Structure of C-terminal Tandem BRCT Repeats of Rtt107 Protein Reveals Critical Role in Interaction with Phosphorylated Histone H2A during DNA Damage Repair - Wikidata - awgldk - TriplyDB

Structure of C-terminal Tandem BRCT Repeats of Rtt107 Protein Reveals Critical Role in Interaction with Phosphorylated Histone H2A during DNA Damage Repair

Structure of C-terminal Tandem BRCT Repeats of Rtt107 Protein Reveals Critical Role in Interaction with Phosphorylated Histone H2A during DNA Damage Repair

http://www.wikidata.org/entity/Q27676802

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Crystal structure of triple-BRCT-domain of ECT2 and insights into the binding characteristics to CYK-4 Slx4 and Rtt107 control checkpoint signalling and DNA resection at double-strand breaks.Assembly of Slx4 signaling complexes behind DNA replication forks Heterochromatin controls γH2A localization in Neurospora crassa.Genetic Interaction Landscape Reveals Critical Requirements for Schizosaccharomyces pombe Brc1 in DNA Damage Response Mutants Dampening DNA damage checkpoint signalling via coordinated BRCT domain interactions.Critical Function of γH2A in S-Phase DNA-repair scaffolds dampen checkpoint signalling by counteracting the adaptor Rad9 Perceiving the epigenetic landscape through histone readers.Histone H1 Limits DNA Methylation in Neurospora crassa.The Rtt107 BRCT scaffold and its partner modification enzymes collaborate to promote replication.Dbf4-dependent kinase and the Rtt107 scaffold promote Mus81-Mms4 resolvase activation during mitosis Readout of epigenetic modifications.Brc1 links replication stress response and centromere function.Slx4 scaffolding in homologous recombination and checkpoint control: lessons from yeast.Multi-BRCT scaffolds use distinct strategies to support genome maintenance.Control of Mus81 nuclease during the cell cycle.γH2A-binding protein Brc1 affects centromere function in fission yeast Replication fork collapse and genome instability in a deoxycytidylate deaminase mutant.Replication checkpoint: tuning and coordination of replication forks in s phase.A novel non-canonical forkhead-associated (FHA) domain-binding interface mediates the interaction between Rad53 and Dbf4 proteins.Reading chromatin signatures after DNA double-strand breaks.

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P2860

Structure of C-terminal Tandem BRCT Repeats of Rtt107 Protein Reveals Critical Role in Interaction with Phosphorylated Histone H2A during DNA Damage Repair

http://www.wikidata.org/entity/Q27676802

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2012 nî lūn-bûn

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2012 թուականի Մարտին հրատարակուած գիտական յօդուած

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2012 թվականի մարտին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Journal of Biological Chemistry

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Structure of C-terminal Tandem ...... e H2A during DNA Damage Repair

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Fudong Li

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Hongda Huang

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Jihui Wu

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Juncheng Wang

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Kaixian Liu

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Xinxin Li

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Yunyu Shi

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P2860

Crystal structure of an Xrcc4-DNA ligase IV complex

Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure

The BRCT domain is a phospho-protein binding domain

MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks

Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor.

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Processing of X-ray diffraction data collected in oscillation mode

γH2A binds Brc1 to maintain genome integrity during S-phase

Structure and function of the Rad9-binding region of the DNA-damage checkpoint adaptor TopBP1

SOLVE and RESOLVE: automated structure solution and density modification

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