| pubmed-article:7753821 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7753821 | lifeskim:mentions | umls-concept:C0086661 | lld:lifeskim |
| pubmed-article:7753821 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:7753821 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
| pubmed-article:7753821 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7753821 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7753821 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7753821 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7753821 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:7753821 | pubmed:dateCreated | 1995-6-16 | lld:pubmed |
| pubmed-article:7753821 | pubmed:abstractText | O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues. Although O-GlcNAc occurs on a myriad of nuclear and cytoplasmic proteins, only a few have thus far been identified. These O-GlcNAc-bearing proteins are also modified by phosphorylation and form reversible multimeric complexes. Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells. O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells. Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster. | lld:pubmed |
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| pubmed-article:7753821 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7753821 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7753821 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7753821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7753821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7753821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7753821 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7753821 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7753821 | pubmed:month | May | lld:pubmed |
| pubmed-article:7753821 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7753821 | pubmed:author | pubmed-author:HartG WGW | lld:pubmed |
| pubmed-article:7753821 | pubmed:author | pubmed-author:DangC VCV | lld:pubmed |
| pubmed-article:7753821 | pubmed:author | pubmed-author:ChowT WTW | lld:pubmed |
| pubmed-article:7753821 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7753821 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:7753821 | pubmed:volume | 92 | lld:pubmed |
| pubmed-article:7753821 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7753821 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7753821 | pubmed:pagination | 4417-21 | lld:pubmed |
| pubmed-article:7753821 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7753821 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7753821 | pubmed:articleTitle | Glycosylation of the c-Myc transactivation domain. | lld:pubmed |
| pubmed-article:7753821 | pubmed:affiliation | Biochemistry, Cellular and Molecular Biology Training Program, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. | lld:pubmed |
| pubmed-article:7753821 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7753821 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
