Reference health

Regulation of oxidized base damage repair by chromatin assembly factor 1 subunit A

https://doi.org/10.1093/nar/gkw1024
CiteStamped reference-health badge
54/54 checkable references clean · checked 2026-07-26

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

The 54 checked references that resolve
resolves10.1093/carcin/bgn250
Base excision repair of oxidative DNA damage and association with cancer and aging
resolves10.1016/S0891-5849(02)00819-5
Choreography of oxidative damage repair in mammalian genomes1,2 1Guest Editor: Miral Dizdaroglu 2This article is part of a series of reviews on “Oxidative DNA Damage and Repair.” The full list of papers may be found on the homepage of the journal.
resolves10.1007/s00018-014-1820-z
New paradigms in the repair of oxidative damage in human genome: mechanisms ensuring repair of mutagenic base lesions during replication and involvement of accessory proteins
resolves10.1101/cshperspect.a012773
Diseases Associated with Defective Responses to DNA Damage
resolves10.1038/cr.2008.8
Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
resolves10.1073/pnas.0509723103
A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA
resolves10.1016/B978-0-12-387665-2.00004-3
The Fpg/Nei Family of DNA Glycosylases
resolves10.1038/sj.onc.1206178
Dynamics and diversions in base excision DNA repair of oxidized abasic lesions
resolves10.1002/em.1070
Complexities of the DNA base excision repair pathway for repair of oxidative DNA damage
resolves10.1074/jbc.M112.384032
Enhancement of NEIL1 Protein-initiated Oxidized DNA Base Excision Repair by Heterogeneous Nuclear Ribonucleoprotein U (hnRNP-U) via Direct Interaction
resolves10.1016/j.cell.2010.01.004
Chaperoning Histones during DNA Replication and Repair
resolves10.3389/fgene.2014.00296
Chromatin modifications and DNA repair: beyond double-strand breaks
resolves10.1038/nature737
Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
resolves10.1016/S1097-2765(02)00453-7
Association of CBP/p300 Acetylase and Thymine DNA Glycosylase Links DNA Repair and Transcription
resolves10.1093/nar/gkq1210
USP7/HAUSP stimulates repair of oxidative DNA lesions
resolves10.1016/j.dnarep.2015.04.021
Accessing DNA damage in chromatin: Preparing the chromatin landscape for base excision repair
resolves10.1016/j.dnarep.2004.09.011
Base excision repair in nucleosomes lacking histone tails
resolves10.1074/jbc.M112.441444
The Structural Location of DNA Lesions in Nucleosome Core Particles Determines Accessibility by Base Excision Repair Enzymes
resolves10.1016/j.dnarep.2010.02.014
RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures
resolves10.1074/jbc.M802712200
Physical and Functional Interaction between Human Oxidized Base-specific DNA Glycosylase NEIL1 and Flap Endonuclease 1
resolves10.1073/pnas.1304231110
Prereplicative repair of oxidized bases in the human genome is mediated by NEIL1 DNA glycosylase together with replication proteins
resolves10.1016/S0092-8674(00)81326-4
Nucleosome Assembly by a Complex of CAF-1 and Acetylated Histones H3/H4
resolves10.1091/mbc.E06-05-0426
Essential Role of Chromatin Assembly Factor-1–mediated Rapid Nucleosome Assembly for DNA Replication and Cell Division in Vertebrate Cells
resolves10.1073/pnas.1635158100
Chromatin assembly factor 1 is essential and couples chromatin assembly to DNA replication <i>in vivo</i>
resolves10.1016/j.bbrc.2014.05.006
Up-regulation of CHAF1A, a poor prognostic factor, facilitates cell proliferation of colon cancer
resolves10.1158/0008-5472.CAN-13-1315
Histone Chaperone CHAF1A Inhibits Differentiation and Promotes Aggressive Neuroblastoma
resolves10.1093/hmg/ddm351
Comprehensive analysis of the role of DNA repair gene polymorphisms on risk of glioma
resolves10.1371/journal.pone.0006529
A Versatile Viral System for Expression and Depletion of Proteins in Mammalian Cells
resolves10.1073/pnas.062053799
Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA
resolves10.1016/S0092-8674(03)00550-6
Telomerase Maintains Telomere Structure in Normal Human Cells
resolves10.1038/onc.2010.435
Human AP endonuclease (APE1/Ref-1) and its acetylation regulate YB-1-p300 recruitment and RNA polymerase II loading in the drug-induced activation of multidrug resistance gene MDR1
resolves10.1073/pnas.0804424105
A RECQ5–RNA polymerase II association identified by targeted proteomic analysis of human chromatin
resolves10.1128/MCB.26.5.1654-1665.2006
Acetylation of Human 8-Oxoguanine-DNA Glycosylase by p300 and Its Role in 8-Oxoguanine Repair In Vivo
resolves10.1093/carcin/bgu087
ATM-mediated Mad1 Serine 214 phosphorylation regulates Mad1 dimerization and the spindle assembly checkpoint
resolves10.1016/S0076-6879(06)08004-9
Analysis of Base Excision DNA Repair of the Oxidative Lesion 2‐Deoxyribonolactone and the Formation of DNA–Protein Cross‐Links
resolves10.1158/0008-5472.CAN-03-2893
Chromatin Assembly Factor-1, a Marker of Clinical Value to Distinguish Quiescent from Proliferating Cells
resolves10.1016/j.bbagrm.2015.05.009
The role of the chromatin assembly complex (CAF-1) and its p60 subunit (CHAF1b) in homeostasis and disease
resolves10.1016/j.bbrc.2015.12.111
Over-expression of CHAF1A promotes cell proliferation and apoptosis resistance in glioblastoma cells via AKT/FOXO3a/Bim pathway
resolves10.1016/j.molcel.2004.06.003
AP Endonuclease-Independent DNA Base Excision Repair in Human Cells
resolves10.1074/jbc.M110.217075
An Analysis of CAF-1-interacting Proteins Reveals Dynamic and Direct Interactions with the KU Complex and 14-3-3 Proteins
resolves10.1128/MCB.26.5.1839-1849.2006
Induction of CAF-1 Expression in Response to DNA Strand Breaks in Quiescent Human Cells
resolves10.1093/emboj/cdg478
Local action of the chromatin assembly factor CAF‐1 at sites of nucleotide excision repair in vivo
resolves10.1073/pnas.1106696109
Interplay between mismatch repair and chromatin assembly
resolves10.1074/jbc.M115.713271
DNA Mismatch Repair Interacts with CAF-1- and ASF1A-H3-H4-dependent Histone (H3-H4)2 Tetramer Deposition
resolves10.1093/embo-reports/kvf068
Human Asf1 and CAF‐1 interact and synergize in a repair‐coupled nucleosome assembly pathway
resolves10.1101/gad.1305005
Histone deposition protein Asf1 maintains DNA replisome integrity and interacts with replication factor C
resolves10.3390/biom2040564
Human DNA Glycosylase NEIL1’s Interactions with Downstream Repair Proteins Is Critical for Efficient Repair of Oxidized DNA Base Damage and Enhanced Cell Survival
resolves10.1074/jbc.M115.642918
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
resolves10.1038/nsmb.1470
The HP1–p150/CAF-1 interaction is required for pericentric heterochromatin replication and S-phase progression in mouse cells
resolves10.1091/mbc.E14-05-1029
A separable domain of the p150 subunit of human chromatin assembly factor-1 promotes protein and chromosome associations with nucleoli
resolves10.1074/jbc.271.16.9573
Two Pathways for Base Excision Repair in Mammalian Cells
resolves10.1073/pnas.97.1.103
Clustered DNA damages induced in isolated DNA and in human cells by low doses of ionizing radiation
resolves10.1093/nar/gkp1070
Hierarchy of lesion processing governs the repair, double-strand break formation and mutability of three-lesion clustered DNA damage
resolves10.18632/oncotarget.9914
Scaffold attachment factor A (SAF-A) and Ku temporally regulate repair of radiation-induced clustered genome lesions
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

checked 2026-07-26 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record

Embed this badge

Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.

<a href="https://citestamp.com/citestamped/10.1093/nar/gkw1024"><img src="https://citestamp.com/citestamped/10.1093/nar/gkw1024/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[![CiteStamped reference-health badge](https://citestamp.com/citestamped/10.1093/nar/gkw1024/badge.svg)](https://citestamp.com/citestamped/10.1093/nar/gkw1024)