| pubmed-article:1900294 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1900294 | lifeskim:mentions | umls-concept:C0919496 | lld:lifeskim |
| pubmed-article:1900294 | lifeskim:mentions | umls-concept:C0968902 | lld:lifeskim |
| pubmed-article:1900294 | lifeskim:mentions | umls-concept:C1705552 | lld:lifeskim |
| pubmed-article:1900294 | lifeskim:mentions | umls-concept:C0032105 | lld:lifeskim |
| pubmed-article:1900294 | lifeskim:mentions | umls-concept:C0055857 | lld:lifeskim |
| pubmed-article:1900294 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:1900294 | pubmed:dateCreated | 1991-4-8 | lld:pubmed |
| pubmed-article:1900294 | pubmed:abstractText | A self-association reaction involving the plasma membrane-associated clathrin assembly protein AP-2 has been detected by incubating AP-2 alone under solution conditions that would favor the assembly of complete coat structures if clathrin were present. Self-association was rapid, unaffected by nonionic detergents, readily reversible, and gave rise to sedimentable aggregates. Only the AP subtype AP-2 exhibited self-association: the structurally or functionally related assembly proteins AP-1 and AP-3 and unrelated proteins neither self-associated nor were incorporated into the AP-2 aggregate. AP-2 interactions responsible for self-association were of high affinity, with an apparent Kd of approximately 10(-8)M. By proteolytic dissection, the self-association domain was localized to the core of the molecule containing the intact 50- and 16-kDa polypeptides in association with the truncated 60-66-kDa moieties of the parent alpha/beta polypeptides. Self-association of the intact AP-2 molecule was pH-dependent, exhibiting an apparent pKa approximately 7.4. While it is unlikely that the large AP-2 aggregates formed in solution are themselves biologically relevant structures, the AP-2 interactions involved in their formation have properties consistent with their occurrence in intact cells and thus may be important in cellular functions of the plasma membrane-localized assembly protein. | lld:pubmed |
| pubmed-article:1900294 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1900294 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1900294 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1900294 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1900294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1900294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1900294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1900294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1900294 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1900294 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1900294 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:1900294 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1900294 | pubmed:author | pubmed-author:KeenJ HJH | lld:pubmed |
| pubmed-article:1900294 | pubmed:author | pubmed-author:BeckK AKA | lld:pubmed |
| pubmed-article:1900294 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1900294 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1900294 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:1900294 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1900294 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1900294 | pubmed:pagination | 4437-41 | lld:pubmed |
| pubmed-article:1900294 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1900294 | pubmed:meshHeading | pubmed-meshheading:1900294-... | lld:pubmed |
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| pubmed-article:1900294 | pubmed:meshHeading | pubmed-meshheading:1900294-... | lld:pubmed |
| pubmed-article:1900294 | pubmed:meshHeading | pubmed-meshheading:1900294-... | lld:pubmed |
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| pubmed-article:1900294 | pubmed:meshHeading | pubmed-meshheading:1900294-... | lld:pubmed |
| pubmed-article:1900294 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1900294 | pubmed:articleTitle | Self-association of the plasma membrane-associated clathrin assembly protein AP-2. | lld:pubmed |
| pubmed-article:1900294 | pubmed:affiliation | Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140. | lld:pubmed |
| pubmed-article:1900294 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1900294 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1900294 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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