| http://purl.uniprot.org/citations/19109428 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19109428 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19109428 | http://www.w3.org/2000/01/rdf-schema#comment | "Centrioles are intriguing cylindrical organelles composed of triplet microtubules. Proteomic data suggest that a large number of proteins besides tubulin are necessary for the formation and maintenance of a centriole's complex structure. Expansion of the preexisting centriole proteome from the green alga Chlamydomonas reinhardtii revealed additional human disease genes, emphasizing the significance of centrioles in normal human tissue homeostasis. We found that two classes of ciliary disease genes were highly represented among the basal body proteome: cystic kidney disease (especially nephronophthisis) syndromes, including Meckel/Joubert-like and oral-facial-digital syndrome, caused by mutations in CEP290, MKS1, OFD1, and AHI1/Jouberin proteins and cone-rod dystrophy syndrome genes, including UNC-119/HRG4, NPHP4, and RPGR1. We further characterized proteome of the centriole (POC) 1, a highly abundant WD40 domain-containing centriole protein. We found that POC1 is recruited to nascent procentrioles and localizes in a highly asymmetrical pattern in mature centrioles corresponding to sites of basal-body fiber attachment. Knockdown of POC1 in human cells caused a reduction in centriole duplication, whereas overexpression caused the appearance of elongated centriole-like structures. Together, these data suggest that POC1 is involved in early steps of centriole duplication as well as in the later steps of centriole length control."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e08-06-0619"xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e08-06-0619"xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Geimer S."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Geimer S."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Marshall W.F."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Marshall W.F."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Yates J. III"xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Yates J. III"xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Keller L.C."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Keller L.C."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Zamora I."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Zamora I."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Romijn E."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/author | "Romijn E."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/pages | "1150-1166"xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/pages | "1150-1166"xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/title | "Molecular architecture of the centriole proteome: the conserved WD40 domain protein POC1 is required for centriole duplication and length control."xsd:string |
| http://purl.uniprot.org/citations/19109428 | http://purl.uniprot.org/core/title | "Molecular architecture of the centriole proteome: the conserved WD40 domain protein POC1 is required for centriole duplication and length control."xsd:string |