- GLRX2
Glutaredoxin 2, also known as GLRX2, is a human
gene .cite web | title = Entrez Gene: GLRX2 glutaredoxin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51022| accessdate = ]PBB_Summary
section_title =
summary_text = Glutaredoxins (e.g., GLRX; MIM 600443) are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions. [supplied by OMIM] cite web | title = Entrez Gene: GLRX2 glutaredoxin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51022| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Davis DA, Newcomb FM, Starke DW, "et al." |title=Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. |journal=J. Biol. Chem. |volume=272 |issue= 41 |pages= 25935–40 |year= 1997 |pmid= 9325327 |doi=
*cite journal | author=Lai CH, Chou CY, Ch'ang LY, "et al." |title=Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. |journal=Genome Res. |volume=10 |issue= 5 |pages= 703–13 |year= 2000 |pmid= 10810093 |doi=
*cite journal | author=Lundberg M, Johansson C, Chandra J, "et al." |title=Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 26269–75 |year= 2001 |pmid= 11297543 |doi= 10.1074/jbc.M011605200
*cite journal | author=Gladyshev VN, Liu A, Novoselov SV, "et al." |title=Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 30374–80 |year= 2001 |pmid= 11397793 |doi= 10.1074/jbc.M100020200
*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=Johansson C, Lillig CH, Holmgren A |title=Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. |journal=J. Biol. Chem. |volume=279 |issue= 9 |pages= 7537–43 |year= 2004 |pmid= 14676218 |doi= 10.1074/jbc.M312719200
*cite journal | author=Lundberg M, Fernandes AP, Kumar S, Holmgren A |title=Cellular and plasma levels of human glutaredoxin 1 and 2 detected by sensitive ELISA systems. |journal=Biochem. Biophys. Res. Commun. |volume=319 |issue= 3 |pages= 801–9 |year= 2004 |pmid= 15184054 |doi= 10.1016/j.bbrc.2004.04.199
*cite journal | author=Peltoniemi M, Kaarteenaho-Wiik R, Säily M, "et al." |title=Expression of glutaredoxin is highly cell specific in human lung and is decreased by transforming growth factor-beta in vitro and in interstitial lung diseases in vivo. |journal=Hum. Pathol. |volume=35 |issue= 8 |pages= 1000–7 |year= 2004 |pmid= 15297967 |doi=
*cite journal | author=Lillig CH, Lönn ME, Enoksson M, "et al." |title=Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 36 |pages= 13227–32 |year= 2004 |pmid= 15328416 |doi= 10.1073/pnas.0401896101
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Enoksson M, Fernandes AP, Prast S, "et al." |title=Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release. |journal=Biochem. Biophys. Res. Commun. |volume=327 |issue= 3 |pages= 774–9 |year= 2005 |pmid= 15649413 |doi= 10.1016/j.bbrc.2004.12.067
*cite journal | author=Lillig CH, Berndt C, Vergnolle O, "et al." |title=Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 23 |pages= 8168–73 |year= 2005 |pmid= 15917333 |doi= 10.1073/pnas.0500735102
*cite journal | author=Gregory SG, Barlow KF, McLay KE, "et al." |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727
*cite journal | author=Fernando MR, Lechner JM, Löfgren S, "et al." |title=Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells. |journal=FASEB J. |volume=20 |issue= 14 |pages= 2645–7 |year= 2007 |pmid= 17065220 |doi= 10.1096/fj.06-5919fje
*cite journal | author=Berndt C, Hudemann C, Hanschmann EM, "et al." |title=How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2? |journal=Antioxid. Redox Signal. |volume=9 |issue= 1 |pages= 151–7 |year= 2007 |pmid= 17115894 |doi= 10.1089/ars.2007.9.151
*cite journal | author=Johansson C, Kavanagh KL, Gileadi O, Oppermann U |title=Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria. |journal=J. Biol. Chem. |volume=282 |issue= 5 |pages= 3077–82 |year= 2007 |pmid= 17121859 |doi= 10.1074/jbc.M608179200
*cite journal | author=Sagemark J, Elgán TH, Bürglin TR, "et al." |title=Redox properties and evolution of human glutaredoxins. |journal=Proteins |volume=68 |issue= 4 |pages= 879–92 |year= 2007 |pmid= 17546662 |doi= 10.1002/prot.21416PBB_Controls
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