Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
about
Neutrophil myeloperoxidase and its substrates: formation of specific markers and reactive compounds during inflammationInhibition of myeloperoxidase: evaluation of 2H-indazoles and 1H-indazolones.Myeloperoxidase Enhances Etoposide and Mitoxantrone-Mediated DNA Damage: A Target for Myeloprotection in Cancer ChemotherapyRole 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 FragmentsMyeloperoxidase-Hepatocyte-Stellate Cell Cross Talk Promotes Hepatocyte Injury and Fibrosis in Experimental Nonalcoholic SteatohepatitisPosttranslational 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.
P2860
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P2860
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
description
2013 nî lūn-bûn
@nan
2013 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@ast
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@en
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@nl
type
label
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@ast
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@en
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@nl
prefLabel
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@ast
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@en
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@nl
P2093
P2860
P356
P1476
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates
@en
P2093
Anthony J Kettle
David Laughton
David W Jenkins
Françoise Auchère
Garry Pairaudeau
Håkan Eriksson
John F Unitt
Louisa V Forbes
Paul Hemsley
P2860
P304
P356
10.1074/JBC.M113.507756
P407
P577
2013-12-20T00:00:00Z