| pubmed-article:8702625 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8702625 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
| pubmed-article:8702625 | lifeskim:mentions | umls-concept:C0084913 | lld:lifeskim |
| pubmed-article:8702625 | lifeskim:mentions | umls-concept:C1415504 | lld:lifeskim |
| pubmed-article:8702625 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:8702625 | pubmed:issue | 32 | lld:pubmed |
| pubmed-article:8702625 | pubmed:dateCreated | 1996-9-16 | lld:pubmed |
| pubmed-article:8702625 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8702625 | pubmed:abstractText | Using the yeast two-hybrid system, we have identified a human ubiquitin-conjugating enzyme (hE2-25K) as a protein that interacts with the gene product for Huntington disease (HD) (Huntingtin). This protein has complete amino acid identity with the bovine E2-25K protein and has striking similarity to the UBC-1, -4 and -5 enzymes of Saccharomyces cerevisiae. This protein is highly expressed in brain and a slightly larger protein recognized by an anti-E2-25K polyclonal antibody is selectively expressed in brain regions affected in HD. The huntingtin-E2-25K interaction is not obviously modulated by CAG length. We also demonstrate that huntingtin is ubiquitinated. These findings have implications for the regulated catabolism of the gene product for HD. | lld:pubmed |
| pubmed-article:8702625 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8702625 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8702625 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8702625 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8702625 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8702625 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:HaydenM RMR | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:PickartC MCM | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:GrahamK CKC | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:GoldbergY PYP | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:XieCC | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:GietzR DRD | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:GrahamR KRK | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:KalchmanM AMA | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:KoideH BHB | lld:pubmed |
| pubmed-article:8702625 | pubmed:author | pubmed-author:HodgsonJ GJG | lld:pubmed |
| pubmed-article:8702625 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8702625 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:8702625 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8702625 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8702625 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8702625 | pubmed:pagination | 19385-94 | lld:pubmed |
| pubmed-article:8702625 | pubmed:dateRevised | 2008-9-13 | lld:pubmed |
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| pubmed-article:8702625 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8702625 | pubmed:articleTitle | Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme. | lld:pubmed |
| pubmed-article:8702625 | pubmed:affiliation | Department of Medical Genetics, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4. | lld:pubmed |
| pubmed-article:8702625 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8702625 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8702625 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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