“GLRX”的意思、由来-开放百科全书

　

词条

GLRX

释义

Interactions
References
Further reading

{{Infobox_gene}}Glutaredoxin-1 is a protein that in humans is encoded by the GLRX gene.^[1]^[2]

Interactions

GLRX has been shown to interact with Wilson disease protein^[3] and ATP7A.^[3]

References

1. ^{{cite journal |vauthors=Padilla CA, Bajalica S, Lagercrantz J, Holmgren A | title = The gene for human glutaredoxin (GLRX) is localized to human chromosome 5q14 | journal = Genomics | volume = 32 | issue = 3 | pages = 455–7 |date=Feb 1997 | pmid = 8838810 | pmc = | doi = 10.1006/geno.1996.0141 }}
2. ^{{cite web | title = Entrez Gene: GLRX glutaredoxin (thioltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2745| accessdate = }}
3. ^¹{{cite journal |last=Lim |first=Chris M |authorlink= |author2=Cater Michael A |author3=Mercer Julian F B |author4=La Fontaine Sharon |date=Sep 2006 |title=Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases |journal=Biochem. Biophys. Res. Commun. |volume=348 |issue=2 |pages=428–36 | issn = 0006-291X| pmid = 16884690 |doi = 10.1016/j.bbrc.2006.07.067 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}

Further reading

{{refbegin | 2}}

{{cite journal | author=Lou MF |title=Redox regulation in the lens. |journal=Progress in Retinal and Eye Research |volume=22 |issue= 5 |pages= 657–82 |year= 2003 |pmid= 12892645 |doi=10.1016/S1350-9462(03)00050-8 }}
{{cite journal |vauthors=Sykes MC, Mowbray AL, Jo H |title=Reversible glutathiolation of caspase-3 by glutaredoxin as a novel redox signaling mechanism in tumor necrosis factor-alpha-induced cell death. |journal=Circ. Res. |volume=100 |issue= 2 |pages= 152–4 |year= 2007 |pmid= 17272816 |doi= 10.1161/01.RES.0000258171.08020.72 }}
{{cite journal |vauthors=Padilla CA, Martínez-Galisteo E, Bárcena JA |title=Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. |journal=Eur. J. Biochem. |volume=227 |issue= 1–2 |pages= 27–34 |year= 1995 |pmid= 7851394 |doi=10.1111/j.1432-1033.1995.tb20356.x |display-authors=etal}}
{{cite journal |vauthors=Bandyopadhyay S, Gronostajski RM |title=Identification of a conserved oxidation-sensitive cysteine residue in the NFI family of DNA-binding proteins. |journal=J. Biol. Chem. |volume=269 |issue= 47 |pages= 29949–55 |year= 1994 |pmid= 7961993 |doi= }}
{{cite journal |vauthors=Fernando MR, Sumimoto H, Nanri H |title=Cloning and sequencing of the cDNA encoding human glutaredoxin. |journal=Biochim. Biophys. Acta |volume=1218 |issue= 2 |pages= 229–31 |year= 1994 |pmid= 8018729 |doi= 10.1016/0167-4781(94)90019-1|display-authors=etal}}
{{cite journal |vauthors=Papov VV, Gravina SA, Mieyal JJ, Biemann K |title=The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells. |journal=Protein Sci. |volume=3 |issue= 3 |pages= 428–34 |year= 1994 |pmid= 8019414 |doi=10.1002/pro.5560030307 | pmc=2142694 }}
{{cite journal |vauthors=Padilla CA, Spyrou G, Holmgren A |title=High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys7 to Ser mutant protein. |journal=FEBS Lett. |volume=378 |issue= 1 |pages= 69–73 |year= 1996 |pmid= 8549805 |doi=10.1016/0014-5793(95)01413-6 }}
{{cite journal |vauthors=Park JB, Levine M |title=Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin. | series=315 |journal=Biochem. J. |volume=( Pt 3) |issue= 3|pages= 931–8 |year= 1996 |pmid= 8645179 |doi= 10.1042/bj3150931| pmc=1217296 }}
{{cite journal |vauthors=Davis DA, Newcomb FM, Starke DW |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=10.1074/jbc.272.41.25935 |display-authors=etal}}
{{cite journal |vauthors=Park JB, Levine M |title=The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis. |journal=Gene |volume=197 |issue= 1–2 |pages= 189–93 |year= 1997 |pmid= 9332366 |doi=10.1016/S0378-1119(97)00262-X }}
{{cite journal |vauthors=Bandyopadhyay S, Starke DW, Mieyal JJ, Gronostajski RM |title=Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor I. |journal=J. Biol. Chem. |volume=273 |issue= 1 |pages= 392–7 |year= 1998 |pmid= 9417094 |doi=10.1074/jbc.273.1.392 }}
{{cite journal |vauthors=Sun C, Berardi MJ, Bushweller JH |title=The NMR solution structure of human glutaredoxin in the fully reduced form. |journal=J. Mol. Biol. |volume=280 |issue= 4 |pages= 687–701 |year= 1998 |pmid= 9677297 |doi= 10.1006/jmbi.1998.1913 |citeseerx=10.1.1.156.1182 }}
{{cite journal |vauthors=Yang Y, Jao S, Nanduri S |title=Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. |journal=Biochemistry |volume=37 |issue= 49 |pages= 17145–56 |year= 1999 |pmid= 9860827 |doi= 10.1021/bi9806504 |display-authors=etal}}
{{cite journal |vauthors=Balijepalli S, Tirumalai PS, Swamy KV |title=Rat brain thioltransferase: regional distribution, immunological characterization, and localization by fluorescent in situ hybridization. |journal=J. Neurochem. |volume=72 |issue= 3 |pages= 1170–8 |year= 1999 |pmid= 10037490 |doi=10.1046/j.1471-4159.1999.0721170.x |display-authors=etal}}
{{cite journal |vauthors=Barrett WC, DeGnore JP, König S |title=Regulation of PTP1B via glutathionylation of the active site cysteine 215. |journal=Biochemistry |volume=38 |issue= 20 |pages= 6699–705 |year= 1999 |pmid= 10350489 |doi= 10.1021/bi990240v |display-authors=etal}}
{{cite journal |vauthors=García-Pardo L, Granados MD, Gaytán F |title=Immunolocalization of glutaredoxin in the human corpus luteum. |journal=Mol. Hum. Reprod. |volume=5 |issue= 10 |pages= 914–9 |year= 1999 |pmid= 10508218 |doi=10.1093/molehr/5.10.914 |display-authors=etal}}
{{cite journal |vauthors=Mallis RJ, Poland BW, Chatterjee TK |title=Crystal structure of S-glutathiolated carbonic anhydrase III. |journal=FEBS Lett. |volume=482 |issue= 3 |pages= 237–41 |year= 2000 |pmid= 11024467 |doi=10.1016/S0014-5793(00)02022-6 |display-authors=etal}}
{{cite journal |vauthors=Balijepalli S, Boyd MR, Ravindranath V |title=Human brain thioltransferase: constitutive expression and localization by fluorescence in situ hybridization. |journal=Brain Res. Mol. Brain Res. |volume=85 |issue= 1–2 |pages= 123–32 |year= 2001 |pmid= 11146114 |doi=10.1016/S0169-328X(00)00206-0 }}
{{cite journal |vauthors=Qiao F, Xing K, Liu A |title=Human lens thioltransferase: cloning, purification, and function. |journal=Invest. Ophthalmol. Vis. Sci. |volume=42 |issue= 3 |pages= 743–51 |year= 2001 |pmid= 11222536 |doi= |display-authors=etal}}

{{refend}}{{PDB Gallery|geneid=2745}}{{Other oxidoreductases}}{{gene-5-stub}}

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