Identification of proteins targeted by the thioredoxin superfamily in Plasmodium falciparum. [PDF]
The malarial parasite Plasmodium falciparum possesses a functional thioredoxin and glutathione system comprising the dithiol-containing redox proteins thioredoxin (Trx) and glutaredoxin (Grx), as well as plasmoredoxin (Plrx), which is exclusively found ...
Sturm, Nicole +23 more
core +1 more source
Exploring the Diversity of the Thioredoxin Systems in Cyanobacteria
Cyanobacteria evolved the ability to perform oxygenic photosynthesis using light energy to reduce CO2 from electrons extracted from water and form nutrients.
Manuel J. Mallén-Ponce +2 more
doaj +1 more source
FRET-based system for probing protein-protein interactions between σR and RsrA from Streptomyces coelicolor in response to the redox environment. [PDF]
Protein-protein interactions between sigma factor σ(R) and its corresponding zinc-binding anti-sigma (ZAS) protein RsrA trigger the thioredoxin system for maintaining cellular redox homeostasis in S. coelicolor.
Zi-Han Wei +3 more
doaj +1 more source
The Barley Grain Thioredoxin System – an Update
Thioredoxin reduces disulfide bonds and play numerous important functions in plants. In cereal seeds, cytosolic h-type thioredoxin facilitates the release of energy reserves during the germination process and is recycled by NADPH-dependent thioredoxin ...
Per eHägglund +13 more
doaj +1 more source
Mitochondrial thiol-disulfide system under acute hypoxia and hypoxic-hyperoxic adaptation [PDF]
The authors investigated the state of mitochondrial glutathione pool (reduced and oxidized glutathione, protein-GSH mixed disulfides), content of carbonyl groups and free sulfhydryl groups of proteins, protein expression of key mitochondrial antioxidant ...
O. A. Gonchar, I. N. Mankovska
doaj +1 more source
Oxidized Forms of Ergothioneine Are Substrates for Mammalian Thioredoxin Reductase
Ergothioneine (EGT) is a sulfur-containing amino acid analog that is biosynthesized in fungi and bacteria, accumulated in plants, and ingested by humans where it is concentrated in tissues under oxidative stress.
Kaelyn A. Jenny +3 more
doaj +1 more source
Cysteine and methionine residues are the amino acids most sensitive to oxidation by reactive oxygen species. However, in contrast to other amino acids, certain cysteine and methionine oxidation products can be reduced within proteins by dedicated ...
Sofia Lourenço dos Santos +2 more
doaj +1 more source
One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx
Glutaredoxins are small proteins of the thioredoxin superfamily that are present throughout life. Most glutaredoxins fall into two major subfamilies.
Jannik Zimmermann +5 more
doaj +1 more source
Thiol/disulfide systems are involved in the maintenance of the redox status of proteins and other molecules that contain thiol/disulfide groups. Leptospirillum ferriphilum DSM14647, an acidophilic bacterium that uses Fe(2+) as electron donor, and ...
Javiera Norambuena +5 more
doaj +1 more source
Interaction of recombinant form of NADPH-dependent thioredoxin reductase from rice with thioredoxin from two plant and bacterial sources [PDF]
Maintaining redox homeostasis in the cell is critical for different cellular metabolisms and signal transduction pathways. In plants different molecular mechanisms are involved in maintaining cellular redox homeostasis.
Hadiyeh Eslam Panah +2 more
doaj +1 more source

