Okumura M - Search Results

1

Visualization of structural dynamics of protein disulfide isomerase enzymes in catalysis of oxidative folding and reductive unfolding.

Okumura M, Noi K, Inaba K. Okumura M, et al. Curr Opin Struct Biol. 2021 Feb;66:49-57. doi: 10.1016/j.sbi.2020.10.004. Epub 2020 Nov 8. Curr Opin Struct Biol. 2021. PMID: 33176263 Review.

2

Crystallization and preliminary crystallographic analysis of the complex between triiodothyronine and the bb' fragment of rat protein disulfide isomerase.

Hashimoto S, Ito L, Okumura M, Shibano T, Nawata M, Kumasaka T, Yamaguchi H, Imaoka S. Hashimoto S, et al. Among authors: okumura m. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):476-8. doi: 10.1107/S1744309112007439. Epub 2012 Mar 28. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012. PMID: 22505424 Free PMC article.

3

Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding.

Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. Sato Y, et al. Among authors: okumura m. Sci Rep. 2013;3:2456. doi: 10.1038/srep02456. Sci Rep. 2013. PMID: 23949117 Free PMC article.

4

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.

Kojima R, Okumura M, Masui S, Kanemura S, Inoue M, Saiki M, Yamaguchi H, Hikima T, Suzuki M, Akiyama S, Inaba K. Kojima R, et al. Among authors: okumura m. Structure. 2014 Mar 4;22(3):431-43. doi: 10.1016/j.str.2013.12.013. Epub 2014 Jan 23. Structure. 2014. PMID: 24462249 Free article.

5

Chemical methods for producing disulfide bonds in peptides and proteins to study folding regulation.

Okumura M, Shimamoto S, Hidaka Y. Okumura M, et al. Curr Protoc Protein Sci. 2014 Apr 1;76:28.7.1-28.7.13. doi: 10.1002/0471140864.ps2807s76. Curr Protoc Protein Sci. 2014. PMID: 24692016 Review.

6

Inhibition of the functional interplay between endoplasmic reticulum (ER) oxidoreduclin-1α (Ero1α) and protein-disulfide isomerase (PDI) by the endocrine disruptor bisphenol A.

Okumura M, Kadokura H, Hashimoto S, Yutani K, Kanemura S, Hikima T, Hidaka Y, Ito L, Shiba K, Masui S, Imai D, Imaoka S, Yamaguchi H, Inaba K. Okumura M, et al. J Biol Chem. 2014 Sep 26;289(39):27004-27018. doi: 10.1074/jbc.M114.564104. Epub 2014 Aug 13. J Biol Chem. 2014. PMID: 25122773 Free PMC article.

7

A PDI-catalyzed thiol-disulfide switch regulates the production of hydrogen peroxide by human Ero1.

Ramming T, Okumura M, Kanemura S, Baday S, Birk J, Moes S, Spiess M, Jenö P, Bernèche S, Inaba K, Appenzeller-Herzog C. Ramming T, et al. Among authors: okumura m. Free Radic Biol Med. 2015 Jun;83:361-72. doi: 10.1016/j.freeradbiomed.2015.02.011. Epub 2015 Feb 17. Free Radic Biol Med. 2015. PMID: 25697776

8

Structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum.

Okumura M, Kadokura H, Inaba K. Okumura M, et al. Free Radic Biol Med. 2015 Jun;83:314-22. doi: 10.1016/j.freeradbiomed.2015.02.010. Epub 2015 Feb 17. Free Radic Biol Med. 2015. PMID: 25697777 Review.

9

One-Dimensional Sliding of p53 Along DNA Is Accelerated in the Presence of Ca(2+) or Mg(2+) at Millimolar Concentrations.

Murata A, Ito Y, Kashima R, Kanbayashi S, Nanatani K, Igarashi C, Okumura M, Inaba K, Tokino T, Takahashi S, Kamagata K. Murata A, et al. Among authors: okumura m. J Mol Biol. 2015 Aug 14;427(16):2663-78. doi: 10.1016/j.jmb.2015.06.016. Epub 2015 Jul 2. J Mol Biol. 2015. PMID: 26143716

10

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover.

Ramming T, Kanemura S, Okumura M, Inaba K, Appenzeller-Herzog C. Ramming T, et al. Among authors: okumura m. Redox Biol. 2016 Apr;7:14-20. doi: 10.1016/j.redox.2015.11.004. Epub 2015 Nov 14. Redox Biol. 2016. PMID: 26609561 Free PMC article.

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