Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases - Wikidata - awgldk - TriplyDB

Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

http://www.wikidata.org/entity/Q27656492

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Inactivation of human myeloperoxidase by hydrogen peroxide Ceruloplasmin: Macromolecular Assemblies with Iron-Containing Acute Phase Proteins Gut Microbiota Conversion of Dietary Ellagic Acid into Bioactive Phytoceutical Urolithin A Inhibits Heme Peroxidases Independent evolution of four heme peroxidase superfamilies Rational drug design applied to myeloperoxidase inhibition.Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation.Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.Heterologous expression and characterization of the manganese-oxidizing protein from Erythrobacter sp. strain SD21.Lactoperoxidase as a potential drug target.Methods for measuring myeloperoxidase activity toward assessing inhibitor efficacy in living systems.Nanoemitters and innate immunity: the role of surfactants and bio-coronas in myeloperoxidase-catalyzed oxidation of pristine single-walled carbon nanotubes.Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated Human Peroxidasin 1 Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.Deglycosylation influences the oxidation activity and antigenicity of myeloperoxidase.Perturbed heme binding is responsible for the blistering phenotype associated with mutations in the Caenorhabditis elegans dual oxidase 1 (DUOX1) peroxidase domain.CO binding and ligand discrimination in human myeloperoxidase A stable bacterial peroxidase with novel halogenating activity and an autocatalytically linked heme prosthetic group Structural stability and heme binding potential of the truncated human dual oxidase 2 (DUOX2) peroxidase domain.How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase.Secreted heme peroxidase from Dictyostelium discoideum: Insights into catalysis, structure, and biological role.Biosynthesis of human myeloperoxidase.

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

http://www.wikidata.org/entity/Q27656492

description

2009 nî lūn-bûn

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2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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JBC.M109.002154

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Journal of Biological Chemistry

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Essential Role of Proximal Histidine-Asparagine Interaction in Mammalian Peroxidases

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Barbara M Calisto

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Johanna Stampler

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Klarissa Schroettner

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Xavier Carpena

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P2860

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

Comparison of simple potential functions for simulating liquid water

Processing of X-ray diffraction data collected in oscillation mode

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

Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution

X-ray crystal structure of canine myeloperoxidase at 3 A resolution

Crystal structure of lactoperoxidase at 2.4 A resolution

Scalable molecular dynamics with NAMD

A new technique for the assay of infectivity of human adenovirus 5 DNA

Refinement of macromolecular structures by the maximum-likelihood method

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