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A Small Molecule Targeting Mutagenic Translesion Synthesis Improves Chemotherapy
Open accessAbstract
Intrinsic and acquired drug resistance and induction of secondary malignancies limit successful chemotherapy. Because mutagenic translesion synthesis (TLS) contributes to chemoresistance as well as treatment-induced mutations, targeting TLS is an attractive avenue for improving chemotherapeutics. However, development of small molecules with high specificity and in vivo efficacy for mutagenic TLS has been challenging. Here, we report the discovery of a small-molecule inhibitor, JH-RE-06, that disrupts mutagenic TLS by preventing recruitment of mutagenic POL ζ. Remarkably, JH-RE-06 targets a nearly featureless surface of REV1 that interacts with the REV7 subunit of POL ζ. Binding of JH-RE-06 induces REV1 dimerization, which blocks the REV1-REV7 interaction and POL ζ recruitment. JH-RE-06 inhibits mutagenic TLS and enhances cisplatin-induced toxicity in cultured human and mouse cell lines. Co-administration of JH-RE-06 with cisplatin suppresses the growth of xenograft human melanomas in mice, establishing a framework for developing TLS inhibitors as a novel class of chemotherapy adjuvants.
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“Recently, a small molecule that disrupts this interaction and sensitizes tumors to cisplatin was developed, also demonstrating in vivo efficacy [120]”
From CDK-Independent and PCNA-Dependent Functions of p21 in DNA Replication (2020) · cites this paper as [120]
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“also demonstrating in vivo efficacy [120]”
From CDK-Independent and PCNA-Dependent Functions of p21 in DNA Replication (2020) · cites this paper as [120]
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“or JH-RE-06, which induces REV1 dimerization to block the REV1-REV7 interaction (Fig. 6).109”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [109]
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Cites
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
REV7 counteracts DNA double-strand break resection and affects PARP inhibition
Xu, G., Chapman, J. R., Brandsma, I., Yuan, J., Mistrík, M., Bouwman, P., Bártková, J., Gogola, E., Warmerdam, D. O., Barazas, M., et al. (2015) · Nature · doi:10.1038/nature14328 · Cited by 611
Estimation of rat mammary tumor volume using caliper and ultrasonography measurements
Faustino‐Rocha, A. I., Oliveira, P. A., Pinho, J. O., Teixeira-Guedes, C., Soares, R. M. M., da Costa, R. M. G., Colaço, B., Pires, M. J., Colaço, J., Ferreira, R. M., et al. (2013) · Lab Animal · doi:10.1038/laban.254 · Cited by 504
Xu, X., Xie, K., Zhang, X.-Q., Pridgen, E. M., Park, G. Y., Cui, D. S., Shi, J., Wu, J., Kantoff, P. W., Lippard, S. J., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303958110 · Cited by 340
Self-citationMAD2L2 controls DNA repair at telomeres and DNA breaks by inhibiting 5′ end resection
Boersma, V., Moatti, N., Segura‐Bayona, S., Peuscher, M. H., van der Torre, J., Wevers, B. A., Orthwein, A., Durocher, D., & Jacobs, J. J. L. (2015) · Nature · doi:10.1038/nature14216 · Cited by 311
Two-polymerase mechanisms dictate error-free and error-prone translesion DNA synthesis in mammals
Shachar, S., Ziv, O., Avkin, S., Adar, S., Wittschieben, J., Reißner, T., Chaney, S., Friedberg, E. C., Wang, Z., Carell, T., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.281 · Cited by 284
Translesion DNA polymerases in eukaryotes: what makes them tick?
Vaisman, A., & Woodgate, R. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1291576 · Cited by 261
Translesion and Repair DNA Polymerases: Diverse Structure and Mechanism
Yang, W., & Gao, Y. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-012405 · Cited by 245
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Bukowski, K., Kciuk, M., & Kontek, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093233 · Cited by 1,853
The rediscovery of platinum-based cancer therapy
Rottenberg, S., Disler, C., & Perego, P. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-00308-y · Cited by 993
Cancer drug-tolerant persister cells: from biological questions to clinical opportunities
Russo, M., Chen, M., Mariella, E., Peng, H., Rehman, S. K., Sancho, E., Sogari, A., Toh, T. S., Balaban, N. Q., Batlle, E., et al. (2024) · Nature Reviews Cancer · doi:10.1038/s41568-024-00737-z · Cited by 210
Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200
Tirman, S., Quinet, A., Wood, M. D., Meroni, A., Cybulla, E., Jackson, J., Pegoraro, S., Simoneau, A., Zou, L., & Vindigni, A. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.013 · Cited by 202
Molecular glues for protein-protein interactions: Progressing toward a new dream
Konstantinidou, M., & Arkin, M. R. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.04.002 · Cited by 200
Taglialatela, A., Leuzzi, G., Sannino, V., Cuella-Martin, R., Huang, J., Wu-Baer, F., Baer, R. J., Costanzo, V., & Ciccia, A. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.016 · Cited by 183
PARP inhibition impedes the maturation of nascent DNA strands during DNA replication
Vaitsiankova, A., Burdová, K., Sobol, M. A., Gautam, A., Benada, O., Hanzlíková, H., & Caldecott, K. W. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00747-1 · Cited by 172
Leveraging the replication stress response to optimize cancer therapy
Cybulla, E., & Vindigni, A. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00518-6 · Cited by 144
Defining molecular glues with a dual-nanobody cannabidiol sensor
Cao, S., Kang, S., Mao, H., Yao, J., Gu, L., & Zheng, N. (2022) · Nature Communications · doi:10.1038/s41467-022-28507-1 · Cited by 125
Nayak, S. U., Calvo, J. A., Cong, K., Peng, M., Berthiaume, E. A., Jackson, J., Zaino, A. M., Vindigni, A., Hadden, M. K., & Cantor, S. B. (2020) · Science Advances · doi:10.1126/sciadv.aaz7808 · Cited by 119
CDK-Independent and PCNA-Dependent Functions of p21 in DNA Replication
Mansilla, S. F., De La Vega, M. B., Calzetta, N. L., Siri, S. O., & Gottifredi, V. (2020) · Genes · doi:10.3390/genes11060593 · Cited by 114
Molecular glues and bifunctional compounds: Therapeutic modalities based on induced proximity
Schreiber, S. L. (2024) · Cell Chemical Biology · doi:10.1016/j.chembiol.2024.05.004 · Cited by 112
DNA polymerase ζ in DNA replication and repair
Martin, S. K., & Wood, R. D. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz705 · Cited by 119
Exploiting replication gaps for cancer therapy
Cong, K., & Cantor, S. B. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.023 · Cited by 107
POLθ processes ssDNA gaps and promotes replication fork progression in BRCA1-deficient cells
Schrempf, A., Bernardo, S., Arasa-Verge, E. A., Ramírez-Otero, M. A., Wilson, J., Kirchhofer, D., Timelthaler, G., Ambros, A. M., Kaya, A., Wieder, M., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111716 · Cited by 92
Tertiary lymphoid structures are critical for cancer prognosis and therapeutic response
Zhang, Q., & Wu, S. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1063711 · Cited by 86
Mehta, K. P. M., Lovejoy, C. A., Zhao, R., Heintzman, D. R., & Cortez, D. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107705 · Cited by 75
Roles of trans-lesion synthesis (TLS) DNA polymerases in tumorigenesis and cancer therapy
Anand, J. R., Chiou, L. F., Sciandra, C. A., Zhang, X., Hong, J., Wu, D., Zhou, P., & Vaziri, C. (2023) · NAR Cancer · doi:10.1093/narcan/zcad005 · Cited by 75
Self-citationPrimPol‐mediated repriming facilitates replication traverse of DNA interstrand crosslinks
González‐Acosta, D., Blanco‐Romero, E., Ubieto‐Capella, P., Mutreja, K., Miguez-Amil, S., Llanos, S., Garcı́a, F., Muñoz, J., Blanco, L., Lopes, M., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106355 · Cited by 73
Russo, M., Pompei, S., Sogari, A., Corigliano, M., Crisafulli, G., Puliafito, A., Lamba, S., Erriquez, J., Bertotti, A., Gherardi, M., et al. (2022) · Nature Genetics · doi:10.1038/s41588-022-01105-z · Cited by 71
Structure and mechanism of B-family DNA polymerase ζ specialized for translesion DNA synthesis
Malik, R., Kopylov, M., Gómez-Llorente, Y., Jain, R., Johnson, R. E., Prakash, L., Prakash, S., Ubarretxena‐Belandia, I., & Aggarwal, A. K. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0476-7 · Cited by 67
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Fielden, J., Siegner, S. M., Gallagher, D. N., Schröder, M., Stritto, M. R. D., Lam, S., Kobel, L., Schlapansky, M. F., Jackson, S. P., Ćejka, P., et al. (2025) · Nature · doi:10.1038/s41586-025-08815-4 · Cited by 66
Wu, H., Yao, H., He, C., Jia, Y., Zhu, Z., Xu, S., Li, D., & Xu, J. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.03.019 · Cited by 63
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Marima, R. M., Hull, R., Penny, C. B., & Dlamini, Z. (2021) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2021.108376 · Cited by 55
Chatterjee, N., Whitman, M. A., Harris, C. A., Min, S. M., Jonas, O. H., Lien, E. C., Luengo, A., Heiden, M. G. V., Hong, J., Zhou, P., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016064117 · Cited by 55
Self-citationLi, J., Zheng, C., Mai, Q., Huang, X., Pan, W., Lu, J., Chen, Z., Zhang, S., Zhang, C., Huang, H., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.10.002 · Cited by 48
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Scelfo, A., Angrisani, A., Grillo, M., Barnes, B. M., Muyas, F., Sauer, C. M., Leung, C. W. B., Dumont, M., Grison, M., Mazaud, D., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.018 · Cited by 50
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Paniagua, I., & Jacobs, J. J. L. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.07.008 · Cited by 50
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Meng, T., Wang, X., Jiang, S., Chen, S., Zhou, S., Zhu, Y., Wu, J., Hu, D., Yan, Y., & Zhang, G. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c10074 · Cited by 42
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Maiorano, D., Etri, J. E., Franchet, C., & Hoffmann, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083924 · Cited by 41
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Li, J., Zheng, C., Wang, M., Umano, A. D., Dai, Q., Zhang, C., Huang, H., Yang, Q., Yang, X., Lu, J., et al. (2022) · Oncogene · doi:10.1038/s41388-021-02149-x · Cited by 40
Cheng, X., An, J., Lou, J., Gu, Q., Ding, W., Droby, G. N., Wang, Y., Wang, C., Gao, Y., Anand, J. R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-45979-5 · Cited by 41
Zhang, S., Zhou, L., Zhang, M., Wang, Y., Wang, M., Du, J., Gu, W., Kui, F., Li, J., Geng, S., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01658 · Cited by 37
RetractedThe Rev1-Polζ translesion synthesis mutasome: Structure, interactions and inhibition
Rizzo, A. A., & Korzhnev, D. M. (2019) · The Enzymes · doi:10.1016/bs.enz.2019.07.001 · Cited by 40
Translesion synthesis inhibitors as a new class of cancer chemotherapeutics
Patel, S. M., Dash, R. C., & Hadden, M. K. (2020) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2021.1850692 · Cited by 39
Progress in Research of Nanotherapeutics for Overcoming Multidrug Resistance in Cancer
Maimaitijiang, A., He, D., Li, D., Li, W., Su, Z., Fan, Z., & Li, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25189973 · Cited by 39
Self-citationRegulation of translesion DNA synthesis in mammalian cells
Ma, X., Tang, T., & Guo, C. (2020) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22359 · Cited by 39
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Ler, A. A. L., & Carty, M. P. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2021.822500 · Cited by 37
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Gyüre, Z., Póti, Á., Németh, E., Szikriszt, B., Lózsa, R., Krawczyk, M., Richardson, A. L., & Szüts, D. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112887 · Cited by 33
Vassel, F.-M., Bian, K., Walker, G. C., & Hemann, M. T. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016067117 · Cited by 32
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Stanzione, M., Zhong, J., Wong, E., LaSalle, T. J., Wise, J. F., Simoneau, A., Myers, D. T., Phat, S., Sade-Feldman, M., Lawrence, M. S., et al. (2022) · Science Advances · doi:10.1126/sciadv.abn1229 · Cited by 32
Zhu, H., Tian, Y., Chen, H., Qian, Y., Li, J., Niu, D., Zhao, W., Wu, Y., Zhang, X., Tang, T., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101287 · Cited by 30
Sakurai, Y., Ichinoe, M., Yoshida, K., Nakazato, Y., Saito, S., Satoh, M., Nakada, N., Sanoyama, I., Umezawa, A., Numata, Y., et al. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.06.001 · Cited by 31
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Wang, X., Pernicone, N., Pertz, L., Hua, D., Zhang, T., Listovsky, T., & Xie, W. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010123 · Cited by 33
Lin, S., Yu, L., Song, X., Bi, J., Jiang, L., Wang, Y., He, M., Xiao, Q., Sun, M., Olopade, O. I., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1871-z · Cited by 29
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Sasatani, M., Zaharieva, E. K., & Kamiya, K. (2020) · Genes and Environment · doi:10.1186/s41021-020-0148-1 · Cited by 27
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Dai, Y., Zhang, F., Wang, L., Shan, S., Gong, Z., & Zhou, Z. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011464 · Cited by 28
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Seppa, I. M., Ceppi, I., Tennakoon, M., Reginato, G., Jackson, J., Rouault, C. D., Agashe, S., Sviderskiy, V. O., Limbu, M., Lantelme, E., et al. (2025) · Genes & Development · doi:10.1101/gad.352421.124 · Cited by 26
Brown, V. E., Moore, S. L., Chen, M., House, N. C. M., Ramsden, P., Wu, H., Ribich, S. A., Grassian, A. R., & Choi, Y. J. (2023) · NAR Cancer · doi:10.1093/narcan/zcad039 · Cited by 25
Aptamers against cancer drug resistance: Small fighters switching tactics in the face of defeat
Sanati, M., Afshari, A. R., Ahmadi, S. S., Kesharwani, P., & Sahebkar, A. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166720 · Cited by 27
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Chen, Y., Jie, X., Xing, B., Wu, Z., Yang, X., Rao, X., Xu, Y., Zhou, D., Dong, X., Zhang, T., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04567-5 · Cited by 25
Quaternary structural diversity in eukaryotic DNA polymerases: monomeric to multimeric form
Acharya, N., Khandagale, P., Thakur, S., Sahu, J. K., & Utkalaja, B. G. (2020) · Current Genetics · doi:10.1007/s00294-020-01071-1 · Cited by 25
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Selective Inhibition of DNA Polymerase β by a Covalent Inhibitor
Yuhas, S. C., Laverty, D. J., Lee, H., Majumdar, A. K., & Greenberg, M. M. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c02453 · Cited by 19
Spanjaard, A., Shah, R., de Groot, D., Buoninfante, O. A., Morris, B., Lieftink, C., Pritchard, C. E. J., Zürcher, L. M., Ormel, S., Catsman, J. J. I., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac545 · Cited by 20
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Sun, X., Hou, W., Liu, X., Chai, J., Guo, H., & Yu, J. (2020) · Cancer Cell International · doi:10.1186/s12935-020-01668-z · Cited by 23
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Hoshino, A., Nakayama, C., Jiang, S., Sakurai, Y., Kato, T., Numata, Y., Umezawa, A., Ichinoe, M., & Murakumo, Y. (2021) · Pathology International · doi:10.1111/pin.13174 · Cited by 19
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Ikeh, K., Lamkin, E. N., Crompton, A., Deutsch, J., Fisher, K., Gray, M., Argyle, D. J., Lim, W. Y., Korzhnev, D. M., Hadden, M. K., et al. (2021) · Cancers · doi:10.3390/cancers13215290 · Cited by 19
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Chen, G., Bao, Y., Weng, Q., Zhao, Y., Lu, X., Fu, L., Chen, L., Liu, Z., Zhang, X., & Liang, G. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01533 · Cited by 19
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Shilkin, E. S., Boldinova, E. O., Stolyarenko, A. D., Гончарова, Р. И., Chuprov‐Netochin, R. N., Smal, M. P., & Makarova, А. V. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920080039 · Cited by 18
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Zhu, N., Zhao, Y., Mi, M., Lu, Y., Tan, Y., Fang, X., Weng, S., & Yuan, Y. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.997970 · Cited by 18
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Sellés‐Baiget, S., Ambjørn, S. M., Carli, A., Hendriks, I. A., Gallina, I., Davey, N. E., Benedict, B., Zarantonello, A., Gadi, S. A., Meeusen, B., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01395-3 · Cited by 23
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Weaver, T., Cortez, L. M., Khoang, T. H., Washington, M. T., Agarwal, P. K., & Freudenthal, B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010484117 · Cited by 18
Tarantino, D., Walker, C., Weekes, D. B., Pemberton, H. N., Davidson, K., Torga, G., Frankum, J. R., Mendes‐Pereira, A. M., Prince, C., Ferro, R., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02369-9 · Cited by 16
Gong, K., Dong, Y., Wang, L., Duan, Y., Yu, J., Sun, Y., Bai, M., & Duan, Y. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s248667 · Cited by 15
Wang, H., Li, J., Qin, J., Li, J., Chen, Y., Song, D., Zeng, H., & Wang, S. (2021) · Journal of Photochemistry and Photobiology. B: Biology · doi:10.1016/j.jphotobiol.2021.112366 · Cited by 11
REV7 in Cancer Biology and Management
Murakumo, Y., Sakurai, Y., Kato, T., Hashimoto, H., & Ichinoe, M. (2023) · Cancers · doi:10.3390/cancers15061721 · Cited by 14
Kim, S., Park, S. H., Kang, N., Ra, J. S., Myung, K., & Lee, K. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae785 · Cited by 14
Chen, T., Tongpeng, S., Lu, Z., Topatana, W., Juengpanich, S., Li, S., Hu, J., Cao, J., Lee, C., Tian, Y., et al. (2022) · Aging and Cancer · doi:10.1002/aac2.12047 · Cited by 15
The mutational impact of Illudin S on human cells
Casimir, L., Zimmer, S., Racine-Brassard, F., Jacques, P., & Maréchal, A. (2022) · DNA repair · doi:10.1016/j.dnarep.2022.103433 · Cited by 15
Mechanism of nucleotide discrimination by the translesion synthesis polymerase Rev1
Weaver, T., Click, T. H., Khoang, T. H., Washington, M. T., Agarwal, P. K., & Freudenthal, B. (2022) · Nature Communications · doi:10.1038/s41467-022-30577-0 · Cited by 13
Feltes, B. C., & Menck, C. F. M. (2022) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2022.108436 · Cited by 15
Intrinsic base substitution patterns in diverse species reveal links to cancer and metabolism
Gelova, S. P., Doherty, K. N., Alasmar, S., & Chan, K. (2022) · Genetics · doi:10.1093/genetics/iyac144 · Cited by 12
RAD51 is chromatin enriched and targetable in BRCA1-deficient cells
Peng, M., Lee, S., Nair, H. G., MacGilvary, N. J., Cong, K., Kraemer, M., Li, R., McConnell, J., Baer, C. E., Deng, B., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.017 · Cited by 11
REV1-POL ζ Inhibition and Cancer Therapy
Taniguchi, T. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.012 · Cited by 12
Cryo-EM reveals conformational flexibility in apo DNA polymerase ζ
Truong, C. D., Craig, T. A., Cui, G., Botuyan, M. V., Serkasevich, R. A., Chan, K.-Y., Mer, G., Chiu, P., & Kumar, R. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100912 · Cited by 13
Protein–Protein Interactions in Translesion Synthesis
Dash, R. C., & Hadden, M. K. (2021) · Molecules · doi:10.3390/molecules26185544 · Cited by 13
Malik, R., Johnson, R. E., Ubarretxena‐Belandia, I., Prakash, L., Prakash, S., & Aggarwal, A. K. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01302-w · Cited by 12
Sanoyama, I., Sakurai, Y., Ichinoe, M., Hoshino, A., Kesen, Y., Kato, T., Numata, Y., Umezawa, A., Jiang, S., & Murakumo, Y. (2020) · Pathology International · doi:10.1111/pin.13040 · Cited by 12
Yoon, J.-H., Johnson, R. E., Prakash, L., & Prakash, S. (2021) · Genes & Development · doi:10.1101/gad.348662.121 · Cited by 15
Sui, L., Xie, X., Fu, P., Du, J., & Peng, C. Y. (2022) · International Journal of Oncology · doi:10.3892/ijo.2022.5391 · Cited by 11
AlSaihati, H., & Rabaan, A. A. (2023) · Saudi Medical Journal · doi:10.15537/smj.2023.44.4.20220600 · Cited by 11
Disrupting the MAD2L2-Rev1 Complex Enhances Cell Death upon DNA Damage
Pernicone, N., Elias, M., Onn, I., Tobi, D., & Listovsky, T. (2022) · Molecules · doi:10.3390/molecules27030636 · Cited by 11
Metadata
- Authors
- Wojtaszek, J. L., Chatterjee, N., Najeeb, J., Ramos, A., Lee, M., Bian, K., Xue, J. Y., Fenton, B. A., Park, H., Li, D., Hemann, M. T., Hong, J., Walker, G. C., & Zhou, P.
- Affiliations
- Duke Medical Center (US)
- Massachusetts Institute of Technology (US)
- Koch Institute for Integrative Cancer Research At MIT (US)
- Duke University (US)
- University of Rhode Island (US)
- Corresponding author
- Hemann, Michael T.
- Hong, Jiyong
- Walker, Graham C.
- Zhou, Pei
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2019-06
- Volume
- 178
- Issue
- 1
- Pages
- 152-159.e11
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC6644000
- OpenAlex
- W2948035094
- Cited by
- 194
- References
- 39
- Citations by year
- 2026: 22 · 2025: 20 · 2024: 42 · 2023: 23 · 2022: 29 · 2021: 18 · 2020: 32 · 2019: 8
- FWCI
- 7.19
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc-nd)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- Alexander and Margaret Stewart Trust
- Duke University
- National Cancer Institute
- National Institute of Environmental Health Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer therapeutics and mechanisms
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Keywords
- Rev1, REV7, small molecule inhibitors, cisplatin, chemoresistance, melanoma, adjuvant chemotherapy, protein dimerization, drug resistance
- MeSH terms
- Y-Family DNA Polymerases, Animals, Antineoplastic Agents, Cell Survival, Cisplatin, DNA Damage, DNA-Directed DNA Polymerase, Female, Humans, Mice, Nude, Mice, Transgenic, Neoplasms, Nucleotidyltransferases, Quinolines, Transfection, Mutagenesis, Xenograft Model Antitumor Assays, Cell Line, Tumor, Tumor Burden, Mice, Gene Knockdown Techniques, Mad2 Proteins
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