Gene Review:
trxA - thioredoxin 1
Escherichia coli str. K-12 substr. MG1655
Synonyms:
ECK3773, JW5856, dasC, fip, fipA, ...
- Cloning, expression, and characterization of a novel Escherichia coli thioredoxin. Miranda-Vizuete, A., Damdimopoulos, A.E., Gustafsson, J., Spyrou, G. J. Biol. Chem. (1997)
- Conformational and functional similarities between glutaredoxin and thioredoxins. Eklund, H., Cambillau, C., Sjöberg, B.M., Holmgren, A., Jörnvall, H., Höög, J.O., Brändén, C.I. EMBO J. (1984)
- Molecular genetic analysis of a thioredoxin gene from Thiobacillus ferrooxidans. Powles, R.E., Deane, S.M., Rawlings, D.E. Microbiology (Reading, Engl.) (1995)
- Crystal structure of thioredoxin-2 from Anabaena. Saarinen, M., Gleason, F.K., Eklund, H. Structure (1995)
- Thioredoxin system in obligate anaerobe Desulfovibrio desulfuricans: Identification and characterization of a novel thioredoxin 2. Sarin, R., Sharma, Y.D. Gene (2006)
- Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Lennon, B.W., Williams, C.H., Ludwig, M.L. Science (2000)
- Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. Shevchik, V.E., Condemine, G., Robert-Baudouy, J. EMBO J. (1994)
- Thionein can serve as a reducing agent for the methionine sulfoxide reductases. Sagher, D., Brunell, D., Hejtmancik, J.F., Kantorow, M., Brot, N., Weissbach, H. Proc. Natl. Acad. Sci. U.S.A. (2006)
- Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways. Segatori, L., Paukstelis, P.J., Gilbert, H.F., Georgiou, G. Proc. Natl. Acad. Sci. U.S.A. (2004)
- Different mechanisms of thioredoxin in its reduced and oxidized forms in defense against hydrogen peroxide in Escherichia coli. Takemoto, T., Zhang, Q.M., Yonei, S. Free Radic. Biol. Med. (1998)
- Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Holmgren, A. Proc. Natl. Acad. Sci. U.S.A. (1976)
- Selenodiglutathione is a highly efficient oxidant of reduced thioredoxin and a substrate for mammalian thioredoxin reductase. Björnstedt, M., Kumar, S., Holmgren, A. J. Biol. Chem. (1992)
- Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli. Jurado, P., Ritz, D., Beckwith, J., de Lorenzo, V., Fernández, L.A. J. Mol. Biol. (2002)
- Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. Dyson, H.J., Gippert, G.P., Case, D.A., Holmgren, A., Wright, P.E. Biochemistry (1990)
- Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress. Prieto-Alamo, M.J., Jurado, J., Gallardo-Madueno, R., Monje-Casas, F., Holmgren, A., Pueyo, C. J. Biol. Chem. (2000)
- Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: a system designed for exploring protein-protein interactions. Lu, Z., Murray, K.S., Van Cleave, V., LaVallie, E.R., Stahl, M.L., McCoy, J.M. Biotechnology (N.Y.) (1995)
- Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli. Ritz, D., Patel, H., Doan, B., Zheng, M., Aslund, F., Storz, G., Beckwith, J. J. Biol. Chem. (2000)
- An in vivo pathway for disulfide bond isomerization in Escherichia coli. Rietsch, A., Belin, D., Martin, N., Beckwith, J. Proc. Natl. Acad. Sci. U.S.A. (1996)
- Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Chung, J., Chen, T., Missiakas, D. Mol. Microbiol. (2000)
- Thioredoxin and related proteins in procaryotes. Gleason, F.K., Holmgren, A. FEMS Microbiol. Rev. (1988)
- Disulfide bond formation and folding of plant peroxidases expressed as inclusion body protein in Escherichia coli thioredoxin reductase negative strains. Teilum, K., Ostergaard, L., Welinder, K.G. Protein Expr. Purif. (1999)
- Tandem copies of a human rotavirus VP8 epitope can induce specific neutralizing antibodies in BALB/c mice. Kovacs-Nolan, J., Mine, Y. Biochim. Biophys. Acta (2006)
- 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)
- The CcmE protein from Escherichia coli is a haem-binding protein. Reid, E., Eaves, D.J., Cole, J.A. FEMS Microbiol. Lett. (1998)
- Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. Waksman, G., Krishna, T.S., Williams, C.H., Kuriyan, J. J. Mol. Biol. (1994)
- Interactions of Escherichia coli thioredoxin, the processivity factor, with bacteriophage T7 DNA polymerase and helicase. Ghosh, S., Hamdan, S.M., Cook, T.E., Richardson, C.C. J. Biol. Chem. (2008)
- High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Jeng, M.F., Campbell, A.P., Begley, T., Holmgren, A., Case, D.A., Wright, P.E., Dyson, H.J. Structure (1994)
- Characterization of Escherichia coli thioredoxins with altered active site residues. Gleason, F.K., Lim, C.J., Gerami-Nejad, M., Fuchs, J.A. Biochemistry (1990)
- The acidic nature of the CcmG redox-active center is important for cytochrome c maturation in Escherichia coli. Edeling, M.A., Ahuja, U., Heras, B., Thöny-Meyer, L., Martin, J.L. J. Bacteriol. (2004)
- Binding properties and solubility of single-chain T cell receptors expressed in E. coli. Schodin, B.A., Schlueter, C.J., Kranz, D.M. Mol. Immunol. (1996)
- Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography. Pigiet, V.P., Conley, R.R. J. Biol. Chem. (1977)
- Assimilatory sulfate reduction in an Escherichia coli mutant lacking thioredoxin activity. Tsang, M.L., Schiff, J.A. J. Bacteriol. (1978)
- Investigation of the 'switch-epitope' concept with random peptide libraries displayed as thioredoxin loop fusions. Tripp, B.C., Lu, Z., Bourque, K., Sookdeo, H., McCoy, J.M. Protein Eng. (2001)
- Amplification and purification of plasmid-encoded thioredoxin from Escherichia coli K12. Lunn, C.A., Kathju, S., Wallace, B.J., Kushner, S.R., Pigiet, V. J. Biol. Chem. (1984)
- Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation. Nagahara, N., Yoshii, T., Abe, Y., Matsumura, T. J. Biol. Chem. (2007)