| Name | glutaredoxin |
|---|---|
| Synonyms | GLRX; GRX; GRX 1; GRX1; Glutaredoxin; Glutaredoxin 1; TTase; TTase 1… |
| Name | sulfur |
|---|---|
| CAS | sulfur |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19505088 | Iwema T, Picciocchi A, Traore DA, Ferrer JL, Chauvat F, Jacquamet L: Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin. Biochemistry. 2009 Jul 7;48(26):6041-3. The dithiol GRX homodimer is proposed to serve as a sequestration form and its iron-sulfur cluster as an oxidative stress sensor. |
2(0,0,0,2) | Details |
| 19561357 | Park JW, Mieyal JJ, Rhee SG, Chock PB: Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin. J Biol Chem. 2009 Aug 28;284(35):23364-74. Epub 2009 Jun 27. Deglutathionylation with Cys mutants showed that Cys (83) and Cys (173) were preferentially catalyzed by Srx, with glutathionylated Srx as the reaction intermediate, whereas glutaredoxin I was more favorable for deglutathionylating Cys (52). (ii) Studies using site-directed mutagenesis coupled with binding and deglutathionylation activities revealed that Pro (174) and Pro (179) of Prx I and Tyr (92) of Srx are essential for both activities. |
2(0,0,0,2) | Details |
| 19748771 | Maulucci G, Pani G, Labate V, Mele M, Panieri E, Papi M, Arcovito G, Galeotti T, De Spirito M: Investigation of the spatial distribution of redox-balance in live cells by using Fluorescence Ratio Imaging Microscopy. Biosens Bioelectron. 2009 Dec 15;25(4):682-7. Epub 2009 Aug 25. Oxidative stress or signaling events can affect sulfur switches differently, thus creating a variation in the spatial distribution of these redox states, which therefore act simultaneously as regulators and indicators of key cellular functions in both physiological and pathological settings. Finally, by transfecting cells with human Glutaredoxin V (GRX-V), an enzyme deputed to maintain reduced the thiol groups of their partner proteins, we can disclose that the significant shift towards more reduced state, with respect to that recovered from non-transfected cells, consists, instead, in a shift towards reduced values of the high R region (reduced), while leaving unaltered the redox-balance of the intracellular side of the plasma membrane. |
1(0,0,0,1) | Details |
| 20064440 | Hoff KG, Culler SJ, Nguyen PQ, McGuire RM, Silberg JJ, Smolke CD: In vivo fluorescent detection of Fe-S clusters coordinated by human GRX2. . Chem Biol. 2009 Dec 24;16(12):1299-308. In addition, we find that maximal fluorescence in the cytosol of mammalian cells requires the iron-sulfur cluster assembly proteins ISCU and NFS1. These findings provide evidence that glutaredoxins can dimerize within mammalian cells through coordination of a 2Fe2S cluster as observed with purified recombinant proteins. |
1(0,0,0,1) | Details |
| 19715344 | Li H, Mapolelo DT, Dingra NN, Naik SG, Lees NS, Hoffman BM, Riggs-Gelasco PJ, Huynh BH, Johnson MK, Outten CE: The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation. Biochemistry. 2009 Oct 13;48(40):9569-81. Nucleocytoplasmic shuttling of Aft1 is dependent upon mitochondrial Fe-S cluster biosynthesis via a signaling pathway that includes the cytosolic monothiol glutaredoxins (Grx3 and Grx4) and the BolA homologue Fra2. |
1(0,0,0,1) | Details |
| 19811920 | Rouhier N, Couturier J, Johnson MK, Jacquot JP: Glutaredoxins: roles in iron homeostasis. Trends Biochem Sci. 2010 Jan;35(1):43-52. Epub 2009 Oct 5. Recent results point to putative roles for glutaredoxins in the sensing of cellular iron and in iron-sulfur cluster biogenesis, either as scaffold proteins for the de novo synthesis of iron-sulfur clusters or as carrier proteins for the transfer of preformed iron-sulfur clusters. |
40(0,1,2,5) | Details |
| 19786205 | Camaschella C: Hereditary sideroblastic anemias: pathophysiology, diagnosis, and treatment. Semin Hematol. 2009 Oct;46(4):371-7. The identification of other genes, such as (ATP) binding cassette B7 (ABCB7) and glutaredoxin 5 (GLRX5), has strengthened the role of iron sulfur cluster biogenesis in sideroblast formation and revealed a complex interplay between pathways of mitochondrial iron utilization and cytosolic iron sensing by the iron-regulatory proteins (IRPs). |
31(0,1,1,1) | Details |
| 20226171 | Haunhorst P, Berndt C, Eitner S, Godoy JR, Lillig CH: Characterization of the human monothiol glutaredoxin 3 (PICOT) as iron-sulfur protein. Biochem Biophys Res Commun. 2010 Apr 2;394(2):372-6. Epub 2010 Mar 10. |
8(0,0,1,3) | Details |
| 19717741 | Rada P, Smid O, Sutak R, Dolezal P, Pyrih J, Zarsky V, Montagne JJ, Hrdy I, Camadro JM, Tachezy J: The monothiol single-domain glutaredoxin is conserved in the highly reduced mitochondria of Giardia intestinalis. Eukaryot Cell. 2009 Oct;8(10):1584-91. Epub 2009 Aug 28. |
5(0,0,0,5) | Details |
| 19478456 | Wang Y, He YX, Yu J, Zhou CZ: Cloning, overproduction, purification, crystallization and preliminary X-ray diffraction analysis of yeast glutaredoxin Grx5. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):651-3. Epub 2009 May 23. Grx5 from the yeast Saccharomyces cerevisiae is a monothiol glutaredoxin that is involved in iron-sulfur cluster biogenesis. |
7(0,0,1,2) | Details |
| 20347849 | Luo M, Jiang YL, Ma XX, Tang YJ, He YX, Yu J, Zhang RG, Chen Y, Zhou CZ: Structural and Biochemical Characterization of Yeast Monothiol Glutaredoxin Grx6. J Mol Biol. 2010 Mar 27. In addition, similar to human Grx2, Grx6 binds GSH via an iron-sulfur cluster in vitro. |
3(0,0,0,3) | Details |
| 20085751 | Kim KD, Chung WH, Kim HJ, Lee KC, Roe JH: Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast. Biochem Biophys Res Commun. 2010 Feb 12;392(3):467-72. Epub 2010 Jan 18. |
3(0,0,0,3) | Details |
| 19958171 | Ugarte N, Petropoulos I, Friguet B: Oxidized Mitochondrial Protein Degradation and Repair in Aging and Oxidative Stress. Antioxid Redox Signal. 2010 Mar 8. Oxidized protein repair is limited to certain oxidation products of the sulfur-containing amino acids and Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin//glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and reductase that reverses back to within proteins, are present in the mitochondrial matrix. |
1(0,0,0,1) | Details |