An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks

scientific article published on 08 December 2008

An oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/MCB.01011-08
P932PMC publication ID2643802
P698PubMed publication ID19064641

P2093author name stringThanos D Halazonetis
Omar Zgheib
Juergen Brugger
Kristopher Pataky
P2860cites workMDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaksQ24299852
RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteinsQ24300411
RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assemblyQ24300428
Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage responseQ24306765
RAP80 targets BRCA1 to specific ubiquitin structures at DNA damage sitesQ24306789
Ubiquitin-binding protein RAP80 mediates BRCA1-dependent DNA damage responseQ24306807
The ubiquitin-interacting motif containing protein RAP80 interacts with BRCA1 and functions in DNA damage repair responseQ24652479
Orchestration of the DNA-damage response by the RNF8 ubiquitin ligaseQ24653776
Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repairQ24669691
Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulationQ27642010
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coilQ27655682
A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutantsQ27731470
Rad9 BRCT domain interaction with phosphorylated H2AX regulates the G1 checkpoint in budding yeastQ27930415
The checkpoint Saccharomyces cerevisiae Rad9 protein contains a tandem tudor domain that recognizes DNAQ27934159
Role of Dot1-dependent histone H3 methylation in G1 and S phase DNA damage checkpoint functions of Rad9.Q27939003
Accumulation of Checkpoint Protein 53BP1 at DNA Breaks Involves Its Binding to Phosphorylated Histone H2AXQ28191330
DNA damage-induced G2-M checkpoint activation by histone H2AX and 53BP1Q28215916
A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouseQ28289637
Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaksQ28291639
Kinetochore localisation of the DNA damage response component 53BP1 during mitosisQ28509503
Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damageQ29614218
Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damageQ29614528
p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaksQ30014828
Negative cell cycle regulation and DNA damage-inducible phosphorylation of the BRCT protein 53BP1.Q30947641
Image-based modeling reveals dynamic redistribution of DNA damage into nuclear sub-domainsQ33293154
Tying the loose ends together in DNA double strand break repair with 53BP1.Q35082739
Histone H2A phosphorylation controls Crb2 recruitment at DNA breaks, maintains checkpoint arrest, and influences DNA repair in fission yeastQ35126538
Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1Q36320732
Surviving the breakup: the DNA damage checkpoint.Q36521813
Preferential dimethylation of histone H4 lysine 20 by Suv4-20Q36585568
Phosphorylation and rapid relocalization of 53BP1 to nuclear foci upon DNA damageQ39457941
Microcollimator for micrometer-wide stripe irradiation of cells using 20-30 keV X rays.Q39821170
The tandem BRCT domain of 53BP1 is not required for its repair functionQ40219964
Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathwaysQ41861185
Histone modification-dependent and -independent pathways for recruitment of checkpoint protein Crb2 to double-strand breaks.Q42150641
Boundaries and physical characterization of a new domain shared between mammalian 53BP1 and yeast Rad9 checkpoint proteins.Q42661170
Potential role for 53BP1 in DNA end-joining repair through direct interaction with DNA.Q44489693
Homo-oligomerization is the essential function of the tandem BRCT domains in the checkpoint protein Crb2.Q44960327
53BP1 exchanges slowly at the sites of DNA damage and appears to require RNA for its association with chromatin.Q46445917
53BP1 oligomerization is independent of its methylation by PRMT1.Q46809487
Histone H2A phosphorylation and H3 methylation are required for a novel Rad9 DSB repair function following checkpoint activation.Q50731881
Docking onto chromatin via the Saccharomyces cerevisiae Rad9 Tudor domain.Q51081692
The BRCT domain of the S. cerevisiae checkpoint protein Rad9 mediates a Rad9-Rad9 interaction after DNA damageQ64131921
53BP1, an activator of ATM in response to DNA damageQ64388924
An engineered four-stranded coiled coil substitutes for the tetramerization domain of wild-type p53 and alleviates transdominant inhibition by tumor-derived p53 mutantsQ70866376
The Tudor tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide bindingQ80515739
P433issue4
P407language of work or nameEnglishQ1860
P304page(s)1050-1058
P577publication date2008-12-08
P1433published inMolecular and Cellular BiologyQ3319478
P1476titleAn oligomerized 53BP1 tudor domain suffices for recognition of DNA double-strand breaks
P478volume29

Reverse relations

cites work (P2860)
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