pubmed-article:20462491 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20462491 | lifeskim:mentions | umls-concept:C0947504 | lld:lifeskim |
pubmed-article:20462491 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:20462491 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:20462491 | lifeskim:mentions | umls-concept:C1553467 | lld:lifeskim |
pubmed-article:20462491 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:20462491 | pubmed:dateCreated | 2010-5-13 | lld:pubmed |
pubmed-article:20462491 | pubmed:abstractText | Apaf-1 coassembles with cytochrome c to form the apoptosome, which then binds and activates procaspase-9 (pc-9). We removed pc-9 catalytic domains from the holoapoptosome by site-directed thrombinolysis. A structure of the resulting apoptosome-pc-9 CARD complex was then determined at approximately 9.5 A resolution. In our model, the central hub is constructed like other AAA+ protein rings but also contains novel features. At higher radius, the regulatory region of each Apaf-1 is comprised of tandem seven and eight blade beta-propellers with cytochrome c docked between them. Remarkably, Apaf-1 CARDs are disordered in the ground state. During activation, each Apaf-1 CARD interacts with a pc-9 CARD and these heterodimers form a flexibly tethered "disk" that sits above the central hub. When taken together, the data reveal conformational changes during Apaf-1 assembly that allow pc-9 activation. The model also provides a plausible explanation for the effects of NOD mutations that have been mapped onto the central hub. | lld:pubmed |
pubmed-article:20462491 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:language | eng | lld:pubmed |
pubmed-article:20462491 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20462491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20462491 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20462491 | pubmed:month | May | lld:pubmed |
pubmed-article:20462491 | pubmed:issn | 1878-4186 | lld:pubmed |
pubmed-article:20462491 | pubmed:author | pubmed-author:WangXiaodongX | lld:pubmed |
pubmed-article:20462491 | pubmed:author | pubmed-author:LudtkeSteven... | lld:pubmed |
pubmed-article:20462491 | pubmed:author | pubmed-author:AkeyChristoph... | lld:pubmed |
pubmed-article:20462491 | pubmed:author | pubmed-author:TopfMayaM | lld:pubmed |
pubmed-article:20462491 | pubmed:author | pubmed-author:YuanShujunS | lld:pubmed |
pubmed-article:20462491 | pubmed:author | pubmed-author:YuXinchaoX | lld:pubmed |
pubmed-article:20462491 | pubmed:copyrightInfo | Copyright 2010 Elsevier Ltd. All rights reserved. | lld:pubmed |
pubmed-article:20462491 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20462491 | pubmed:day | 12 | lld:pubmed |
pubmed-article:20462491 | pubmed:volume | 18 | lld:pubmed |
pubmed-article:20462491 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20462491 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20462491 | pubmed:pagination | 571-83 | lld:pubmed |
pubmed-article:20462491 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
pubmed-article:20462491 | pubmed:meshHeading | pubmed-meshheading:20462491... | lld:pubmed |
pubmed-article:20462491 | pubmed:meshHeading | pubmed-meshheading:20462491... | lld:pubmed |
pubmed-article:20462491 | pubmed:meshHeading | pubmed-meshheading:20462491... | lld:pubmed |
pubmed-article:20462491 | pubmed:meshHeading | pubmed-meshheading:20462491... | lld:pubmed |
pubmed-article:20462491 | pubmed:meshHeading | pubmed-meshheading:20462491... | lld:pubmed |
pubmed-article:20462491 | pubmed:meshHeading | pubmed-meshheading:20462491... | lld:pubmed |
pubmed-article:20462491 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20462491 | pubmed:articleTitle | Structure of an apoptosome-procaspase-9 CARD complex. | lld:pubmed |
pubmed-article:20462491 | pubmed:affiliation | Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA 02118-2526, USA. | lld:pubmed |
pubmed-article:20462491 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20462491 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:20462491 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20462491 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20462491 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20462491 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20462491 | lld:pubmed |