| pubmed-article:11422376 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11422376 | lifeskim:mentions | umls-concept:C0028630 | lld:lifeskim |
| pubmed-article:11422376 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:11422376 | lifeskim:mentions | umls-concept:C0109271 | lld:lifeskim |
| pubmed-article:11422376 | lifeskim:mentions | umls-concept:C0109272 | lld:lifeskim |
| pubmed-article:11422376 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:11422376 | lifeskim:mentions | umls-concept:C1149552 | lld:lifeskim |
| pubmed-article:11422376 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11422376 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:11422376 | pubmed:dateCreated | 2001-6-25 | lld:pubmed |
| pubmed-article:11422376 | pubmed:abstractText | Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. The goal of this study was to investigate the structure and function of the mammalian mitochondrial chaperonin system. We present evidence that the 60 kDa chaperonin (mt-cpn60) exists in solution in dynamic equilibrium between monomers, heptameric single rings and double-ringed tetradecamers. In the presence of ATP and the 10 kDa cochaperonin (mt-cpn10), the formation of a double ring is favored. ADP at very high concentrations does not inhibit malate dehydrogenase refolding or ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10. We propose that the cis (mt-cpn60)14.nucleotide.(mt-cpn10)7 complex is not a stable species and does not bind ADP effectively at its trans binding site. | lld:pubmed |
| pubmed-article:11422376 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11422376 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11422376 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11422376 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11422376 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11422376 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11422376 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11422376 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11422376 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11422376 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:LustigAA | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:WeissCC | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:NiiTT | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:GreenbergAA | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:AzemAA | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:ViitanenPP | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:SharkiaRR | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:DelareaYY | lld:pubmed |
| pubmed-article:11422376 | pubmed:author | pubmed-author:Levy-RimlerGG | lld:pubmed |
| pubmed-article:11422376 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11422376 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:11422376 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11422376 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11422376 | pubmed:pagination | 3465-72 | lld:pubmed |
| pubmed-article:11422376 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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| pubmed-article:11422376 | pubmed:meshHeading | pubmed-meshheading:11422376... | lld:pubmed |
| pubmed-article:11422376 | pubmed:meshHeading | pubmed-meshheading:11422376... | lld:pubmed |
| pubmed-article:11422376 | pubmed:meshHeading | pubmed-meshheading:11422376... | lld:pubmed |
| pubmed-article:11422376 | pubmed:meshHeading | pubmed-meshheading:11422376... | lld:pubmed |
| pubmed-article:11422376 | pubmed:meshHeading | pubmed-meshheading:11422376... | lld:pubmed |
| pubmed-article:11422376 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11422376 | pubmed:articleTitle | The effect of nucleotides and mitochondrial chaperonin 10 on the structure and chaperone activity of mitochondrial chaperonin 60. | lld:pubmed |
| pubmed-article:11422376 | pubmed:affiliation | Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Israel. | lld:pubmed |
| pubmed-article:11422376 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11422376 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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