LEADER 00787nam a22002291i 4500 001 991004300434007536 005 20231218124732.0 008 181223m18681955it |||||||||||||||||mul d 040 $aBibl. Interfacoltà T. Pellegrino$bita 082 04$a945.511 100 1 $aCompagni, Dino$0191760 245 10$aCronaca fiorentina :$b1280-1312 /$cdi Dino Compagni ; preceduta da un discorso di Atto Vannucci 250 $a4. ed. 260 $aMilano :$bM. Guigoni,$c1868 300 $a133 p. ;$c16 cm 490 0 $aBiblioteca delle famiglie ;$v52 500 $aNr. della collana su dorso della cop. editoriale orig. 650 4$aFirenze$xStoria$y1280-1312$xFonti documentarie 700 1 $aVannucci, Atto 912 $a991004300434007536 996 $aCronaca fiorentina$91115378 997 $aUNISALENTO LEADER 03445nam 22009013a 450 001 9910346679603321 005 20250203235434.0 010 $a9783038979357 010 $a303897935X 024 8 $a10.3390/books978-3-03897-935-7 035 $a(CKB)4920000000094871 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/56030 035 $a(ScCtBLL)3d38fb3f-8d5a-47ab-86f4-c2f83d44618b 035 $a(OCoLC)1117907930 035 $a(oapen)doab56030 035 $a(EXLCZ)994920000000094871 100 $a20250203i20192019 uu 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$aPeroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family$fAron B. Fisher 210 $cMDPI - Multidisciplinary Digital Publishing Institute$d2019 210 1$aBasel, Switzerland :$cMDPI,$d2019. 215 $a1 electronic resource (152 p.) 311 08$a9783038979340 311 08$a3038979341 330 $aThe 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. 606 $aMedicine$2bicssc 610 $aNADPH (nicotinamide adenine dinucleotide phosphate) oxidase 610 $asperm capacitation 610 $aphospholipid hydroperoxide 610 $acornea 610 $aperoxidase 610 $aphospholipase A2 610 $a1-Cys Prdx 610 $aknock-in mouse 610 $adrug delivery 610 $aantioxidant activity 610 $asulfinic acid 610 $aradioprotection 610 $aspermatozoa 610 $aperoxiredoxin 6 610 $amass spectroscopic analysis 610 $aknockout mouse 610 $aphospholipase A2 activity 610 $aliposomes 610 $amitochondrial membrane potential 610 $alipid peroxidation 610 $aPLA2 activity 610 $aionizing radiation 610 $aglutathione peroxidase 610 $aPeroxiredoxin 610 $aPrdx6 structure 610 $amembrane repair 610 $asubstrate binding 610 $ainflammation 610 $areactive oxygen species 610 $aPrdx6 610 $asulfonic/sulfinic acid 610 $aFuchs' endothelial corneal dystrophy 610 $aendothelium 610 $afertilization 610 $aperoxidatic cysteine 610 $athioredoxin fold 610 $aredox balance 610 $asurfactant protein A 610 $adiabetes 610 $aoxidative stress 615 7$aMedicine 700 $aFisher$b Aron B.$01331910 801 0$bScCtBLL 801 1$bScCtBLL 906 $aBOOK 912 $a9910346679603321 996 $aPeroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family$93040640 997 $aUNINA