Results 211 to 220 of about 6,985 (261)

Unveiling a novel broad-host-range cyanomyovirus cross-infecting Prochlorococcus and Synechococcus. [PDF]

BMC Biol
Wei S, Cai L, Zheng H, Wei S, Xu B, Zhang R, Xu Y, Li J.   +7 more
europepmc   +1 more source

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Intron position as an evolutionary marker of thioredoxins and thioredoxin domains

Journal of Molecular Evolution, 1996
In contrast to prokaryotes, which typically possess one thioredoxin gene per genome, three different thioredoxin types have been described in higher plants. All are encoded by nuclear genes, but thioredoxins m and f are chloroplastic while thioredoxins h have no transit peptide and are probably cytoplasmic.
Mariam Sahrawy, Valerie Hecht, Ana Chueca   +2 more
exaly   +3 more sources

Measurement of Thioredoxin and Thioredoxin Reductase

Current Protocols in Toxicology, 2005
AbstractThe thioredoxin system is ubiquitous, providing reducing equivalents to essential biosynthetic enzymes like ribonucleotide reductase. It is essential for cellular redox regulation, control of oxidative stress, and protection against oxidative damage.
E S, Arnér, A, Holmgren
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Thioredoxins and thioredoxin reductase in chloroplasts: A review

Gene, 2019
The chloroplastic thioredoxins (Trxs), a family of thiol-disulphide oxidoreductases, are reduced by either ferredoxin (Fd)-dependent Trx reductase (FTR) or reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent Trx reductase (NTR). Two Trx systems are present in chloroplasts including Trxs, Trx-like proteins, and reductase FTR and NTRC ...
Zhenhui Kang, Tong Qin, Zhiping Zhao
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Thioredoxin Superfamily and Thioredoxin‐Inducing Agents

Annals of the New York Academy of Sciences, 2002
Abstract: Mammalian thioredoxin (TRX) with redox‐active dithiol in the active site plays multiple roles in intracellular signaling and resistance against oxidative stress. TRX is induced by a variety of stresses including infectious agents as well as hormones and chemicals.
Kiichi, Hirota, Hajime, Nakamura, Hiroshi, Masutani, Junji, Yodoi   +3 more
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Thioredoxins in chloroplasts

Current Genetics, 2007
Thioredoxins (TRXs) are small disulfide oxidoreductases of ca. 12 kDa found in all free living organisms. In plants, two chloroplastic TRXs, named TRX f and TRX m, were originally identified as light dependent regulators of several carbon metabolism enzymes including Calvin cycle enzymes.
Lemaire SD, Michelet L, ZAFFAGNINI, MIRKO, Massot V, Issakidis Bourguet E.   +4 more
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Preparation and assay of mammalian thioredoxin and thioredoxin reductase

1999
Publisher Summary This chapter describes the preparation and assay of mammalian thioredoxin and thioredoxin reductase (TrxR). The amino acid sequences of mammalian TrxR revealed a strikingly high homology to glutathione reductase. 14,19 The conserved features of all the structural components of glutathione reductase are preserved in mammalian TrxR ...
E S, Arnér, L, Zhong, A, Holmgren
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Kinetics of electron transfer from thioredoxin reductase to thioredoxin

Biochemistry, 1991
The reduction of Escherichia coli thioredoxin by thioredoxin reductase was studied by stopped-flow spectrophotometry. The reaction showed no dependence on thioredoxin concentration, indicating that complex formation was rapid and occurred during the dead time of the instrument.
J A, Navarro, F K, Gleason, M A, Cusanovich, J A, Fuchs, T E, Meyer, G, Tollin   +5 more
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Cytosolic, Mitochondrial Thioredoxins and Thioredoxin Reductases in Arabidopsis Thaliana

Photosynthesis Research, 2004
Thioredoxins, by reducing disulfide bridges are one of the main participants that regulate cellular redox balance. In plants, the thioredoxin system is particularly complex. The most well-known thioredoxins are the chloroplastic ones, that participate in the regulation of enzymatic activities during the transition between light and dark phases.
Bréhélin, Claire, Laloi, Christophe, Setterdahl, Aaron, Knaff, David, Meyer, Yves   +4 more
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Rat liver thioredoxin and thioredoxin reductase: purification and characterization

Biochemistry, 1982
A reproducible scheme has been developed for the preparation of rat liver thioredoxin and thioredoxin reductase (EC 1.6.4.5) by using assays based on reduction of insulin and 5,5'-dithiobis(2-nitrobenzoic acid), respectively. Both proteins were purified to homogeneity, as judged from polyacrylamide gel electrophoresis.
M, Luthman, A, Holmgren
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