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BRCA2 associates with MCM10 to suppress PRIMPOL-mediated repriming and single-stranded gap formation after DNA damage
BRCA2 associates with MCM10 to suppress PRIMPOL-mediated repriming and single-stranded gap formation after DNA damage
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BRCA2 associates with MCM10 to suppress PRIMPOL-mediated repriming and single-stranded gap formation after DNA damage

Nature communications, 2021-10, Vol.12 (1), p.5966-5966, Article 5966 [Peer Reviewed Journal]

2021. The Author(s). ;The Author(s) 2021. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2021 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-021-26227-6 ;PMID: 34645815

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2
PRIMPOL-Mediated Adaptive Response Suppresses Replication Fork Reversal in BRCA-Deficient Cells
PRIMPOL-Mediated Adaptive Response Suppresses Replication Fork Reversal in BRCA-Deficient Cells
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PRIMPOL-Mediated Adaptive Response Suppresses Replication Fork Reversal in BRCA-Deficient Cells

Molecular cell, 2020-02, Vol.77 (3), p.461-474.e9 [Peer Reviewed Journal]

2020 MRC Laboratory of Molecular Biology ;Copyright © 2019 Elsevier Inc. All rights reserved. ;2020 MRC Laboratory of Molecular Biology. Published by Elsevier Inc. 2019 Elsevier Inc. ;ISSN: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2019.10.008 ;PMID: 31676232

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3
Role of Human DNA Glycosylase Nei-like 2 (NEIL2) and Single Strand Break Repair Protein Polynucleotide Kinase 3′-Phosphatase in Maintenance of Mitochondrial Genome
Role of Human DNA Glycosylase Nei-like 2 (NEIL2) and Single Strand Break Repair Protein Polynucleotide Kinase 3′-Phosphatase in Maintenance of Mitochondrial Genome
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Role of Human DNA Glycosylase Nei-like 2 (NEIL2) and Single Strand Break Repair Protein Polynucleotide Kinase 3′-Phosphatase in Maintenance of Mitochondrial Genome

The Journal of biological chemistry, 2012, Vol.287 (4), p.2819-2829 [Peer Reviewed Journal]

2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2012 by The American Society for Biochemistry and Molecular Biology, Inc. 2012 ;ISSN: 0021-9258 ;ISSN: 1083-351X ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M111.272179 ;PMID: 22130663

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4
Structural basis of long-range to short-range synaptic transition in NHEJ
Structural basis of long-range to short-range synaptic transition in NHEJ
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Structural basis of long-range to short-range synaptic transition in NHEJ

Nature (London), 2021-05, Vol.593 (7858), p.294-298 [Peer Reviewed Journal]

COPYRIGHT 2021 Nature Publishing Group ;Copyright Nature Publishing Group May 13, 2021 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-021-03458-7 ;PMID: 33854234

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5
Molecular basis of microhomology-mediated end-joining by purified full-length Polθ
Molecular basis of microhomology-mediated end-joining by purified full-length Polθ
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Molecular basis of microhomology-mediated end-joining by purified full-length Polθ

Nature communications, 2019-09, Vol.10 (1), p.4423-16, Article 4423 [Peer Reviewed Journal]

The Author(s) 2019. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;The Author(s) 2019 ;ISSN: 2041-1723 ;EISSN: 2041-1723 ;DOI: 10.1038/s41467-019-12272-9 ;PMID: 31562312

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6
Mimivirus encodes a multifunctional primase with DNA/RNA polymerase, terminal transferase and translesion synthesis activities
Mimivirus encodes a multifunctional primase with DNA/RNA polymerase, terminal transferase and translesion synthesis activities
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Mimivirus encodes a multifunctional primase with DNA/RNA polymerase, terminal transferase and translesion synthesis activities

Nucleic acids research, 2019-07, Vol.47 (13), p.6932-6945 [Peer Reviewed Journal]

The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. ;The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research. 2019 ;ISSN: 0305-1048 ;EISSN: 1362-4962 ;DOI: 10.1093/nar/gkz236 ;PMID: 31001622

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7
Repriming of DNA synthesis at stalled replication forks by human PrimPol
Repriming of DNA synthesis at stalled replication forks by human PrimPol
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Repriming of DNA synthesis at stalled replication forks by human PrimPol

Nature structural & molecular biology, 2013-12, Vol.20 (12), p.1383-1389 [Peer Reviewed Journal]

COPYRIGHT 2013 Nature Publishing Group ;COPYRIGHT 2013 Nature Publishing Group ;Copyright Nature Publishing Group Dec 2013 ;Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. 2013. ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/nsmb.2719 ;PMID: 24240614

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8
Replication fork stability confers chemoresistance in BRCA-deficient cells
Replication fork stability confers chemoresistance in BRCA-deficient cells
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Replication fork stability confers chemoresistance in BRCA-deficient cells

Nature (London), 2016-07, Vol.535 (7612), p.382-387 [Peer Reviewed Journal]

COPYRIGHT 2016 Nature Publishing Group ;COPYRIGHT 2016 Nature Publishing Group ;Copyright Nature Publishing Group Jul 21, 2016 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/nature18325 ;PMID: 27443740 ;CODEN: NATUAS

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9
Rad53 limits CMG helicase uncoupling from DNA synthesis at replication forks
Rad53 limits CMG helicase uncoupling from DNA synthesis at replication forks
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Rad53 limits CMG helicase uncoupling from DNA synthesis at replication forks

Nature structural & molecular biology, 2020-05, Vol.27 (5), p.461-471 [Peer Reviewed Journal]

COPYRIGHT 2020 Nature Publishing Group ;COPYRIGHT 2020 Nature Publishing Group ;The Author(s), under exclusive licence to Springer Nature America, Inc. 2020. ;ISSN: 1545-9993 ;EISSN: 1545-9985 ;DOI: 10.1038/s41594-020-0407-7 ;PMID: 32341532

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10
Function of a strand-separation pin element in the PriA DNA replication restart helicase
Function of a strand-separation pin element in the PriA DNA replication restart helicase
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Function of a strand-separation pin element in the PriA DNA replication restart helicase

The Journal of biological chemistry, 2019-02, Vol.294 (8), p.2801-5614 [Peer Reviewed Journal]

2019 © 2019 Windgassen et al. ;2019 Windgassen et al. ;2019 Windgassen et al. 2019 Windgassen et al. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.RA118.006870 ;PMID: 30593500

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11
REV1-Polζ maintains the viability of homologous recombination-deficient cancer cells through mutagenic repair of PRIMPOL-dependent ssDNA gaps
REV1-Polζ maintains the viability of homologous recombination-deficient cancer cells through mutagenic repair of PRIMPOL-dependent ssDNA gaps
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REV1-Polζ maintains the viability of homologous recombination-deficient cancer cells through mutagenic repair of PRIMPOL-dependent ssDNA gaps

Molecular cell, 2021-10, Vol.81 (19), p.4008-4025.e7 [Peer Reviewed Journal]

2021 Elsevier Inc. ;Copyright © 2021 Elsevier Inc. All rights reserved. ;ISSN: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2021.08.016 ;PMID: 34508659

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12
PDIP38/PolDIP2 controls the DNA damage tolerance pathways by increasing the relative usage of translesion DNA synthesis over template switching
PDIP38/PolDIP2 controls the DNA damage tolerance pathways by increasing the relative usage of translesion DNA synthesis over template switching
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PDIP38/PolDIP2 controls the DNA damage tolerance pathways by increasing the relative usage of translesion DNA synthesis over template switching

PloS one, 2019-03, Vol.14 (3), p.e0213383-e0213383 [Peer Reviewed Journal]

COPYRIGHT 2019 Public Library of Science ;COPYRIGHT 2019 Public Library of Science ;2019 Tsuda et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;Distributed under a Creative Commons Attribution 4.0 International License ;2019 Tsuda et al 2019 Tsuda et al ;ISSN: 1932-6203 ;EISSN: 1932-6203 ;DOI: 10.1371/journal.pone.0213383 ;PMID: 30840704

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13
HLTF Promotes Fork Reversal, Limiting Replication Stress Resistance and Preventing Multiple Mechanisms of Unrestrained DNA Synthesis
HLTF Promotes Fork Reversal, Limiting Replication Stress Resistance and Preventing Multiple Mechanisms of Unrestrained DNA Synthesis
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HLTF Promotes Fork Reversal, Limiting Replication Stress Resistance and Preventing Multiple Mechanisms of Unrestrained DNA Synthesis

Molecular cell, 2020-06, Vol.78 (6), p.1237-1251.e7 [Peer Reviewed Journal]

2020 ;Published by Elsevier Inc. ;ISSN: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2020.04.031 ;PMID: 32442397

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14
Rad51 filaments assembled in the absence of the complex formed by the Rad51 paralogs Rad55 and Rad57 are outcompeted by translesion DNA polymerases on UV-induced ssDNA gaps
Rad51 filaments assembled in the absence of the complex formed by the Rad51 paralogs Rad55 and Rad57 are outcompeted by translesion DNA polymerases on UV-induced ssDNA gaps
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Rad51 filaments assembled in the absence of the complex formed by the Rad51 paralogs Rad55 and Rad57 are outcompeted by translesion DNA polymerases on UV-induced ssDNA gaps

PLoS genetics, 2023-02, Vol.19 (2), p.e1010639-e1010639 [Peer Reviewed Journal]

Copyright: © 2023 Maloisel et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. ;COPYRIGHT 2023 Public Library of Science ;2023 Maloisel et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;Distributed under a Creative Commons Attribution 4.0 International License ;2023 Maloisel et al 2023 Maloisel et al ;ISSN: 1553-7404 ;ISSN: 1553-7390 ;EISSN: 1553-7404 ;DOI: 10.1371/journal.pgen.1010639 ;PMID: 36749784

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15
Fast and efficient DNA replication with purified human proteins
Fast and efficient DNA replication with purified human proteins
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Fast and efficient DNA replication with purified human proteins

Nature (London), 2022-06, Vol.606 (7912), p.204-210 [Peer Reviewed Journal]

2022. The Author(s), under exclusive licence to Springer Nature Limited. ;Copyright Nature Publishing Group Jun 2, 2022 ;ISSN: 0028-0836 ;EISSN: 1476-4687 ;DOI: 10.1038/s41586-022-04759-1 ;PMID: 35585232

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16
Temporally distinct post-replicative repair mechanisms fill PRIMPOL-dependent ssDNA gaps in human cells
Temporally distinct post-replicative repair mechanisms fill PRIMPOL-dependent ssDNA gaps in human cells
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Temporally distinct post-replicative repair mechanisms fill PRIMPOL-dependent ssDNA gaps in human cells

Molecular cell, 2021-10, Vol.81 (19), p.4026-4040.e8 [Peer Reviewed Journal]

2021 Elsevier Inc. ;Copyright © 2021 Elsevier Inc. All rights reserved. ;ISSN: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2021.09.013 ;PMID: 34624216

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17
hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity
hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity
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hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity

EMBO reports, 2013-12, Vol.14 (12), p.1104-1112 [Peer Reviewed Journal]

Copyright © 2013 European Molecular Biology Organization ;Copyright © 2013 Wiley Periodicals, Inc ;Copyright © 2013, European Molecular Biology Organization 2013 European Molecular Biology Organization ;ISSN: 1469-221X ;EISSN: 1469-3178 ;DOI: 10.1038/embor.2013.159 ;PMID: 24126761 ;CODEN: ERMEAX

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18
PrimPol, an Archaic Primase/Polymerase Operating in Human Cells
PrimPol, an Archaic Primase/Polymerase Operating in Human Cells
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PrimPol, an Archaic Primase/Polymerase Operating in Human Cells

Molecular cell, 2013-11, Vol.52 (4), p.541-553 [Peer Reviewed Journal]

Copyright © 2013 Elsevier Inc. All rights reserved. ;2013 ELL & Excerpta Medica. 2013 Elsevier Inc. ;ISSN: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2013.09.025 ;PMID: 24207056

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19
Rolling circle amplification (RCA)-based DNA hydrogel
Rolling circle amplification (RCA)-based DNA hydrogel
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Rolling circle amplification (RCA)-based DNA hydrogel

Nature protocols, 2021-12, Vol.16 (12), p.5460-5483 [Peer Reviewed Journal]

2021. The Author(s), under exclusive licence to Springer Nature Limited. ;COPYRIGHT 2021 Nature Publishing Group ;The Author(s), under exclusive licence to Springer Nature Limited 2021. ;ISSN: 1754-2189 ;EISSN: 1750-2799 ;DOI: 10.1038/s41596-021-00621-2 ;PMID: 34716450

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20
Distinct roles of RAD52 and POLQ in chromosomal break repair and replication stress response
Distinct roles of RAD52 and POLQ in chromosomal break repair and replication stress response
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Distinct roles of RAD52 and POLQ in chromosomal break repair and replication stress response

PLoS genetics, 2019-08, Vol.15 (8), p.e1008319 [Peer Reviewed Journal]

COPYRIGHT 2019 Public Library of Science ;COPYRIGHT 2019 Public Library of Science ;2019 Kelso et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. ;2019 Kelso et al 2019 Kelso et al ;ISSN: 1553-7404 ;ISSN: 1553-7390 ;EISSN: 1553-7404 ;DOI: 10.1371/journal.pgen.1008319 ;PMID: 31381562

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