Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center. - Wikidata - awgldk - TriplyDB

Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

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Prolyl 4-Hydroxylase: Substrate Isosteres in Which an (E)- or (Z)-Alkene Replaces the Prolyl Peptide Bond.

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Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

http://www.wikidata.org/entity/Q37479020

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article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 16 May 2016

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vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

@en

Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

@nl

type

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Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

@en

Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

@nl

prefLabel

Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

@en

Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

@nl

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ACS.BIOCHEM.6B00251

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Human Collagen Prolyl 4-Hydroxylase Is Activated by Ligands for Its Iron Center.

@en

P2093

James D Vasta

http://www.w3.org/2001/XMLSchema#string

P2860

Collagen structure and stability

Prolyl 4-hydroxylase

Decarboxylation of alpha-ketoglutarate coupled to collagen proline hydroxylase

The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen

FeII/alpha-ketoglutarate-dependent hydroxylases and related enzymes

Prolyl 4-hydroxylase activity in relation to the oxidation state of enzyme-bound iron. The role of ascorbate in peptidyl proline hydroxylation

Stoicheiometry and kinetics of the prolyl 4-hydroxylase partial reaction

Loss of assembly of the main basement membrane collagen, type IV, but not fibril-forming collagens and embryonic death in collagen prolyl 4-hydroxylase I null mice

Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans

Enzymatic assembly of overlapping DNA fragments.

P304

3224-3233

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scholarly article

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10.1021/ACS.BIOCHEM.6B00251

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23

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55

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Ronald T Raines

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2016-05-16T00:00:00Z

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27183028

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5141248

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