| pubmed-article:11163224 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C0040715 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C0101555 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C0175631 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C1522702 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C2827662 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C0599718 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C0599813 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
| pubmed-article:11163224 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:11163224 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:11163224 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11163224 | pubmed:abstractText | Binding and internalization of a protein substrate by E. coli ClpXP was investigated by electron microscopy. In sideviews of ATP gamma S-stabilized ClpXP complexes, a narrow axial channel was visible in ClpX, surrounded by protrusions on its distal surface. When substrate lambda O protein was added, extra density attached to this surface. Upon addition of ATP, this density disappeared as lambda O was degraded. When ATP was added to proteolytically inactive ClpXP-lambda O complexes, the extra density transferred to the center of ClpP and remained inside ClpP after separation from ClpX. We propose that substrates of ATP-dependent proteases bind to specific sites on the distal surface of the ATPase, and are subsequently unfolded and translocated into the internal chamber of the protease. | lld:pubmed |
| pubmed-article:11163224 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11163224 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11163224 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11163224 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11163224 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11163224 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:11163224 | pubmed:author | pubmed-author:IshikawaTT | lld:pubmed |
| pubmed-article:11163224 | pubmed:author | pubmed-author:OrtegaJJ | lld:pubmed |
| pubmed-article:11163224 | pubmed:author | pubmed-author:SinghS KSK | lld:pubmed |
| pubmed-article:11163224 | pubmed:author | pubmed-author:MauriziM RMR | lld:pubmed |
| pubmed-article:11163224 | pubmed:author | pubmed-author:StevenA CAC | lld:pubmed |
| pubmed-article:11163224 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11163224 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:11163224 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11163224 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11163224 | pubmed:pagination | 1515-21 | lld:pubmed |
| pubmed-article:11163224 | pubmed:dateRevised | 2009-9-3 | lld:pubmed |
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| pubmed-article:11163224 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11163224 | pubmed:articleTitle | Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. | lld:pubmed |
| pubmed-article:11163224 | pubmed:affiliation | Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |
| pubmed-article:11163224 | pubmed:publicationType | Journal Article | lld:pubmed |
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