PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9668540-4 1998 The toxicity of NTPI is much higher than of transferrin-iron as judged by its ability to promote hydroxyl radical formation resulting in peroxidative damage to membrane lipids and proteins. Hydroxyl Radical 97-113 transferrin Homo sapiens 44-55 11380478-1 2001 Hydroxyl radical formation catalysed by non-transferrin-bound iron (NTBI) might contribute to transplantation-related complications. Hydroxyl Radical 0-16 transferrin Homo sapiens 44-55 7769095-0 1995 Protease-cleaved iron-transferrin augments oxidant-mediated endothelial cell injury via hydroxyl radical formation. Hydroxyl Radical 88-104 transferrin Homo sapiens 22-33 7769095-1 1995 Previous work has shown that the Pseudomonas-derived protease, pseudomonas elastase (PAE), can modify transferrin to form iron complexes capable of catalyzing the formation of hydroxyl radical (.OH) from neutrophil (PMN)-derived superoxide (.O2-) and hydrogen peroxide (H2O2). Hydroxyl Radical 176-192 transferrin Homo sapiens 102-113 8225581-3 1993 This cleavage also generates new iron chelates which, in contrast to iron bound to transferrin, are able to catalyze formation of the highly cytotoxic hydroxyl radical from neutrophil-derived superoxide and hydrogen peroxide via the Haber-Weiss reaction. Hydroxyl Radical 151-167 transferrin Homo sapiens 83-94 34310960-6 2021 Then H2O2 not only damaged structure of Tf to release Fe3+, but also was converted to hydroxyl radicals via ferric ions mediated Fenton reaction for ferroptosis. Hydroxyl Radical 86-103 transferrin Homo sapiens 40-42 1991211-7 1991 The results are discussed in the light of earlier suggestions that the TfC2 subtype confers an increased risk of cellular damage by enhancing hydroxyl radical formation, although it is possible that there exists a genetic linkage of Tf variant to some other locus which is influencing susceptibility to RA. Hydroxyl Radical 142-158 transferrin Homo sapiens 71-73 26549031-5 2016 The hydroxyl radical, which is produced in a Fenton reaction catalyzed by an iron ion, serves as a potent DNA-DSB-inducing molecule, raising the potential of an iron ion transporter of transferrin in the formation of DNA-DSBs. Hydroxyl Radical 4-20 transferrin Homo sapiens 185-196 3157637-5 1985 Since transferrin (iron) is known to catalyze the formation of hydroxyl radicals we hypothesize that the Tf C2 variant is more efficient in promoting radical formation and thereby cell damage. Hydroxyl Radical 63-80 transferrin Homo sapiens 6-17 6092375-0 1984 The effect of human serum transferrin and milk lactoferrin on hydroxyl radical formation from superoxide and hydrogen peroxide. Hydroxyl Radical 62-78 transferrin Homo sapiens 26-37 6092375-4 1984 Partially saturated transferrin and lactoferrin present in normal subjects may protect cells from damage by binding iron that might catalyze hydroxyl radical formation from superoxide and hydrogen peroxide. Hydroxyl Radical 141-157 transferrin Homo sapiens 20-31 6305716-0 1983 Superoxide-dependent formation of hydroxyl radical catalyzed by transferrin. Hydroxyl Radical 34-50 transferrin Homo sapiens 64-75 6305716-1 1983 Hydroxyl radicals are generated in the hypoxanthine-xanthine oxidase system in the presence of iron-saturated transferrin isolated from human serum. Hydroxyl Radical 0-17 transferrin Homo sapiens 110-121 3032157-1 1987 Are lactoferrin and transferrin promoters of hydroxyl-radical generation? Hydroxyl Radical 45-61 transferrin Homo sapiens 20-31 3032157-2 1987 Apo-lactoferrin and apo-transferrin protect against iron-ion-dependent hydroxyl-radical (.OH) generation from H2O2 in the presence of superoxide radicals or ascorbic acid at pH 7.4, whether the necessary iron is added as ionic iron or as ferritin. Hydroxyl Radical 71-87 transferrin Homo sapiens 24-35 26988468-5 2016 Apo-transferrin increased the formation of hydroxyl radicals and this related with a faster degradation of beta-glucan. Hydroxyl Radical 43-60 transferrin Homo sapiens 4-15 26432959-2 2015 Herein, we have reported the interaction of three different biological macromolecules such as hemoglobin, gamma globulin and transferrin with hydroxyl group functionalized Multi-Walled Carbon Nanotubes (OH-MWCNTs). Hydroxyl Radical 142-150 transferrin Homo sapiens 125-136 12020627-2 2002 Transferrin has also been proposed as a mediator of tubular toxicity because the reabsorption of transferrin results in the release of reactive iron in proximal tubular cells, promoting the formation of hydroxyl radicals. Hydroxyl Radical 203-220 transferrin Homo sapiens 0-11 12020627-2 2002 Transferrin has also been proposed as a mediator of tubular toxicity because the reabsorption of transferrin results in the release of reactive iron in proximal tubular cells, promoting the formation of hydroxyl radicals. Hydroxyl Radical 203-220 transferrin Homo sapiens 97-108 11958437-5 2002 Hydrogen peroxide possibly converted to hydroxyl radical by iron due to lower transferrin level might have led to increased serum lipid peroxidation in patients with rheumatoid arthritis. Hydroxyl Radical 40-56 transferrin Homo sapiens 78-89 15271890-0 2004 Cleavage of human transferrin by Porphyromonas gingivalis gingipains promotes growth and formation of hydroxyl radicals. Hydroxyl Radical 102-119 transferrin Homo sapiens 18-29 15271890-2 2004 The aims of this study were to investigate the degradation of human transferrin by gingipain cysteine proteinases of P. gingivalis and to demonstrate the production of toxic hydroxyl radicals (HO*) catalyzed by the iron-containing transferrin fragments generated or by release of iron itself. Hydroxyl Radical 174-191 transferrin Homo sapiens 68-79 15271890-2 2004 The aims of this study were to investigate the degradation of human transferrin by gingipain cysteine proteinases of P. gingivalis and to demonstrate the production of toxic hydroxyl radicals (HO*) catalyzed by the iron-containing transferrin fragments generated or by release of iron itself. Hydroxyl Radical 174-191 transferrin Homo sapiens 231-242 14580189-3 2003 We used hydroxyl radical-mediated protein footprinting and mass spectrometry to reveal the conformational changes that occur upon complex formation for the human transferrin C-lobe (residues 334-679) bound to the ectodomain of human transferrin receptor 1 (residues 121-760). Hydroxyl Radical 8-24 transferrin Homo sapiens 162-173 14580189-3 2003 We used hydroxyl radical-mediated protein footprinting and mass spectrometry to reveal the conformational changes that occur upon complex formation for the human transferrin C-lobe (residues 334-679) bound to the ectodomain of human transferrin receptor 1 (residues 121-760). Hydroxyl Radical 8-24 transferrin Homo sapiens 233-244