Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4 - Test2 - elhamkhani - TriplyDB

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

http://www.wikidata.org/entity/Q24675041

about

Ku recruits XLF to DNA double-strand breaks The E3 ligase RNF8 regulates KU80 removal and NHEJ repair A dual role for UVRAG in maintaining chromosomal stability independent of autophagy The dynamics of Ku70/80 and DNA-PKcs at DSBs induced by ionizing radiation is dependent on the complexity of damage Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications Eukaryotic DNA ligases: structural and functional insights Up-regulation of WRN and DNA ligase IIIalpha in chronic myeloid leukemia: consequences for the repair of DNA double-strand breaks Chromosome breakage after G2 checkpoint release C1D family proteins in coordinating RNA processing, chromosome condensation and DNA damage response The role of RecQ helicases in non-homologous end-joining Chemotherapeutic compounds targeting the DNA double-strand break repair pathways: the good, the bad, and the promising DNA-PK: a dynamic enzyme in a versatile DSB repair pathway Genotypic characteristics of resistant tumors to pre-operative ionizing radiation in rectal cancer Bub3-BubR1-dependent sequestration of Cdc20Fizzy at DNA breaks facilitates the correct segregation of broken chromosomes Systems modelling of NHEJ reveals the importance of redox regulation of Ku70/80 in the dynamics of dna damage foci Differentiation driven changes in the dynamic organization of Basal transcription initiation Impact of histone H4 lysine 20 methylation on 53BP1 responses to chromosomal double strand breaks Yeast Nej1 is a key participant in the initial end binding and final ligation steps of nonhomologous end joining.Recruitment and dissociation of nonhomologous end joining proteins at a DNA double-strand break in Saccharomyces cerevisiae.Ubiquitylation, neddylation and the DNA damage response TRF2 interaction with Ku heterotetramerization interface gives insight into c-NHEJ prevention at human telomeres Factors determining DNA double-strand break repair pathway choice in G2 phase Do polymorphisms in XRCC4 influence prostate cancer susceptibility in North Indian population?Non-homologous end-joining, a sticky affair Role of non-homologous end joining in V(D)J recombination A noncatalytic function of the ligation complex during nonhomologous end joining.Comparative analysis of different laser systems to study cellular responses to DNA damage in mammalian cells The protein phosphatase 1 regulator PNUTS is a new component of the DNA damage response.Analysis of DNA double-strand break response and chromatin structure in mitosis using laser microirradiation.Autophosphorylation of DNA-PKCS regulates its dynamics at DNA double-strand breaks.A novel role of the chromokinesin Kif4A in DNA damage response.Rapid recruitment of BRCA1 to DNA double-strand breaks is dependent on its association with Ku80 Radiation microbeams as spatial and temporal probes of subcellular and tissue response.Biological dose estimation of UVA laser microirradiation utilizing charged particle-induced protein foci.Dynamics of the PI3K-like protein kinase members ATM and DNA-PKcs at DNA double strand breaks.Identification of rep-associated factors in herpes simplex virus type 1-induced adeno-associated virus type 2 replication compartments.Orphan receptor TR3 enhances p53 transactivation and represses DNA double-strand break repair in hepatoma cells under ionizing radiation.A fine-scale dissection of the DNA double-strand break repair machinery and its implications for breast cancer therapy.Mechanisms of chromosomal rearrangements in solid tumors: the model of papillary thyroid carcinoma.Non-homologous end joining: emerging themes and unanswered questions.

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P2860

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

http://www.wikidata.org/entity/Q24675041

description

2006 nî lūn-bûn

@nan

2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@ast

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@en

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@nl

type

label

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@ast

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@en

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@nl

prefLabel

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@ast

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@en

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@nl

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PNAS.0609061103

P1433

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

P1476

Dynamic assembly of end-joining complexes requires interaction between Ku70/80 and XRCC4

@en

P2093

Adriaan B Houtsmuller

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

Hennie T Brüggenwirth

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

Karel Bezstarosti

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

Nicole S Verkaik

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

Stephan P Persengiev

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

Theo M Luider

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

P2860

Cernunnos, a novel nonhomologous end-joining factor, is mutated in human immunodeficiency with microcephaly

XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining

Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells

Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV

DNA binding of Xrcc4 protein is associated with V(D)J recombination but not with stimulation of DNA ligase IV activity

Synapsis of DNA ends by DNA-dependent protein kinase

Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV

Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks.

Defining interactions between DNA-PK and ligase IV/XRCC4.

Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair.

P304

18597-18602

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

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scholarly article

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5113907

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10.1073/PNAS.0609061103

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P407

P433

49

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103

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

P50

Bogdan I Florea

Giuseppina Giglia-Mari

P577

2006-11-21T00:00:00Z

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

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6674386

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17124166

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1693708

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