MDC1 Directly Binds Phosphorylated Histone H2AX to Regulate Cellular Responses to DNA Double-Strand Breaks

2005/12/01 by Manuel Stucki, Julie A. Clapperton, Duaa H. Mohammad +4 · 1 citation
Biochemistry, Genetics and Molecular Biology · Medicine · #Cancer-related Molecular Pathways #DNA Repair Mechanisms #Genomics and Chromatin Dynamics

paper · pdf · doi:10.1016/j.cell.2005.09.038

crossref issued 2005/12/01 · crossref published 2005/12/01 · crossref published-print 2005/12/01 · openalex publication_date 2005/12/01 · crossref created 2005/12/30 · crossref deposited 2023/01/28 · openalex created_date 2025/10/10 · crossref indexed 2026/07/24 · openalex updated_date 2026/07/28

Citations

• MDC1 is a mediator of the mammalian DNA damage checkpoint
• DNA Double-stranded Breaks Induce Histone H2AX Phosphorylation on Serine 139
• Histone H2A variants H2AX and H2AZ
• A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
• Megabase Chromatin Domains Involved in DNA Double-Strand Breaks in Vivo
• Genomic Instability in Mice Lacking Histone H2AX
• Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor
• Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure

Cited by

• Chromatin remodeling [wikipedia]