MDC1 Directly Binds Phosphorylated Histone H2AX to Regulate Cellular Responses to DNA Double-Strand Breaks
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- 29 December 2005
- journal article
- research article
- Published by Elsevier BV in Cell
- Vol. 123 (7), 1213-1226
- https://doi.org/10.1016/j.cell.2005.09.038
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Structural Basis of BACH1 Phosphopeptide Recognition by BRCA1 Tandem BRCT DomainsStructure, 2004
- Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1Nature Structural & Molecular Biology, 2004
- Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancerNature Structural & Molecular Biology, 2004
- Structure of the BRCT Repeats of BRCA1 Bound to a BACH1 Phosphopeptide: Implications for SignalingMolecular Cell, 2004
- Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaksNature, 2003
- NFBD1, Like 53BP1, Is an Early and Redundant Transducer Mediating Chk2 Phosphorylation in Response to DNA DamagePublished by Elsevier BV ,2003
- MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathwaysNature, 2003
- DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociationNature, 2003
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997