Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress
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Nucleotide excision repair is associated with the replisome and its efficiency depends on a direct interaction between XPA and PCNAInterplay between human DNA repair proteins at a unique double-strand break in vivoAlpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicityCtIP is required to initiate replication-dependent interstrand crosslink repairMetnase promotes restart and repair of stalled and collapsed replication forksTumor suppressor protein C53 antagonizes checkpoint kinases to promote cyclin-dependent kinase 1 activationFBH1 co-operates with MUS81 in inducing DNA double-strand breaks and cell death following replication stressInteraction between human MCM7 and Rad17 proteins is required for replication checkpoint signalingHuman UPF1 interacts with TPP1 and telomerase and sustains telomere leading-strand replicationA role for DEAD box 1 at DNA double-strand breaksVaccinia-related kinase 1 (VRK1) is an upstream nucleosomal kinase required for the assembly of 53BP1 foci in response to ionizing radiation-induced DNA damagePhospho-epitope binding by the BRCT domains of hPTIP controls multiple aspects of the cellular response to DNA damageA genome-scale DNA repair RNAi screen identifies SPG48 as a novel gene associated with hereditary spastic paraplegiaUV-induced replication arrest in the xeroderma pigmentosum variant leads to DNA double-strand breaks, gamma -H2AX formation, and Mre11 relocalizationPreferential localization of hyperphosphorylated replication protein A to double-strand break repair and checkpoint complexes upon DNA damageLoss of rereplication control in Saccharomyces cerevisiae results in extensive DNA damageNucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryoEpigenetic modifications in double-strand break DNA damage signaling and repairDynamics of DNA damage response proteins at DNA breaks: a focus on protein modificationsA PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA replicationBMI1-mediated histone ubiquitylation promotes DNA double-strand break repairClaspin operates downstream of TopBP1 to direct ATR signaling towards Chk1 activationHuman Mcm10 regulates the catalytic subunit of DNA polymerase-alpha and prevents DNA damage during replicationLentiviral Vpr usurps Cul4-DDB1[VprBP] E3 ubiquitin ligase to modulate cell cycleMre11 assembles linear DNA fragments into DNA damage signaling complexesTrial Watch: Targeting ATM-CHK2 and ATR-CHK1 pathways for anticancer therapyReplication Stress: A Lifetime of Epigenetic ChangeModulation of DNA damage and repair pathways by human tumour virusesA peek into the complex realm of histone phosphorylationTopBP1 Governs Hematopoietic Stem/Progenitor Cells Survival in Zebrafish Definitive HematopoiesisConditional inactivation of the DNA damage response gene Hus1 in mouse testis reveals separable roles for components of the RAD9-RAD1-HUS1 complex in meiotic chromosome maintenanceHormad1 mutation disrupts synaptonemal complex formation, recombination, and chromosome segregation in mammalian meiosisPeriodic Exposure of Keratinocytes to Cold Physical Plasma: An In Vitro Model for Redox-Related Diseases of the Skin.Dephosphorylation of gamma H2A by Glc7/protein phosphatase 1 promotes recovery from inhibition of DNA replication.Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair.Yeast G1 DNA damage checkpoint regulation by H2A phosphorylation is independent of chromatin remodelingNFBD1, a novel nuclear protein with signature motifs of FHA and BRCT, and an internal 41-amino acid repeat sequence, is an early participant in DNA damage responseNFBD1/KIAA0170 is a chromatin-associated protein involved in DNA damage signaling pathwaysRecruitment of the cell cycle checkpoint kinase ATR to chromatin during S-phaseMutation at the polymerase active site of mouse DNA polymerase delta increases genomic instability and accelerates tumorigenesis
P2860
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P2860
Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Histone H2AX is phosphorylated ...... sponse to replicational stress
@ast
Histone H2AX is phosphorylated ...... sponse to replicational stress
@en
Histone H2AX is phosphorylated ...... sponse to replicational stress
@nl
type
label
Histone H2AX is phosphorylated ...... sponse to replicational stress
@ast
Histone H2AX is phosphorylated ...... sponse to replicational stress
@en
Histone H2AX is phosphorylated ...... sponse to replicational stress
@nl
prefLabel
Histone H2AX is phosphorylated ...... sponse to replicational stress
@ast
Histone H2AX is phosphorylated ...... sponse to replicational stress
@en
Histone H2AX is phosphorylated ...... sponse to replicational stress
@nl
P2860
P3181
P356
P1476
Histone H2AX is phosphorylated ...... sponse to replicational stress
@en
P2860
P304
P3181
P356
10.1074/JBC.C100569200
P407
P577
2001-12-21T00:00:00Z