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http://purl.uniprot.org/citations/24075991http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24075991http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24075991http://www.w3.org/2000/01/rdf-schema#comment"Accurate segregation of genetic material in eukaryotes relies on the kinetochore, a multiprotein complex that connects centromeric DNA with microtubules. In yeast and humans, two proteins-Mif2/CENP-C and Chl4/CNEP-N-interact with specialized centromeric nucleosomes and establish distinct but cross-connecting axes of chromatin-microtubule linkage. Proteins recruited by Chl4/CENP-N include a subset that regulates chromosome transmission fidelity. We show that Chl4 and a conserved member of this subset, Iml3, both from Saccharomyces cerevisiae, form a stable protein complex that interacts with Mif2 and Sgo1. We have determined the structures of an Iml3 homodimer and an Iml3-Chl4 heterodimer, which suggest a mechanism for regulating the assembly of this functional axis of the kinetochore. We propose that at the core centromere, the Chl4-Iml3 complex participates in recruiting factors, such as Sgo1, that influence sister chromatid cohesion and encourage sister kinetochore biorientation."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2013.08.036"xsd:string
http://purl.uniprot.org/citations/24075991http://purl.org/dc/terms/identifier"doi:10.1016/j.celrep.2013.08.036"xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/author"Harrison S.C."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/author"Harrison S.C."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/author"Hinshaw S.M."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/author"Hinshaw S.M."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/name"Cell Rep."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/pages"29-36"xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/pages"29-36"xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/title"An Iml3-Chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/title"An Iml3-Chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation."xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/24075991http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/24075991http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24075991
http://purl.uniprot.org/citations/24075991http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24075991
http://purl.uniprot.org/citations/24075991http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24075991
http://purl.uniprot.org/citations/24075991http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24075991
http://purl.uniprot.org/uniprot/P38265http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/24075991
http://purl.uniprot.org/uniprot/P38907http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/24075991