Multiple O-glucosylation sites on Notch function as a buffer against temperature-dependent loss of signaling.
about
The protein O-glucosyltransferase Rumi modifies eyes shut to promote rhabdomere separation in DrosophilaNegative regulation of notch signaling by xyloseDelta-Notch signalling in segmentationMolecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notchLoss of the tumor suppressor Pten promotes proliferation of Drosophila melanogaster cells in vitro and gives rise to continuous cell linesA POGLUT1 mutation causes a muscular dystrophy with reduced Notch signaling and satellite cell loss.A mutation in EGF repeat-8 of Notch discriminates between Serrate/Jagged and Delta family ligandsThe EGF repeat-specific O-GlcNAc-transferase Eogt interacts with notch signaling and pyrimidine metabolism pathways in Drosophila.Protein O-fucosyltransferase 1 expression impacts myogenic C2C12 cell commitment via the Notch signaling pathwayO-fucose monosaccharide of Drosophila Notch has a temperature-sensitive function and cooperates with O-glucose glycan in Notch transport and Notch signaling activationGenetic manipulation of genes and cells in the nervous system of the fruit fly.Site-specific O-glucosylation of the epidermal growth factor-like (EGF) repeats of notch: efficiency of glycosylation is affected by proper folding and amino acid sequence of individual EGF repeatsXylosylation of the Notch receptor preserves the balance between its activation by trans-Delta and inhibition by cis-ligands in Drosophila.Jagged1 heterozygosity in mice results in a congenital cholangiopathy which is reversed by concomitant deletion of one copy of Poglut1 (Rumi)Diverse hormone response networks in 41 independent Drosophila cell lines.Intrinsic selectivity of Notch 1 for Delta-like 4 over Delta-like 1.Structural analysis of Notch-regulating Rumi reveals basis for pathogenic mutations.Significance of glycosylation in Notch signaling.The multiple roles of epidermal growth factor repeat O-glycans in animal development.Mapping Sites of O-Glycosylation and Fringe Elongation on Drosophila Notch.Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1).Antibodies against the extracellular domain of human Notch1 receptor reveal the critical role of epidermal-growth-factor-like repeats 25-26 in ligand binding and receptor activation.Tyrosine phosphorylation and proteolytic cleavage of Notch are required for non-canonical Notch/Abl signaling in Drosophila axon guidance.MIB-1 Is Required for Spermatogenesis and Facilitates LIN-12 and GLP-1 Activity in Caenorhabditis elegans.
P2860
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P2860
Multiple O-glucosylation sites on Notch function as a buffer against temperature-dependent loss of signaling.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Multiple O-glucosylation sites ...... e-dependent loss of signaling.
@ast
Multiple O-glucosylation sites ...... e-dependent loss of signaling.
@en
type
label
Multiple O-glucosylation sites ...... e-dependent loss of signaling.
@ast
Multiple O-glucosylation sites ...... e-dependent loss of signaling.
@en
prefLabel
Multiple O-glucosylation sites ...... e-dependent loss of signaling.
@ast
Multiple O-glucosylation sites ...... e-dependent loss of signaling.
@en
P2093
P2860
P356
P1433
P1476
Multiple O-glucosylation sites ...... e-dependent loss of signaling.
@en
P2093
Amanda A Simcox
Hamed Jafar-Nejad
Jessica Leonardi
Rodrigo Fernandez-Valdivia
Yi-Dong Li
P2860
P304
P356
10.1242/DEV.068361
P407
P577
2011-07-19T00:00:00Z