N-acylethanolamines as novel alcohol dehydrogenase 3 substrates. - Wikidata - wikimedia - TriplyDB

N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

http://www.wikidata.org/entity/Q34538297

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Primary fatty acid amide metabolism: conversion of fatty acids and an ethanolamine in N18TG2 and SCP cells Glycine N-acyltransferase-like 3 is responsible for long-chain N-acylglycine formation in N18TG2 cells.N-FATTY ACYLGLYCINES: UNDERAPPRECIATED ENDOCANNABINOID-LIKE FATTY ACID AMIDES?

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N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

http://www.wikidata.org/entity/Q34538297

description

2010 nî lūn-bûn

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2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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type

label

N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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prefLabel

N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

@en

N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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J.ABB.2010.12.002

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Archives of Biochemistry and Biophysics

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N-acylethanolamines as novel alcohol dehydrogenase 3 substrates.

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Daniel R Dempsey

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David J Merkler

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Edward W Lowe

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Joshua H Hilton

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Milena Ivkovic

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Sumit Handa

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P2860

Physical and enzymatic properties of a class III isozyme of human liver alcohol dehydrogenase: chi-ADH

The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

The endocannabinoid anandamide is a precursor for the signaling lipid N-arachidonoyl glycine by two distinct pathways

Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes

Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation

Structure-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase)

Fatty acid amide biosynthesis: a possible new role for peptidylglycine alpha-amidating enzyme and acyl-coenzyme A: glycine N-acyltransferase

Effects of homologues and analogues of palmitoylethanolamide upon the inactivation of the endocannabinoid anandamide

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157-164

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scholarly article

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10.1016/J.ABB.2010.12.002

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2

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21144815

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