| pubmed-article:1680872 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1680872 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
| pubmed-article:1680872 | lifeskim:mentions | umls-concept:C0521390 | lld:lifeskim |
| pubmed-article:1680872 | lifeskim:mentions | umls-concept:C0033666 | lld:lifeskim |
| pubmed-article:1680872 | lifeskim:mentions | umls-concept:C0019409 | lld:lifeskim |
| pubmed-article:1680872 | lifeskim:mentions | umls-concept:C0002318 | lld:lifeskim |
| pubmed-article:1680872 | lifeskim:mentions | umls-concept:C0033268 | lld:lifeskim |
| pubmed-article:1680872 | lifeskim:mentions | umls-concept:C0205195 | lld:lifeskim |
| pubmed-article:1680872 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1680872 | pubmed:dateCreated | 1991-10-31 | lld:pubmed |
| pubmed-article:1680872 | pubmed:abstractText | We describe the presence of alpha-tubulin and MAP2 acetyltransferase activities in mouse brain. The enzyme(s) copurified with microtubules through two cycles of assembly-disassembly. Incubation of microtubule proteins with [3H]acetyl CoA resulted in a strong labeling of both alpha-tubulin and MAP2. To determine the site of the modification, tubulin was purified and digested with Glu-C endoproteinase. A unique radioactive peptide was detected and purified by HPLC. Edman degradation sequencing showed that this peptide contained epsilon N-acetyllysine at position 40 of the alpha-tubulin molecule. This result demonstrates that mouse brain alpha-tubulin was acetylated at the same site as in Chlamydomonas. Isoelectric focusing analysis showed that acetylated alpha-tubulin was resolved into five isoelectric variants, denoted alpha 3 and alpha 5 to alpha 8. This heterogeneity is not due to acetylation of other sites but results from a single acetylation of Lys40 of an heterogeneous population of alpha-tubulin isoforms. These isoforms are produced by posttranslational addition of one to five glutamyl units. Thus, neuronal alpha-tubulin is extensively modified by a combination of modifications including acetylation, glutamylation, tyrosylation, and other yet unknown modifications. | lld:pubmed |
| pubmed-article:1680872 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1680872 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1680872 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1680872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1680872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1680872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1680872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1680872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1680872 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1680872 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1680872 | pubmed:issn | 0730-2312 | lld:pubmed |
| pubmed-article:1680872 | pubmed:author | pubmed-author:RossierJJ | lld:pubmed |
| pubmed-article:1680872 | pubmed:author | pubmed-author:GrosFF | lld:pubmed |
| pubmed-article:1680872 | pubmed:author | pubmed-author:Berwald-Nette... | lld:pubmed |
| pubmed-article:1680872 | pubmed:author | pubmed-author:Le CaerJ PJP | lld:pubmed |
| pubmed-article:1680872 | pubmed:author | pubmed-author:EddéBB | lld:pubmed |
| pubmed-article:1680872 | pubmed:author | pubmed-author:DenouletPP | lld:pubmed |
| pubmed-article:1680872 | pubmed:author | pubmed-author:KoulakoffAA | lld:pubmed |
| pubmed-article:1680872 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1680872 | pubmed:volume | 46 | lld:pubmed |
| pubmed-article:1680872 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1680872 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1680872 | pubmed:pagination | 134-42 | lld:pubmed |
| pubmed-article:1680872 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1680872 | pubmed:meshHeading | pubmed-meshheading:1680872-... | lld:pubmed |
| pubmed-article:1680872 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1680872 | pubmed:articleTitle | A combination of posttranslational modifications is responsible for the production of neuronal alpha-tubulin heterogeneity. | lld:pubmed |
| pubmed-article:1680872 | pubmed:affiliation | Laboratoire de Biochimie Cellulaire, Collège de France, Paris. | lld:pubmed |
| pubmed-article:1680872 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1680872 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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