The resistance of transferrin, lactoferrin and caeruloplasmin to oxidative damage: a reply

Por Winterbourn, Christine C.
Publicado em 1988

Superoxide-dependent production of hydroxyl radicals in the presence of iron salts

Por Winterbourn, Christine C.
Publicado em 1982

Reactive oxidants and myeloperoxidase and their involvement in neutrophil extracellular traps

Por Parker, Heather, Winterbourn, Christine C.
Publicado em 2013

Studies of Hemoglobin Denaturation and Heinz Body Formation in the Unstable Hemoglobins

Por Winterbourn, Christine C., Carrell, R. W.
Publicado em 1974

Kinetic Approaches to Measuring Peroxiredoxin Reactivity

Por Winterbourn, Christine C., Peskin, Alexander V.
Publicado no Mol Cells (2016)

Superoxide-mediated Formation of Tyrosine Hydroperoxides and Methionine Sulfoxide in Peptides through Radical Addition and Intramolecular Oxygen Transfer

Por Nagy, Péter, Kettle, Anthony J., Winterbourn, Christine C.
Publicado em 2009

Proteomic detection of hydrogen peroxide-sensitive thiol proteins in Jurkat cells

Por Baty, James W., Hampton, Mark B., Winterbourn, Christine C.
Publicado em 2005

Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC–MS/MS method

Por Harwood, D. Tim, Kettle, Anthony J., Winterbourn, Christine C.
Publicado em 2006

Mechanism of nitrite oxidation by eosinophil peroxidase: implications for oxidant production and nitration by eosinophils

Por van Dalen, Christine J., Winterbourn, Christine C., Kettle, Anthony J.
Publicado em 2006

Conjugation of Glutathione to Oxidized Tyrosine Residues in Peptides and Proteins

Por Nagy, Peter, Lechte, Thomas P., Das, Andrew B., Winterbourn, Christine C.
Publicado em 2012

Conjugation of glutathione to oxidized tyrosine residues in peptides and proteins.

Por Nagy, Peter, Lechte, Thomas P., Das, Andrew B., Winterbourn, Christine C.
Publicado no J Biol Chem (2015)

IκB is a sensitive target for oxidation by cell-permeable chloramines: inhibition of NF-κB activity by glycine chloramine through methionine oxidation

Por Midwinter, Robyn G., Cheah, Fook-Choe, Moskovitz, Jackob, Vissers, Margret C., Winterbourn, Christine C.
Publicado em 2006

Myeloperoxidase: a front-line defender against phagocytosed microorganisms

Por Klebanoff, Seymour J., Kettle, Anthony J., Rosen, Henry, Winterbourn, Christine C., Nauseef, William M.
Publicado em 2013

Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides

Por Winterbourn, Christine C., Parsons-Mair, Helena N., Gebicki, Silvia, Gebicki, Janusz M., Davies, Michael J.
Publicado em 2004

Characterization of non-covalent oligomers of proteins treated with hypochlorous acid.

Por Chapman, Anna L P, Winterbourn, Christine C, Brennan, Stephen O, Jordan, T William, Kettle, Anthony J
Publicado em 2003

Design of ultrasensitive probes for human neutrophil elastase through hybrid combinatorial substrate library profiling

Por Kasperkiewicz, Paulina, Poreba, Marcin, Snipas, Scott J., Parker, Heather, Winterbourn, Christine C., Salvesen, Guy S., Drag, Marcin
Publicado em 2014

Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation

Por Poynton, Rebecca A., Peskin, Alexander V., Haynes, Alexina C., Lowther, W. Todd, Hampton, Mark B., Winterbourn, Christine C.
Publicado no Biochem J (2015)

Hyperoxidation of Peroxiredoxins 2 and 3: RATE CONSTANTS FOR THE REACTIONS OF THE SULFENIC ACID OF THE PEROXIDATIC CYSTEINE

Por Peskin, Alexander V., Dickerhof, Nina, Poynton, Rebecca A., Paton, Louise N., Pace, Paul E., Hampton, Mark B., Winterbourn, Christine C.
Publicado em 2013

Glutathionylation of the Active Site Cysteines of Peroxiredoxin 2 and Recycling by Glutaredoxin

Por Peskin, Alexander V., Pace, Paul E., Behring, Jessica B., Paton, Louise N., Soethoudt, Marjolein, Bachschmid, Markus M., Winterbourn, Christine C.
Publicado no J Biol Chem (2016)

Thioredoxin reductase 1 and NADPH directly protect protein tyrosine phosphatase 1B from inactivation during H(2)O(2) exposure

Por Dagnell, Markus, Pace, Paul E., Cheng, Qing, Frijhoff, Jeroen, Östman, Arne, Arnér, Elias S. J., Hampton, Mark B., Winterbourn, Christine C.
Publicado no J Biol Chem (2017)