Localization of O-GlcNAc modification on the serum response transcription factor
about
Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentrationc-fos transcriptional activation and repression correlate temporally with the phosphorylation status of TCFO glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactionsThe potential mechanism of the diabetogenic action of streptozotocin: inhibition of pancreatic beta-cell O-GlcNAc-selective N-acetyl-beta-D-glucosaminidaseRegulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.The hexosamine signaling pathway: O-GlcNAc cycling in feast or famineO-GlcNAc signaling in the cardiovascular system.Glycosylation of the c-Myc transactivation domainO-GlcNAcylation: a novel post-translational mechanism to alter vascular cellular signaling in health and disease: focus on hypertension.Proteomic approaches for site-specific O-GlcNAcylation analysis.Streptolysin O-permeabilized cell system for studying trans-acting activities of exogenous nuclear proteins.Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.Initiation binding repressor, a factor that binds to the transcription initiation site of the histone h5 gene, is a glycosylated member of a family of cell growth regulators [corrected]Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.Site-specific glycosylation of the human cytomegalovirus tegument basic phosphoprotein (UL32) at serine 921 and serine 952Overexpression of glutamine:fructose-6-phosphate amidotransferase in transgenic mice leads to insulin resistance.O-GlcNAc profiling: from proteins to proteomes.Journey to the surface of the cell: Fos regulation and the SRE.Molecular weight abnormalities of the CTCF transcription factor: CTCF migrates aberrantly in SDS-PAGE and the size of the expressed protein is affected by the UTRs and sequences within the coding region of the CTCF gene.Antitumor activities of D-glucosamine and its derivatives.Recognition of carbohydrate by major histocompatibility complex class I-restricted, glycopeptide-specific cytotoxic T lymphocytes.Heterogeneous nuclear ribonucleoprotein R enhances transcription from the naturally configured c-fos promoter in vitro.Nutrient-driven O-GlcNAc in proteostasis and neurodegeneration.
P2860
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P2860
Localization of O-GlcNAc modification on the serum response transcription factor
description
1992 nî lūn-bûn
@nan
1992 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Localization of O-GlcNAc modification on the serum response transcription factor
@ast
Localization of O-GlcNAc modification on the serum response transcription factor
@en
Localization of O-GlcNAc modification on the serum response transcription factor
@nl
type
label
Localization of O-GlcNAc modification on the serum response transcription factor
@ast
Localization of O-GlcNAc modification on the serum response transcription factor
@en
Localization of O-GlcNAc modification on the serum response transcription factor
@nl
prefLabel
Localization of O-GlcNAc modification on the serum response transcription factor
@ast
Localization of O-GlcNAc modification on the serum response transcription factor
@en
Localization of O-GlcNAc modification on the serum response transcription factor
@nl
P2093
P1476
Localization of O-GlcNAc modification on the serum response transcription factor
@en
P2093
A J Reason
H R Morris
R H Treisman
R S Haltiwanger
P304
P407
P577
1992-08-25T00:00:00Z