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| pubmed-article:18278057 | lifeskim:mentions | umls-concept:C0243041 | lld:lifeskim |
| pubmed-article:18278057 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:18278057 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:18278057 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:18278057 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:18278057 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:18278057 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:18278057 | pubmed:dateCreated | 2008-3-5 | lld:pubmed |
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| pubmed-article:18278057 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18278057 | pubmed:abstractText | Eukaryotic 20S proteasomes are composed of two alpha-rings and two beta-rings, which form an alphabetabetaalpha stacked structure. Here we describe a proteasome-specific chaperone complex, designated Dmp1-Dmp2, in budding yeast. Dmp1-Dmp2 directly bound to the alpha5 subunit to facilitate alpha-ring formation. In Deltadmp1 cells, alpha-rings lacking alpha4 and decreased formation of 20S proteasomes were observed. Dmp1-Dmp2 interacted with proteasome precursors early during proteasome assembly and dissociated from the precursors before the formation of half-proteasomes. Notably, the crystallographic structures of Dmp1 and Dmp2 closely resemble that of PAC3-a mammalian proteasome-assembling chaperone; nonetheless, neither Dmp1 nor Dmp2 showed obvious sequence similarity to PAC3. The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled. | lld:pubmed |
| pubmed-article:18278057 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18278057 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18278057 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18278057 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18278057 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18278057 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18278057 | pubmed:issn | 1545-9985 | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:TanakaKeijiK | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:KatoKoichiK | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:MizushimaTsun... | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:TakagiKenjiK | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:YamaneTakashi... | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:YashirodaHide... | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:MurataShigeoS | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:KasaharaMasan... | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:SuzukiAtsuoA | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:HiranoYukoY | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:SakataEriE | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:KurimotoEijiE | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:OkamotoKentaK | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:KameyamaTomie... | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:NiwaShin-ichi... | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:HayashiHidemi... | lld:pubmed |
| pubmed-article:18278057 | pubmed:author | pubmed-author:KishimotoTosh... | lld:pubmed |
| pubmed-article:18278057 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18278057 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:18278057 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18278057 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18278057 | pubmed:pagination | 228-36 | lld:pubmed |
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| pubmed-article:18278057 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18278057 | pubmed:articleTitle | Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. | lld:pubmed |
| pubmed-article:18278057 | pubmed:affiliation | Laboratory of Frontier Science, Core Technology and Research Center, Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, Tokyo 113-8613, Japan. | lld:pubmed |
| pubmed-article:18278057 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18278057 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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