Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:15731008rdf:typepubmed:Citationlld:pubmed
pubmed-article:15731008lifeskim:mentionsumls-concept:C0012634lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C0028754lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C0010813lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C0033684lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1179435lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C0752166lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1858054lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1417174lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1705248lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C0679622lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1704666lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1546857lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1517892lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C0205314lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1556066lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1548799lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1619636lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1524073lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C1514873lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C0449432lld:lifeskim
pubmed-article:15731008lifeskim:mentionsumls-concept:C0208973lld:lifeskim
pubmed-article:15731008pubmed:issuePt 5lld:pubmed
pubmed-article:15731008pubmed:dateCreated2005-2-25lld:pubmed
pubmed-article:15731008pubmed:abstractTextChaperonins are multisubunit, cylinder-shaped molecular chaperones involved in folding newly synthesized polypeptides. Here we show that MKKS/BBS6, one of several proteins associated with Bardet-Biedl syndrome (BBS), is a Group II chaperonin-like protein that has evolved recently in animals from a subunit of the eukaryotic chaperonin CCT/TRiC, and diverged rapidly to acquire distinct functions. Unlike other chaperonins, cytosolic BBS6 does not oligomerize, and the majority of BBS6 resides within the pericentriolar material (PCM), a proteinaceous tube surrounding centrioles. During interphase, BBS6 is confined to the lateral surfaces of the PCM but during mitosis it relocalizes throughout the PCM and is found at the intercellular bridge. Its predicted substrate-binding apical domain is sufficient for centrosomal association, and several patient-derived mutations in this domain cause mislocalization of BBS6. Consistent with an important centrosomal function, silencing of the BBS6 transcript by RNA interference in different cell types leads to multinucleate and multicentrosomal cells with cytokinesis defects. The restricted tissue distribution of BBS6 further suggests that it may play important roles in ciliated epithelial tissues, which is consistent with the probable functions of BBS proteins in basal bodies (modified centrioles) and cilia. Our findings provide the first insight into the nature and cellular function of BBS6, and shed light on the potential causes of several ailments, including obesity, retinal degeneration, kidney dysfunction and congenital heart disease.lld:pubmed
pubmed-article:15731008pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:languageenglld:pubmed
pubmed-article:15731008pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:citationSubsetIMlld:pubmed
pubmed-article:15731008pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:15731008pubmed:statusMEDLINElld:pubmed
pubmed-article:15731008pubmed:monthMarlld:pubmed
pubmed-article:15731008pubmed:issn0021-9533lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:KatsanisNicho...lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:ArchibaldJohn...lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:OuYoung YYYlld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:RattnerJerome...lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:BealesPhilip...lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:BadanoJose...lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:LeitchCarmen...lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:LerouxMichel...lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:KimJun ChulJClld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:EsmailMuneer...lld:pubmed
pubmed-article:15731008pubmed:authorpubmed-author:FiedrichElsaElld:pubmed
pubmed-article:15731008pubmed:issnTypePrintlld:pubmed
pubmed-article:15731008pubmed:day1lld:pubmed
pubmed-article:15731008pubmed:volume118lld:pubmed
pubmed-article:15731008pubmed:ownerNLMlld:pubmed
pubmed-article:15731008pubmed:authorsCompleteYlld:pubmed
pubmed-article:15731008pubmed:pagination1007-20lld:pubmed
pubmed-article:15731008pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:meshHeadingpubmed-meshheading:15731008...lld:pubmed
pubmed-article:15731008pubmed:year2005lld:pubmed
pubmed-article:15731008pubmed:articleTitleMKKS/BBS6, a divergent chaperonin-like protein linked to the obesity disorder Bardet-Biedl syndrome, is a novel centrosomal component required for cytokinesis.lld:pubmed
pubmed-article:15731008pubmed:affiliationDepartment of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC, V5A 1S6, Canada.lld:pubmed
pubmed-article:15731008pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15731008pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:15731008pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
pubmed-article:15731008pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
entrez-gene:393134entrezgene:pubmedpubmed-article:15731008lld:entrezgene
entrez-gene:59030entrezgene:pubmedpubmed-article:15731008lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:15731008lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:15731008lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:15731008lld:pubmed
More...