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Posttranslational redox modification of ADP-glucose pyrophosphorylase in response to light is not a major determinant of fine regulation of transitory starch accumulation in Arabidopsis leaves.

Li J, Almagro G, Muñoz FJ, Baroja-Fernández E, Bahaji A, Montero M, Hidalgo M, Sánchez-López AM, Ezquer I, Sesma MT, Pozueta-Romero J.Source(1) Instituto de Agrobiotecnología (CSIC/UPNA/Gobierno de Navarra). Mutiloako etorbidea z/g, 31192 Mutiloa, Nafarroa, Spain.
Plant & cell physiology.Plant Cell Physiol.2011 Dec 30. [Epub ahead of print]
ADP-glucose pyrophosphorylase (AGP) is a heterotetrameric enzyme comprising two small and two large subunits that catalyze the production of ADP-glucose linked to starch biosynthesis. The current paradigm on leaf starch metabolism assumes that posttranslational redox modification of AGP in response
PMID 22210900

A recombinant thioredoxin-glutathione reductase from Fasciola hepatica induces a protective response in rabbits.

Maggioli G, Silveira F, Martín-Alonso JM, Salinas G, Carmona C, Parra F.SourceDepartamento de Bioquímica y Biología Molecular, Instituto Universitario de Biotecnología de Asturias, Universidad de Oviedo, 33006 Oviedo, Spain.
Experimental parasitology.Exp Parasitol.2011 Dec;129(4):323-30. Epub 2011 Oct 1.
Antioxidant systems are fundamental components of host-parasite interactions, and often play a key role in parasite survival. Here, we report the cloning, heterologous expression, and characterization of a thioredoxin glutathione reductase (TGR) from Fasciola hepatica. The deduced polypeptide sequen
PMID 21985914

Transactivation of gene expression by NF-κB is dependent on thioredoxin reductase activity.

Heilman JM, Burke TJ, McClain CJ, Watson WH.SourceDivision of Toxicology, Department of Environmental Health Sciences, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD 21205, USA.
Free radical biology & medicine.Free Radic Biol Med.2011 Oct 15;51(8):1533-42. Epub 2011 Jul 4.
The redox-sensitive transcription factor NF-κB mediates the expression of genes involved in inflammation and cell survival. Thioredoxin reductase-1 (TR1) and its substrate thioredoxin-1 act together to reduce oxidized cysteine residues within the DNA-binding domain of NF-κB and promote maximal DNA
PMID 21782934