| http://purl.uniprot.org/citations/37491363 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/37491363 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/37491363 | http://www.w3.org/2000/01/rdf-schema#comment | "The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers contributed by three dimers explaining the role of the unusual higher-order assembly. By contrast, the right-end is bound to no BED domains at all. Thus, this work supports a model in which Hermes multimerizes to gather enough BED domains to find its left-end among the abundant genomic DNA, facilitating the subsequent interaction with the right-end."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-023-40210-3"xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-023-40210-3"xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/author | "Dyda F."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/author | "Dyda F."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/author | "Hickman A.B."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/author | "Hickman A.B."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/author | "Furman C.M."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/author | "Furman C.M."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/author | "Lannes L."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/author | "Lannes L."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/name | "Nat. Commun."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/name | "Nat Commun"xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/pages | "4470"xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/pages | "4470"xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/title | "Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/title | "Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding."xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://purl.uniprot.org/core/volume | "14"xsd:string |
| http://purl.uniprot.org/citations/37491363 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/37491363 |
| http://purl.uniprot.org/citations/37491363 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/37491363 |