Martin D. Rees

Superoxide radicals can act synergistically with hypochlorite to induce damage to proteins.

Hypochlorite-mediated fragmentation of hyaluronan, chondroitin sulfates, and related N-acetyl glycosamines: evidence for chloramide intermediates, free radical transfer reactions, and site-specific fragmentation.

Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondroitin sulphates.

Oxidation of heparan sulphate by hypochlorite: role of N-chloro derivatives and dichloramine-dependent fragmentation.

Heparan sulfate degradation via reductive homolysis of its N-chloro derivatives.

Degradation of extracellular matrix and its components by hypobromous acid.

Mammalian heme peroxidases: from molecular mechanisms to health implications.

Oxidative damage to extracellular matrix and its role in human pathologies.

Inhibition of myeloperoxidase-mediated hypochlorous acid production by nitroxides.

Myeloperoxidase-derived oxidants selectively disrupt the protein core of the heparan sulfate proteoglycan perlecan.

Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations.

Peroxynitrite modifies the structure and function of the extracellular matrix proteoglycan perlecan by reaction with both the protein core and the heparan sulfate chains.

Heparan sulfate-dependent signaling of fibroblast growth factor 18 by chondrocyte-derived perlecan.

Urate as a physiological substrate for myeloperoxidase: implications for hyperuricemia and inflammation.

Targeted subendothelial matrix oxidation by myeloperoxidase triggers myosin II-dependent de-adhesion and alters signaling in endothelial cells.

Human indoleamine 2,3-dioxygenase is a catalyst of physiological heme peroxidase reactions: implications for the inhibition of dioxygenase activity by hydrogen peroxide.

Mechanism and regulation of peroxidase-catalyzed nitric oxide consumption in physiological fluids: critical protective actions of ascorbate and thiocyanate.