Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H
about
The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogenyPost-translational modifications of intermediate filament proteins: mechanisms and functionsOrder and disorder in intermediate filament proteinsStructure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activityDecreased O-linked GlcNAcylation protects from cytotoxicity mediated by huntingtin exon1 protein fragmentQuantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.Chemical approaches to understanding O-GlcNAc glycosylation in the brain.Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.Does O-GlcNAc play a role in neurodegenerative diseases?Advanced glycation endproducts in neurofilament conglomeration of motoneurons in familial and sporadic amyotrophic lateral sclerosis.Neurofilaments at a glance.Regulation between O-GlcNAcylation and phosphorylation of neurofilament-M and their dysregulation in Alzheimer diseaseCytoskeletal keratin glycosylation protects epithelial tissue from injury.AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivationO-GlcNAc cycling: implications for neurodegenerative disorders.The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways.Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation.O-GlcNAcylation of tubulin inhibits its polymerization.Mechanism, Structure, and Inhibition of O-GlcNAc Processing Enzymes.Reciprocal keratin 18 Ser48 O-GlcNAcylation and Ser52 phosphorylation using peptide analysis.Plasma profiling reveals three proteins associated to amyotrophic lateral sclerosis.Prostaglandin J2 promotes O-GlcNAcylation raising APP processing by α- and β-secretases: relevance to Alzheimer's disease.A Sweet Embrace: Control of Protein-Protein Interactions by O-Linked β-N-Acetylglucosamine.Nutrient-driven O-GlcNAc in proteostasis and neurodegeneration.O-linked N-acetylglucosamine levels in cerebellar neurons respond reciprocally to pertubations of phosphorylation.Identification of phosphorylation sites on neurofilament proteins by nanoelectrospray mass spectrometry.Site-specific glycosylation regulates the form and function of the intermediate filament cytoskeleton.
P2860
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P2860
Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H
description
1996 nî lūn-bûn
@nan
1996 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@ast
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@en
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@nl
type
label
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@ast
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@en
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@nl
prefLabel
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@ast
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@en
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@nl
P2093
P356
P1476
Cytoplasmic O-GlcNAc modificat ...... lament protein neurofilament-H
@en
P2093
P304
20845-20852
P356
10.1074/JBC.271.34.20845
P407
P577
1996-08-01T00:00:00Z