Results 111 to 120 of about 1,937 (151)

Research progress on Nrf2 intervention in the treatment of diabetic retinopathy. [PDF]

Front Endocrinol (Lausanne)
Yang Y, Zou H.
europepmc   +1 more source

Molecular Mechanisms and Therapeutic Targets for Pain Following Osteoporotic Vertebral Fractures. [PDF]

J Pain Res
Zhou H, Wu K.
europepmc   +1 more source

From Carcinogenesis to Drug Resistance: The Multifaceted Role of Oxidative Stress in Head and Neck Cancer. [PDF]

Cancers (Basel)
Bani-Ahmad E, Dass J, Dass CR.
europepmc   +1 more source

Heterochromatin epimutations impose mitochondrial dysfunction to confer antifungal resistance. [PDF]

EMBO J
Fellas A, Pidoux AL, Tong P, Hewes HH, Wallace EC, Allshire RC.   +5 more
europepmc   +1 more source

Sulfiredoxin: a potential therapeutic agent? [PDF]

Biomedicine and Pharmacotherapy, 2005
The importance of antioxidants in maintaining homeostasis has long been accepted and includes antioxidant proteins such as, peroxiredoxin (Prx), superoxide dismutase and glutathione S transferases. Sulfiredoxin (Srx) is a recently identified antioxidant protein with a role in signaling through catalytic reduction of oxidative modifications.
Victoria J Findlay
exaly   +3 more sources

Transcriptional Regulation of the AP-1 and Nrf2 Target Gene Sulfiredoxin [PDF]

Molecules and Cells, 2009
"Two-cysteine" peroxiredoxins are antioxidant enzymes that exert a cytoprotective effect in many models of oxidative stress. However, under highly oxidizing conditions they can be inactivated through hyperoxidation of their peroxidatic active site cysteine residue. Sulfiredoxin can reverse this hyperoxidation, thus reactivating peroxiredoxins.
Francesc X Soriano, Michael B Sporn, Thomas H Gillingwater   +2 more
exaly   +3 more sources

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Reversal of 2-Cys peroxiredoxin oligomerization by sulfiredoxin

Biochemical and Biophysical Research Communications, 2013
Hydrogen peroxide (H(2)O(2)) regulates the structure and function of 2-Cys peroxiredoxins (Prxs). Upon oxidation by excess H(2)O(2), Prxs become overoxidized to a sulfinic acid of its peroxidatic cysteine residue, resulting in a structural change from a small oligomer with peroxidase function to a large oligomer with chaperone function.
Jeong Chan Moon, Sang Yeol Lee, Ho Hee Jang   +2 more
exaly   +6 more sources