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Brandon J. Reeder
Researcher at University of Essex
Publications - 64
Citations - 3183
Brandon J. Reeder is an academic researcher from University of Essex. The author has contributed to research in topics: Heme & Myoglobin. The author has an hindex of 26, co-authored 61 publications receiving 2854 citations. Previous affiliations of Brandon J. Reeder include North Carolina State University.
Papers
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Journal ArticleDOI
Imaging the production of singlet oxygen in vivo using a new fluorescent sensor, Singlet Oxygen Sensor Green®
Cristina Flors,Michael J. Fryer,Jen Waring,Brandon J. Reeder,Ulrike Bechtold,Philip M. Mullineaux,Santi Nonell,Michael T. Wilson,Neil R. Baker +8 more
TL;DR: SOSG is a useful in vivo probe for the detection of singlet oxygen, which is thought to have a very short half-life in biological systems and, consequently, it is difficult to detect.
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A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure.
Kevin P. Moore,Steve Holt,Rakesh P. Patel,Dimitri A. Svistunenko,William E. Zackert,David Goodier,Brandon J. Reeder,Martine Clozel,Radhi Anand,Chris E. Cooper,Jason D. Morrow,Michael T. Wilson,Victor M. Darley-Usmar,L. Jackson Roberts +13 more
TL;DR: Data strongly support a causative role for oxidative injury in the renal failure of rhabdomyolysis and suggest that the protective effect of alkalinization may be attributed to inhibition of myoglobin-induced lipid peroxidation.
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The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms
TL;DR: The functions of various globins and the mechanisms by which these globins act as redox enzymes under physiologic conditions are examined and evidence that redox reactions also occur under disease conditions, leading to pathologic complications, is examined.
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The radical and redox chemistry of myoglobin and hemoglobin: from in vitro studies to human pathology
TL;DR: This review focuses on the peroxide-induced formation of radicals, their assignment to specific protein residues, and the pseudoperoxidase and prooxidant activities of the heme proteins.
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Hemoglobin and myoglobin associated oxidative stress: from molecular mechanisms to disease States.
TL;DR: Evidence that peroxidase-like enzymic activity, in which a catalytic cycle, driven by peroxides, leads to oxidation of bio molecules, occurs in vivo is reviewed and the role of iron chelators such as desferrioxamine is discussed in terms of their often neglected properties as reducing agents.