Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases. - Wikidata - awgldk - TriplyDB

Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

http://www.wikidata.org/entity/Q35167515

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Lactoperoxidase as a potential drug target.Chemistry and Biology in the Biosynthesis and Action of Thyroid Hormones.Chemie und Biologie der Schilddrüsenhormon-Biosynthese und -Wirkung

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P2860

Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

http://www.wikidata.org/entity/Q35167515

description

2015 nî lūn-bûn

@nan

2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի փետրվարին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

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Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

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type

label

Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

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Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

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prefLabel

Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

@ast

Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

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Acta crystallographica. Section F, Structural biology communications

P1476

Mode of binding of the antithyroid drug propylthiouracil to mammalian haem peroxidases.

@en

P2093

A K Singh

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A Singh

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G S Kushwaha

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P Kaur

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R P Singh

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S Sharma

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T P Singh

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

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

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Inhibition of Lactoperoxidase by Its Own Catalytic Product: Crystal Structure of the Hypothiocyanate-Inhibited Bovine Lactoperoxidase at 2.3-Å Resolution

Structural Evidence of Substrate Specificity in Mammalian Peroxidases: STRUCTURE OF THE THIOCYANATE COMPLEX WITH LACTOPEROXIDASE AND ITS INTERACTIONS AT 2.4 A RESOLUTION

Binding Modes of Aromatic Ligands to Mammalian Heme Peroxidases with Associated Functional Implications: CRYSTAL STRUCTURES OF LACTOPEROXIDASE COMPLEXES WITH ACETYLSALICYLIC ACID, SALICYLHYDROXAMIC ACID, AND BENZYLHYDROXAMIC ACID

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First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases

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304-310

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scholarly article

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10.1107/S2053230X15001806

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Pt 3

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71

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2015-02-19T00:00:00Z

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25760705

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4356306

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