scispace - formally typeset
A

Albert van der Vliet

Researcher at University of Vermont

Publications -  157
Citations -  12781

Albert van der Vliet is an academic researcher from University of Vermont. The author has contributed to research in topics: Inflammation & Nitric oxide. The author has an hindex of 54, co-authored 149 publications receiving 11632 citations. Previous affiliations of Albert van der Vliet include University of Bonn & University of California, Davis.

Papers
More filters
Journal ArticleDOI

Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils

TL;DR: The data reveal that NO2− may regulate inflammatory processes through oxidative mechanisms, perhaps by contributing to the tyrosine nitration and chlorination observed in vivo.
Journal ArticleDOI

Formation of Reactive Nitrogen Species during Peroxidase-catalyzed Oxidation of Nitrite A POTENTIAL ADDITIONAL MECHANISM OF NITRIC OXIDE-DEPENDENT TOXICITY

TL;DR: The results suggest that NO2−, at physiological or pathological levels, is a substrate for the mammalian peroxidases MPO and lactoperoxidase and that formation of NO2· via per oxidase-catalyzed oxidation ofNO2− may provide an additional pathway contributing to cytotoxicity or host defense associated with increased NO· production.
Journal ArticleDOI

Redox-based regulation of signal transduction : Principles, pitfalls, and promises

TL;DR: Some of the recent findings that illuminate the significance of redox signaling and exciting future perspectives are reviewed to highlight some of the current pitfalls and the approaches needed to advance this important area of biochemical and biomedical research.
Journal ArticleDOI

Formation of Nitrating and Chlorinating Species by Reaction of Nitrite with Hypochlorous Acid A NOVEL MECHANISM FOR NITRIC OXIDE-MEDIATED PROTEIN MODIFICATION

TL;DR: It is proposed that NO−2 reacts with HOCl by Cl+ transfer to form both cis- and trans-chlorine nitrite (Cl-ONO) and Cl-NO2 as intermediates that modify tyrosine by either direct reaction or after decomposition to reactive free and solvent-caged Cl· and ·NO1 as reactive species.
Journal ArticleDOI

Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation

TL;DR: In this article, peroxynitrite and GSH-dependent proMMP activation was found to be a potent oxidizing agent formed during inflammatory processes, and extensive S-glutathiolation of the pro-MMP protein occurred during activation.