pubmed-article:9428517 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:9428517 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
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pubmed-article:9428517 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:9428517 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
pubmed-article:9428517 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:9428517 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
pubmed-article:9428517 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9428517 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:9428517 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9428517 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:9428517 | pubmed:dateCreated | 1998-2-2 | lld:pubmed |
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pubmed-article:9428517 | pubmed:abstractText | ClpX, a molecular chaperone and the regulatory subunit of the ClpXP protease, is shown to contain tandem modular domains that bind to the C-terminal sequences of target proteins in a manner that parallels functional specificity. Nuclear magnetic resonance studies show that these C-terminal sequences are displayed as disordered peptides on the surface of otherwise folded proteins. The ClpX substrate-binding domains are homologous to sequences in other Clp/Hsp100 proteins and are related more distantly to PDZ domains, which also mediate C-terminal specific protein-protein interactions. Conservation of these binding domains indicates that the mode of substrate recognition characterized here for ClpX will be a conserved feature among Clp/Hsp100 family members and a distinguishing characteristic between this chaperone family and the Hsp70 chaperones. | lld:pubmed |
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pubmed-article:9428517 | pubmed:language | eng | lld:pubmed |
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pubmed-article:9428517 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9428517 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9428517 | pubmed:month | Dec | lld:pubmed |
pubmed-article:9428517 | pubmed:issn | 0092-8674 | lld:pubmed |
pubmed-article:9428517 | pubmed:author | pubmed-author:TABERPP | lld:pubmed |
pubmed-article:9428517 | pubmed:author | pubmed-author:SmithC KCK | lld:pubmed |
pubmed-article:9428517 | pubmed:author | pubmed-author:WalshN PNP | lld:pubmed |
pubmed-article:9428517 | pubmed:author | pubmed-author:CAUERHH | lld:pubmed |
pubmed-article:9428517 | pubmed:author | pubmed-author:LevchenkoII | lld:pubmed |
pubmed-article:9428517 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9428517 | pubmed:day | 26 | lld:pubmed |
pubmed-article:9428517 | pubmed:volume | 91 | lld:pubmed |
pubmed-article:9428517 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9428517 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9428517 | pubmed:pagination | 939-47 | lld:pubmed |
pubmed-article:9428517 | pubmed:dateRevised | 2009-9-3 | lld:pubmed |
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pubmed-article:9428517 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9428517 | pubmed:articleTitle | PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. | lld:pubmed |
pubmed-article:9428517 | pubmed:affiliation | Department of Biology, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge 02139, USA. | lld:pubmed |
pubmed-article:9428517 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9428517 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9428517 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:9428517 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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