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| http://purl.uniprot.org/citations/23790282 | http://www.w3.org/2000/01/rdf-schema#comment | "Histones are among the most conserved proteins in eukaryotes: the structural constraints of the nucleosome pose a challenge to evolving novel function. Nevertheless, confined histone surfaces have diversified, allowing the modulation of basic chromatin function through specialized histone chaperones. Recent structures of three histone-chaperone complexes, DAXX, HJURP, and Scm3, exemplify a common parsimonious solution to the restricted evolutionary space of histone recognition by their cognate histone chaperones: the reutilization of existing themes in histone structural biology."xsd:string |
| http://purl.uniprot.org/citations/23790282 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.tibs.2013.04.002"xsd:string |
| http://purl.uniprot.org/citations/23790282 | http://purl.uniprot.org/core/author | "Elsasser S.J."xsd:string |
| http://purl.uniprot.org/citations/23790282 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23790282 | http://purl.uniprot.org/core/name | "Trends Biochem Sci"xsd:string |
| http://purl.uniprot.org/citations/23790282 | http://purl.uniprot.org/core/pages | "333-336"xsd:string |
| http://purl.uniprot.org/citations/23790282 | http://purl.uniprot.org/core/title | "A common structural theme in histone chaperones mimics interhistone contacts."xsd:string |
| http://purl.uniprot.org/citations/23790282 | http://purl.uniprot.org/core/volume | "38"xsd:string |
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