Professor Christine Winterbourn is an Auckland University chemistry graduate who received her PhD in biochemistry from Massey University.
She did postdoctoral work at the University of British Columbia, Canada before returning to the Pathology Department, University of Otago, Christchurch, where she now has a personal chair.
Research interests
Professor Winterbourn has published more than 250 scientific papers. Her field of research is the biological chemistry of free radicals and other reactive oxidants and their involvement in health and disease.
Professor Winterbourn's focus is on understanding mechanisms of reactive oxidant production, the biochemistry of biological damage and the consequences for disease pathology.
Her current interests include:
the production of reactive oxidants by neutrophils and their involvement in microbial killing and inflammation
how neutrophils form extracellular traps (NETs)
how thiol proteins contribute to antioxidant defence and redox regulated cell signaling
biochemistry and cellular functions of mammalian peroxiredoxins
mechanisms of oxidative protein crosslinking
oxidant-antioxidant interactions in red blood cells
Other positions
Past member of the Health Research Council
Past member of the Marsden Fund Council
Editor of the Biochemical Journal
Editorial Board of Free Radical Biology and Medicine
Awards
University of Auckland Distinguished Alumni 2015
Royal Society of New Zealand's Rutherford Medal - the first woman to receive the award in its 20 year history
NZ Association of Scientists' Marsden Medal
Massey University 75th Anniversary Medal
Society for Free Radical Research (Australasia) Distinguished Service Award
University of Otago Distinguished Research Medal and Society for Free Radical Research (International) Trevor Slater Award
Winterbourn, C. C., Peskin, A., Kleffmann, T., Radi, R., & Pace, P. E. (2023). Carbon dioxide/bicarbonate is required for sensitive inactivation of mammalian glyceraldehyde-3-phosphate dehydrogenase by hydrogen peroxide. PNAS, 120(18), e2221047120. doi: 10.1073/pnas.2221047120
Journal - Research Article
Magon, N. J., Turner, R., Kettle, A. J., & Winterbourn, C. C. (2023). Cross-linking between cysteine and lysine, tryptophan or tyrosine in peptides and proteins treated with hypochlorous acid and other reactive halogens. Redox Biochemistry & Chemistry. Advance online publication. doi: 10.1016/j.rbc.2023.100002
Journal - Research Article
Kettle, A. J., Ashby, L. V., Winterbourn, C. C., & Dickerhof, N. (2023). Superoxide: The enigmatic chemical chameleon in neutrophil biology [Invited review]. Immunological Reviews. Advance online publication. doi: 10.1111/imr.13183
Journal - Research Other
Hampton, M., Winterbourn, C., Dick, T., & Murphy, M. (2022, December). What are redox signals telling us? Panel discussion at the Society for Free Radical Research (SFRR) Australasia & Japan Conference: Redox Pathways in Biology & Medicine, Christchurch, New Zealand.
Conference Contribution - Verbal presentation and other Conference outputs
Pace, P. E., Peskin, A. V., Winterbourn, C. C., & Hampton, M. B. (2022, August). Disrupting the oligomeric structure of peroxiredoxins in cancer cells using CRISPR. Poster session presented at the CRISPR Technologies Satellite Meeting: Queenstown Research Week, Queenstown, New Zealand.
Conference Contribution - Poster Presentation (not in published proceedings)
Königstorfer, A., Ashby, L. V., Bollar, G. E., Billiot, C. E., Gray, M. J., Jakob, U., Hampton, M. B., & Winterbourn, C. C. (2021). Induction of the reactive chlorine-responsive transcription factor RclR in Escherichia coli following ingestion by neutrophils. Pathogens & Disease, 79, ftaa079. doi: 10.1093/femspd/ftaa079
Journal - Research Article
Parker, H. A., Jones, H. M., Kaldor, C. D., Hampton, M. B., & Winterbourn, C. C. (2021). Neutrophil NET formation with microbial stimuli requires late stage NADPH oxidase activity. Antioxidants, 10, 1791. doi: 10.3390/antiox10111791
Journal - Research Article
Paumann-Page, M., Kienzl, N. F., Motwani, J., Bathish, B., Paton, L. N., Magon, N. J., … Eccles, M. R., & Winterbourn, C. C. (2021). Peroxidasin protein expression and enzymatic activity in metastatic melanoma cell lines are associated with invasive potential. Redox Biology, 46, 102090. doi: 10.1016/j.redox.2021.102090
Journal - Research Article
Peskin, A. V., & Winterbourn, C. C. (2021). The enigma of 2-Cys peroxiredoxins: What are their roles? Biochemistry (Moscow), 86(1), 84-91. doi: 10.1134/S0006297921010089
Journal - Research Article
Peskin, A. V., Meotti, F. C., Kean, K. M., Göbl, C., Peixoto, A. S., Pace, P. E., … Winterbourn, C. C. (2021). Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2. Journal of Biological Chemistry, 296, 100494. doi: 10.1016/j.jbc.2021.100494
Journal - Research Article
Queiroz, R. F., Stanley, C. P., Wolhuter, K., Kong, S. M. Y., Rajivan, R., McKinnon, N., … Winterbourn, C. C., … Stocker, R. (2021). Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation. Nature Communications, 12, 6626. doi: 10.1038/s41467-021-26991-5
Journal - Research Article
Bathish, B., Paumann-Page, M., Paton, L. N., Kettle, A. J., & Winterbourn, C. C. (2020). Peroxidasin mediates bromination of tyrosine residues in the extracellular matrix. Journal of Biological Chemistry, 295(36), 12697-12705. doi: 10.1074/jbc.RA120.014504
Journal - Research Article
Mohammad, A., Saini, R. V., Kumar, R., Sharma, D., Saini, N. K., Gupta, A., … Winterbourn, C. C., & Saini, A. K. (2020). A curious case of cysteines in human peroxiredoxin I. Redox Biology, 37, 101738. doi: 10.1016/j.redox.2020.101738
Journal - Research Article
O'Connor, K. M., Das, A. B., Winterbourn, C. C., & Hampton, M. B. (2020). Inhibition of DNA methylation in proliferating human lymphoma cells by immune cell oxidants. Journal of Biological Chemistry, 295(23), 7839-7848. doi: 10.1074/jbc.RA120.013092
Journal - Research Article
Peskin, A. V., Meotti, F. C., de Souza, L. F., Anderson, R. F., Winterbourn, C. C., & Salvador, A. (2020). Intra-dimer cooperativity between the active site cysteines during the oxidation of peroxiredoxin 2. Free Radical Biology & Medicine, 158, 115-125. doi: 10.1016/j.freeradbiomed.2020.07.007
Journal - Research Article
Winterbourn, C. C. (2020). Biological chemistry of superoxide radicals. ChemTexts, 6, 7. doi: 10.1007/s40828-019-0101-8
Journal - Research Article
Winterbourn, C. C. (2019). Reactive oxygen species in biological systems. In E. Niki (Ed.), Food chemistry, function and analysis. (pp. 98-117). London, UK: Royal Society of Chemistry. doi: 10.1039/9781788016216-00098
Chapter in Book - Research
Dagnell, M., Cheng, Q., Rizvi, S. H. M., Pace, P. E., Boivin, B., Winterbourn, C. C., & Arnér, E. S. J. (2019). Bicarbonate is essential for protein-tyrosine phosphatase 1B (PTP1B) oxidation and cellular signaling through EGF-triggered phosphorylation cascades. Journal of Biological Chemistry, 294(33), 12330-12338. doi: 10.1074/jbc.RA119.009001
Journal - Research Article
de Souza, L. F., Pearson, A. G., Pace, P. E., Dafre, A. L., Hampton, M. B., Meotti, F. C., & Winterbourn, C. C. (2019). Peroxiredoxin expression and redox status in neutrophils and HL-60 cells. Free Radical Biology & Medicine, 135, 227-234. doi: 10.1016/j.freeradbiomed.2019.03.007
Journal - Research Article
Kumar, R., Mohammad, A., Saini, R. V., Chahal, A., Wong, C.-M., Sharma, D., … Winterbourn, C. C., & Saini, A. K. (2019). Deciphering the in vivo redox behavior of human peroxiredoxins I and II by expressing in budding yeast. Free Radical Biology & Medicine, 145, 321-329. doi: 10.1016/j.freeradbiomed.2019.09.034
Journal - Research Article
Peskin, A. V., Pace, P. E., & Winterbourn, C. C. (2019). Enhanced hyperoxidation of peroxiredoxin 2 and peroxiredoxin 3 in the presence of bicarbonate/CO2. Free Radical Biology & Medicine, 145, 1-7. doi: 10.1016/j.freeradbiomed.2019.09.010
Journal - Research Article
Albrett, A. M., Ashby, L. V., Dickerhof, N., Kettle, A. J., & Winterbourn, C. C. (2018). Heterogeneity of hypochlorous acid production in individual neutrophil phagosomes revealed by a rhodamine-based probe. Journal of Biological Chemistry, 293(40), 15715-15724. doi: 10.1074/jbc.RA118.004789
Journal - Research Article
Bathish, B., Turner, R., Paumann-Page, M., Kettle, A. J., & Winterbourn, C. C. (2018). Characterisation of peroxidasin activity in isolated extracellular matrix and direct detection of hypobromous acid formation. Archives of Biochemistry & Biophysics, 646, 120-127. doi: 10.1016/j.abb.2018.03.038
Journal - Research Article
Coker, M. S., Forbes, L. V., Plowman-Holmes, M., Murdoch, D. R., Winterbourn, C. C., & Kettle, A. J. (2018). Interactions of staphyloxanthin and enterobactin with myeloperoxidase and reactive chlorine species. Archives of Biochemistry & Biophysics, 646, 80-89. doi: 10.1016/j.abb.2018.03.039
Journal - Research Article
Das, A. B., Sadowska-Bartosz, I., Königstorfer, A., Kettle, A. J., & Winterbourn, C. C. (2018). Superoxide dismutase protects ribonucleotide reductase from inactivation in yeast. Free Radical Biology & Medicine, 116, 114-122. doi: 10.1016/j.freeradbiomed.2018.01.001
Journal - Research Article
Pace, P. E., Peskin, A. V., Konigstorfer, A., Jasoni, C. L., Winterbourn, C. C., & Hampton, M. B. (2018). Peroxiredoxin interaction with the cytoskeletal-regulatory protein CRMP2: Investigation of a putative redox relay. Free Radical Biology & Medicine, 129, 383-393. doi: 10.1016/j.freeradbiomed.2018.10.407
Journal - Research Article
Dagnell, M., Pace, P. E., Cheng, Q., Frijhoff, J., Östman, A., Arnér, E. S. J., Hampton, M. B., & Winterbourn, C. C. (2017). Thioredoxin reductase 1 and NADPH directly protect protein tyrosine phosphatase 1B from inactivation during H2O2 exposure. Journal of Biological Chemistry, 292(35), 14371-14380. doi: 10.1074/jbc.M117.793745
Journal - Research Article
Green, J. N., Chapman, A. L. P., Bishop, C. J., Winterbourn, C. C., & Kettle, A. J. (2017). Neutrophil granule proteins generate bactericidal ammonia chloramine on reaction with hydrogen peroxide. Free Radical Biology & Medicine, 113, 363-371. doi: 10.1016/j.freeradbiomed.2017.10.343
Journal - Research Article
Peskin, A. V., & Winterbourn, C. C. (2017). Assay of superoxide dismutase activity in a plate assay using WST-1. Free Radical Biology & Medicine, 103, 188-191. doi: 10.1016/j.freeradbiomed.2016.12.033
Journal - Research Article
Kettle, A. J., & Winterbourn, C. C. (2016). Myeloperoxidase: Structure and function of the green heme peroxidase of neutrophils. In E. Raven & B. Dunford (Eds.), Heme peroxidases. (pp. 272-308). Cambridge, UK: Royal Society of Chemistry. doi: 10.1039/9781782622628-00272
Chapter in Book - Research
Bayer, S. B., Low, F. M., Hampton, M. B., & Winterbourn, C. C. (2016). Interactions between peroxiredoxin 2, hemichrome and the erythrocyte membrane. Free Radical Research, 50(12), 1329-1339. doi: 10.1080/10715762.2016.1241995
Journal - Research Article
Bekeschus, S., Winterbourn, C. C., Kolata, J., Masur, K., Hasse, S., Bröker, B. M., & Parker, H. A. (2016). Neutrophil extracellular trap formation is elicited in response to cold physical plasma. Journal of Leukocyte Biology, 100(4), 791-799. doi: 10.1189/jlb.3A0415-165RR
Journal - Research Article
Peskin, A. V., Pace, P. E., Behring, J. B., Paton, L. N., Soethoudt, M., Bachschmid, M. M., & Winterbourn, C. C. (2016). Glutathionylation of the active site cysteines of peroxiredoxin 2 and recycling by glutaredoxin. Journal of Biological Chemistry, 291(6), 3053-3062. doi: 10.1074/jbc.M115.692798
Journal - Research Article
Poynton, R. A., Peskin, A. V., Haynes, A. C., Lowther, W. T., Hampton, M. B., & Winterbourn, C. C. (2016). Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation. Biochemical Journal, 473, 411-421. doi: 10.1042/bj20150572
Journal - Research Article
Winterbourn, C. C. (2016). Revisiting the reactions of superoxide with glutathione and other thiols. Archives of Biochemistry & Biophysics, 595, 68-71. doi: 10.1016/j.abb.2015.11.028
Journal - Research Article
Winterbourn, C. C., & Peskin, A. V. (2016). Kinetic approaches to measuring peroxiredoxin reactivity. Molecules & Cells, 39(1), 26-30. doi: 10.14348/molcells.2016.2325
Journal - Research Article
Bayer, S. B., Hampton, M. B., & Winterbourn, C. C. (2015). Accumulation of oxidized peroxiredoxin 2 in red blood cells and its prevention. Transfusion, 55(8), 1909-1918. doi: 10.1111/trf.13039
Journal - Research Article
Wilkie-Grantham, R. P., Magon, N. J., Harwood, D. T., Kettle, A. J., Vissers, M. C., Winterbourn, C. C., & Hampton, M. B. (2015). Myeloperoxidase-dependent lipid peroxidation promotes the oxidative modification of cytosolic proteins in phagocytic neutrophils. Journal of Biological Chemistry, 290(15), 9896-9905. doi: 10.1074/jbc.M114.613422
Journal - Research Article
Parker, H. A., Magon, N. J., Green, J. N., Hampton, M. B., & Winterbourn, C. C. (2014). Analysis of neutrophil bactericidal activity. In M. T. Quinn & F. R. DeLeo (Eds.), Neutrophil methods and protocols: Methods in Molecular Biology (Vol. 1124). (2nd ed.) (pp. 291-306). New York, NY: Springer. doi: 10.1007/978-1-62703-845-4_19
Chapter in Book - Research
Bekeschus, S., Kolata, J., Winterbourn, C., Kramer, A., Turner, R., Weltmann, K. D., … Masur, K. (2014). Hydrogen peroxide: A central player in physical plasma-induced oxidative stress in human blood cells. Free Radical Research, 48(5), 542-549. doi: 10.3109/10715762.2014.892937
Journal - Research Article
Cheah, F.-C., Peskin, A. V., Wong, F.-L., Ithnin, A., Othman, A., & Winterbourn, C. C. (2014). Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants. FASEB Journal, 28(7), 3205-3210. doi: 10.1096/fj.14-250050
Journal - Research Article
Das, A. B., Nauser, T., Koppenol, W. H., Kettle, A. J., Winterbourn, C. C., & Nagy, P. (2014). Rapid reaction of superoxide with insulin-tyrosyl radicals to generate a hydroperoxide with subsequent glutathione addition. Free Radical Biology & Medicine, 70, 86-95. doi: 10.1016/j.freeradbiomed.2014.02.006
Journal - Research Article
Green, J. N., Kettle, A. J., & Winterbourn, C. C. (2014). Protein chlorination in neutrophil phagosomes and correlation with bacterial killing. Free Radical Biology & Medicine, 77, 49-56. doi: 10.1016/j.freeradbiomed.2014.08.013
Journal - Research Article
Kasperkiewicz, P., Poreba, M., Snipas, S. J., Parker, H., Winterbourn, C. C., Salvesen, G. S., & Drag, M. (2014). Design of ultrasensitive probes for human neutrophil elastase through hybrid combinatorial substrate library profiling. PNAS, 111(7), 2518-2523. doi: 10.1073/pnas.1318548111
Journal - Research Article
Kettle, A. J., Turner, R., Gangell, C. L., Harwood, D. T., Khalilova, I. S., Chapman, A. L., Winterbourn, C. C., … on behalf of AREST CF. (2014). Oxidation contributes to low glutathione in the airways of children with cystic fibrosis. European Respiratory Journal, 44, 122-129. doi: 10.1183/09031936.00170213
Journal - Research Article
Nedoboy, P., Morgan, P. E., Mocatta, T. J., Richards, A. M., Winterbourn, C. C., & Davies, M. J. (2014). High plasma thiocyanate levels are associated with enhanced myeloperoxidase-induced thiol oxidation and long-term survival in subjects following a first myocardial infarction. Free Radical Research, 48(10), 1256-1266. doi: 10.3109/10715762.2014.947286
Journal - Research Article
Ronsein, G. E., Winterbourn, C. C., Di Mascio, P., & Kettle, A. J. (2014). Cross-linking methionine and amine residues with reactive halogen species. Free Radical Biology & Medicine, 70, 278-287. doi: 10.1016/j.freeradbiomed.2014.01.023
Journal - Research Article
Schwarzländer, M., Wagner, S., Ermakova, Y. G., Belousov, V. V., Radi, R., Beckman, J. S., … Winterbourn, C. C., … Murphy, M. P. (2014). The 'mitoflash' probe cpYFP does not respond to superoxide [Brief communication arising]. Nature, 514(7523), E12-E14. doi: 10.1038/nature13858
Journal - Research Article
Soethoudt, M., Peskin, A. V., Dickerhof, N., Paton, L. N., Pace, P. E., & Winterbourn, C. C. (2014). Interaction of adenanthin with glutathione and thiol enzymes: Selectivity for thioredoxin reductase and inhibition of peroxiredoxin recycling. Free Radical Biology & Medicine, 77, 331-339. doi: 10.1016/j.freeradbiomed.2014.09.025
Journal - Research Article
Winterbourn, C. C. (2014). The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells. Biochimica et Biophysica Acta: General Subjects, 1840(2), 730-738. doi: 10.1016/j.bbagen.2013.05.004
Journal - Research Article
Winterbourn, C. C. (2013). The biological chemistry of hydrogen peroxide. In E. Cadenas & L. Packer (Eds.), Methods in enzymology: Hydrogen peroxide and cell signaling: Part C (Vol. 528). (pp. 3-25). Waltham, MA: Academic Press. doi: 10.1016/B978-0-12-405881-1.00001-X
Chapter in Book - Research
Bayer, S. B., Maghzal, G., Stocker, R., Hampton, M. B., & Winterbourn, C. C. (2013). Neutrophil-mediated oxidation of erythrocyte peroxiredoxin 2 as a potential marker of oxidative stress in inflammation. FASEB Journal, 27(8), 3315-3322. doi: 10.1096/fj.13-227298
Journal - Research Article
Chapman, A. L. P., Mocatta, T. J., Shiva, S., Seidel, A., Chen, B., Khalilova, I., Paumann-Page, M. E., Jameson, G. N. L., Winterbourn, C. C., & Kettle, A. J. (2013). Ceruloplasmin is an endogenous inhibitor of myeloperoxidase. Journal of Biological Chemistry, 288(9), 6465-6477. doi: 10.1074/jbc.M112.418970
Journal - Research Article
Klebanoff, S. J., Kettle, A. J., Rosen, H., Winterbourn, C. C., & Nauseef, W. M. (2013). Myeloperoxidase: A front-line defender against phagocytosed microorganisms. Journal of Leukocyte Biology, 93(2), 185-198. doi: 10.1189/jlb.0712349
Journal - Research Article
Kumar, V., Kleffmann, T., Hampton, M. B., Cannell, M. B., & Winterbourn, C. C. (2013). Redox proteomics of thiol proteins in mouse heart during ischemia/reperfusion using ICAT reagents and mass spectrometry. Free Radical Biology & Medicine, 58, 109-117. doi: 10.1016/j.freeradbiomed.2013.01.021
Journal - Research Article
Pace, P. E., Peskin, A. V., Han, M.-H., Hampton, M. B., & Winterbourn, C. C. (2013). Hyperoxidized peroxiredoxin 2 interacts with the protein disulphide isomerase ERp46. Biochemical Journal, 453, 475-485. doi: 10.1042/BJ20130030
Journal - Research Article
Parker, H., & Winterbourn, C. C. (2013). Reactive oxidants and myeloperoxidase and their involvement in neutrophil extracellular traps. Frontiers in Immunology, 3, 424. doi: 10.3389/fimmu.2012.00424
Journal - Research Article
Peskin, A. V., Dickerhof, N., Poynton, R. A., Paton, L. N., Pace, P. E., Hampton, M. B., & Winterbourn, C. C. (2013). Hyperoxidation of peroxiredoxins 2 and 3: Rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine. Journal of Biological Chemistry, 288, 14170-14177. doi: 10.1074/jbc.M113.460881
Journal - Research Article
Winterbourn, C. C., & Kettle, A. J. (2013). Redox reactions and microbial killing in the neutrophil phagosome. Antioxidants & Redox Signaling, 18(6), 642-660. doi: 10.1089/ars.2012.4827
Journal - Research Article
Winterbourn, C. C. (2012). Biological chemistry of reactive oxygen species. In C. Chatgilialoglu & A. Studer (Eds.), Encyclopedia of radicals in chemistry, biology and materials. (pp. 1259-1281). Chichester, UK: Wiley. doi: 10.1002/9781119953678.rad077
Chapter in Book - Research
Kelso, G. F., Maroz, A., Cochemé, H. M., Logan, A., Prime, T. A., Peskin, A. V., Winterbourn, C. C., James, A. M., … Brooker, S., Porteous, C. M., … Smith, R. A. J. (2012). A mitochondria-targeted macrocyclic Mn(II) superoxide dismutase mimetic. Chemistry & Biology, 19(10), 1237-1246. doi: 10.1016/j.chembiol.2012.08.005
Journal - Research Article
Nagy, P., Lechte, T. P., Das, A. B., & Winterbourn, C. C. (2012). Conjugation of glutathione to oxidized tyrosine residues in peptides and proteins. Journal of Biological Chemistry, 287(31), 26068-26076. doi: 10.1074/jbc.M112.371690
Journal - Research Article
Parker, H., Albrett, A. M., Kettle, A. J., & Winterbourn, C. C. (2012). Myeloperoxidase associated with neutrophil extracellular traps is active and mediates bacterial killing in the presence of hydrogen peroxide. Journal of Leukocyte Biology, 91(3), 369-376. doi: 10.1189/jlb.0711387
Journal - Research Article
Parker, H., Dragunow, M., Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (2012). Requirements for NADPH oxidase and myeloperoxidase in neutrophil extracellular trap formation differ depending on the stimulus. Journal of Leukocyte Biology, 92(4), 841-849. doi: 10.1189/jlb.1211601
Journal - Research Article
Stacey, M. M., Cuddihy, S. L., Hampton, M. B., & Winterbourn, C. C. (2012). Protein thiol oxidation and formation of S-glutathionylated cyclophilin A in cells exposed to chloramines and hypochlorous acid. Archives of Biochemistry & Biophysics, 527(1), 45-54. doi: 10.1016/j.abb.2012.07.011
Journal - Research Article
Stacey, M. M., Vissers, M. C., & Winterbourn, C. C. (2012). Oxidation of 2-Cys peroxiredoxins in human endothelial cells by hydrogen peroxide, hypochlorous acid and chloramines. Antioxidants & Redox Signaling, 17(3), 411-421. doi: 10.1089/ars.2011.4348
Journal - Research Article
Cuddihy, S. L., Winterbourn, C. C., & Hampton, M. B. (2011). Assessment of redox changes to hydrogen peroxide-sensitive proteins during EGF signaling. Antioxidants & Redox Signaling, 15(1), 167-174. doi: 10.1089/ars.2010.3843
Journal - Research Article
Harwood, D. T., Darlow, B. A., Cheah, F. C., McNeill, N., Graham, P., & Winterbourn, C. C. (2011). Biomarkers of neutrophil-mediated glutathione and protein oxidation in tracheal aspirates from preterm infants: Association with bacterial infection. Pediatric Research, 69(1), 28-33. doi: 10.1203/PDR.0b013e3181ff2378
Journal - Research Article
Karton, A., Nagy, P., Betz, A., Peskin, A. V., Pace, P., O'Reilly, R. J., Hampton, M. B., … Winterbourn, C. C. (2011). Model for the exceptional reactivity of peroxiredoxins 2 and 3 with hydrogen peroxide; a kinetic and computational study. Journal of Biological Chemistry, 286(20), 18048-18055. doi: 10.1074/jbc.M111.232355
Journal - Research Article
Kettle, A. J., Maroz, A., Woodroffe, G., Winterbourn, C. C., & Anderson, R. F. (2011). Spectral and kinetic evidence for reaction of superoxide with compound I of myeloperoxidase. Free Radical Biology & Medicine, 51(12), 2190-2194. doi: 10.1016/j.freeradbiomed.2011.09.019
Journal - Research Article
Murphy, M. P., Holmgren, A., Larsson, N.-G., Halliwell, B., Chang, C. J., Kalyanaraman, B., … Winterbourn, C. C. (2011). Unraveling the biological roles of reactive oxygen species. Cell Metabolism, 13(4), 361-366. doi: 10.1016/j.cmet.2011.03.010
Journal - Research Article
Parker, A., Cuddihy, S. L., Son, T. G., Vissers, M. C. M., & Winterbourn, C. C. (2011). Roles of superoxide and myeloperoxidase in ascorbate oxidation in stimulated neutrophils and H2O2-treated HL60 cells. Free Radical Biology & Medicine, 51(7), 1399-1405. doi: 10.1016/j.freeradbiomed.2011.06.029
Journal - Research Article
Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2010). Measuring the redox state of cellular peroxiredoxins by immunoblotting. In E. Cadenas & L. Packer (Eds.), Methods in enzymology: Thiol redox transitions in cell signaling: Part B: Cellular localization and signaling (Vol. 474). (pp. 51-66). San Diego, CA: Academic Press. doi: 10.1016/S0076-6879(10)74004-0
Chapter in Book - Research
Nagy, P., & Winterbourn, C. C. (2010). Redox chemistry of biological thiols. In J. C. Fishbein (Ed.), Advances in molecular toxicology (Vol. 4). (pp. 223-266). Amsterdam, The Netherlands: Elsevier.
Chapter in Book - Research
Cox, A. G., Winterbourn, C. C., & Hampton, M. B. (2010). Mitochondrial peroxiredoxin involvement in antioxidant defence and redox signalling. Biochemical Journal, 425(2), 313-325. doi: 10.1042/BJ20091541
Journal - Research Article
Das, A. B., Nagy, P., Abbott, H. F., Winterbourn, C. C., & Kettle, A. J. (2010). Reactions of superoxide with the myoglobin tyrosyl radical. Free Radical Biology & Medicine, 48, 1540-1547. doi: 10.1016/j.freeradbiomed.2010.02.039
Journal - Research Article
Marshall, C. J., Nallaratnam, M., Mocatta, T., Smyth, D., Richards, M., Elliott, J. M., Blake, J., Winterbourn, C. C., Kettle, A. J., & McClean, D. R. (2010). Factors influencing local and systemic levels of plasma myeloperoxidase in ST-segment elevation acute myocardial infarction. American Journal of Cardiology, 106(3), 316-322. doi: 10.1016/j.amjcard.2010.03.028
Journal - Research Article
Nagy, P., & Winterbourn, C. C. (2010). Rapid reaction of hydrogen sulfide with the neutrophil oxidant hypochlorous acid to generate polysulfides. Chemical Research in Toxicology, 23(10), 1541-1543. doi: 10.1021/tx100266a
Journal - Research Article
Nagy, P., Kettle, A. J., & Winterbourn, C. C. (2010). Neutrophil-mediated oxidation of enkephalins via myeloperoxidase-dependent addition of superoxide. Free Radical Biology & Medicine, 49, 792-799. doi: 10.1016/j.freeradbiomed.2010.05.033
Journal - Research Article
Paton, L. N., Mocatta, T. J., Richards, A. M., & Winterbourn, C. C. (2010). Increased thrombin-induced polymerization of fibrinogen associated with high protein carbonyl levels in plasma from patients post myocardial infarction. Free Radical Biology & Medicine, 48(2), 223-229. doi: 10.1016/j.freeradbiomed.2009.10.044
Journal - Research Article
Peskin, A. V., Cox, A. G., Nagy, P., Morgan, P. E., Hampton, M. B., Davies, M. J., & Winterbourn, C. C. (2010). Removal of amino acid, peptide and protein hydroperoxides by reaction with peroxiredoxins 2 and 3. Biochemical Journal, 432, 313-321. doi: 10.1042/BJ20101156
Journal - Research Article
Ximenes, V. F., Maghzal, G. J., Turner, R., Kato, Y., Winterbourn, C. C., & Kettle, A. J. (2010). Serotonin as a physiological substrate for myeloperoxidase and its superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione. Biochemical Journal, 425(1), 285-293. doi: 10.1042/BJ20090776
Journal - Research Article
Brown, K. K., Blaikie, F. H., Smith, R. A. J., Tyndall, J. D. A., Lue, H., Bernhagen, J., Winterbourn, C. C., & Hampton, M. B. (2009). Direct modification of the proinflammatory cytokine macrophage migration inhibitory factor by dietary isothiocyanates. Journal of Biological Chemistry, 284(47), 32425-32433. doi: 10.1074/jbc.M109.047092
Journal - Research Article
Cox, A. G., Pearson, A. G., Pullar, J. M., Jönsson, T. J., Lowther, W. T., Winterbourn, C. C., & Hampton, M. B. (2009). Mitochondrial peroxiredoxin 3 is more resilient to hyperoxidation than cytoplasmic peroxiredoxins. Biochemical Journal, 421(1), 51-58. doi: 10.1042/BJ20090242
Journal - Research Article
Cox, A. G., Peskin, A. V., Paton, L. N., Winterbourn, C. C., & Hampton, M. B. (2009). Redox potential and peroxide reactivity of human peroxiredoxin 3. Biochemistry, 48(27), 6495-6501. doi: 10.1021/bi900558g
Journal - Research Article
Cuddihy, S. L., Baty, J. W., Brown, K. K., Winterbourn, C. C., & Hampton, M. B. (2009). Proteomic detection of oxidized and reduced thiol proteins in cultured cells. Methods in Molecular Biology, 519, 363-375. doi: 10.1007/978-1-59745-281-6_23
Journal - Research Article
Harwood, D. T., Kettle, A. J., Brennan, S., & Winterbourn, C. C. (2009). Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fluids by isotope dilution liquid chromatography-tandem mass spectrometry. Journal of Chromatography B, 877, 3393-3399. doi: 10.1016/j.jchromb.2009.04.018
Journal - Research Article
Kumar, V., Kitaeff, N., Hampton, M. B., Cannell, M. B., & Winterbourn, C. C. (2009). Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion. FEBS Letters, 583(6), 997-1000. doi: 10.1016/j.febslet.2009.02.018
Journal - Research Article
Nagy, P., Jameson, G. N. L., & Winterbourn, C. C. (2009). Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione. Chemical Research in Toxicology, 22(11), 1833-1840. doi: 10.1021/tx900249d
Journal - Research Article
Nagy, P., Kettle, A. J., & Winterbourn, C. C. (2009). Superoxide-mediated formation of tyrosine hydroperoxides and methionine sulfoxide in peptides through radical addition and intramolecular oxygen transfer. Journal of Biological Chemistry, 284(22), 14723-14733. doi: 10.1074/jbc.M809396200
Journal - Research Article
Palmer, B. R., Devereaux, C. L., Dhamrait, S. S., Mocatta, T. J., Pilbrow, A. P., Frampton, C. M., Skelton, L., Yandle, T. G., Winterbourn, C. C., Richards, A. M., … Cameron, V. A. (2009). The common G-866A polymorphism of the UCP2 gene and survival in diabetic patients following myocardial infarction. Cardiovascular Diabetology, 8. doi: 10.1186/1475-2840-8-31
Journal - Research Article
Peskin, A. V., Turner, R., Maghzal, G. J., Winterbourn, C. C., & Kettle, A. J. (2009). Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils. Biochemistry, 48(42), 10175-10182. doi: 10.1021/bi901266w
Journal - Research Article
Stacey, M. M., Peskin, A. V., Vissers, M. C., & Winterbourn, C. C. (2009). Chloramines and hypochlorous acid oxidize erythrocyte peroxiredoxin 2. Free Radical Biology & Medicine, 47(10), 1468-1476. doi: 10.1016/j.freeradbiomed.2009.08.022
Journal - Research Article
Cuddihy, S. L., Parker, A., Harwood, D. T., Vissers, M. C. M., & Winterbourn, C. C. (2008). Ascorbate interacts with reduced glutathione to scavenge phenoxyl radicals in HL60 cells. Free Radical Biology & Medicine, 44(8), 1637-1644. doi: 10.1016/j.freeradbiomed.2008.01.021
Journal - Research Article
Green, J. N., Winterbourn, C. C., & Hampton, M. B. (2007). Analysis of neutrophil bactericidal activity. In M. T. Quinn, F. R. DeLeo & G. M. Bokoch (Eds.), Neutrophil methods and protocols. (pp. 319-332). Totowa, USA: Humana Press.
Chapter in Book - Research
Hampton, M. B., Baty, J. W., & Winterbourn, C. C. (2006). Use of a proteomic technique to identify oxidant-sensitive thiol proteins in cultured cells. In I. Dalle-Donne, A. Scaloni & D. A. Butterfield (Eds.), Redox Proteomics: From protein modifications to cellular dysfunction and diseases. (pp. 253-265). Hoboken, NJ: John Wiley & Sons.
Chapter in Book - Research
Winterbourn, C. C. (2003). Radical scavenging by thiols: Biological significance and implications for redox signaling and antioxidant defense. In C. Gitler & A. Danon (Eds.), Cellular implications of redox signaling. (pp. 175-190). London: Imperial College Press.
Chapter in Book - Research
Buss, I. H., Winterbourn, C. C., & Armstrong, D. A. (2002). Protein carbonyl measurement by ELISA. In Free Radicals and Antioxidants Protocols, Volume 186, Totowa. (pp. 123-128). Gainsville, Florida: The Humana Press Inc.
Chapter in Book - Research
Winterbourn, C. C., van Dalen, C. J., Hampton, M. B., & Kettle, A. J. (2000). Reactions of myeloperoxidase and production of hypochlorous acid in neutrophil phagosomes. In P. E. Petrides & W. M. Nauseef (Eds.), The Peroxidase Multigene Family of Enzymes. (pp. 58-67). Berlin: Springer.
Chapter in Book - Research
McPherson, K. G., Kettle, A. J., & Winterbourn, C. C. (1997). Mechanism of activation of NFKB by hydrogen peroxide in Jurkat JR cells. In L. Montagnier, R. Olivier & C. Pasquier (Eds.), Oxidative Stress and Redox Regulation: Cellular Signalling, Aids, Cancer and Other Diseases. (pp. 83-87). New York: Marcel Dekker.
Chapter in Book - Research
Kettle, A. J., & Winterbourn, C. C. (1996). Reaction mechanisms of myeloperoxidase. In C. Obinger, U. Burner, R. Ebermann, C. Penel & H. Greppin (Eds.), Plant Peroxidases: Biochemistry and Physiology. (pp. 134-139). Geneva: University of Geneva.
Chapter in Book - Research
Winterbourn, C. C. (1996). Free radicals, oxidants and antioxidants. In R. D. G. Milner (Ed.), Perinatal and Pediatric Pathophysiology: A Clinical Perspective. 2nd edn. (pp. 108-115). London: Edward Arnold.
Chapter in Book - Research