pubmed-article:20074573 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20074573 | lifeskim:mentions | umls-concept:C2245017 | lld:lifeskim |
pubmed-article:20074573 | lifeskim:mentions | umls-concept:C1537990 | lld:lifeskim |
pubmed-article:20074573 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
pubmed-article:20074573 | lifeskim:mentions | umls-concept:C1708632 | lld:lifeskim |
pubmed-article:20074573 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
pubmed-article:20074573 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:20074573 | lifeskim:mentions | umls-concept:C0104353 | lld:lifeskim |
pubmed-article:20074573 | lifeskim:mentions | umls-concept:C1522485 | lld:lifeskim |
pubmed-article:20074573 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:20074573 | pubmed:dateCreated | 2010-2-23 | lld:pubmed |
pubmed-article:20074573 | pubmed:abstractText | NADH:ubiquinone oxidoreductase (complex I) is the entry enzyme of mitochondrial oxidative phosphorylation. To obtain the structural information on inhibitor/quinone binding sites, we synthesized [3H]benzophenone-asimicin ([3H]BPA), a photoaffinity analogue of asimicin, which belongs to the acetogenin family known as the most potent complex I inhibitor. We found that [3H]BPA was photo-crosslinked to ND2, ND1 and ND5 subunits, by the three dimensional separation (blue-native/doubled SDS-PAGE) of [3H]BPA-treated bovine heart submitochondrial particles. The cross-linking was blocked by rotenone. This is the first finding that ND2 was photo-crosslinked with a potent complex I inhibitor, suggesting its involvement in the inhibitor/quinone-binding. | lld:pubmed |
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pubmed-article:20074573 | pubmed:language | eng | lld:pubmed |
pubmed-article:20074573 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20074573 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:20074573 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20074573 | pubmed:month | Mar | lld:pubmed |
pubmed-article:20074573 | pubmed:issn | 1873-3468 | lld:pubmed |
pubmed-article:20074573 | pubmed:author | pubmed-author:Nakamaru-Ogis... | lld:pubmed |
pubmed-article:20074573 | pubmed:author | pubmed-author:OhnishiTomoko... | lld:pubmed |
pubmed-article:20074573 | pubmed:author | pubmed-author:YagiTakaoT | lld:pubmed |
pubmed-article:20074573 | pubmed:author | pubmed-author:KeinanEhudE | lld:pubmed |
pubmed-article:20074573 | pubmed:author | pubmed-author:Matsuno-YagiA... | lld:pubmed |
pubmed-article:20074573 | pubmed:author | pubmed-author:SinhaSubhash... | lld:pubmed |
pubmed-article:20074573 | pubmed:author | pubmed-author:HanHongnaH | lld:pubmed |
pubmed-article:20074573 | pubmed:copyrightInfo | Copyright (c) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | lld:pubmed |
pubmed-article:20074573 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20074573 | pubmed:day | 5 | lld:pubmed |
pubmed-article:20074573 | pubmed:volume | 584 | lld:pubmed |
pubmed-article:20074573 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20074573 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20074573 | pubmed:pagination | 883-8 | lld:pubmed |
pubmed-article:20074573 | pubmed:dateRevised | 2011-7-26 | lld:pubmed |
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pubmed-article:20074573 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20074573 | pubmed:articleTitle | The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor. | lld:pubmed |
pubmed-article:20074573 | pubmed:affiliation | Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. eikoo@mail.med.upenn.edu | lld:pubmed |
pubmed-article:20074573 | pubmed:publicationType | Journal Article | lld:pubmed |