| http://purl.uniprot.org/citations/16377563 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16377563 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16377563 | http://www.w3.org/2000/01/rdf-schema#comment | "Histone variant H2AX phosphorylation in response to DNA damage is the major signal for recruitment of DNA-damage-response proteins to regions of damaged chromatin. Loss of H2AX causes radiosensitivity, genome instability, and DNA double-strand-break repair defects, yet the mechanisms underlying these phenotypes remain obscure. Here, we demonstrate that mammalian MDC1/NFBD1 directly binds to phospho-H2AX (gammaH2AX) by specifically interacting with the phosphoepitope at the gammaH2AX carboxyl terminus. Moreover, through a combination of biochemical, cell-biological, and X-ray crystallographic approaches, we reveal the molecular details of the MDC1/NFBD1-gammaH2AX complex. These data provide compelling evidence that the MDC1/NFBD1 BRCT repeat domain is the major mediator of gammaH2AX recognition following DNA damage. We further show that MDC1/NFBD1-gammaH2AX complex formation regulates H2AX phosphorylation and is required for normal radioresistance and efficient accumulation of DNA-damage-response proteins on damaged chromatin. Thus, binding of MDC1/NFBD1 to gammaH2AX plays a central role in the mammalian response to DNA damage."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2005.09.038"xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2005.09.038"xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Jackson S.P."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Jackson S.P."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Smerdon S.J."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Smerdon S.J."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Yaffe M.B."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Yaffe M.B."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Stucki M."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Stucki M."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Clapperton J.A."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Clapperton J.A."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Mohammad D."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/author | "Mohammad D."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/pages | "1213-1226"xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/pages | "1213-1226"xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/title | "MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks."xsd:string |
| http://purl.uniprot.org/citations/16377563 | http://purl.uniprot.org/core/title | "MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks."xsd:string |