Inhibition of lipid peroxidation by the iron-binding protein lactoferrin. - Wikidata - wikimedia - TriplyDB

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

http://www.wikidata.org/entity/Q46596924

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Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation How neutrophils kill microbes Desferrioxamine decreases NAD redox potential of intact red blood cells: evidence for desferrioxamine as an inducer of oxidant stress in red blood cells NADPH oxidases as electrochemical generators to produce ion fluxes and turgor in fungi, plants and humans Effect of a specific iron chelating agent on animal models of inflammation Identification of unprecedented anticancer properties of high molecular weight biomacromolecular complex containing bovine lactoferrin (HMW-bLf)Dietary lactoferrin alleviates age-related lacrimal gland dysfunction in mice Oxygen toxicity, oxygen radicals, transition metals and disease Evidence for role of hydroxyl radical in complement and neutrophil-dependent tissue injury.Inhibition of iron/ascorbate-induced lipid peroxidation by an N-terminal peptide of bovine lactoferrin and its acylated derivatives.Pseudomonas and neutrophil products modify transferrin and lactoferrin to create conditions that favor hydroxyl radical formation.Protease-cleaved iron-transferrin augments oxidant-mediated endothelial cell injury via hydroxyl radical formation.Iron, radiation, and cancer Iron, lipocalin, and kidney epithelia.The NADPH oxidase of professional phagocytes--prototype of the NOX electron transport chain systems.Lactotransferrin immunocytochemistry in Alzheimer and normal human brain.The role of recombinant proteins in the development of serum-free media.Transient iron overload with bleomycin detectable iron in the plasma of patients with adult respiratory distress syndrome.The function of the NADPH oxidase of phagocytes and its relationship to other NOXs in plants, invertebrates, and mammals.Expression and localization of lactotransferrin messenger RNA in the cortex of Alzheimer's disease.Radioprotection of mice by lactoferrin against irradiation with sublethal X-rays Growth inhibition of Plasmodium falciparum involving carbon centered iron-chelate radical (L., X-)-Fe(III) based on pyridoxal-betaine. A novel type of antimalarials active against chloroquine-resistant parasites.The molecular and cellular pathology of chronic granulomatous disease.Novel alginate-enclosed chitosan-calcium phosphate-loaded iron-saturated bovine lactoferrin nanocarriers for oral delivery in colon cancer therapy.An iron-messenger system--a hypothesis.Protease cleavage of iron-transferrin augments pyocyanin-mediated endothelial cell injury via promotion of hydroxyl radical formation.Effects of iron-unsaturated human lactoferrin on hydrogen peroxide-induced oxidative damage in intestinal epithelial cells.Role of free radicals and antioxidants in the pathogenesis of the inflammatory periodontal diseases.Myeloperoxidase as an effective inhibitor of hydroxyl radical production. Implications for the oxidative reactions of neutrophils.Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases.Mechanism of metallothionein gene regulation by heme-hemopexin. Roles of protein kinase C, reactive oxygen species, and cis-acting elements.Reactive oxygen species and antioxidants in inflammatory diseases.Lactoferrin is a survival factor for neutrophils in rheumatoid synovial fluid.Neutrophil degranulation inhibits potential hydroxyl-radical formation. Relative impact of myeloperoxidase and lactoferrin release on hydroxyl-radical production by iron-supplemented neutrophils assessed by spin-trapping techniques.Prooxidant activity of transferrin and lactoferrin.Evidence for a role of hydroxyl radical in immune-complex-induced vasculitis.The resistance of transferrin, lactoferrin and caeruloplasmin to oxidative damage.The superoxide-dependent transfer of iron from ferritin to transferrin and lactoferrin.Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Are lactoferrin and transferrin promoters of hydroxyl-radical generation?Lactoferrin-catalysed hydroxyl radical production. Additional requirement for a chelating agent.

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P2860

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

http://www.wikidata.org/entity/Q46596924

description

1981 nî lūn-bûn

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1981年の論文

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1981年学术文章

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1981年学术文章

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1981年学术文章

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1981年学术文章

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1981年学术文章

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1981年学术文章

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1981年學術文章

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1981年學術文章

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name

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

@en

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

@nl

type

label

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

@en

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

@nl

prefLabel

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

@en

Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

@nl

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Inhibition of lipid peroxidation by the iron-binding protein lactoferrin.

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Gutteridge JM

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Halliwell B

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Paterson SK

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Segal AW

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P2860

Lactoferrin deficiency as a consequence of a lack of specific granules in neutrophils from a patient with recurrent infections. Detection by immunoperoxidase staining for lactoferrin and cytochemical electron microscopy.

Oxygen-dependent microbial killing by phagocytes (first of two parts).

Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions, and an enzymatic generating system.

The role of lactoferrin in the bactericidal function of polymorphonuclear leucocytes.

Evidence for superoxide-dependent reduction of Fe3+ and its role in enzyme-generated hydroxyl radical formation.

The production of hydroxyl and superoxide radicals by stimulated human neutrophils- measurements by EPR spectroscopy.

Inhibition of the iron-catalysed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine.

Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Detection of 'free' iron in biological systems by using bleomycin-dependent degradation of DNA.

The measurement of malondialdehyde in peroxidised ox-brain phospholipid liposomes.

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