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http://purl.uniprot.org/citations/11983169http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11983169http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11983169http://www.w3.org/2000/01/rdf-schema#comment"Sister chromatids are held together by the multisubunit cohesin complex, which contains two SMC (Smc1 and Smc3) and two non-SMC (Scc1 and Scc3) proteins. The crystal structure of a bacterial SMC "hinge" region along with EM studies and biochemical experiments on yeast Smc1 and Smc3 proteins show that SMC protamers fold up individually into rod-shaped molecules. A 45 nm long intramolecular coiled coil separates the hinge region from the ATPase-containing "head" domain. Smc1 and Smc3 bind to each other via heterotypic interactions between their hinges to form a V-shaped heterodimer. The two heads of the V-shaped dimer are connected by different ends of the cleavable Scc1 subunit. Cohesin therefore forms a large proteinaceous loop within which sister chromatids might be entrapped after DNA replication."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(02)00515-4"xsd:string
http://purl.uniprot.org/citations/11983169http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(02)00515-4"xsd:string
http://purl.uniprot.org/citations/11983169http://purl.org/dc/terms/identifier"doi:10.1016/S1097-2765(02)00515-4"xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Loewe J."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Loewe J."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Lowe J."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Nasmyth K."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Nasmyth K."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Haering C.H."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Haering C.H."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Hochwagen A."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/author"Hochwagen A."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/pages"773-788"xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/pages"773-788"xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/title"Molecular architecture of SMC proteins and the yeast cohesin complex."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/title"Molecular architecture of SMC proteins and the yeast cohesin complex."xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/11983169http://purl.uniprot.org/core/volume"9"xsd:string