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The UNG2 Arg88Cys variant abrogates RPA-mediated recruitment of UNG2 to single-stranded DNA

https://doi.org/10.1016/j.dnarep.2012.03.006

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb00710.xopenalex-snapshot

Excision of cytosine and thymine from DNA by mutants of human uracil‐DNA glycosylase.

inferredcites →https://doi.org/10.1007/s00018-010-0485-5openalex-snapshot

Functions of disordered regions in mammalian early base excision repair proteins

inferredcites →https://doi.org/10.1016/j.dnarep.2005.02.007openalex-snapshot

Xenopus CENP-A assembly into chromatin requires base excision repair proteins

inferredcites →https://doi.org/10.1016/j.dnarep.2005.08.004openalex-snapshot

Monoclonal B-cell hyperplasia and leukocyte imbalance precede development of B-cell malignancies in uracil-DNA glycosylase deficient mice

inferredcites →https://doi.org/10.1016/j.dnarep.2006.10.014openalex-snapshot

Uracil in DNA—General mutagen, but normal intermediate in acquired immunity

inferredcites →https://doi.org/10.1016/j.dnarep.2010.04.002openalex-snapshot

Direct interaction between XRCC1 and UNG2 facilitates rapid repair of uracil in DNA by XRCC1 complexes

inferredcites →https://doi.org/10.1016/j.dnarep.2011.10.026openalex-snapshot

mtSSB may sequester UNG1 at mitochondrial ssDNA and delay uracil processing until the dsDNA conformation is restored

inferredcites →https://doi.org/10.1016/j.jmb.2005.01.041openalex-snapshot

Uncoupling of Unwinding from DNA Synthesis Implies Regulation of MCM Helicase by Tof1/Mrc1/Csm3 Checkpoint Complex

inferredcites →https://doi.org/10.1016/j.mam.2007.04.006openalex-snapshot

DNA-uracil and human pathology

inferredcites →https://doi.org/10.1016/j.molcel.2004.08.007openalex-snapshot

The p53-Induced Oncogenic Phosphatase PPM1D Interacts with Uracil DNA Glycosylase and Suppresses Base Excision Repair

inferredcites →https://doi.org/10.1016/j.molcel.2011.09.013openalex-snapshot

Sub1 and RPA Associate with RNA Polymerase II at Different Stages of Transcription

inferredcites →https://doi.org/10.1016/s0021-9258(18)89032-9openalex-snapshot

Relations between synthesis of deoxyribonucleotides and DNA replication in 3T6 fibroblasts.

inferredcites →https://doi.org/10.1016/s0021-9258(19)39750-9openalex-snapshot

The primary structure of the 32-kDa subunit of human replication protein A.

inferredcites →https://doi.org/10.1016/s0021-9258(19)78100-9openalex-snapshot

Recombinant replication protein A: expression, complex formation, and functional characterization

inferredcites →https://doi.org/10.1016/s0092-8674(00)00136-7openalex-snapshot

Structural Basis for the Recognition of DNA Repair Proteins UNG2, XPA, and RAD52 by Replication Factor RPA

inferredcites →https://doi.org/10.1016/s0921-8777(00)00063-xopenalex-snapshot

Sequence variation in the human uracil-DNA glycosylase (UNG) gene

inferredcites →https://doi.org/10.1016/s0960-9822(02)01215-0openalex-snapshot

Immunoglobulin Isotype Switching Is Inhibited and Somatic Hypermutation Perturbed in UNG-Deficient Mice

inferredcites →https://doi.org/10.1016/s1097-2765(02)00729-3openalex-snapshot

DNA Polymerase Clamp Shows Little Turnover at Established Replication Sites but Sequential De Novo Assembly at Adjacent Origin Clusters

inferredcites →https://doi.org/10.1038/362709a0openalex-snapshot

Instability and decay of the primary structure of DNA

inferredcites →https://doi.org/10.1038/nature02821openalex-snapshot

Replication protein A interacts with AID to promote deamination of somatic hypermutation targets

inferredcites →https://doi.org/10.1038/ni.1964openalex-snapshot

Deep-sequencing identification of the genomic targets of the cytidine deaminase AID and its cofactor RPA in B lymphocytes

inferredcites →https://doi.org/10.1038/ni974openalex-snapshot

Human uracil–DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination

inferredcites →https://doi.org/10.1038/sj.emboj.7601958openalex-snapshot

Cell cycle‐specific UNG2 phosphorylations regulate protein turnover, activity and association with RPA

inferredcites →https://doi.org/10.1038/sj.onc.1206860openalex-snapshot

Gene-targeted mice lacking the Ung uracil-DNA glycosylase develop B-cell lymphomas

inferredcites →https://doi.org/10.1046/j.1365-2443.2003.00646.xopenalex-snapshot

Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro

inferredcites →https://doi.org/10.1073/pnas.0805139105openalex-snapshot

A quantitative atlas of mitotic phosphorylation

inferredcites →https://doi.org/10.1074/jbc.272.10.6561openalex-snapshot

A Sequence in the N-terminal Region of Human Uracil-DNA Glycosylase with Homology to XPA Interacts with the C-terminal Part of the 34-kDa Subunit of Replication Protein A

inferredcites →https://doi.org/10.1074/jbc.272.21.13916openalex-snapshot

Translesional Synthesis on DNA Templates Containing a Single Abasic Site

inferredcites →https://doi.org/10.1074/jbc.274.26.18470openalex-snapshot

Specific Expression of Activation-induced Cytidine Deaminase (AID), a Novel Member of the RNA-editing Deaminase Family in Germinal Center B Cells

inferredcites →https://doi.org/10.1074/jbc.m111.230052openalex-snapshot

Uracil-DNA Glycosylase in Base Excision Repair and Adaptive Immunity

inferredcites →https://doi.org/10.1074/jbc.m207107200openalex-snapshot

hUNG2 Is the Major Repair Enzyme for Removal of Uracil from U:A Matches, U:G Mismatches, and U in Single-stranded DNA, with hSMUG1 as a Broad Specificity Backup

inferredcites →https://doi.org/10.1083/jcb.149.2.271openalex-snapshot

Dynamics of DNA Replication Factories in Living Cells

inferredcites →https://doi.org/10.1083/jcb.200312048openalex-snapshot

Dynamic targeting of the replication machinery to sites of DNA damage

inferredcites →https://doi.org/10.1084/jem.20050042openalex-snapshot

B cells from hyper-IgM patients carrying UNG mutations lack ability to remove uracil from ssDNA and have elevated genomic uracil

inferredcites →https://doi.org/10.1093/carcin/13.10.1769openalex-snapshot

Expression of O6-methylguanine-DNA methyltransferase and uracil-DNA glycosylase in human placentae from smokers and non-smokers

inferredcites →https://doi.org/10.1093/emboj/18.13.3834openalex-snapshot

Post‐replicative base excision repair in replication foci

inferredcites →https://doi.org/10.1093/genetics/154.1.109openalex-snapshot

Genetic Analysis of Transcription-Associated Mutation in Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1093/nar/25.24.4876openalex-snapshot

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

inferredcites →https://doi.org/10.1093/nar/26.20.4611openalex-snapshot

Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively

inferredcites →https://doi.org/10.1093/nar/26.21.4953openalex-snapshot

Human mitochondrial uracil-DNA glycosylase preform (UNG1) is processed to two forms one of which is resistant to inhibition by AP sites

inferredcites →https://doi.org/10.1093/nar/9.11.2599openalex-snapshot

Uracil DNA-glycosylase from HeLa cells: general properties, substrate specificity and effect of uracil analogs

inferredcites →https://doi.org/10.1093/nar/gkh872openalex-snapshot

Repair of U/G and U/A in DNA by UNG2-associated repair complexes takes place predominantly by short-patch repair both in proliferating and growth-arrested cells

inferredcites →https://doi.org/10.1093/nar/gkl550openalex-snapshot

A dynamic model for replication protein A (RPA) function in DNA processing pathways

inferredcites →https://doi.org/10.1111/j.0105-2896.2005.00222.xopenalex-snapshot

Hyper‐immunoglobulin M syndromes caused by intrinsic B‐lymphocyte defects

inferredcites →https://doi.org/10.1126/science.1175371openalex-snapshot

Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

inferredcites →https://doi.org/10.1128/jvi.05163-11openalex-snapshot

Recruitment of the Nuclear Form of Uracil DNA Glycosylase into Virus Particles Participates in the Full Infectivity of HIV-1

inferredcites →https://doi.org/10.1146/annurev.biochem.76.061705.090740openalex-snapshot

Molecular Mechanisms of Antibody Somatic Hypermutation

inferredcites →https://doi.org/10.1186/1471-2407-6-243openalex-snapshot

Evaluation of NTHL1, NEIL1, NEIL2, MPG, TDG, UNG and SMUG1genes in familial colorectal cancer predisposition

inferredcites →https://doi.org/10.1371/journal.pone.0017151openalex-snapshot

Uracil DNA N-Glycosylase Promotes Assembly of Human Centromere Protein A

inferredcites →https://doi.org/10.4049/jimmunol.1101406openalex-snapshot

AID Binds Cooperatively with UNG and Msh2-Msh6 to Ig Switch Regions Dependent upon the AID C Terminus

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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N6-Methyladenosine in DNA Promotes Genome Stability

inferred← citeshttps://doi.org/10.1002/cbic.202200765openalex-snapshot

Replication Protein A Enhances Kinetics of Uracil DNA Glycosylase on ssDNA and Across DNA Junctions: Explored with a DNA Repair Complex Produced with SpyCatcher/SpyTag Ligation

inferred← citeshttps://doi.org/10.1016/b978-0-128-24465-4.00095-8openalex-snapshot

DNA Repair Factors Involved in Class Switch Recombination

inferred← citeshttps://doi.org/10.1016/j.bbapap.2019.140347openalex-snapshot

Analysis of uracil DNA glycosylase (UNG2) stimulation by replication protein A (RPA) at ssDNA-dsDNA junctions

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Host proteins interacting with integrase of human immunodeficiency virus type 1

inferred← citeshttps://doi.org/10.1016/j.bpj.2017.06.016openalex-snapshot

Investigation of N-Terminal Phospho-Regulation of Uracil DNA Glycosylase Using Protein Semisynthesis

inferred← citeshttps://doi.org/10.1016/j.dnarep.2013.05.002openalex-snapshot

A robust, sensitive assay for genomic uracil determination by LC/MS/MS reveals lower levels than previously reported

inferred← citeshttps://doi.org/10.1016/j.dnarep.2021.103077openalex-snapshot

The N-terminal domain of uracil-DNA glycosylase: Roles for disordered regions

inferred← citeshttps://doi.org/10.1016/j.dnarep.2025.103918openalex-snapshot

Efficient activity of uracil DNA glycosylase (UNG2) in proliferating cells requires binding to proliferating cell nuclear antigen (PCNA) and replication protein A (RPA)

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2016.12.002openalex-snapshot

Single nucleotide polymorphisms in DNA glycosylases: From function to disease

inferred← citeshttps://doi.org/10.1038/s41467-024-49343-5openalex-snapshot

Development of deaminase-free T-to-S base editor and C-to-G base editor by engineered human uracil DNA glycosylase

inferred← citeshttps://doi.org/10.1038/s41598-024-84408-xopenalex-snapshot

The kinetics of uracil-N-glycosylase distribution inside replication foci

inferred← citeshttps://doi.org/10.1093/abbs/gmw044openalex-snapshot

Human single-stranded DNA binding proteins: guardians of genome stability

inferred← citeshttps://doi.org/10.1093/nar/gkab195openalex-snapshot

RPA2 winged-helix domain facilitates UNG-mediated removal of uracil from ssDNA; implications for repair of mutagenic uracil at the replication fork

inferred← citeshttps://doi.org/10.1093/nar/gkad1115openalex-snapshot

RPA guides UNG to uracil in ssDNA to facilitate antibody class switching and repair of mutagenic uracil at the replication fork

inferred← citeshttps://doi.org/10.1093/nar/gkag441openalex-snapshot

UNG–RPA interaction governs the choice between high-fidelity and mutagenic uracil repair

inferred← citeshttps://doi.org/10.1093/nar/gkv977openalex-snapshot

Detection of uracil within DNA using a sensitive labeling method forin vitroand cellular applications

inferred← citeshttps://doi.org/10.1093/nar/gky525openalex-snapshot

N-terminal domain of human uracil DNA glycosylase (hUNG2) promotes targeting to uracil sites adjacent to ssDNA–dsDNA junctions

inferred← citeshttps://doi.org/10.1093/nar/gkz145openalex-snapshot

Uracil–DNA glycosylase UNG1 isoform variant supports class switch recombination and repairs nuclear genomic uracil

inferred← citeshttps://doi.org/10.1093/nar/gkz651openalex-snapshot

Repair of base damage within break-induced replication intermediates promotes kataegis associated with chromosome rearrangements

inferred← citeshttps://doi.org/10.1101/cshperspect.a012583openalex-snapshot

Base Excision Repair

inferred← citeshttps://doi.org/10.1111/febs.12867openalex-snapshot

Structure of RPA 32 bound to the N‐terminus of SMARCAL 1 redefines the binding interface between RPA 32 and its interacting proteins

inferred← citeshttps://doi.org/10.1172/jci.insight.184435openalex-snapshot

Ablating UNG activity in a mouse model inhibits colorectal cancer growth by increasing tumor immunogenicity

inferred← citeshttps://doi.org/10.1186/s12977-016-0257-xopenalex-snapshot

Uracil DNA glycosylase interacts with the p32 subunit of the replication protein A complex to modulate HIV-1 reverse transcription for optimal virus dissemination

inferred← citeshttps://doi.org/10.3390/ijms22083902openalex-snapshot

Detection of Genomic Uracil Patterns

inferred← citeshttps://doi.org/10.3390/jdb13030032openalex-snapshot

Zebrafish Unga Is Required for Genomic Maintenance upon Genotoxic Stress and Male Fertility

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Putative modifier genes in mevalonate kinase deficiency

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The Human Single-Stranded DNA Binding Protein 2 (HSSB2) and Its Novel Role in the Base Excision Repair Pathway

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N6-methyladenosine in DNA promotes genome stability

inferred← citeshttps://doi.org/10.7554/elife.101626.1openalex-snapshot

N6-methyladenosine in DNA promotes genome stability

inferred← citeshttps://doi.org/10.7554/elife.101626.2openalex-snapshot

N6-methyladenosine in DNA promotes genome stability

inferred← citeshttps://doi.org/10.7554/elife.101626.3openalex-snapshot

N6-methyladenosine in DNA promotes genome stability

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