Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates - Wikidata - wikimedia - TriplyDB

Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

http://www.wikidata.org/entity/Q27680535

about

Neutrophil myeloperoxidase and its substrates: formation of specific markers and reactive compounds during inflammation Inhibition of myeloperoxidase: evaluation of 2H-indazoles and 1H-indazolones.Myeloperoxidase Enhances Etoposide and Mitoxantrone-Mediated DNA Damage: A Target for Myeloprotection in Cancer Chemotherapy Role of the Vanins-Myeloperoxidase Axis in Colorectal Carcinogenesis.Ordered cleavage of myeloperoxidase ester bonds releases active site heme leading to inactivation of myeloperoxidase by benzoic acid hydrazide analogs.ESR and X-ray Structure Investigations on the Binding and Mechanism of Inhibition of the Native State of Myeloperoxidase with Low Molecular Weight Fragments Myeloperoxidase-Hepatocyte-Stellate Cell Cross Talk Promotes Hepatocyte Injury and Fibrosis in Experimental Nonalcoholic Steatohepatitis Posttranslational protein modifications by reactive nitrogen and chlorine species and strategies for their prevention and elimination.Lactoperoxidase as a potential drug target.Methods for measuring myeloperoxidase activity toward assessing inhibitor efficacy in living systems.Characterization of chemical features of potent myeloperoxidase inhibitors.Potential roles of myeloperoxidase and hypochlorous acid in metabolism and toxicity of alkene hydrocarbons and drug molecules containing olefinic moieties.Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.Thioxo-dihydroquinazolin-one Compounds as Novel Inhibitors of Myeloperoxidase.Myeloperoxidase Inhibition Increases Neurogenesis after Ischemic Stroke.Redox Regulation of Inflammatory Processes Is Enzymatically Controlled.Baccharis dracunculifolia DC (Asteraceae) selectively modulates the effector functions of human neutrophils.Comparison of metabolic profiles and bioactivities of the leaves of three edible Congolese Hibiscus species.Design of anti-thyroid drugs: Binding studies and structure determination of the complex of lactoperoxidase with 2-mercaptoimidazole at 2.30 Å resolution.

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

http://www.wikidata.org/entity/Q27680535

description

2013 nî lūn-bûn

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2013 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2013 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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JBC.M113.507756

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Journal of Biological Chemistry

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Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates

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Anthony J Kettle

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Bob Thong

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David Laughton

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David W Jenkins

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Françoise Auchère

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Garry Pairaudeau

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Håkan Eriksson

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John F Unitt

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Louisa V Forbes

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Paul Hemsley

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P2860

Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide

Improved methods for building protein models in electron density maps and the location of errors in these models

Isolation of mononuclear cells and granulocytes from human blood. Isolation of monuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g

X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution

Crystal structure of lactoperoxidase at 2.4 A resolution

2-Thioxanthines Are Mechanism-based Inactivators of Myeloperoxidase That Block Oxidative Stress during Inflammation

Integration of macromolecular diffraction data

The CCP4 suite: programs for protein crystallography

Inhibition of myeloperoxidase by benzoic acid hydrazides

Inhibition of myeloperoxidase-mediated hypochlorous acid production by nitroxides

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10.1074/JBC.M113.507756

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51

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