The human Werner syndrome protein stimulates repair of oxidative DNA base damage by the DNA glycosylase NEIL1
about
Human RECQL5 participates in the removal of endogenous DNA damageRoles of Werner syndrome protein in protection of genome integrityEarly steps in the DNA base excision/single-strand interruption repair pathway in mammalian cellsHuman premature aging, DNA repair and RecQ helicasesA novel function for the Mre11-Rad50-Xrs2 complex in base excision repair.RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures.Mutation versus repair: NEIL1 removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts.Substrate specific stimulation of NEIL1 by WRN but not the other human RecQ helicases.Specific Inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases.DNA repair deficiency in neurodegeneration.Involvement of Werner syndrome protein in MUTYH-mediated repair of oxidative DNA damage.A bioinformatics filtering strategy for identifying radiation response biomarker candidates.Prereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins.The Werner syndrome protein limits the error-prone 8-oxo-dG lesion bypass activity of human DNA polymerase kappa.Non-B DNA-forming sequences and WRN deficiency independently increase the frequency of base substitution in human cells.Bone marrow cell transcripts from Fanconi anaemia patients reveal in vivo alterations in mitochondrial, redox and DNA repair pathways.Generation of induced pluripotent stem cell lines from 3 distinct laminopathies bearing heterogeneous mutations in lamin A/CThe DNA repair endonuclease XPG interacts directly and functionally with the WRN helicase defective in Werner syndromeThe role of the mammalian DNA end-processing enzyme polynucleotide kinase 3'-phosphatase in spinocerebellar ataxia type 3 pathogenesis.ATP Depletion Via Mitochondrial F1F0 Complex by Lethal Factor is an Early Event in B. Anthracis-Induced Sudden Cell Death.Oxidative genome damage and its repair: implications in aging and neurodegenerative diseases.The C-terminal Domain (CTD) of Human DNA Glycosylase NEIL1 Is Required for Forming BERosome Repair Complex with DNA Replication Proteins at the Replicating Genome: DOMINANT NEGATIVE FUNCTION OF THE CTD.Depletion of WRN protein causes RACK1 to activate several protein kinase C isoformsProteome-wide identification of WRN-interacting proteins in untreated and nuclease-treated samples.Human RecQ helicases in DNA repair, recombination, and replication.DNA binding residues in the RQC domain of Werner protein are critical for its catalytic activities.Psoralen-induced DNA adducts are substrates for the base excision repair pathway in human cellsEnhancement of NEIL1 protein-initiated oxidized DNA base excision repair by heterogeneous nuclear ribonucleoprotein U (hnRNP-U) via direct interaction.Coordination of DNA repair by NEIL1 and PARP-1: a possible link to agingNeil3, the final frontier for the DNA glycosylases that recognize oxidative damage.Base excision repair, aging and health span.Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1Superior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1The RECQL4 protein, deficient in Rothmund-Thomson syndrome is active on telomeric D-loops containing DNA metabolism blocking lesionsRising from the RecQ-age: the role of human RecQ helicases in genome maintenanceMice expressing an error-prone DNA polymerase in mitochondria display elevated replication pausing and chromosomal breakage at fragile sites of mitochondrial DNA.The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactionsDirect and indirect roles of RECQL4 in modulating base excision repair capacity.Functions of disordered regions in mammalian early base excision repair proteins.RecQ helicases; at the crossroad of genome replication, repair, and recombination.
P2860
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P2860
The human Werner syndrome protein stimulates repair of oxidative DNA base damage by the DNA glycosylase NEIL1
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@ast
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@en
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@en-gb
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@nl
type
label
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@ast
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@en
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@en-gb
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@nl
prefLabel
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@ast
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@en
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@en-gb
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@nl
P2093
P2860
P921
P356
P1476
The human Werner syndrome prot ...... e by the DNA glycosylase NEIL1
@en
P2093
Istvan Boldogh
Jae Wan Lee
Jason Piotrowski
Jeanine A Harrigan
Marc M Greenberg
Nadja de Souza Pinto
Sankar Mitra
Tapas K Hazra
Vilhelm A Bohr
P2860
P304
26591-26602
P356
10.1074/JBC.M703343200
P407
P577
2007-07-03T00:00:00Z