Mårten Hägglund

Mårten Hägglund serves as a Special Consultant in the Department of Biomedical Sciences within the Faculty of Health and Medical Sciences at the University of Copenhagen. He maintains an active research profile through the Inflammation, Metabolism and Oxidation research group (Davies Group), focusing on protein oxidation mechanisms and advanced analytical methodologies. His laboratory is situated at Blegdamsvej 3B in Copenhagen N.

Hägglund's research centers on understanding how oxidative modifications alter protein structure and function, with particular emphasis on supramolecular assemblies and protein aggregates. He has pioneered mass-spectrometry-based approaches for detecting intra- and intermolecular cross-links, while maintaining a longstanding investigation into thioredoxin systems and thiol-disulphide exchange reactions. His work bridges fundamental biochemistry with implications for inflammatory and metabolic diseases, utilizing cutting-edge proteomic techniques to map oxidative damage at molecular resolution.

Analysis of his recent publications (2024-2025) reveals consistent methodological innovation in oxidative proteomics, with applications spanning mitochondrial metabolism, neutrophil biology, vascular systems, and lung tissue models. His research demonstrates particular expertise in singlet oxygen chemistry, hypochlorous acid modifications, and halogen speciation effects on protein function. Hägglund frequently collaborates with the Davies research group and international partners, publishing in high-impact journals including Free Radical Biology and Medicine and Redox Biology.

Hägglund maintains active research collaborations across multiple countries as indicated by international co-authorship networks. His work receives recognition through citations in Wikipedia pages and academic platforms like Mendeley. The Davies Group laboratory environment provides the infrastructure for his mass spectrometry-based research on protein oxidation, with particular focus on the biochemical consequences of oxidative modifications in disease-relevant contexts.