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Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family

dc.contributor.authorFisher, Aron B.*
dc.date.accessioned2021-02-11T22:37:00Z
dc.date.available2021-02-11T22:37:00Z
dc.date.issued2019*
dc.date.submitted2019-06-26 08:44:06*
dc.identifier33640*
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/56030
dc.description.abstractThe 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 several unique and crucial activities. These include the ability to reduce phospholipid hydroperoxides, phospholipase A2 activity, and an acyl transferase activity that is important in phospholipid remodeling. This book describes the available models for investigating the unique functions of PRDX6 and its role in normal physiological function, as well its roles in the pathophysiology of diseases including cancer, diseases of the eye, and male fertility.*
dc.languageEnglish*
dc.subjectR5-920*
dc.subjectRM1-950*
dc.subject.classificationthema EDItEUR::M Medicine and Nursingen_US
dc.subject.othern/a*
dc.subject.otherNADPH (nicotinamide adenine dinucleotide phosphate) oxidase*
dc.subject.othersperm capacitation*
dc.subject.otherphospholipid hydroperoxide*
dc.subject.othercornea*
dc.subject.otherperoxidase*
dc.subject.otherphospholipase A2*
dc.subject.other1-Cys Prdx*
dc.subject.otherknock-in mouse*
dc.subject.otherdrug delivery*
dc.subject.otherantioxidant activity*
dc.subject.othersulfinic acid*
dc.subject.otherradioprotection*
dc.subject.otherspermatozoa*
dc.subject.otherperoxiredoxin 6*
dc.subject.othermass spectroscopic analysis*
dc.subject.otherknockout mouse*
dc.subject.otherphospholipase A2 activity*
dc.subject.otherliposomes*
dc.subject.othermitochondrial membrane potential*
dc.subject.otherlipid peroxidation*
dc.subject.otherPLA2 activity*
dc.subject.otherionizing radiation*
dc.subject.otherglutathione peroxidase*
dc.subject.otherPeroxiredoxin*
dc.subject.otherPrdx6 structure*
dc.subject.othermembrane repair*
dc.subject.othersubstrate binding*
dc.subject.otherinflammation*
dc.subject.otherreactive oxygen species*
dc.subject.otherPrdx6*
dc.subject.othersulfonic/sulfinic acid*
dc.subject.otherFuchs’ endothelial corneal dystrophy*
dc.subject.otherendothelium*
dc.subject.otherfertilization*
dc.subject.otherperoxidatic cysteine*
dc.subject.otherthioredoxin fold*
dc.subject.otherredox balance*
dc.subject.othersurfactant protein A*
dc.subject.otherdiabetes*
dc.subject.otheroxidative stress*
dc.titlePeroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family*
dc.typebook
oapen.identifier.doi10.3390/books978-3-03897-935-7*
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0*
oapen.relation.isbn9783038979340*
oapen.relation.isbn9783038979357*
oapen.pages152*
oapen.edition1st*


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