X-ray crystal structure of canine myeloperoxidase at 3 A resolution
about
Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phoxIdentification and characterization of VPO1, a new animal heme-containing peroxidaseHereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defectPeroxidasin: a novel enzyme-matrix protein of Drosophila developmentX-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolutionInhibition of Lactoperoxidase by Its Own Catalytic Product: Crystal Structure of the Hypothiocyanate-Inhibited Bovine Lactoperoxidase at 2.3-Å ResolutionBinding Modes of Aromatic Ligands to Mammalian Heme Peroxidases with Associated Functional Implications: CRYSTAL STRUCTURES OF LACTOPEROXIDASE COMPLEXES WITH ACETYLSALICYLIC ACID, SALICYLHYDROXAMIC ACID, AND BENZYLHYDROXAMIC ACIDEssential Role of Proximal Histidine-Asparagine Interaction in Mammalian PeroxidasesMode of Binding of the Tuberculosis Prodrug Isoniazid to Heme Peroxidases: BINDING STUDIES AND CRYSTAL STRUCTURE OF BOVINE LACTOPEROXIDASE WITH ISONIAZID AT 2.7 A RESOLUTIONAutoimmune response to the thyroid in humans: thyroid peroxidase--the common autoantigenic denominatorCovalently linked heme in cytochrome p4504a fatty acid hydroxylasesCalreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidaseNitric oxide is a physiological substrate for mammalian peroxidasesThe roles of myeloperoxidase in coronary artery disease and its potential implication in plaque rupture.Rational drug design applied to myeloperoxidase inhibition.Identification and characterization of a cyclooxygenase-like enzyme from Entamoeba histolyticaDetermination of the carbohydrate composition and the disulfide bond linkages of bovine lactoperoxidase by mass spectrometry.Spin trapping and protein cross-linking of the lactoperoxidase protein radical.Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase.Characterization of the heme environment in Arabidopsis thaliana fatty acid alpha-dioxygenase-1Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.Purification and characterization of chorion peroxidase from Aedes aegypti eggsHeme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties.Impact of missense mutations on biosynthesis of myeloperoxidase.Myeloperoxidase-derived oxidation: mechanisms of biological damage and its preventionHeterologous expression and characterization of the manganese-oxidizing protein from Erythrobacter sp. strain SD21.Epitope analysis of anti-myeloperoxidase antibodies in patients with ANCA-associated vasculitis.Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.Disruption of heme-peptide covalent cross-linking in mammalian peroxidases by hypochlorous acid.T47D Cells Expressing Myeloperoxidase Are Able to Process, Traffic and Store the Mature Protein in Lysosomes: Studies in T47D Cells Reveal a Role for Cys319 in MPO Biosynthesis that Precedes Its Known Role in Inter-Molecular Disulfide Bond FormationFrom phosphatases to vanadium peroxidases: a similar architecture of the active site.Proconvertase proteolytic processing of an enzymatically active myeloperoxidase precursorMolecular evolution of enzymes involved in the arachidonic acid cascade.Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins.Resonance Raman microspectroscopic characterization of eosinophil peroxidase in human eosinophilic granulocytesMyeloperoxidase: a target for new drug development?Dual binding mode of antithyroid drug methimazole to mammalian heme peroxidases - structural determination of the lactoperoxidase-methimazole complex at 1.97 Å resolutionDuox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation.A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation.Thirty years of heme peroxidase structural biology.
P2860
Q24291589-3F074BD5-0A08-4CB5-8F9E-3721238E233EQ24324211-1606BB7C-52DB-4CDF-BAA2-278936AADB79Q24564183-E1C24FD8-9D0E-4336-926A-2106C5538EAFQ24594709-F9FAE0DA-1F1C-475F-B18E-A45609B14E3EQ27622235-31294E2F-E146-4225-9850-C8F5AD16FE6BQ27653510-6F52935C-2AAA-4A90-90CE-1008790E9C41Q27655586-DB073992-444E-45CB-A30F-8252AC67F127Q27656492-83B13725-6057-4FB6-8DBF-DFAE31FA2630Q27658143-C2FC5D56-135D-4B5B-AB81-E525F9423D0CQ28140998-05FA23EE-21DA-4ABC-B203-DB35CF73269BQ28141678-D10596C7-3A4B-4A72-9ED5-15292CB53513Q28610241-15131D37-3024-44E6-8558-3CC574B3B20FQ28645799-BABB78CA-4A21-45FE-8EE5-E2711DC3BAFAQ30240734-3E6FA5B1-8AB9-4948-BF35-F74CD5B4182DQ30372838-94B41022-1A7F-4EA3-A00D-71626D5859ABQ30449610-C4E57C0D-B4AC-4FAF-9037-7DC65251CCE1Q30644409-67D2719A-19DE-4F7C-A69D-3EDF76CB3026Q30822622-AB541680-00AC-4EA0-BBA1-609DC58F1AF9Q33818264-5F1D4805-54D9-4248-9A39-E116A4785B82Q33820133-437E01DB-5069-439C-905F-879C40414CE1Q33855320-C870D840-E384-49DF-AC62-617A726AE2EDQ33892527-C09A8EEA-3759-42B6-A8D7-771DAAB8C148Q34004418-3EDCA89F-3A59-4068-9BA6-E6FB718D40FDQ34037721-DEA1F385-7070-40FF-B724-6F6A07313E8FQ34162955-76B55E19-3DC9-451F-9C9F-C97DE68D2B3FQ34594407-B269C294-2DEF-45DA-AD48-5887EE518895Q34663785-0D87DF17-4CF4-469F-8A0F-893D76954255Q35167515-E77C8C86-E604-4180-BDFD-E894A7BE2739Q35668057-4448877D-A98E-4514-B2F7-2C459863E4D6Q35927277-D8619B32-7101-48C0-92DD-B0B7E301FB6EQ36033031-34F5904E-D696-4017-877A-382BA57C7633Q36282271-6C7D5464-28B4-41CB-969A-43B6D766EEA8Q36627002-D3FA551B-0E32-45CB-BEE2-D4E37BEDAB14Q36666229-CFD8338B-F72C-4AF6-B1C9-4EDA689976B6Q36722607-B6E1AEF9-8402-429C-A635-6130790B4902Q36860606-A533CC02-C1B3-43FA-9586-50815FCA1B01Q37063823-9B74A03C-B632-4BEA-A758-85FD846B7C54Q37139797-EE48D8B7-1591-494A-8398-3AFD695F444DQ37383836-5EAC5D9E-F066-45DD-BE27-22EC4230BD85Q37703495-C0B1FEAC-435B-46F1-97A5-0CC1CBF584A9
P2860
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
description
1992 nî lūn-bûn
@nan
1992 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
name
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@ast
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@en
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@nl
type
label
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@ast
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@en
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@nl
prefLabel
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@ast
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@en
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@nl
P3181
P1476
X-ray crystal structure of canine myeloperoxidase at 3 A resolution
@en
P2093
P304
P3181
P356
10.1016/0022-2836(92)90133-5
P407
P577
1992-07-05T00:00:00Z