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Corinne M. Spickett

Researcher at Aston University

Publications -  125
Citations -  5345

Corinne M. Spickett is an academic researcher from Aston University. The author has contributed to research in topics: Lipid oxidation & Lipid peroxidation. The author has an hindex of 38, co-authored 121 publications receiving 4654 citations. Previous affiliations of Corinne M. Spickett include Strathclyde Institute of Pharmacy and Biomedical Sciences & University of Strathclyde.

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A high-fat meal induces low-grade endotoxemia: evidence of a novel mechanism of postprandial inflammation

TL;DR: Low-grade endotoxemia may contribute to the postprandial inflammatory state and could represent a novel potential contributor to endothelial activation and the development of atherosclerosis.
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Chemistry of phospholipid oxidation

TL;DR: The challenges for the future will be to adopt lipidomic approaches to map the profile of oxidized phospholipid formation in different biological conditions, and relate this to their effects in vivo.
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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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Oxidized phospholipid inhibition of Toll-like receptor (TLR) signaling is restricted to TLR2 and TLR4 - Roles for CD14, LPS-binding protein, and MD2 as targets for specificity of inhibition

TL;DR: Results suggest that oxidized phospholipid-mediated inhibition of TLR signaling occurs mainly by competitive interaction with accessory proteins that interact directly with bacterial lipids to promote signaling via TLR2 or TLR4.
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The lipid peroxidation product 4-hydroxy-2-nonenal: Advances in chemistry and analysis

TL;DR: Combinations of enrichment strategies with targetted mass spectrometry routines such as neutral loss scanning are now facilitating detection of H NE-modified proteins in complex biological samples, important for characterizing the interactions of HNE with redox sensitive cell signalling proteins and understanding how it may modulate their activities either physiologically or in disease.