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Cooper, CE and Silkstone, GGA and Simons, M and Rajagopal, B and Syrett, N and Shaik, T and Gretton, S and Welbourn, E and Bülow, L and Eriksson, NL and Ronda, L and Mozzarelli, A and Eke, A and Mathe, D and Reeder, BJ (2019) Engineering tyrosine residues into hemoglobin enhances heme reduction, decreases oxidative stress and increases vascular retention of a hemoglobin based blood substitute. Free Radical Biology and Medicine, 134. pp. 106-118. DOI https://doi.org/10.1016/j.freeradbiomed.2018.12.030
Alomari, EAM and Ronda, L and Bruno, S and Paredi, G and Marchetti, M and Bettati, S and Olivari, D and Fumagalli, F and Novelli, D and Ristagno, G and Latini, R and Cooper, CE and Reeder, BJ and Mozzarelli, A (2018) High- and low-affinity PEGylated hemoglobin-based oxygen carriers: differential oxidative stress in a Guinea pig transfusion model. Free Radical Biology and Medicine, 124. pp. 299-310. DOI https://doi.org/10.1016/j.freeradbiomed.2018.06.018
Mullineaux, PM and Exposito-Rodriguez, M and Laissue, PP and Smirnoff, N (2018) ROS-dependent signaling pathways in plants and algae exposed to high light: Comparisons with other eukaryotes. Free Radical Biology and Medicine, 122. pp. 52-64. DOI https://doi.org/10.1016/j.freeradbiomed.2018.01.033
Welbourn, Elizabeth M and Wilson, Michael T and Yusof, Ashril and Metodiev, Metodi V and Cooper, Chris E (2017) The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane. Free Radical Biology and Medicine, 103. pp. 95-106. DOI https://doi.org/10.1016/j.freeradbiomed.2016.12.024
Tomalin, Lewis Elwood and Day, Alison Michelle and Underwood, Zoe Elizabeth and Smith, Graham Robert and Dalle Pezze, Piero and Rallis, Charalampos and Patel, Waseema and Dickinson, Bryan Craig and Bähler, Jürg and Brewer, Thomas Francis and Chang, Christopher Joh-Leung and Shanley, Daryl Pierson and Veal, Elizabeth Ann (2016) Increasing extracellular H₂O₂ produces a bi-phasic response in intracellular H₂O₂, with peroxiredoxin hyperoxidation only triggered once the cellular H₂O₂-buffering capacity is overwhelmed. Free Radical Biology and Medicine, 95. pp. 333-348. DOI https://doi.org/10.1016/j.freeradbiomed.2016.02.035
Kadiiska, Maria B and Basu, Samar and Brot, Nathan and Cooper, Christopher and Saari Csallany, A and Davies, Michael J and George, Magdalene M and Murray, Dennis M and Jackson Roberts, L and Shigenaga, Mark K and Sohal, Rajindar S and Stocker, Roland and Van Thiel, David H and Wiswedel, Ingrid and Hatch, Gary E and Mason, Ronald P (2013) Biomarkers of oxidative stress study V: Ozone exposure of rats and its effect on lipids, proteins, and DNA in plasma and urine. Free Radical Biology and Medicine, 61. pp. 408-415. DOI https://doi.org/10.1016/j.freeradbiomed.2013.04.023
Reeder, Brandon J and Hider, Robert C and Wilson, Michael T (2008) Iron chelators can protect against oxidative stress through ferryl heme reduction. Free Radical Biology and Medicine, 44 (3). pp. 264-273. DOI https://doi.org/10.1016/j.freeradbiomed.2007.08.006
Reeder, Brandon J and Cutruzzola, Francesca and Bigotti, Maria Giulia and Hider, Robert C and Wilson, Michael T (2008) Tyrosine as a redox-active center in electron transfer to ferryl heme in globins. Free Radical Biology and Medicine, 44 (3). pp. 274-283. DOI https://doi.org/10.1016/j.freeradbiomed.2007.06.030
Lam, Ernest WN and Zwacka, Ralf and Seftor, Elizabeth A and Nieva, Daniel RC and Davidson, Beverly L and Engelhardt, John F and Hendrix, Mary JC and Oberley, Larry W (1999) Effects of antioxidant enzyme overexpression on the invasive phenotype of hamster cheek pouch carcinoma cells. Free Radical Biology and Medicine, 27 (5-6). pp. 572-579. DOI https://doi.org/10.1016/s0891-5849(99)00109-4