsunaga Y, Tsukamoto S, Kawano N, Miyado K, Shitara H, Yokota S, Nomura M, Mihara K, Mizushima N, Ishihara N. Udagawa O, et al. Curr Biol. 2014 Oct 20;24(20):2451-8. doi: 10.1016/j.cub.2014.08.060. Epub 2014 Sep 25. Curr Biol. 2014. PMID: 25264261 Free article.

2

Mitochondrial dynamics and interorganellar communication in the development and dysmorphism of mammalian oocytes.

Udagawa O, Ishihara N. Udagawa O, et al. J Biochem. 2020 Mar 1;167(3):257-266. doi: 10.1093/jb/mvz093. J Biochem. 2020. PMID: 31816050 Review.

3

Promyelocytic leukemia nuclear body-like structures can assemble in mouse oocytes.

Udagawa O, Kato-Udagawa A, Hirano S. Udagawa O, et al. Biol Open. 2022 Jun 15;11(6):bio059130. doi: 10.1242/bio.059130. Epub 2022 Jun 6. Biol Open. 2022. PMID: 35579421 Free PMC article.

4

LPIAT1 regulates arachidonic acid content in phosphatidylinositol and is required for cortical lamination in mice.

Lee HC, Inoue T, Sasaki J, Kubo T, Matsuda S, Nakasaki Y, Hattori M, Tanaka F, Udagawa O, Kono N, Itoh T, Ogiso H, Taguchi R, Arita M, Sasaki T, Arai H. Lee HC, et al. Among authors: udagawa o. Mol Biol Cell. 2012 Dec;23(24):4689-700. doi: 10.1091/mbc.E12-09-0673. Epub 2012 Oct 24. Mol Biol Cell. 2012. PMID: 23097495 Free PMC article.

5

Oligo-astheno-teratozoospermia in mice lacking ORP4, a sterol-binding protein in the OSBP-related protein family.

Udagawa O, Ito C, Ogonuki N, Sato H, Lee S, Tripvanuntakul P, Ichi I, Uchida Y, Nishimura T, Murakami M, Ogura A, Inoue T, Toshimori K, Arai H. Udagawa O, et al. Genes Cells. 2014 Jan;19(1):13-27. doi: 10.1111/gtc.12105. Epub 2013 Nov 19. Genes Cells. 2014. PMID: 24245814 Free article.

6

Effects of diesel exhaust-derived secondary organic aerosol (SOA) on oocytes: Potential risks to meiotic maturation.

Udagawa O, Furuyama A, Imai K, Fujitani Y, Hirano S. Udagawa O, et al. Reprod Toxicol. 2018 Jan;75:56-64. doi: 10.1016/j.reprotox.2017.11.006. Epub 2017 Nov 20. Reprod Toxicol. 2018. PMID: 29158200

7

Solubility shift and SUMOylaltion of promyelocytic leukemia (PML) protein in response to arsenic(III) and fate of the SUMOylated PML.

Hirano S, Tadano M, Kobayashi Y, Udagawa O, Kato A. Hirano S, et al. Among authors: udagawa o. Toxicol Appl Pharmacol. 2015 Sep 15;287(3):191-201. doi: 10.1016/j.taap.2015.05.018. Epub 2015 Jun 3. Toxicol Appl Pharmacol. 2015. PMID: 26049103

8

Solubility changes of promyelocytic leukemia (PML) and SUMO monomers and dynamics of PML nuclear body proteins in arsenite-treated cells.

Hirano S, Udagawa O, Kobayashi Y, Kato A. Hirano S, et al. Among authors: udagawa o. Toxicol Appl Pharmacol. 2018 Dec 1;360:150-159. doi: 10.1016/j.taap.2018.10.001. Epub 2018 Oct 5. Toxicol Appl Pharmacol. 2018. PMID: 30292834

9

SUMOylation regulates the number and size of promyelocytic leukemia-nuclear bodies (PML-NBs) and arsenic perturbs SUMO dynamics on PML by insolubilizing PML in THP-1 cells.

Hirano S, Udagawa O. Hirano S, et al. Among authors: udagawa o. Arch Toxicol. 2022 Feb;96(2):545-558. doi: 10.1007/s00204-021-03195-w. Epub 2022 Jan 10. Arch Toxicol. 2022. PMID: 35001170

10

Effects of arsenic on the topology and solubility of promyelocytic leukemia (PML)-nuclear bodies.

Hirano S, Udagawa O. Hirano S, et al. Among authors: udagawa o. PLoS One. 2022 May 20;17(5):e0268835. doi: 10.1371/journal.pone.0268835. eCollection 2022. PLoS One. 2022. PMID: 35594310 Free PMC article.

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