175 related articles for article (PubMed ID: 18456836)
1. Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways.
Faulkner MJ; Veeravalli K; Gon S; Georgiou G; Beckwith J
Proc Natl Acad Sci U S A; 2008 May; 105(18):6735-40. PubMed ID: 18456836
[TBL] [Abstract][Full Text] [Related]
2. Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity.
Yamamoto Y; Ritz D; Planson AG; Jönsson TJ; Faulkner MJ; Boyd D; Beckwith J; Poole LB
Mol Cell; 2008 Jan; 29(1):36-45. PubMed ID: 18206967
[TBL] [Abstract][Full Text] [Related]
3. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins.
Stewart EJ; Aslund F; Beckwith J
EMBO J; 1998 Oct; 17(19):5543-50. PubMed ID: 9755155
[TBL] [Abstract][Full Text] [Related]
4. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm.
Prinz WA; Aslund F; Holmgren A; Beckwith J
J Biol Chem; 1997 Jun; 272(25):15661-7. PubMed ID: 9188456
[TBL] [Abstract][Full Text] [Related]
5. Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion.
Ritz D; Lim J; Reynolds CM; Poole LB; Beckwith J
Science; 2001 Oct; 294(5540):158-60. PubMed ID: 11588261
[TBL] [Abstract][Full Text] [Related]
6. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.
Bessette PH; Aslund F; Beckwith J; Georgiou G
Proc Natl Acad Sci U S A; 1999 Nov; 96(24):13703-8. PubMed ID: 10570136
[TBL] [Abstract][Full Text] [Related]
7. S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione.
Jung CH; Thomas JA
Arch Biochem Biophys; 1996 Nov; 335(1):61-72. PubMed ID: 8914835
[TBL] [Abstract][Full Text] [Related]
8. Disulfide bond formation by exported glutaredoxin indicates glutathione's presence in the E. coli periplasm.
Eser M; Masip L; Kadokura H; Georgiou G; Beckwith J
Proc Natl Acad Sci U S A; 2009 Feb; 106(5):1572-7. PubMed ID: 19164554
[TBL] [Abstract][Full Text] [Related]
9. Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways in
Feng X; Guo K; Gao H
J Biol Chem; 2020 Aug; 295(32):11118-11130. PubMed ID: 32532818
[TBL] [Abstract][Full Text] [Related]
10. The levels of ribonucleotide reductase, thioredoxin, glutaredoxin 1, and GSH are balanced in Escherichia coli K12.
Miranda-Vizuete A; Rodríguez-Ariza A; Toribio F; Holmgren A; López-Barea J; Pueyo C
J Biol Chem; 1996 Aug; 271(32):19099-103. PubMed ID: 8702583
[TBL] [Abstract][Full Text] [Related]
11. SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm.
Lobstein J; Emrich CA; Jeans C; Faulkner M; Riggs P; Berkmen M
Microb Cell Fact; 2012 May; 11():56. PubMed ID: 22569138
[TBL] [Abstract][Full Text] [Related]
12. Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli.
Feeney MA; Veeravalli K; Boyd D; Gon S; Faulkner MJ; Georgiou G; Beckwith J
Proc Natl Acad Sci U S A; 2011 May; 108(19):7991-6. PubMed ID: 21521794
[TBL] [Abstract][Full Text] [Related]
13. The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol.
Höög JO; Jörnvall H; Holmgren A; Carlquist M; Persson M
Eur J Biochem; 1983 Oct; 136(1):223-32. PubMed ID: 6352262
[TBL] [Abstract][Full Text] [Related]
14. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.
Derman AI; Prinz WA; Belin D; Beckwith J
Science; 1993 Dec; 262(5140):1744-7. PubMed ID: 8259521
[TBL] [Abstract][Full Text] [Related]
15. Evidence for an additional disulfide reduction pathway in Escherichia coli.
Knapp KG; Swartz JR
J Biosci Bioeng; 2007 Apr; 103(4):373-6. PubMed ID: 17502280
[TBL] [Abstract][Full Text] [Related]
16. Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli.
Hatahet F; Nguyen VD; Salo KE; Ruddock LW
Microb Cell Fact; 2010 Sep; 9():67. PubMed ID: 20836848
[TBL] [Abstract][Full Text] [Related]
17. The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm.
Debarbieux L; Beckwith J
Proc Natl Acad Sci U S A; 1998 Sep; 95(18):10751-6. PubMed ID: 9724776
[TBL] [Abstract][Full Text] [Related]
18. In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli.
Gon S; Faulkner MJ; Beckwith J
Antioxid Redox Signal; 2006; 8(5-6):735-42. PubMed ID: 16771665
[TBL] [Abstract][Full Text] [Related]
19. Kinetic characterization of wild-type and mutant human thioredoxin glutathione reductase defines its reaction and regulatory mechanisms.
Brandstaedter C; Fritz-Wolf K; Weder S; Fischer M; Hecker B; Rahlfs S; Becker K
FEBS J; 2018 Feb; 285(3):542-558. PubMed ID: 29222842
[TBL] [Abstract][Full Text] [Related]
20. A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase.
Fernandes AP; Fladvad M; Berndt C; Andrésen C; Lillig CH; Neubauer P; Sunnerhagen M; Holmgren A; Vlamis-Gardikas A
J Biol Chem; 2005 Jul; 280(26):24544-52. PubMed ID: 15833738
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
