Helge Uhrigshardt

TL;DR: Results indicate a possible mechanism for the cell to gauge the magnitude of oxidative stimuli through the progressive and specific accumulation of modified redox-switches through the specific detection of SNO-modifications and determination of individual protein thiol-reactivity.

TL;DR: The data indicate important structural and functional alterations to the cardiac sarcomere and the contribution of protein citrullination to this process.

TL;DR: Functional annotation and site-specificity analysis revealed a twofold greater nitric oxide-susceptibility for proteins involved in transport; including regulators of mitochondrial permeability transition suggesting SNO-regulation and a possible protective mechanism.

TL;DR: The cysTMT(6) reagent provides a simplified and powerful approach to SNO detection by combining unambiguous identification of the modified cysteine residue and relative quantification of up to six samples by mass spectrometry analysis.

TL;DR: The protein citrullination originates from enzymatic deimination of amino acid arginine in a protein and is involved in various biological processes during health and disease as discussed by the authors.