Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family
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...
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| Aineistotyyppi: | Online |
| Kieli: | englanti |
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MDPI - Multidisciplinary Digital Publishing Institute
2021
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| Linkit: | 33640 |
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| _version_ | 1869517287270121472 |
|---|---|
| author | Fisher, Aron B. |
| author_browse | Fisher, Aron B. |
| author_facet | Fisher, Aron B. |
| author_sort | Fisher, Aron B. |
| collection | Directory of Open Access Books |
| description | 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 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. |
| format | Online |
| id | doab-20.500.12854ir-56030 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2021 |
| publishDateRange | 2021 |
| publishDateSort | 2021 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | ojs |
| spelling | doab-20.500.12854ir-560302024-03-30T23:22:04Z Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family Fisher, Aron B. R5-920 RM1-950 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 thema EDItEUR::M Medicine and Nursing 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 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. 2021-02-11T22:37:00Z 2021-02-11T22:37:00Z 2019-06-26 08:44:06 2019 book 33640 9783038979340 9783038979357 https://directory.doabooks.org/handle/20.500.12854/56030 eng image/jpeg Attribution-NonCommercial-NoDerivatives 4.0 International https://mdpi.com/books/pdfview/book/1293 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-03897-935-7 10.3390/books978-3-03897-935-7 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783038979340 9783038979357 152 open access |
| spellingShingle | R5-920 RM1-950 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 thema EDItEUR::M Medicine and Nursing Fisher, Aron B. Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family |
| title | Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family |
| title_full | Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family |
| title_fullStr | Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family |
| title_full_unstemmed | Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family |
| title_short | Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family |
| title_sort | peroxiredoxin 6 as a unique member of the peroxiredoxin family |
| topic | R5-920 RM1-950 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 thema EDItEUR::M Medicine and Nursing |
| topic_facet | R5-920 RM1-950 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 thema EDItEUR::M Medicine and Nursing |
| url | 33640 |
| work_keys_str_mv | AT fisheraronb peroxiredoxin6asauniquememberoftheperoxiredoxinfamily |