PRDX6

PRDX6

Peroxiredoxin 6, also known as PRDX6, is a human gene.cite web | title = Entrez Gene: PRDX6 peroxiredoxin 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9588| accessdate = ]

PBB_Summary
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summary_text = The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.cite web | title = Entrez Gene: PRDX6 peroxiredoxin 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9588| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Phelan SA |title=AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant. |journal=Antioxid. Redox Signal. |volume=1 |issue= 4 |pages= 571–84 |year= 2001 |pmid= 11233154 |doi=
*cite journal | author=Manevich Y, Fisher AB |title=Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. |journal=Free Radic. Biol. Med. |volume=38 |issue= 11 |pages= 1422–32 |year= 2005 |pmid= 15890616 |doi= 10.1016/j.freeradbiomed.2005.02.011
*cite journal | author=Akesson B |title=Work in progress. Occurrence of phospholipase A1 and A2 in human decidua. |journal=Prostaglandins |volume=9 |issue= 5 |pages= 667–73 |year= 1975 |pmid= 240188 |doi=
*cite journal | author=Hochstrasser DF, Frutiger S, Paquet N, "et al." |title=Human liver protein
journal=Electrophoresis |volume=13 |issue= 12 |pages= 992–1001 |year= 1993 |pmid= 1286669 |doi=

*cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=
*cite journal | author=Yeats DA, Bakhle YS |title=Phospholipases A2 and C of human lung; subcellular distribution and substrate selectivity. |journal=Biochim. Biophys. Acta |volume=1003 |issue= 2 |pages= 189–95 |year= 1989 |pmid= 2730891 |doi=
*cite journal | author=Nagase T, Miyajima N, Tanaka A, "et al." |title=Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. |journal=DNA Res. |volume=2 |issue= 1 |pages= 37–43 |year= 1995 |pmid= 7788527 |doi=
*cite journal | author=Golaz O, Hughes GJ, Frutiger S, "et al." |title=Plasma and red blood cell protein maps: update 1993. |journal=Electrophoresis |volume=14 |issue= 11 |pages= 1223–31 |year= 1994 |pmid= 8313871 |doi=
*cite journal | author=Kim TS, Sundaresh CS, Feinstein SI, "et al." |title=Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2542–50 |year= 1997 |pmid= 8999971 |doi=
*cite journal | author=Frank S, Munz B, Werner S |title=The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene. |journal=Oncogene |volume=14 |issue= 8 |pages= 915–21 |year= 1997 |pmid= 9050990 |doi= 10.1038/sj.onc.1200905
*cite journal | author=Kang SW, Baines IC, Rhee SG |title=Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. |journal=J. Biol. Chem. |volume=273 |issue= 11 |pages= 6303–11 |year= 1998 |pmid= 9497358 |doi=
*cite journal | author=Choi HJ, Kang SW, Yang CH, "et al." |title=Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. |journal=Nat. Struct. Biol. |volume=5 |issue= 5 |pages= 400–6 |year= 1998 |pmid= 9587003 |doi=
*cite journal | author=Chen JW, Dodia C, Feinstein SI, "et al." |title=1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 28421–7 |year= 2000 |pmid= 10893423 |doi= 10.1074/jbc.M005073200
*cite journal | author=Fatma N, Singh DP, Shinohara T, Chylack LT |title=Transcriptional regulation of the antioxidant protein 2 gene, a thiol-specific antioxidant, by lens epithelium-derived growth factor to protect cells from oxidative stress. |journal=J. Biol. Chem. |volume=276 |issue= 52 |pages= 48899–907 |year= 2002 |pmid= 11677226 |doi= 10.1074/jbc.M100733200
*cite journal | author=Wagner E, Luche S, Penna L, "et al." |title=A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress. |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 777–85 |year= 2002 |pmid= 12059788 |doi= 10.1042/BJ20020525
*cite journal | author=Leavey PJ, Gonzalez-Aller C, Thurman G, "et al." |title=A 29-kDa protein associated with p67phox expresses both peroxiredoxin and phospholipase A2 activity and enhances superoxide anion production by a cell-free system of NADPH oxidase activity. |journal=J. Biol. Chem. |volume=277 |issue= 47 |pages= 45181–7 |year= 2003 |pmid= 12121978 |doi= 10.1074/jbc.M202869200
*cite journal | author=Manevich Y, Sweitzer T, Pak JH, "et al." |title=1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 18 |pages= 11599–604 |year= 2002 |pmid= 12193653 |doi= 10.1073/pnas.182384499
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Krapfenbauer K, Engidawork E, Cairns N, "et al." |title=Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders. |journal=Brain Res. |volume=967 |issue= 1-2 |pages= 152–60 |year= 2003 |pmid= 12650976 |doi=

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  • Peroxiredoxin — Dekamer des AhpC aus Salmonella typhimurium, ein bakterielles Peroxiredoxin nach PDB …   Deutsch Wikipedia

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