pubmed-article:2174423 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2174423 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:2174423 | lifeskim:mentions | umls-concept:C0041538 | lld:lifeskim |
pubmed-article:2174423 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:2174423 | lifeskim:mentions | umls-concept:C1148926 | lld:lifeskim |
pubmed-article:2174423 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:2174423 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:2174423 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:2174423 | pubmed:issue | 34 | lld:pubmed |
pubmed-article:2174423 | pubmed:dateCreated | 1991-1-17 | lld:pubmed |
pubmed-article:2174423 | pubmed:abstractText | In the ubiquitin pathway for intracellular protein breakdown, proteins ligated to ubiquitin are degraded by a large (26 S) ATP-dependent protease complex. It was found previously that the 26 S complex is assembled from three different enzyme components by a process that requires MgATP. In addition, MgATP is also required for the continued action of the 26 S complex in the breakdown of ubiquitin-protein conjugates. In the present study we have tried to gain some insight into the mode of action of ATP by following ATP hydrolysis by the 26 S complex and its three components. It was found that none of the three unassembled components had significant ATPase activity, but such activity appeared following their entry into the 26 S complex. The presence of all three components and of MgATP was required for the formation of complex-associated ATPase activity. GTP and UTP cannot replace ATP for complex assembly, but these nucleotides can substitute for ATP in the stimulation of the conjugate-degrading activity of the 26 S complex. Unlabeled GTP and UTP inhibit the hydrolysis of [gamma-32P] ATP by complex-associated ATPase, indicating that this activity is related to the latter site of ATP action in this system. | lld:pubmed |
pubmed-article:2174423 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174423 | pubmed:language | eng | lld:pubmed |
pubmed-article:2174423 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174423 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2174423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2174423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2174423 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2174423 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2174423 | pubmed:month | Dec | lld:pubmed |
pubmed-article:2174423 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2174423 | pubmed:author | pubmed-author:HershkoAA | lld:pubmed |
pubmed-article:2174423 | pubmed:author | pubmed-author:GanothDD | lld:pubmed |
pubmed-article:2174423 | pubmed:author | pubmed-author:ArmonTT | lld:pubmed |
pubmed-article:2174423 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2174423 | pubmed:day | 5 | lld:pubmed |
pubmed-article:2174423 | pubmed:volume | 265 | lld:pubmed |
pubmed-article:2174423 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2174423 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2174423 | pubmed:pagination | 20723-6 | lld:pubmed |
pubmed-article:2174423 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:2174423 | pubmed:meshHeading | pubmed-meshheading:2174423-... | lld:pubmed |
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pubmed-article:2174423 | pubmed:meshHeading | pubmed-meshheading:2174423-... | lld:pubmed |
pubmed-article:2174423 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2174423 | pubmed:articleTitle | Assembly of the 26 S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity. | lld:pubmed |
pubmed-article:2174423 | pubmed:affiliation | Unit of Biochemistry, Faculty of Medicine, Technion-Israel Institute of Technology, Haifa. | lld:pubmed |
pubmed-article:2174423 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2174423 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2174423 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:2174423 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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