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Human XRCC4 Protein expressed in HEK-293 Cells - ABIN2735698
Myers, Maxwell, Wang: Quantification of XRCC and DNA-PK proteins in cancer cell lines and human tumors by LC-MS/MS. in Bioanalysis 2014
XRCC4 has a negative role in Agrobacterium T-DNA integration.
Three-locus model of gene-gene interactions OGG1 (show OGG1 Proteins) (rs1052133) * ADPRT (show PARP1 Proteins) (rs1136410) * XRCC4 (rs6869366) was associated with high genotoxic risk in coal miners.
Results showed that eNOS (show NOS3 Proteins) and XRCC4 VNTR variants might play a potential role in schizophrenia + nicotine dependence and/or nicotine dependence pathophysiology.
Phospho-blocking and -mimicking mutations impact both the stability and DNA bridging capacity of XRCC4/XLF (show NHEJ1 Proteins) complexes, but without affecting their ability to stimulate LIG4 (show LIG4 Proteins) activity. Implicit in this finding is that phosphorylation may regulate DNA bridging by XRCC4/XLF (show NHEJ1 Proteins) filaments.
This study demonstrated both ligase IV and XRCC4 may act in concert to modulate the development of glioma.
Data suggest that genetic variants of XRCC4 and ERCC1 (show ERCC1 Proteins) may independently or jointly affect survival in chemotherapy-treated gastric cancer (GCa (show NPR1 Proteins)) patients by modulating the gene expression in the tumors.
In a recombinant PNKP (show PNKP Proteins)-XRCC4-LigIV complex, stable binding of PNKP (show PNKP Proteins) requires XRCC4 phosphorylation. Only one PNKP (show PNKP Proteins) protomer binds per XRCC4 dimer. Both the PNKP (show PNKP Proteins) FHA (show CRY2 Proteins) and catalytic domains contact the XRCC4 coiled-coil and LigIV BRCT repeats. Multipoint contacts between PNKP (show PNKP Proteins) and XRCC4-LigIV regulate PNKP (show PNKP Proteins) recruitment and activity within NHEJ.
Data suggest that stimulation of Artemis nuclease/DCLRE1C (show DCLRE1C Proteins) activity by XRCC4-DNA ligase IV (show LIG4 Proteins) hetero-complex and efficiency of blunt-end ligation are determined by structural configurations at the DNA ends. (XRCC4 = X-ray repair cross complementing 4)
involvement of ZNF281 (show ZNF281 Proteins) in the cellular response to genotoxic stress through the control exercised on the expression of genes that act in different repair mechanisms
the various XRCC4 mutations that lead to primordial dwarfism and their impact on non-homologous end joining and V(D)J recombination are discussed (Review)
XRCC4 expression might have an influence on results of radiotherapy for patients with esophageal squamous cell carcinoma.
We find that non-canonical HR termination can occur in the absence of the classical non-homologous end joining gene XRCC4. We observe obligatory use of microhomology (MH)-mediated end joining and/or nucleotide addition during rejoining with the second end of the break
Data show that combined deletion of X-ray repair cross-complementing protein 4 (Xrcc4) and tumor suppressor p53 (Trp53 (show TP53 Proteins)) predisposes B cells to lymphomagenesis.
FBXW7 (show FBXW7 Proteins) facilitates nonhomologous end-joining via K63-linked polyubiquitylation of XRCC4 in tumor cells.
The present results collectively indicated that Lys271, but not Lys210, of XRCC4 is required for the nuclear localization of XRCC4 and LIG4 (show LIG4 Proteins) and that the nuclear localizing ability is essential for DSB repair function of XRCC4.
DNA-PK and ATM (show ATM Proteins) acts in parallel upstream of XRCC4, regulating through phosphorylation
XRCC4 C-terminal point mutants, R325F and N326L, are functionally deficient in terms of cell survival after irradiation.
These results establish that nonrecurrent CNVs can be, and frequently are, formed by mechanisms other than Xrcc4-dependent NHEJ.
analysis of the association of radiation-induced XRCC4 with chromatin DNA, by biochemical fractionation
conditional inactivation of the XRCC4 in nestin (show NES Proteins)-expressing neuronal progenitor cells, although leading to no obvious phenotype in a WT background, leads to early onset of neuronally differentiated medulloblastomas (MBs (show NEU2 Proteins)) in a p53 (show TP53 Proteins)-deficient background
The protein encoded by this gene functions together with DNA ligase IV and the DNA-dependent protein kinase in the repair of DNA double-strand break by non-homologous end joining and the completion of V(D)J recombination events. The non-homologous end-joining pathway is required both for normal development and for suppression of tumors. This gene functionally complements XR-1 Chinese hamster ovary cell mutant, which is impaired in DNA double-strand breaks produced by ionizing radiation and restriction enzymes. Alternative transcription initiation and alternative splicing generates several transcript variants.
DNA repair protein XRCC4
, X-ray repair complementing defective repair in Chinese hamster cells 4
, DNA-repair protein XRCC4
, X-ray repair cross complementing protein 4
, X-ray repair cross-complementing protein 4
, X-ray repair, complementing defective, repair in Chinese hamster