Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: mutational analysis of a malonyl-CoA affinity domain

Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: mutational analysis of a malonyl-CoA affinity domain

Item
http://www.wikidata.org/entity/Q28564300
Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transferThe extreme C terminus of rat liver carnitine palmitoyltransferase I is not involved in malonyl-CoA sensitivity but in initial protein foldingIdentification of conserved amino acid residues in rat liver carnitine palmitoyltransferase I critical for malonyl-CoA inhibition. Mutation of methionine 593 abolishes malonyl-CoA inhibitionData-driven docking for the study of biomolecular complexes.Alternative exon usage in the single CPT1 gene of Drosophila generates functional diversity in the kinetic properties of the enzyme: differential expression of alternatively spliced variants in Drosophila tissues.C75 increases peripheral energy utilization and fatty acid oxidation in diet-induced obesityStructural systems biology: modelling protein interactions.Carnitine palmitoyltransferase IA polymorphism P479L is common in Greenland Inuit and is associated with elevated plasma apolipoprotein A-IFunctional complementation in yeast allows molecular characterization of missense argininosuccinate lyase mutations.A Novel Mutation in CPT1A Resulting in Hepatic CPT Deficiency.Carnitine palmitoyltransferase I control of acetogenesis, the major pathway of fatty acid {beta}-oxidation in liver of neonatal swine.Genome duplication events have led to a diversification in the CPT I gene family in fish.CPT1A;B transfers PALM to CARFunctional and structural basis of carnitine palmitoyltransferase 1A deficiency.Rat liver carnitine palmitoyltransferase 1 forms an oligomeric complex within the outer mitochondrial membrane.
P2860

Structural model of a malonyl-CoA-binding site of carnitine octanoyltransferase and carnitine palmitoyltransferase I: mutational analysis of a malonyl-CoA affinity domain

Item
http://www.wikidata.org/entity/Q28564300
description
2002 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մարտին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2002
@ast
im März 2002 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2002/03/29)
@sk
vědecký článek publikovaný v roce 2002
@cs
wetenschappelijk artikel (gepubliceerd op 2002/03/29)
@nl
наукова стаття, опублікована в березні 2002
@uk
name
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@ast
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@en
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@nl
type
label
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@ast
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@en
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@nl
prefLabel
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@ast
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@en
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698
P356
P1433
P1476
Structural model of a malonyl- ...... a malonyl-CoA affinity domain
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P5875
P698