- Arabidopsis cotyledon chloroplast biogenesis factor CYO1 uses glutathione as an electron donor and interacts with PSI (A1 and A2) and PSII (CP43 and CP47) subunits.
- Muranaka A, Watanabe S, Sakamoto A, Shimada H.SourceDepartment of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8526, Japan.
- Journal of plant physiology.J Plant Physiol.2012 Aug 15;169(12):1212-5. Epub 2012 May 7.
- CYO1 is required for thylakoid biogenesis in cotyledons of Arabidopsis thaliana. To elucidate the enzymatic characteristics of CYO1, we analyzed the protein disulfide isomerase (PDI) activity of CYO1 using dieosin glutathione disulfide (Di-E-GSSG) as a substrate. The reductase activity of CYO1 incre
- PMID 22572242
- Oxidation of 2-cys peroxiredoxins in human endothelial cells by hydrogen peroxide, hypochlorous Acid, and chloramines.
- Stacey MM, Vissers MC, Winterbourn CC.SourceDepartment of Pathology, University of Otago , Christchurch, Christchurch, New Zealand .
- Antioxidants & redox signaling.Antioxid Redox Signal.2012 Aug 1;17(3):411-21. Epub 2012 Mar 2.
- Abstract Aims: Reactive oxygen species released from neutrophils during vascular inflammation could contribute to endothelial dysfunction seen in diseases such as atherosclerosis. Activated neutrophils generate hydrogen peroxide (H(2)O(2)) and hypochlorous acid (HOCl), as well as chloramines that
- PMID 22229717
- Production of keratinolytic enzyme by an indigenous feather-degrading strain Bacillus cereus Wu2(ENVIRONMENTAL BIOTECHNOLOGY)
- Lo Wei-Hsun,Too Jui-Rze,Wu Jane-Yii
- Journal of bioscience and bioengineering 114(6), 640-647, 2012-12-00
- … The experimental results indicated that the extra carbon sources (glucose, fructose, starch, sucrose, or lactose) could act as a catabolite repressor to the enzyme secretion or keratinolytic activity when keratinous substrates were employed as protein sources. … cereus Wu2 possessed disulfide reductase activity along with keratinolytic activity. …
- NAID 110009578159
- Structural Basis of an ERAD Pathway Mediated by the ER-Resident Protein Disulfide Reductase ERdj5
- Hagiwara Masatoshi,Maegawa Ken-ichi,Suzuki Mamoru,Ushioda Ryo,Araki Kazutaka,Matsumoto Yushi,Hoseki Jun,Nagata Kazuhiro,Inaba Kenji,萩原 誠智,前川 憲一,鈴木 守,潮田 亮,新木 和孝,松本 悠史,寳関 淳,永田 和宏,稲葉 謙次,ハギワラ マサトシ,マエガワ ケンイチ,スズキ マモル,ウシオダ リョウ,アラキ カズタカ,マツモト ユウシ,ホウセキ ジュン,ナガタ カズヒロ,イナバ ケンジ
- Molecular Cell 41(4), 432-444, 2011-02-18
- … ERdj5 was recently discovered to be a key ER-resident PDI family member protein that acceleratesERAD by reducing incorrect disulfide bonds inmisfolded glycoproteins recognized by EDEM1. …
- NAID 120003836694
- Increased Nitrosoglutathione Reductase Activity in Hypoxic Pulmonary Hypertension in Mice
- Wu Xiling,Du Lizhong,Xu Xuefeng [他],Tan Linhua,Li Ruyi
- Journal of Pharmacological Sciences 113(1), 32-40, 2010
- … Recent studies have shown that S-nitrosoglutathione (GSNO) reductase (GSNOR) catalyzes the degradation of GSNO and indirectly regulates the level of RSNO in vivo. … The protein expression of GSNOR increased significantly in the lung tissue after 7 days of hypoxic exposure and its enzymatic activities also increased. … Both the ratios of glutathione to glutathione disulfide and nitrate to nitrite were significantly lower in the hypoxic groups than in the normoxic controls. …
- NAID 130000253399