The intra-S phase checkpoint affects both DNA replication initiation and elongation: single-cell and -DNA fiber analyses

DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139

Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5858 · Cited by 5,438

Cell-cycle checkpoints and cancer

Kastan, M. B., & Bartek, J. (2004) · Nature · doi:10.1038/nature03097 · Cited by 2,836

DNA Topoisomerases: Structure, Function, and Mechanism

Champoux, J. J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.369 · Cited by 2,804

Megabase Chromatin Domains Involved in DNA Double-Strand Breaks in Vivo

Rogakou, E. P., Boon, C., Redon, C., & Bonner, W. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.905 · Cited by 2,422

Cellular roles of DNA topoisomerases: a molecular perspective

Wang, J. C. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm831 · Cited by 2,364

Camptothecin induces protein-linked DNA breaks via mammalian DNA topoisomerase I.

Hsiang, Y. H., Hertzberg, R., Hecht, S., & Liu, L. F. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38654-4 · Cited by 2,362

Topoisomerase I inhibitors: camptothecins and beyond

Pommier, Y. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1977 · Cited by 2,362

Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptothecin.

Hsiang, Y. H., Lihou, M. G., & Liu, L. F. (1989) · PubMed · Cited by 1,028

Replicon Clusters Are Stable Units of Chromosome Structure: Evidence That Nuclear Organization Contributes to the Efficient Activation and Propagation of S Phase in Human Cells

Jackson, D., & Pombo, A. (1998) · Journal of Cell Biology · doi:10.1083/jcb.140.6.1285 · Cited by 881

JMJD2 promotes acquired cisplatin resistance in non-small cell lung carcinoma cells

Duan, L., Perez, R. E., Chastain, P. D., Mathew, M. T., Bijukumar, D. R., & Maki, C. G. (2019) · Oncogene · doi:10.1038/s41388-019-0814-6 · Cited by 38

A replicator-specific binding protein essential for site-specific initiation of DNA replication in mammalian cells

Zhang, Y., Huang, L., Fu, H., Smith, O. K., Lin, C. M., Utani, K., Rao, M., Reinhold, W. C., Redon, C. E., Ryan, M., et al. (2016) · Nature Communications · doi:10.1038/ncomms11748 · Cited by 37

Molecular and Cellular Pharmacology of the Novel Noncamptothecin Topoisomerase I Inhibitor Genz-644282

Sooryakumar, D., Dexheimer, T. S., Teicher, B. A., & Pommier, Y. G. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-1043 · Cited by 38

Association of epigenetic inactivation of the WRN gene with anticancer drug sensitivity in cervical cancer cells

Masuda, K., Banno, K., Yanokura, M., Tsuji, K., Kobayashi, Y., Kisu, I., Ueki, A., Yamagami, W., Nomura, H., Tominaga, E., et al. (2012) · Oncology Reports · doi:10.3892/or.2012.1912 · Cited by 37

Degradation of p12 Subunit by CRL4Cdt2 E3 Ligase Inhibits Fork Progression after DNA Damage

Terai, K., Shibata, E., Abbas, T., & Dutta, A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.505586 · Cited by 36

Structure-Specific Endonucleases and the Resolution of Chromosome Underreplication

Falquet, B., & Rass, U. (2019) · Genes · doi:10.3390/genes10030232 · Cited by 36

Spatiotemporal recruitment of human DNA polymerase delta to sites of UV damage

Chea, J., Zhang, S., Zhao, H. L., Zhang, Z., Lee, E. Y. C., Darżynkiewicz, Z., & Lee, M. (2012) · Cell Cycle · doi:10.4161/cc.21280 · Cited by 37

The role of HDAC2 in chromatin remodelling and response to chemotherapy in ovarian cancer

Huang, R., Langdon, S. P., Tse, M., Mullen, P., Um, I. H., Faratian, D., & Harrison, D. J. (2015) · Oncotarget · doi:10.18632/oncotarget.6618 · Cited by 36

Targeting radioresistant breast cancer cells by single agent CHK1 inhibitor via enhancing replication stress

Zhang, Y., Lai, J., Du, Z., Gao, J., Yang, S., Gorityala, S., Xiong, X., Deng, O., Ma, Z., Yan, C., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9156 · Cited by 39

Mus81, Rhp51(Rad51), and Rqh1 Form an Epistatic Pathway Required for the S-Phase DNA Damage Checkpoint

Willis, N. A., & Rhind, N. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-08-0798 · Cited by 35

Targeting triple-negative breast cancer cells with 6,7-bis(hydroxymethyl)-1H,3H-pyrrolo[1,2-c]thiazoles

Santos, K., Laranjo, M., Abrantes, A. M., Brito, A., Gonçalves, A. C., Sarmento‐Ribeiro, A. B., Botelho, M. F., Soares, M. I. L., Oliveira, A. S. R., & Melo, T. M. V. D. P. E. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.04.008 · Cited by 35

Potentiation of the Novel Topoisomerase I Inhibitor Indenoisoquinoline LMP-400 by the Cell Checkpoint and Chk1-Chk2 Inhibitor AZD7762

Aris, S. M., & Pommier, Y. G. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-2579 · Cited by 36

Introduction to Molecular Combing: Genomics, DNA Replication, and Cancer

Herrick, J., & Bensimon, A. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-815-7_5 · Cited by 39

Looping out of control: R-loops in transcription-replication conflict

Kumar, C., & Remus, D. (2023) · Chromosoma · doi:10.1007/s00412-023-00804-8 · Cited by 34

Loss of NEIL3 DNA glycosylase markedly increases replication associated double strand breaks and enhances sensitivity to ATR inhibitor in glioblastoma cells

Klattenhoff, A. W., Thakur, M. A., Chu, C. S., Ray, D., Habib, S. L., & Kidane, D. (2017) · Oncotarget · doi:10.18632/oncotarget.22896 · Cited by 35

Shape‐dependent adhesion and endocytosis of hydroxyapatite nanoparticles on A7R5 aortic smooth muscle cells

Huang, L., Han, J., Ouyang, J., & Gui, B. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28987 · Cited by 34

Replication-dependent cytotoxicity and Spartan-mediated repair of trapped PARP1–DNA complexes

Saha, L. K., Murai, Y., Saha, S. T., Jo, U., Tsuda, M., Takeda, S., & Pommier, Y. G. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab777 · Cited by 34

Structural Characterization and Repair Mechanism of Gracilaria lemaneiformis Sulfated Polysaccharides of Different Molecular Weights on Damaged Renal Epithelial Cells

Guo, D., Yu, K., Sun, X., & Ouyang, J. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7410389 · Cited by 33

SFPQ Depletion Is Synthetically Lethal with BRAFV600E in Colorectal Cancer Cells

Klotz‐Noack, K., Klinger, B., Rivera, M., Bublitz, N., Uhlitz, F., Riemer, P., Lüthen, M., Sell, T., Kasack, K., Gastl, B., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108184 · Cited by 35

The Mechanism by Which MYCN Amplification Confers an Enhanced Sensitivity to a PCNA-Derived Cell Permeable Peptide in Neuroblastoma Cells

Gu, L., Chu, P. G., Lingeman, R. G., McDaniel, H., Kechichian, S., Hickey, R. J., Liu, Z., Yuan, Y., Sandoval, J. A., Fields, G. B., et al. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.11.016 · Cited by 32

MRE11 and TREX1 control senescence by coordinating replication stress and interferon signaling

Técher, H., Gopaul, D., Heuzé, J., Bouzalmad, N., Leray, B., Vernet, A., Mettling, C., Moreaux, J., Pasero, P., & Lin, Y. (2024) · Nature Communications · doi:10.1038/s41467-024-49740-w · Cited by 33

The helicase domain and C-terminus of human RecQL4 facilitate replication elongation on DNA templates damaged by ionizing radiation

Kohzaki, M., Chiourea, M., Versini, G., Adachi, N., Takeda, S., Gagos, S., & Halazonetis, T. D. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs149 · Cited by 32

PrimPol-deficient cells exhibit a pronounced G2 checkpoint response following UV damage

Bailey, L. J., Bianchi, J., Hégarat, N., Hochegger, H., & Doherty, A. J. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1128597 · Cited by 30

Topoisomerase Inhibitor Coralyne Photosensitizes DNA, Leading to Elicitation of Chk2-Dependent S-phase Checkpoint and p53-Independent Apoptosis in Cancer Cells

Patro, B. S., Maity, B., & Chattopadhyay, S. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2508 · Cited by 30

Replication licensing and the DNA damage checkpoint

Cook, J. G. (2009) · Frontiers in bioscience · doi:10.2741/3584 · Cited by 30

Chk1 inhibitor synergizes quinacrine mediated apoptosis in breast cancer cells by compromising the base excision repair cascade

Preet, R., Siddharth, S., Satapathy, S. R., Das, S., Nayak, A., Das, D., Wyatt, M. D., & Kundu, C. N. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.01.017 · Cited by 31

Disruption of Src function potentiates Chk1-inhibitor–induced apoptosis in human multiple myeloma cells in vitro and in vivo

Dai, Y., Chen, S., Shah, R., Pei, X., Wang, L., Almenara, J. A., Kramer, L. B., Dent, P., & Grant, S. (2010) · Blood · doi:10.1182/blood-2010-06-291146 · Cited by 28

Recombinase and translesion DNA polymerase decrease the speed of replication fork progression during the DNA damage response in Escherichia coli cells

Tan, K. W., Pham, T. M., Furukohri, A., Maki, H., & Akiyama, M. T. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv044 · Cited by 27

The Tip of an Iceberg: Replication-Associated Functions of the Tumor Suppressor p53

Gottifredi, V., & Wiesmüller, L. (2018) · Cancers · doi:10.3390/cancers10080250 · Cited by 30

Checkpoint-Dependent Regulation of Origin Firing and Replication Fork Movement in Response to DNA Damage in Fission Yeast

Kumar, S., & Huberman, J. A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01319-08 · Cited by 26

Relationships between cell cycle pathway gene polymorphisms and risk of hepatocellular carcinoma

Nan, Y., Hu, Y., Liu, Z., Duan, F.-F., Xu, Y., Li, S., Li, T., Chen, D., & Zeng, X. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i24.5558 · Cited by 25

USP13 regulates the replication stress response by deubiquitinating TopBP1

Kim, W., Zhao, F., Gao, H., Qin, S., Hou, J., Deng, M., Kloeber, J. A., Huang, J., Zhou, Q., Guo, G., et al. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103063 · Cited by 26

Unscheduled expression of CDC25B in S-phase leads to replicative stress and DNA damage

Bugler, B., Schmitt, E., Aressy, B., & Ducommun, B. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-29 · Cited by 26

The CDK-PLK1 axis targets the DNA damage checkpoint sensor protein RAD9 to promote cell proliferation and tolerance to genotoxic stress

Wakida, T., Ikura, M., Kuriya, K., Ito, S., Shiroiwa, Y., Habu, T., Kawamoto, T., Okumura, K., Ikura, T., & Furuya, K. (2017) · eLife · doi:10.7554/elife.29953 · Cited by 25

Cancer Therapy and Replication Stress

Kotsantis, P., Jones, R. M., Higgs, M. R., & Petermann, E. (2015) · Advances in clinical chemistry · doi:10.1016/bs.acc.2014.12.003 · Cited by 24

Myosin 16 levels fluctuate during the cell cycle and are downregulated in response to DNA replication stress

Cameron, R. S., Liu, C., & Pihkala, J. P. S. (2013) · Cytoskeleton · doi:10.1002/cm.21109 · Cited by 25

PIDD mediates the association of DNA-PKcs and ATR at stalled replication forks to facilitate the ATR signaling pathway

Lin, Y., Shih, H.-Y., Shang, Z., Kuo, C., Guo, J., Du, C., Lee, H., & Chen, B. P. C. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1298 · Cited by 23

Chromatin remodeler ALC1 prevents replication-fork collapse by slowing fork progression

Ooka, M., Abe, T., Cho, K., Koike, K., Takeda, S., & Hirota, K. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192421 · Cited by 22

Synergistic effects of pemetrexed and amrubicin in non-small cell lung cancer cell lines: Potential for combination therapy

Hatakeyama, Y., Kobayashi, K., Nagano, T., Tamura, D., Yamamoto, M., TACHIHARA, M. Y., Kotani, Y., & Nishimura, Y. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.09.019 · Cited by 21

Inhibition of Chk1 with the small molecule inhibitor V158411 induces DNA damage and cell death in an unperturbed S-phase

Wayne, J., Brooks, T., & Massey, A. J. (2016) · Oncotarget · doi:10.18632/oncotarget.13119 · Cited by 21

Excision of translesion synthesis errors orchestrates responses to helix-distorting DNA lesions

Tsaalbi‐Shtylik, A., Ferrás, C., Pauw, B., Hendriks, G., Temviriyanukul, P., Carlée, L., Calléja, F. M. G. R., van Hees‐Stuivenberg, S., Akagi, J., Iwai, S., et al. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201408017 · Cited by 20

Checkpoint regulation of replication forks: global or local?

Iyer, D., & Rhind, N. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130197 · Cited by 18

The ATR-Activation Domain of TopBP1 Is Required for the Suppression of Origin Firing during the S Phase

Sokka, M., Koalick, D., Hemmerich, P. H., Syväoja, J. E., & Pospiech, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082376 · Cited by 18

Spatial organization and functions of Chk1 activation by TopBP1 biomolecular condensates

Egger, T., Morano, L., Blanchard, M., Basbous, J., & Constantinou, A. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114064 · Cited by 17

Functional regulation of the structure-specific endonuclease FEN1 by the human cytomegalovirus protein IE1 suggests a role for the re-initiation of stalled viral replication forks

Schilling, E.-M., Scherer, M., Rothemund, F., & Stamminger, T. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009460 · Cited by 17

Tipin Functions in the Protection against Topoisomerase I Inhibitor

Hosono, Y., Abe, T., Higuchi, M., Kajii, K., Sakuraba, S., Tada, S., Enomoto, T., & Seki, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.531707 · Cited by 17

Non‐enzymatic function of WRN RECQL helicase regulates removal of topoisomerase‐I‐DNA covalent complexes and triggers NF‐κB signaling in cancer

Gupta, P., Majumdar, A. G., & Patro, B. S. (2022) · Aging Cell · doi:10.1111/acel.13625 · Cited by 13

Distinct CPT-induced deaths in lung cancer cells caused by clathrin-mediated internalization of CP micelles

Liu, Y., Cheng, R.-Y., Lo, Y., Hsu, C., Chen, S., Chiu, C., & Wang, L. (2016) · Nanoscale · doi:10.1039/c5nr08345a · Cited by 16

Posttranscriptional control of the replication stress response via TTP-mediated Claspin mRNA stabilization

Lee, T.-H., Choi, J. Y., Park, J., & Kang, T. (2020) · Oncogene · doi:10.1038/s41388-020-1220-9 · Cited by 16

The Indenoisoquinoline LMP517: A Novel Antitumor Agent Targeting both TOP1 and TOP2

Marzi, L., Sun, Y., Huang, S.-Y. N., James, A. E., Difilippantonio, S., & Pommier, Y. G. (2020) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-1064 · Cited by 16

Replicating Damaged DNA in EukaryotesPreprint

Chatterjee, N., & Siede, W. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019836 · Cited by 17

Histone chaperone HIRA dictate proliferation vs differentiation of chronic myeloid leukemia cells

Majumder, A., Dharan, A. T., Baral, I., Varghese, P. C., Mukherjee, A., Subhadradevi, L., Narayanan, G., & Dutta, D. (2019) · FASEB BioAdvances · doi:10.1096/fba.2019-00014 · Cited by 15

Antiproliferative activity of bicyclic benzimidazole nucleosides: synthesis, DNA-binding and cell cycle analysis

Sontakke, V. A., Lawande, P. P., Kate, A. N., Khan, A., Joshi, R. S., Kumbhar, A. A., & Shinde, V. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00527f · Cited by 15

Endogenous single-strand DNA breaks at RNA polymerase II promoters in Saccharomyces cerevisiae

Hegedüs, É., Kókai, E., Nánási, P. P., Imre, L., Halász, L., Jossé, R., Antunovics, Z., Webb, M. R., Hage, A. E., Pommier, Y. G., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky743 · Cited by 15

ATR Kinase Is a Crucial Player Mediating the DNA Damage Response in Trypanosoma brucei

Marín, P. M., Obonaga, R., Pavani, R., da Silva, M. S., de Araujo, C. B., Lima, A. A., Avila, C. C., Cestari, I. D. S., Machado, C. R., & Elias, M. C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.602956 · Cited by 15

BRCA2 is needed for both repair and cell cycle arrest in mammalian cells exposed to S23906, an anticancer monofunctional DNA binder

Rocca, C. J., Soares, D. G., Bouzid, H., Henriques, J. A. P., Larsen, A. K., & Escargueil, A. E. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1042632 · Cited by 14

Checkpoint Regulation of DNA Replication

Boye, E., Skjølberg, H. C., & Grallert, B. (2009) · Methods in molecular biology · doi:10.1007/978-1-60327-815-7_4 · Cited by 17

Ring finger protein 126 promotes breast cancer metastasis and serves as a potential target to improve the therapeutic sensitivity of ATR inhibitors

You, P., Yang, Y., Huang, R., Yang, H., Huang, Q., Ji, Y., Dai, J., Qiao, K., Tang, W., Xie, L., et al. (2022) · Breast Cancer Research · doi:10.1186/s13058-022-01586-0 · Cited by 13

Cyclobutane Pyrimidine Dimer Density as a Predictive Biomarker of the Biological Effects of Ultraviolet Radiation in Normal Human Fibroblast

Sproul, C. D., Mitchell, D. L., Rao, S., Ibrahim, J. G., Kaufmann, W. K., & Cordeiro‐Stone, M. (2013) · Photochemistry and Photobiology · doi:10.1111/php.12194 · Cited by 14

Immunofluorescence Analysis of γ-H2AX Foci in Mammalian Fibroblasts at Different Phases of the Cell Cycle

Solovjeva, L. V., Firsanov, D., Pleskach, N., & Svetlova, M. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7187-9_17 · Cited by 13

Hepatitis B virus X protein disrupts DNA interstrand crosslinking agent mitomycin C induced ATR dependent intra-S-phase checkpoint

Wu, X.-Y., Qian, J., Lin, Y., & Zheng, M. (2008) · European Journal of Cancer · doi:10.1016/j.ejca.2008.04.012 · Cited by 14

Mitomycin C reduces abundance of replication forks but not rates of fork progression in primary and transformed human cells

Kehrli, K., & Sidorova, J. M. (2014) · Oncoscience · doi:10.18632/oncoscience.70 · Cited by 11

F10 Cytotoxicity Via Topoisomerase I Cleavage Complex Repair Consistent With a Unique Mechanism for Thymineless Death

Gmeiner, W. H., Gearhart, P. J., Pommier, Y. G., & Nakamura, J. (2016) · Future Oncology · doi:10.2217/fon-2016-0127 · Cited by 12

The Spi1/PU.1 transcription factor accelerates replication fork progression by increasing PP1 phosphatase in leukemia

Rimmelé, P., Esposito, M., Delestré, L., Guervilly, J.-H., Ridinger-Saison, M., Despras, E., Moreau-Gachelin, F., Rosselli, F., & Guillouf, C. (2017) · Oncotarget · doi:10.18632/oncotarget.16183 · Cited by 12

Activation of new replication foci under conditions of replication stress

Rybak, P., Waligórska, A., Bujnowicz, Ł., Hoang, A., & Dobrucki, J. W. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1064566 · Cited by 11

Regulation of DNA Replication Timing on Human Chromosome by a Cell-Type Specific DNA Binding Protein SATB1

Oda, M., Kanoh, Y., Watanabe, Y., & Masai, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042375 · Cited by 11

Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines

Lewis, J. S., van Oijen, A. M., & Spenkelink, L. M. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00436 · Cited by 12

Time-dependent subcellular structure injuries induced by nano-/micron-sized calcium oxalate monohydrate and dihydrate crystals

Sun, X., Yu, K., & Ouyang, J. (2017) · Materials Science and Engineering C · doi:10.1016/j.msec.2017.05.081 · Cited by 12

DNA Damage Checkpoint Responses in the S Phase of Synchronized Diploid Human Fibroblasts

Chastain, P. D., Brylawski, B. P., Zhou, Y., Rao, S., Chu, H., Ibrahim, J. G., Kaufmann, W. K., & Cordeiro‐Stone, M. (2014) · Photochemistry and Photobiology · doi:10.1111/php.12361 · Cited by 11

The Caenorhabditis elegans Werner syndrome protein participates in DNA damage checkpoint and DNA repair in response to CPT-induced double-strand breaks

Hyun, M., Choi, S., Stevnsner, T., & Ahn, B. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.12.006 · Cited by 11

Pinus kesiya Royle ex Gordon induces apoptotic cell death in hepatocellular carcinoma HepG2 cell via intrinsic pathway by PARP and Topoisomerase I suppression

Pocasap, P., Nonpunya, A., & Weerapreeyakul, N. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111628 · Cited by 10

An Acetamide Derivative as a Camptothecin Sensitizer for Human Non‐Small‐Cell Lung Cancer Cells through Increased Oxidative Stress and JNK Activation

Chou, H.-L., Fong, Y., Lin, H.-H., Tsai, E., Chen, J. Y., Chang, W., Wu, C., Wang, H., Huang, H., & Chiu, C. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/9128102 · Cited by 9

Cell cycle profiling by image and flow cytometry: The optimised protocol for the detection of replicational activity using 5-Bromo-2′-deoxyuridine, low concentration of hydrochloric acid and exonuclease III

Ligasová, A., Konečný, P., Frydrych, I., & Koberna, K. (2017) · PLoS ONE · doi:10.1371/journal.pone.0175880 · Cited by 9

Nuclear cGAS mediated replication stress and mitotic catastrophe can overcome gemcitabine resistance

Park, S., Jeong, K., Poire, A., Jeong, B. Y., Sheng, Y., Ozmen, T. Y., Rames, M. J., English, I. A., Brody, J. R., Sears, R. C., et al. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.218009 · Cited by 7

Organization of DNA Replication Origin Firing in Xenopus Egg Extracts: The Role of Intra-S Checkpoint

Ciardo, D., Haccard, O., Narassimprakash, H., Arbona, J., Hyrien, O., Audit, B., Marheineke, K., & Goldar, A. (2021) · Genes · doi:10.3390/genes12081224 · Cited by 7

Induction of glutathione-dependent DNA double-strand breaks by the novel anticancer drug brostallicin

Guirouilh‐Barbat, J., Zhang, Y., & Pommier, Y. G. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0320 · Cited by 7

Critical role of SMG7 in activation of the ATR-CHK1 axis in response to genotoxic stress

Ho, K., Luo, H., Zhu, W., & Tang, Y. (2021) · Scientific Reports · doi:10.1038/s41598-021-86957-x · Cited by 7

Methods for Inferring Cell Cycle Parameters Using Thymidine Analogues

Martı́, J. (2023) · Biology · doi:10.3390/biology12060885 · Cited by 5

Oncogenic KIT Induces Replication Stress and Confers Cell Cycle Checkpoint Vulnerability in Melanoma

Njauw, C.-N. J., Ji, Z., Pham, D. M., Simoneau, A., Kumar, R., Flaherty, K. T., Zou, L., & Tsao, H. (2021) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2021.07.188 · Cited by 5

Chk1 prevents abnormal mitosis of S-phase HeLa cells containing DNA damage

Li, X., Ward, T. L., Yao, X., & Wu, J. (2009) · Chinese Science Bulletin · doi:10.1007/s11434-009-0633-1 · Cited by 4

Is activation of the intra-S checkpoint in human fibroblasts an important factor in protection against UV-induced mutagenesis?

Sproul, C. D., Rao, S., Ibrahim, J. G., Kaufmann, W. K., & Cordeiro‐Stone, M. (2013) · Cell Cycle · doi:10.4161/cc.26590 · Cited by 3

DNA Replication Profiling Using Deep Sequencing

Saayman, X., Ramos-Pérez, C., & Brown, G. W. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7306-4_15 · Cited by 3

Old Passengers as New Drivers: Chromosomal Passenger Proteins Engage in Translesion Synthesis

Falke, K., Schröder, E., Mosel, S., Yürük, C. N., Feldmann, S., Gül, D., Stahl, P., Stauber, R. H., & Knauer, S. K. (2024) · Cells · doi:10.3390/cells13211804 · Cited by 2

PARP Activity Fine-tunes the DNA Replication Choreography of Chk1-depleted Cells

Calzetta, N. L., Besteiro, M. A. G., & Gottifredi, V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166949 · Cited by 3

Tyrosyl-DNA-Phosphodiesterase

Dexheimer, T. S., Huang, S.-Y. N., Das, B. B., & Pommier, Y. G. (2011) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-1-4614-0323-4_16 · Cited by 2

Chl1 helicase controls replication fork progression by regulating dNTP pools

Batté, A., van der Horst, S. C., Tittel-Elmer, M., Sun, S. M., Sharma, S., van Leeuwen, J. S., Chabes, A., & van Attikum, H. (2022) · Life Science Alliance · doi:10.26508/lsa.202101153 · Cited by 5

DNA damaged-induced phosphorylation of a viral replicative DNA helicase results in inhibition of DNA replication through attenuation of helicase functionPreprint

Homiski, C., Dey-Rao, R., Shen, S., Qu, J., & Melendy, T. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.29.560221 · Cited by 2

Slx4 and Fun30/SMARCAD1 coordinate S-phase checkpoint regulation and replication fork protection in response to Top1–DNA crosslinks

Courtes, M., Boissière, T., Barthe, A., Pasero, P., & Pardo, B. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag295 · Cited by 1

Assaying for Radioresistant DNA Synthesis, the Hallmark Feature of the Intra-S-Phase Checkpoint Using a DNA Fiber Technique

Kijas, A. W., & Lavin, M. F. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6955-5_2 · Cited by 1

The DNA Replication Initiation Machinery as a Target for Cancer Diagnosis and Therapy

Wollenschlaeger, A. (2011) · EUR Research Repository (Erasmus University Rotterdam) · Cited by 1

Chk1 and Chk2 as Checkpoint Targets

Zhang, H., Xiao, Z., & Sowin, T. (2009) · Humana Press eBooks · doi:10.1007/978-1-60761-178-3_16 · Cited by 1

Chk1防止DNA损伤的S期肿瘤细胞进行异常的有丝分裂

吴, 家., 姚, 雪., Tarsha, W., & 李, 小. (2009) · Chinese Science Bulletin (Chinese Version) · doi:10.1360/csb2009-54-18-2797 · Cited by 1

Regulation of oncogene-induced senescence by the MRE11 and TREX1 nucleasesPreprint

Técher, H., Gopaul, D., Heuzé, J., Leray, B., Vernet, A., Mettling, C., Moreaux, J., Lin, Y., & Pasero, P. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.30.534897 · Cited by 1

Topoisomerase I inhibition suppresses nuclear blebbing via RNA Pol II stalling and nuclear stiffeningPreprint

Borowski, N., Li, A., & Stephens, A. D. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.09.698681 · Cited by 1

Role of checkpoint kinase 1 in malignant melanoma

Smith, J. (2013) · Enlighten: Theses (The University of Glasgow)

A bright Quantum of Time in the Cleaver Laboratory; a Tribute and Retrospective

Kaufmann, W. K. (2015) · Photochemistry and Photobiology · doi:10.1111/php.12384

Replication fork dynamics and the DNA damage

Petermann, E. (2016)

Cell Cycle Responses to Hyperthermia

Furusawa, Y. (2016) · Springer eBooks · doi:10.1007/978-981-10-0719-4_6

Chapter 16 Chk1 and Chk2 as Checkpoint Targets

Zhang, H., Xiao, Z., & Sowin, T. (2009)

Nascent DNA Proteomics Reveals a Chromatin Remodeler Required for Topoisomerase I Loading at

Ribeyre, C., Zellweger, R., Chauvin, M. Y., Bec, N., Larroque, C., Lopes, M., & Constantinou, A. (2016)

The Mammalian DNA Replication Elongation Checkpoint: Implication of Chk1 and Relationship with Origin Firing as Determined by Single DNA Molecule and Single Cell Analyses

Conti, C., Seiler, J. A., & Pommier, Y. G. (2007) · Cell Cycle · doi:10.4161/cc.6.22.4932 · Cited by 75

JCB Article Activation of mammalian Chk1 during DNA replication arrest: a role for Chk1 in the intra-S phase checkpoint monitoring replication origin firing

Feijoo, C., Hall-Jackson, C. A., Wu, R., Jenkins, D., Leitch, J., Gilbert, D. M., & Smythe, C. (2013)

Down-regulation of DNA replication in extracts of camptothecin-treated cells: activation of an S-phase checkpoint?

Wang, Y., Perrault, A. R., & Iliakis, G. E. (1997) · PubMed · Cited by 29

Activation of mammalian Chk1 during DNA replication arrest

Feijóo, C. G., Hall-Jackson, C. A., Wu, R., Jenkins, D., Leitch, J., Gilbert, D. M., & Smythe, C. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104099 · Cited by 318

Characterization of a novel ATR-dependent, Chk1-independent, intra-S-phase checkpoint that suppresses initiation of replication inXenopus

Luciani, M. G., Oehlmann, M., & Blow, J. J. (2004) · Journal of Cell Science · doi:10.1242/jcs.01400 · Cited by 83