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PolDIP2 interacts with human PrimPol and enhances its DNA polymerase activities

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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/pmic.201000616openalex-snapshot

COMPASS: A suite of pre‐ and post‐search proteomics software tools for OMSSA

inferredcites →https://doi.org/10.1007/978-1-59745-521-3_5openalex-snapshot

Preparation of Human Mitochondrial Single-Stranded DNA-Binding Protein

inferredcites →https://doi.org/10.1007/s13361-011-0261-2openalex-snapshot

StavroX—A Software for Analyzing Crosslinked Products in Protein Interaction Studies

inferredcites →https://doi.org/10.1016/j.dnarep.2010.04.010openalex-snapshot

Crosstalk between replicative and translesional DNA polymerases: PDIP38 interacts directly with Polη

inferredcites →https://doi.org/10.1016/j.ijms.2015.07.028openalex-snapshot

Histone H2AX Y142 phosphorylation is a low abundance modification

inferredcites →https://doi.org/10.1016/j.jsb.2010.10.014openalex-snapshot

The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes

inferredcites →https://doi.org/10.1016/j.molcel.2008.03.024openalex-snapshot

PCNA Ubiquitination and REV1 Define Temporally Distinct Mechanisms for Controlling Translesion Synthesis in the Avian Cell Line DT40

inferredcites →https://doi.org/10.1016/j.molcel.2013.09.025openalex-snapshot

PrimPol, an Archaic Primase/Polymerase Operating in Human Cells

inferredcites →https://doi.org/10.1016/j.molcel.2013.10.034openalex-snapshot

PPL2 Translesion Polymerase Is Essential for the Completion of Chromosomal DNA Replication in the African Trypanosome

inferredcites →https://doi.org/10.1016/j.molcel.2013.10.035openalex-snapshot

PrimPol Bypasses UV Photoproducts during Eukaryotic Chromosomal DNA Replication

inferredcites →https://doi.org/10.1016/j.molcel.2015.10.038openalex-snapshot

PrimPol Is Required for Replicative Tolerance of G Quadruplexes in Vertebrate Cells

inferredcites →https://doi.org/10.1038/cr.2008.1openalex-snapshot

Homologous recombination in DNA repair and DNA damage tolerance

inferredcites →https://doi.org/10.1038/embor.2013.159openalex-snapshot

hPrimpol1/CCDC111 is a human DNA primase‐polymerase required for the maintenance of genome integrity

inferredcites →https://doi.org/10.1038/nature04329openalex-snapshot

Replication fork reactivation downstream of a blocked nascent leading strand

inferredcites →https://doi.org/10.1038/nature05843openalex-snapshot

8-oxo-guanine bypass by human DNA polymerases in the presence of auxiliary proteins

inferredcites →https://doi.org/10.1038/nature09196openalex-snapshot

Structure and mechanism of human DNA polymerase η

inferredcites →https://doi.org/10.1038/nprot.2006.468openalex-snapshot

In-gel digestion for mass spectrometric characterization of proteins and proteomes

inferredcites →https://doi.org/10.1038/nrg2268openalex-snapshot

Genome instability: a mechanistic view of its causes and consequences

inferredcites →https://doi.org/10.1038/nrm3289openalex-snapshot

Y-family DNA polymerases and their role in tolerance of cellular DNA damage

inferredcites →https://doi.org/10.1073/pnas.1308760110openalex-snapshot

DNA polymerase δ-interacting protein 2 is a processivity factor for DNA polymerase λ during 8-oxo-7,8-dihydroguanine bypass

inferredcites →https://doi.org/10.1073/pnas.1412982112openalex-snapshot

Archaeal replicative primases can perform translesion DNA synthesis

inferredcites →https://doi.org/10.1074/jbc.m208694200openalex-snapshot

Identification of a Novel Protein, PDIP38, That Interacts with the p50 Subunit of DNA Polymerase δ and Proliferating Cell Nuclear Antigen

inferredcites →https://doi.org/10.1074/jbc.m414597200openalex-snapshot

Further Characterization of Human DNA Polymerase δ Interacting Protein 38

inferredcites →https://doi.org/10.1093/jb/mvi169openalex-snapshot

PDIP38 Associates with Proteins Constituting the Mitochondrial DNA Nucleoid

inferredcites →https://doi.org/10.1093/nar/gkm822openalex-snapshot

Dynamics of human replication factors in the elongation phase of DNA replication

inferredcites →https://doi.org/10.1093/nar/gku1321openalex-snapshot

Human PrimPol is a highly error-prone polymerase regulated by single-stranded DNA binding proteins

inferredcites →https://doi.org/10.1093/nar/gku214openalex-snapshot

Molecular dissection of the domain architecture and catalytic activities of human PrimPol

inferredcites →https://doi.org/10.1093/nar/gkv625openalex-snapshot

Primase-polymerases are a functionally diverse superfamily of replication and repair enzymes

inferredcites →https://doi.org/10.1161/circresaha.109.193722openalex-snapshot

Poldip2, a Novel Regulator of Nox4 and Cytoskeletal Integrity in Vascular Smooth Muscle Cells

inferredcites →https://doi.org/10.4161/23723548.2014.960754openalex-snapshot

PrimPol—A new polymerase on the block

inferredcites →https://doi.org/10.4161/cc.26221openalex-snapshot

PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UV-induced alternative splicing of MDM2

inferredcites →https://doi.org/10.4161/cc.7.20.6813openalex-snapshot

PDIP38 is a novel mitotic spindle-associated protein that affects spindle organization and chromosome segregation

What points at this work

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

inferred← citeshttps://doi.org/10.2139/ssrn.3185110openalex-extracted

Phosphorylation Alters the Properties of Pol η: Implications for Translesion Synthesis and Cancer Etiology

inferred← citeshttps://doi.org/10.1002/pro.4085openalex-snapshot

Crystal structure and molecular dynamics of human POLDIP2 , a multifaceted adaptor protein in metabolism and genome stability

inferred← citeshttps://doi.org/10.1007/978-3-030-41283-8_3openalex-snapshot

A Multifunctional Protein PolDIP2 in DNA Translesion Synthesis

inferred← citeshttps://doi.org/10.1016/j.dnarep.2016.11.003openalex-snapshot

Significant impact of divalent metal ions on the fidelity, sugar selectivity, and drug incorporation efficiency of human PrimPol

inferred← citeshttps://doi.org/10.1016/j.dnarep.2020.102943openalex-snapshot

Time for remodeling: SNF2-family DNA translocases in replication fork metabolism and human disease

inferred← citeshttps://doi.org/10.1016/j.dnarep.2020.102947openalex-snapshot

Mechanisms of direct replication restart at stressed replisomes

inferred← citeshttps://doi.org/10.1016/j.dnarep.2024.103740openalex-snapshot

Bulk synthesis and beyond: The roles of eukaryotic replicative DNA polymerases

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2016.10.015openalex-snapshot

Cells redox environment modulates BRCA1 expression and DNA homologous recombination repair

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2023.02.019openalex-snapshot

New insights in the molecular regulation of the NADPH oxidase 2 activity: Negative modulation by Poldip2

inferred← citeshttps://doi.org/10.1016/j.isci.2018.07.009openalex-snapshot

Phosphorylation Alters the Properties of Pol η: Implications for Translesion Synthesis

inferred← citeshttps://doi.org/10.1016/j.mrfmmm.2017.08.002openalex-snapshot

Role of specialized DNA polymerases in the limitation of replicative stress and DNA damage transmission

inferred← citeshttps://doi.org/10.1016/j.postharvbio.2024.112795openalex-snapshot

PpPrimPol helps delay postharvest-decay in peach fruit by maintaining mitochondrial function

inferred← citeshttps://doi.org/10.1021/acschembio.2c00717openalex-snapshot

Translesion Synthesis across the N2-Ethyl-deoxyguanosine Adduct by Human PrimPol

inferred← citeshttps://doi.org/10.1038/ncomms15222openalex-snapshot

Molecular basis for PrimPol recruitment to replication forks by RPA

inferred← citeshttps://doi.org/10.1038/s41419-019-2088-xopenalex-snapshot

Characterization of the role of TMEM45A in cancer cell sensitivity to cisplatin

inferred← citeshttps://doi.org/10.1038/s41467-021-24317-zopenalex-snapshot

Structural basis of DNA synthesis opposite 8-oxoguanine by human PrimPol primase-polymerase

inferred← citeshttps://doi.org/10.1038/s41598-019-38680-xopenalex-snapshot

Comparative genomics sheds light on the predatory lifestyle of accipitrids and owls

inferred← citeshttps://doi.org/10.1038/s41598-021-96692-yopenalex-snapshot

Translesion activity of PrimPol on DNA with cisplatin and DNA–protein cross-links

inferred← citeshttps://doi.org/10.1038/s42003-020-01358-6openalex-snapshot

Polymerase delta-interacting protein 38 (PDIP38) modulates the stability and activity of the mitochondrial AAA+ protease CLPXP

inferred← citeshttps://doi.org/10.1042/bst20160162openalex-snapshot

Mitochondrial DNA replication: a PrimPol perspective

inferred← citeshttps://doi.org/10.1080/10409238.2020.1811630openalex-snapshot

An updated perspective on the polymerase division of labor during eukaryotic DNA replication

inferred← citeshttps://doi.org/10.1080/10409238.2020.1841089openalex-snapshot

PRIMPOL ready, set, reprime!

inferred← citeshttps://doi.org/10.1093/nar/gkaa1090openalex-snapshot

The deubiquitinase USP36 Regulates DNA replication stress and confers therapeutic resistance through PrimPol stabilization

inferred← citeshttps://doi.org/10.1093/nar/gkab049openalex-snapshot

A unique arginine cluster in PolDIP2 enhances nucleotide binding and DNA synthesis by PrimPol

inferred← citeshttps://doi.org/10.1093/nar/gkab176openalex-snapshot

Repriming DNA synthesis: an intrinsic restart pathway that maintains efficient genome replication

inferred← citeshttps://doi.org/10.1093/nar/gkab634openalex-snapshot

Motif WFYY of human PrimPol is crucial to stabilize the incoming 3′-nucleotide during replication fork restart

inferred← citeshttps://doi.org/10.1093/nar/gkad507openalex-snapshot

The role of catalytic and regulatory domains of human PrimPol in DNA binding and synthesis

inferred← citeshttps://doi.org/10.1093/nar/gkae078openalex-snapshot

Human CST complex restricts excessive PrimPol repriming upon UV induced replication stress by suppressing p21

inferred← citeshttps://doi.org/10.1093/nar/gkw1275openalex-snapshot

Ribonucleotide incorporation by human DNA polymerase η impacts translesion synthesis and RNase H2 activity

inferred← citeshttps://doi.org/10.1093/nar/gkz056openalex-snapshot

PrimPol is required for the maintenance of efficient nuclear and mitochondrial DNA replication in human cells

inferred← citeshttps://doi.org/10.1093/nar/gkz236openalex-snapshot

Mimivirus encodes a multifunctional primase with DNA/RNA polymerase, terminal transferase and translesion synthesis activities

inferred← citeshttps://doi.org/10.1097/fjc.0000000000000465openalex-snapshot

Polymerase δ-interacting Protein 2: A Multifunctional Protein

inferred← citeshttps://doi.org/10.1111/tpj.14463openalex-snapshot

Structural insights into the interaction between phytoplasmal effector causing phyllody 1 and MADS transcription factors

inferred← citeshttps://doi.org/10.1126/sciadv.abn1229openalex-snapshot

Translesion DNA synthesis mediates acquired resistance to olaparib plus temozolomide in small cell lung cancer

inferred← citeshttps://doi.org/10.1134/s0006297923080084openalex-snapshot

Regulation of Human DNA Primase-Polymerase PrimPol

inferred← citeshttps://doi.org/10.1134/s0006297923110214openalex-snapshot

Response of PRIMPOL-Knockout Human Lung Adenocarcinoma A549 Cells to Genotoxic Stress

inferred← citeshttps://doi.org/10.1152/ajpcell.00208.2018openalex-snapshot

Polymerase-δ-interacting protein 2 activates the RhoGEF epithelial cell transforming sequence 2 in vascular smooth muscle cells

inferred← citeshttps://doi.org/10.1371/journal.pone.0213383openalex-snapshot

PDIP38/PolDIP2 controls the DNA damage tolerance pathways by increasing the relative usage of translesion DNA synthesis over template switching

inferred← citeshttps://doi.org/10.1371/journal.pone.0247261openalex-snapshot

Characterization of Poldip2 knockout mice: Avoiding incorrect gene targeting

inferred← citeshttps://doi.org/10.2131/fts.4.1openalex-snapshot

Simultaneous depletion of WRNIP1 and RAD52 restores resistance to oxidative stress

inferred← citeshttps://doi.org/10.2741/4510openalex-snapshot

DNA polymerases in the mitochondria A critical review of the evidence

inferred← citeshttps://doi.org/10.31857/s0320972523080080openalex-snapshot

Regulation of human dna primase-polymerase primpol

inferred← citeshttps://doi.org/10.31857/s0320972523110222openalex-snapshot

Characteristics of PRIMPOL knockout А549 cell response to genоtoxic stress

inferred← citeshttps://doi.org/10.32607/20758251-2017-9-3-12-26openalex-snapshot

Non-bulky Lesions in Human DNA: The Ways of Formation, Repair, and Replication

inferred← citeshttps://doi.org/10.3389/fmed.2022.1026931openalex-snapshot

The polymerase δ-interacting protein family and their emerging roles in diseases

inferred← citeshttps://doi.org/10.3389/fmolb.2021.712971openalex-snapshot

Mechanisms for Maintaining Eukaryotic Replisome Progression in the Presence of DNA Damage

inferred← citeshttps://doi.org/10.3390/biom12020248openalex-snapshot

PrimPol: A Breakthrough among DNA Replication Enzymes and a Potential New Target for Cancer Therapy

inferred← citeshttps://doi.org/10.3390/genes8010020openalex-snapshot

PrimPol—Prime Time to Reprime

inferred← citeshttps://doi.org/10.3390/genes8070190openalex-snapshot

Regulation and Modulation of Human DNA Polymerase δ Activity and Function

inferred← citeshttps://doi.org/10.3390/ijms18071584openalex-snapshot

DNA Damage Tolerance by Eukaryotic DNA Polymerase and Primase PrimPol

inferred← citeshttps://doi.org/10.3390/ijms21239027openalex-snapshot

Strand Displacement Activity of PrimPol

inferred← citeshttps://doi.org/10.3390/ijms241310488openalex-snapshot

The Adaptive Mechanisms and Checkpoint Responses to a Stressed DNA Replication Fork

inferred← citeshttps://doi.org/10.3390/toxins11040233openalex-snapshot

Structural Insights to the Heterotetrameric Interaction between the Vibrio parahaemolyticus PirAvp and PirBvp Toxins and Activation of the Cry-Like Pore-Forming Domain

inferred← citeshttps://doi.org/10.3410/f.739107025.793585223openalex-snapshot

Faculty Opinions recommendation of The deubiquitinase USP36 Regulates DNA replication stress and confers therapeutic resistance through PrimPol stabilization.

inferred← citeshttps://doi.org/10.3892/mco.2018.1608openalex-snapshot

Gene expression changes associated with chemotherapy resistance in Ewing sarcoma cells

inferred← citeshttps://doi.org/10.64898/2026.03.14.711777openalex-snapshot

Redox-dependent dimerization of PolDIP2 and a conserved ApaG-domain motif required for CHCHD2 interaction

inferred← citeshttps://doi.org/10.70675/59a3b87cz2014z4929za909z0b9dd19302c0openalex-snapshot

Poldip2 : caractérisation et implication dans l’activité des NADPH oxydases

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