About: Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc

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About: Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc Goto Sponge NotDistinct Permalink

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scientific article published on 01 March 1984

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в березні 1984 (uk) artículu científicu espublizáu en marzu de 1984 (ast) im März 1984 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 01 March 1984 (en)
publication date	wds:Q70466786-14DC5605-BB19-48FA-B264-56B4EC36E5E6
publication date	1984-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q70466786-EF8FD0E1-244D-4A85-A5EC-6C663F5FC7DC
language of work or name	English
author name string	wds:Q70466786-55761C46-CD91-49A0-8BC5-9377A4DE8DE7 wds:Q70466786-BCF1BD0A-F386-4999-9E34-3AF2D888ACA2
author name string	Hart GW Torres CR
rdfs:label	Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc (en) Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc (nl)
skos:prefLabel	Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc (en) Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc (nl)
name	Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc (en) Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc (nl)
title	wds:Q70466786-35ACBBE0-80F2-466D-BE95-F4D32EB51585
title	Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc (en)
page(s)	wds:Q70466786-3ED44EE2-A1DE-48FB-AA13-B3FC7EE7B0D6
page(s)	3308-3317
instance of	wds:Q70466786-C3DDC4C0-0BCC-40B8-9606-16B8345C3CD8
instance of	scholarly article
PubMed ID	wds:Q70466786-A0C1F9EA-4B98-48AB-8728-8E7C49F3BCC8
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/6421821
PubMed ID	6421821
published in	wds:Q70466786-A459A099-1B1D-4657-87CB-BAEFB6F62BD6
published in	Journal of Biological Chemistry
issue	wds:Q70466786-DBFDF023-E3BF-4B91-807B-A92B3CD67792
volume	wds:Q70466786-BDB3C308-0C07-4189-BAC8-104FE2E9C820
issue	5
volume	259
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q70466786
is cites work of	O-GlcNAcylation regulates EZH2 protein stability and function O-GlcNAcylation: The Sweet Side of the Cancer NFkappaB activation is associated with its O-GlcNAcylation state under hyperglycemic conditions Cross-talk between GlcNAcylation and phosphorylation: roles in insulin resistance and glucose toxicity O-GlcNAcylation and oxidation of proteins: is signalling in the cardiovascular system becoming sweeter? Elevated O-GlcNAc levels activate epigenetically repressed genes and delay mouse ESC differentiation without affecting naïve to primed cell transition. Biological roles of glycans Minireview series on the thirtieth anniversary of research on O-GlcNAcylation of nuclear and cytoplasmic proteins: Nutrient regulation of cellular metabolism and physiology by O-GlcNAcylation A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant Relative accessibility of N-acetylglucosamine in trimers of the adenovirus types 2 and 5 fiber proteins Site-specific glycosylation of the human cytomegalovirus tegument basic phosphoprotein (UL32) at serine 921 and serine 952 Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease. GlcNAcstatins are nanomolar inhibitors of human O -GlcNAcase inducing cellular hyper- O -GlcNAcylation Screening-based discovery of drug-likeO-GlcNAcase inhibitor scaffolds Tumor cell surface beta 1-4-linked galactose binds to lectin(s) on microvascular endothelial cells and contributes to organ colonization Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus Cytologic assessment of nuclear and cytoplasmic O-linked N-acetylglucosamine distribution by using anti-streptococcal monoclonal antibodies Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores Monoclonal antibodies identify a group of nuclear pore complex glycoproteins Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine O-GlcNAc signaling in cancer metabolism and epigenetics Glycosylation disorders of membrane trafficking O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions The emerging link between O-GlcNAc and Alzheimer disease. Substrate and product analogues as human O-GlcNAc transferase inhibitors Structural snapshots of the reaction coordinate for O-GlcNAc transferase A chemical approach for identifying O-GlcNAc-modified proteins in cells Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates. O-GlcNAc protein modification in cancer cells increases in response to glucose deprivation through glycogen degradation Modulation of transcription factor function by O-GlcNAc modification O-GlcNAc cycling mutants modulate proteotoxicity in Caenorhabditis elegans models of human neurodegenerative diseases Structure of human O-GlcNAc transferase and its complex with a peptide substrate Cracking the O-GlcNAc code in metabolism. O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability Cell-Penetrant, Nanomolar O-GlcNAcase Inhibitors Selective against Lysosomal Hexosaminidases O-linked-N-acetylglucosamine on extracellular protein domains mediates epithelial cell-matrix interactions. Structural insights into mechanism and specificity of O-GlcNAc transferase O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System Analysis of proteins and peptides on a chromatographic timescale by electron-transfer dissociation MS. Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation Three-dimensional structure of aStreptomyces sviceusGNAT acetyltransferase with similarity to the C-terminal domain of the human GH84O-GlcNAcase X-inactivation normalizes O-GlcNAc transferase levels and generates an O-GlcNAc-depleted Barr body X marks the spot: does it matter that O-GlcNAc transferase is an X-linked gene? Nutrient-driven O-GlcNAc cycling - think globally but act locally Protein O-GlcNAcylation in diabetes and diabetic complications Divide and conquer: the application of organelle proteomics to heart failure O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat. Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity Decreased UDP-GlcNAc levels abrogate proliferation control in EMeg32-deficient cells. A high-throughput assay for O-GlcNAc transferase detects primary sequence preferences in peptide substrates The O-GlcNAc transferase gene resides on the X chromosome and is essential for embryonic stem cell viability and mouse ontogeny Altered glycan-dependent signaling induces insulin resistance and hyperleptinemia Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways Hijacking the Hexosamine Biosynthetic Pathway to Promote EMT-Mediated Neoplastic Phenotypes O-GlcNAc regulates FoxO activation in response to glucose O-GlcNAc signalling: implications for cancer cell biology O-linked N-acetylglucosamine modification on CCAAT enhancer-binding protein beta: role during adipocyte differentiation O-GlcNAcylation plays a role in tumor recurrence of hepatocellular carcinoma following liver transplantation Flagellin from Listeria monocytogenes is glycosylated with beta-O-linked N-acetylglucosamine

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