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Elizabeth A. Veal

Researcher at Newcastle University

Publications -  36
Citations -  4106

Elizabeth A. Veal is an academic researcher from Newcastle University. The author has contributed to research in topics: Thioredoxin peroxidase activity & Peroxiredoxin. The author has an hindex of 25, co-authored 35 publications receiving 3577 citations. Previous affiliations of Elizabeth A. Veal include University of Liverpool & University of Newcastle.

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Hydrogen Peroxide Sensing and Signaling

TL;DR: The molecular mechanisms by which hydrogen peroxide is sensed and the increasing evidence that antioxidant enzymes play multiple, key roles as sensors and regulators of signal transduction in response to hydrogen peroxy are discussed.
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European contribution to the study of ROS : a summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)

Javier Egea, +151 more
- 01 Oct 2017 - 
TL;DR: The European Cooperation in Science and Technology (COST) provides an ideal framework to establish multi-disciplinary research networks and EU-ROS represents a consortium of researchers from different disciplines who are dedicated to providing new insights and tools for better understanding redox biology and medicine.
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A 2-Cys Peroxiredoxin Regulates Peroxide-Induced Oxidation and Activation of a Stress-Activated MAP Kinase

TL;DR: It is revealed that Tpx1, the single 2-Cys Prx in Schizosaccharomyces pombe, is required for the peroxide-induced activation of the p38/JNK homolog, Sty1, which provides new insight into the response of SAPKs to diverse stimuli by revealing a mechanism for SAPK activation specifically by oxidative stress.
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Hydrogen Peroxide as a Signaling Molecule

TL;DR: Some of the mechanisms by which hydrogen peroxide is sensed and utilized as a signaling molecule to regulate diverse biological processes are discussed.
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Inactivation of a Peroxiredoxin by Hydrogen Peroxide Is Critical for Thioredoxin-Mediated Repair of Oxidized Proteins and Cell Survival

TL;DR: It is shown that, in cells treated with hydrogen peroxide, the Prx Tpx1 is a major substrate for thioredoxin in the fission yeast Schizosaccharomyces pombe and, as such, competitively inhibits thiOREDoxin-mediated reduction of other oxidized proteins.