Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1 - Test2 - elhamkhani - TriplyDB

Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1

Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1

http://www.wikidata.org/entity/Q27671621

about

DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links Cross talk of tyrosine kinases with the DNA damage signaling pathways Protein and DNA modifications: evolutionary imprints of bacterial biochemical diversification and geochemistry on the provenance of eukaryotic epigenetics Structural Insights into Recognition of MDC1 by TopBP1 in DNA Replication Checkpoint Control DNA IR-Double Strand Breaks (DSBs) and cellular response via ATM MCPH1: a window into brain development and evolution.Sensing core histone phosphorylation - a matter of perfect timing.BAZ1B is dispensable for H2AX phosphorylation on Tyrosine 142 during spermatogenesis DNA damage response defect in Williams-Beuren syndrome.Reversion of the ErbB malignant phenotype and the DNA damage response.Systematic analysis of histone modification readout.Chromatin and the genome integrity network.Readout of epigenetic modifications.Histone variants: key players of chromatin.Chromatin modifications and DNA repair: beyond double-strand breaks.Functional assays provide a robust tool for the clinical annotation of genetic variants of uncertain significance.H-Ferritin-nanocaged olaparib: a promising choice for both BRCA-mutated and sporadic triple negative breast cancer The proteomic investigation of chromatin functional domains reveals novel synergisms among distinct heterochromatin components.Chromosome structure deficiencies in MCPH1 syndrome.Non-canonical reader modules of BAZ1A promote recovery from DNA damage.ATM Localization and Heterochromatin Repair Depend on Direct Interaction of the 53BP1-BRCT2 Domain with γH2AX.EYA1-4 dephosphorylates tyrosine Y142 of H2AFX Reading chromatin signatures after DNA double-strand breaks.Targeting Phosphopeptide Recognition by the Human BRCA1 Tandem BRCT Domain to Interrupt BRCA1-Dependent Signaling.

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P2860

Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1

http://www.wikidata.org/entity/Q27671621

description

2012 nî lūn-bûn

@nan

2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2012年の論文

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2012年論文

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2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Dual recognition of phosphoser ...... damage response protein MCPH1

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Dual recognition of phosphoser ...... damage response protein MCPH1

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Dual recognition of phosphoser ...... damage response protein MCPH1

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type

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Dual recognition of phosphoser ...... damage response protein MCPH1

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Dual recognition of phosphoser ...... damage response protein MCPH1

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Dual recognition of phosphoser ...... damage response protein MCPH1

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Dual recognition of phosphoser ...... damage response protein MCPH1

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Dual recognition of phosphoser ...... damage response protein MCPH1

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Dual recognition of phosphoser ...... damage response protein MCPH1

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PNAS.1212366109

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Proceedings of the National Academy of Sciences of the United States of America

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Dual recognition of phosphoser ...... damage response protein MCPH1

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P2093

Annie Héroux

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Duaa H Mohammad

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Georges Mer

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Harihar Basnet

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James R Thompson

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Maria Victoria Botuyan

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Michael B Yaffe

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Michael G Rosenfeld

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Namit Singh

http://www.w3.org/2001/XMLSchema#string

Timothy D Wiltshire

http://www.w3.org/2001/XMLSchema#string

P2860

Identification of microcephalin, a protein implicated in determining the size of the human brain

Microcephalin Is a DNA Damage Response Protein Involved in Regulation of CHK1 and BRCA1

MDC1 is a mediator of the mammalian DNA damage checkpoint

The BRCT domain is a phospho-protein binding domain

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

WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity

Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions

Dephosphorylation of the C-terminal tyrosyl residue of the DNA damage-related histone H2A.X is mediated by the protein phosphatase eyes absent

Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains

Structural and functional analysis of the Crb2-BRCT2 domain reveals distinct roles in checkpoint signaling and DNA damage repair

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36

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109

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Fergus J. Couch

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2012-09-04T00:00:00Z

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230712390

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