Carboxy-terminal mutations of bile acid CoA:N-acyltransferase alter activity and substrate specificity

about

Carboxy-terminal mutations of bile acid CoA:N-acyltransferase alter activity and substrate specificity

Item

http://www.wikidata.org/entity/Q37033100

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 25 May 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Carboxy-terminal mutations of ...... vity and substrate specificity

@en

Carboxy-terminal mutations of ...... ity and substrate specificity.

@nl

type

Item

label

Carboxy-terminal mutations of ...... vity and substrate specificity

@en

Carboxy-terminal mutations of ...... ity and substrate specificity.

@nl

prefLabel

Carboxy-terminal mutations of ...... vity and substrate specificity

@en

Carboxy-terminal mutations of ...... ity and substrate specificity.

@nl

P1476

Carboxy-terminal mutations of ...... vity and substrate specificity

@en

P2093

Amber L Guidry

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

Charles N Falany

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

Erin M Shonsey

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

Josie L Falany

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

Nathan A Styles

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

Stephen Barnes

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

P2860

Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase

Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase

2-Fluoro-beta-alanine, a previously unrecognized substrate for bile acid coenzyme A:amino acid:N-acyltransferase from human liver

The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha /beta hydrolase

Molecular cloning and expression of rat liver bile acid CoA ligase

Cloning, expression, and chromosomal localization of mouse liver bile acid CoA:amino acid N-acyltransferase

Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver

Subcellular organization of bile acid amidation in human liver: a key issue in regulating the biosynthesis of bile salts

Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization.

Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT.

P304

1133-1143

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

P31

scholarly article

P356

10.1194/JLR.M064428

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

P433

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

P478

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

P577

2016-05-25T00:00:00Z

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

P698

27230263

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

P932

4918843

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