Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
about
The Gup1 homologue of Trypanosoma brucei is a GPI glycosylphosphatidylinositol remodelase.Chemical validation of GPI biosynthesis as a drug target against African sleeping sickness.Lipid remodelling of glycosylphosphatidylinositol (GPI) glycoconjugates in procyclic-form trypanosomes: biosynthesis and processing of GPIs revisited.Biosynthesis of glycosylphosphatidylinositols in mammals and unicellular microbes.Trypanosoma brucei: reduction of GPI-phospholipase C protein during differentiation is dependent on replication of newly transformed cells.Lipid remodeling leads to the introduction and exchange of defined ceramides on GPI proteins in the ER and Golgi of Saccharomyces cerevisiae.Recent developments in the cell biology and biochemistry of glycosylphosphatidylinositol lipids (review).Acylation in trypanosomatids: an essential process and potential drug targetA passion for parasites.Lipidomic analysis of bloodstream and procyclic form Trypanosoma bruceiLipid metabolism in Trypanosoma bruceiTrypanosoma brucei: a model micro-organism to study eukaryotic phospholipid biosynthesis.Multiple triclosan targets in Trypanosoma brucei.Alkylacylglycerolipid domain of GPI molecules of Leishmania is responsible for inhibition of PKC-mediated c-fos expression.Evidence for phospholipases from Trypanosoma cruzi active on phosphatidylinositol and inositolphosphoceramide.Parasite and mammalian GPI biosynthetic pathways can be distinguished using synthetic substrate analoguesActivation of endocytosis as an adaptation to the mammalian host by trypanosomesThe glycosylphosphatidylinositol (GPI) biosynthetic pathway of bloodstream-form Trypanosoma brucei is dependent on the de novo synthesis of inositol.The essential neutral sphingomyelinase is involved in the trafficking of the variant surface glycoprotein in the bloodstream form of Trypanosoma brucei.Lipid metabolism in Trypanosoma brucei: utilization of myristate and myristoyllysophosphatidylcholine for myristoylation of glycosyl phosphatidylinositols.A novel glycosylphosphatidylinositol in African trypanosomes. A possible catabolic intermediate.In vitro translation in a cell-free system from Trypanosoma brucei yields glycosylated and glycosylphosphatidylinositol-anchored proteins.Biosynthesis of Inositol Phosphoceramides and Remodeling of Glycosylphosphatidylinositol Anchors inSaccharomyces cerevisiaeAre Mediated by Different EnzymesCloning, Expression, and Characterization of the acyl-CoA-binding Protein in African Trypanosomes
P2860
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P2860
Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
@en
Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
@nl
type
label
Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
@en
Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
@nl
prefLabel
Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
@en
Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
@nl
P2093
P2860
P356
P1476
Myristate exchange on the Trypanosoma brucei variant surface glycoprotein.
@en
P2093
K A Werbovetz
L U Buxbaum
P T Englund
P2860
P304
P356
10.1073/PNAS.93.3.1178
P407
P577
1996-02-01T00:00:00Z