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pro vyhledávání: '"Olga Gorelenkova Miller"'
Autor:
Olga Gorelenkova Miller, Kyle S Cole, Corey C Emerson, Dharmaraja Allimuthu, Marcin Golczak, Phoebe L Stewart, Eranthie Weerapana, Drew J Adams, John J Mieyal
Publikováno v:
PLoS ONE, Vol 12, Iss 11, p e0187991 (2017)
Glutaredoxin (Grx1) is a ubiquitously expressed thiol-disulfide oxidoreductase that specifically catalyzes reduction of S-glutathionylated substrates. Grx1 is known to be a key regulator of pro-inflammatory signaling, and Grx1 silencing inhibits infl
Externí odkaz:
https://doaj.org/article/1946c27c3e7a4148add6193db46da8d3
Autor:
Markus Bachschmid, Olga Gorelenkova Miller, Sandra L. Siedlak, John J. Mieyal, Sirui Jiang, Xiongwei Zhu, Jessica B. Behring, Reiko Matsui
Publikováno v:
Antioxidants & Redox Signaling. 25:967-982
Neuroinflammation and redox dysfunction are recognized factors in Parkinson's disease (PD) pathogenesis, and diabetes is implicated as a potentially predisposing condition. Remarkably, upregulation of glutaredoxin-1 (Grx1) is implicated in regulation
Autor:
Amy L. Wilson-Delfosse, Shu G. Chen, Nicole M. Milkovic, John J. Mieyal, Mark A. Wilson, Pierce L. Curran, Kyonghwan Choe, Chen Yao, Ajit Ray, Olga Gorelenkova Miller, Vijayalakshmi Ravindranath, Marcin Golczak, Wenzhang Wang, William M. Johnson, Xiongwei Zhu, Jiusheng Lin
Publikováno v:
Biochemistry. 55:4519-4532
Parkinson's disease (PD) is the second most common neurodegenerative disease worldwide, caused by the degeneration of the dopaminergic neurons in the substantia nigra. Mutations in PARK7 (DJ-1) result in early onset autosomal recessive PD, and oxidat
Publikováno v:
Archives of Toxicology. 89:1439-1467
Posttranslational modifications of cysteine sulfhydryl (-SH) moieties, e.g., S-nitrosylation, S-glutathionylation, or S-sulfuration, play an important role in cellular response to oxidative stress. Reversible cysteine modifications alter protein func
Publikováno v:
Antioxidantsredox signaling. 30(10)
Significance: Glutaredoxin (Grx)1, an evolutionarily conserved and ubiquitous enzyme, regulates redox signal transduction and protein redox homeostasis by catalyzing reversible S-glutathionylation. Grx1 plays different roles in different cell types.
Publikováno v:
Archives of toxicology. 90(4)
Autor:
Marcin Golczak, Eranthie Weerapana, Dharmaraja Allimuthu, John J. Mieyal, Olga Gorelenkova Miller, Corey C. Emerson, Phoebe L. Stewart, Kyle S. Cole, Drew J. Adams
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 11, p e0187991 (2017)
PLoS ONE, Vol 12, Iss 11, p e0187991 (2017)
Glutaredoxin (Grx1) is a ubiquitously expressed thiol-disulfide oxidoreductase that specifically catalyzes reduction of S-glutathionylated substrates. Grx1 is known to be a key regulator of pro-inflammatory signaling, and Grx1 silencing inhibits infl