PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
about
PER1 is required for GPI-phospholipase A2 activity and involved in lipid remodeling of GPI-anchored proteinsBiosynthesis and deficiencies of glycosylphosphatidylinositolGlycosyl phosphatidylinositol anchor biosynthesis is essential for maintaining epithelial integrity during Caenorhabditis elegans embryogenesisThe Gup1 homologue of Trypanosoma brucei is a GPI glycosylphosphatidylinositol remodelase.Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid moiety of GPI anchors to ceramidesYeast ARV1 is required for efficient delivery of an early GPI intermediate to the first mannosyltransferase during GPI assembly and controls lipid flow from the endoplasmic reticulum.GUP1 of Saccharomyces cerevisiae encodes an O-acyltransferase involved in remodeling of the GPI anchor.CWH43 is required for the introduction of ceramides into GPI anchors in Saccharomyces cerevisiae.Limited ER quality control for GPI-anchored proteins.Obif, a Transmembrane Protein, Is Required for Bone Mineralization and Spermatogenesis in MiceSorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPIPost-Golgi anterograde transport requires GARP-dependent endosome-to-TGN retrograde transportTEX101, a glycoprotein essential for sperm fertility, is required for stable expression of Ly6k on testicular germ cells.Lipid remodelling of glycosylphosphatidylinositol (GPI) glycoconjugates in procyclic-form trypanosomes: biosynthesis and processing of GPIs revisited.Null mutation in PGAP1 impairing Gpi-anchor maturation in patients with intellectual disability and encephalopathyMolecular switching system using glycosylphosphatidylinositol to select cells highly expressing recombinant proteinsComparative Analysis of Protein Glycosylation Pathways in Humans and the Fungal Pathogen Candida albicans.Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling.Structural remodeling of GPI anchors during biosynthesis and after attachment to proteins.New insight into CCN3 interactions--nuclear CCN3 : fact or fantasy?Identification of Stim1 as a candidate gene for exaggerated sympathetic response to stress in the stroke-prone spontaneously hypertensive rat.Fatty acid remodeling of GPI-anchored proteins is required for their raft associationGenome-Wide Screening of Genes Required for Glycosylphosphatidylinositol Biosynthesis.Leukemic blasts with the paroxysmal nocturnal hemoglobinuria phenotype in children with acute lymphoblastic leukemia.Glycosylphosphatidylinositol anchors regulate glycosphingolipid levels.Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface.Cerebral visual impairment and intellectual disability caused by PGAP1 variantsHypomorphic mutations in PGAP2, encoding a GPI-anchor-remodeling protein, cause autosomal-recessive intellectual disability.PGAP2 mutations, affecting the GPI-anchor-synthesis pathway, cause hyperphosphatasia with mental retardation syndromeThematic review series: lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: how we learned to stop worrying and love glycophospholipids.Apical sorting of lysoGPI-anchored proteins occurs independent of association with detergent-resistant membranes but dependent on their N-glycosylation.Significance of glycosylphosphatidylinositol-anchored protein enrichment in lipid rafts for the control of autoimmunity.Biosynthesis, remodelling and functions of mammalian GPI-anchored proteins: recent progress.Trypanosome glycosylphosphatidylinositol biosynthesis.Peroxisome dependency of alkyl-containing GPI-anchor biosynthesis in the endoplasmic reticulum.A GPI processing phospholipase A2, PGAP6, modulates Nodal signaling in embryos by shedding CRIPTO.Mutations in PGAP3 impair GPI-anchor maturation, causing a subtype of hyperphosphatasia with mental retardation.Chemical biology of glycosylphosphatidylinositol anchors.The Molecular Genetics of Autosomal Recessive Nonsyndromic Intellectual Disability: a Mutational Continuum and Future Recommendations.Implications of lipid moiety in oligomerization and immunoreactivities of GPI-anchored proteins.
P2860
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P2860
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
description
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2006
@ast
im März 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/03/01)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/03/01)
@nl
наукова стаття, опублікована в березні 2006
@uk
مقالة علمية (نشرت في مارس 2006)
@ar
name
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@ast
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@en
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@nl
type
label
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@ast
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@en
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@nl
prefLabel
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@ast
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@en
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@nl
P2093
P2860
P3181
P356
P1476
PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins
@en
P2093
Chie Murata
Ryo Taguchi
Taroh Kinoshita
Yuko Tashima
Yusuke Maeda
P2860
P304
P3181
P356
10.1091/MBC.E05-11-1005
P577
2006-01-11T00:00:00Z