| pubmed-article:3027066 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3027066 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:3027066 | lifeskim:mentions | umls-concept:C0964863 | lld:lifeskim |
| pubmed-article:3027066 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:3027066 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3027066 | pubmed:dateCreated | 1987-2-25 | lld:pubmed |
| pubmed-article:3027066 | pubmed:abstractText | Chymotryptic digestion of bovine brain uncoating ATPase produced a 60-kDa fragment that was subsequently proteolyzed to 44 kDa. Loss of clathrin cage uncoating activity paralleled the conversion of the intact 70-kDa enzyme to the 60-kDa fragment, while clathrin binding activity was lost as the 60-kDa fragment was degraded to 44 kDa. This 44-kDa fragment has been purified to homogeneity and characterized as a clathrin-independent ATPase. The 44-kDa ATPase domain has been localized within the intact enzyme by the use of amino-terminal specific antibodies. This localization relates to the conserved nature of the 70-kDa heat shock protein family, of which bovine brain uncoating ATPase is a constitutively expressed member. | lld:pubmed |
| pubmed-article:3027066 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3027066 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3027066 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3027066 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3027066 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3027066 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3027066 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3027066 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:3027066 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3027066 | pubmed:author | pubmed-author:RothmanJ EJE | lld:pubmed |
| pubmed-article:3027066 | pubmed:author | pubmed-author:KonfortiB BBB | lld:pubmed |
| pubmed-article:3027066 | pubmed:author | pubmed-author:SchmidS LSL | lld:pubmed |
| pubmed-article:3027066 | pubmed:author | pubmed-author:ChappellT GTG | lld:pubmed |
| pubmed-article:3027066 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3027066 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3027066 | pubmed:volume | 262 | lld:pubmed |
| pubmed-article:3027066 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3027066 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3027066 | pubmed:pagination | 746-51 | lld:pubmed |
| pubmed-article:3027066 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3027066 | pubmed:meshHeading | pubmed-meshheading:3027066-... | lld:pubmed |
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| pubmed-article:3027066 | pubmed:meshHeading | pubmed-meshheading:3027066-... | lld:pubmed |
| pubmed-article:3027066 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3027066 | pubmed:articleTitle | The ATPase core of a clathrin uncoating protein. | lld:pubmed |
| pubmed-article:3027066 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3027066 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:3027066 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3027066 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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