Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family

• Main Author: Fisher, Aron B. (auth)
• Format: Electronic Book Chapter
• Language: English
• Published: MDPI - Multidisciplinary Digital Publishing Institute 2019
• Subjects: Medicine; n/a; NADPH (nicotinamide adenine dinucleotide phosphate) oxidase; sperm capacitation; phospholipid hydroperoxide; cornea; peroxidase; phospholipase A2; 1-Cys Prdx; knock-in mouse; drug delivery; antioxidant activity; sulfinic acid; radioprotection; spermatozoa; peroxiredoxin 6; mass spectroscopic analysis; knockout mouse; phospholipase A2 activity; liposomes; mitochondrial membrane potential; lipid peroxidation; PLA2 activity; ionizing radiation; glutathione peroxidase; Peroxiredoxin; Prdx6 structure; membrane repair; substrate binding; inflammation; reactive oxygen species; Prdx6; sulfonic/sulfinic acid; Fuchs' endothelial corneal dystrophy; endothelium; fertilization; peroxidatic cysteine; thioredoxin fold; redox balance; surfactant protein A; diabetes; oxidative stress
• Online Access: DOAB: download the publication; DOAB: description of the publication

The peroxiredoxin family was discovered approximately 30 years ago and is now recognized as one of the most important families of enzymes related to antioxidant defense and cellular signaling. Peroxiredoxin 6 shares the basic enzymatic functions that characterize this family, but also exhibits sever...