Identification of the first small-molecule inhibitor of the REV7 DNA repair protein interaction
Open accessAbstract
DNA interstrand crosslink (ICL) repair (ICLR) has been implicated in the resistance of cancer cells to ICL-inducing chemotherapeutic agents. Despite the clinical significance of ICL-inducing chemotherapy, few studies have focused on developing small-molecule inhibitors for ICLR. The mammalian DNA polymerase ζ, which comprises the catalytic subunit REV3L and the non-catalytic subunit REV7, is essential for ICLR. To identify small-molecule compounds that are mechanistically capable of inhibiting ICLR by targeting REV7, high-throughput screening and structure-activity relationship (SAR) analysis were performed. Compound 1 was identified as an inhibitor of the interaction of REV7 with the REV7-binding sequence of REV3L. Compound 7 (an optimized analog of compound 1) bound directly to REV7 in nuclear magnetic resonance analyses, and inhibited the reactivation of a reporter plasmid containing an ICL in between the promoter and reporter regions. The normalized clonogenic survival of HeLa cells treated with cisplatin and compound 7 was lower than that for cells treated with cisplatin only. These findings indicate that a small-molecule inhibitor of the REV7/REV3L interaction can chemosensitize cells by inhibiting ICLR.
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Inhibiting the mutagenic branch of TLS by disrupting pol ζ and Rev1 protein interactions is a strategy.
“Another strategy is to inhibit the mutagenic branch of TLS by disrupting pol ζ and Rev1 protein interactions [118,119]”
From CDK-Independent and PCNA-Dependent Functions of p21 in DNA Replication (2020) · cites this paper as [119]
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Cites
DNA interstrand crosslink repair and cancer
Deans, A. J., & West, S. C. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3088 · Cited by 1,019 · see citing works
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 594 · see citing works
WaterLOGSY as a method for primary NMR screening: Practical aspects and range of applicability
Dalvit, C., Fogliatto, G., Stewart, A., Veronesi, M., & Stockman, B. J. (2001) · Journal of Biomolecular NMR · doi:10.1023/a:1013302231549 · Cited by 570 · see citing works
Mechanism of Replication-Coupled DNA Interstrand Crosslink Repair
Räschle, M., Knipscheer, P., Enoiu, M., Angelov, T., Sun, J., Griffith, J. D., Ellenberger, T., Schärer, O. D., & Walter, J. C. (2008) · Cell · doi:10.1016/j.cell.2008.08.030 · Cited by 507 · see citing works
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 · see citing works
MAD2L2 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 304 · see citing works
Advances in Understanding the Complex Mechanisms of DNA Interstrand Cross-Link RepairPreprint
Clauson, C. L., Schärer, O. D., & Niedernhofer, L. J. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012732 · Cited by 245 · see citing works
DNA polymerase zeta (pol ζ) in higher eukaryotes
Gan, G. N., Wittschieben, J. P., Wittschieben, B. Ø., & Wood, R. D. (2007) · Cell Research · doi:10.1038/cr.2007.117 · Cited by 202 · see citing works
Doles, J., Oliver, T. G., Cameron, E. R., Hsu, G., Jacks, T., Walker, G. C., & Hemann, M. T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011409107 · Cited by 190 · see citing works
Murakumo, Y., Roth, T., Ishii, H., Rasio, D., Numata, S., Croce, C. M., & Fishel, R. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4391 · Cited by 181 · see citing works
Lee, Y., Gregory, M., & Yang, W. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324001111 · Cited by 167 · see citing works
MAD2B is an inhibitor of the anaphase-promoting complexPreprint
Chen, J., & Fang, G. (2001) · Genes & Development · doi:10.1101/gad.898701 · Cited by 144 · see citing works
Inhibition of Cdh1–APC by the MAD2-related protein MAD2L2: a novel mechanism for regulating Cdh1Preprint
Pfleger, C. M., Salic, A. N., Lee, E. N., & Kirschner, M. W. (2001) · Genes & Development · doi:10.1101/gad.897901 · Cited by 140 · see citing works
Cellular Functions of DNA Polymerase ζ and Rev1 Protein
Lawrence, C. W. (2004) · Advances in protein chemistry · doi:10.1016/s0065-3233(04)69006-1 · Cited by 137 · see citing works
Hicks, J. K., Chute, C. L., Paulsen, M. T., Ragland, R. L., Howlett, N. G., Guéranger, Q., Glover, T. W., & Canman, C. E. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00993-09 · Cited by 129 · see citing works
Translesion DNA synthesis polymerases in DNA interstrand crosslink repair
Ho, T. V., & Schärer, O. D. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20573 · Cited by 126 · see citing works
Hara, K., Hashimoto, H., Murakumo, Y., Kobayashi, S., Kogame, T., Unzai, S., Akashi, S., Takeda, S., Shimizu, T., & Sato, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.092403 · Cited by 123 · see citing works
Self-citationWojtaszek, J. L., Lee, C., D’Souza, S., Minesinger, B. K., Kim, H., D’Andrea, A. D., Walker, G. C., & Zhou, P. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394841 · Cited by 111 · see citing works
Wu, F., Lin, X., Okuda, T., & Howell, S. B. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-3942 · Cited by 110 · see citing works
Structural Basis of Recruitment of DNA Polymerase ζ by Interaction between REV1 and REV7 Proteins
Kikuchi, S., Hara, K., Shimizu, T., Sato, M., & Hashimoto, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.396838 · Cited by 103 · see citing works
Self-citationInoue, A., Kikuchi, S., Hishiki, A., Shao, Y., Heath, R. J., Evison, B. J., Actis, M. L., Canman, C. E., Hashimoto, H., & Fujii, N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.520429 · Cited by 99 · see citing works
Self-citationShen, X. H., Jun, S., O'Neal, L. E., Sonoda, E., Bemark, M., Sale, J. E., & Li, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600071200 · Cited by 97 · see citing works
Cheung, H. W., Chun, A. C. S., Wang, Q., Deng, W., Hu, L., Guan, X., Nicholls, J. M., Ling, M., Wong, Y. C., Tsao, S. W., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3602 · Cited by 91 · see citing works
Zhou, P., & Wagner, G. H. (2009) · Journal of Biomolecular NMR · doi:10.1007/s10858-009-9371-6 · Cited by 84 · see citing works
REV7 is essential for DNA damage tolerance via two REV3L binding sites in mammalian DNA polymerase ζ
Tomida, J., Takata, K., Lange, S. S., Schibler, A. C., Yousefzadeh, M. J., Bhetawal, S., Dent, S., & Wood, R. D. (2015) · Nucleic Acids Research · doi:10.1093/nar/gku1385 · Cited by 64 · see citing works
Suppression of REV 7 enhances cisplatin sensitivity in ovarian clear cell carcinoma cells
Niimi, K., Murakumo, Y., Watanabe, N., Kato, T., Mii, S., Enomoto, A., Asai, M., Asai, N., Yamamoto, E., Kajiyama, H., et al. (2014) · Cancer Science · doi:10.1111/cas.12390 · Cited by 56 · see citing works
REV1 and DNA polymerase zeta in DNA interstrand crosslink repair
Sharma, S., & Canman, C. E. (2012) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21736 · Cited by 54 · see citing works
Punchihewa, C., Ferreira, A. M., Cassell, R. J., Rodrigues, P., & Fujii, N. (2009) · Protein Science · doi:10.1002/pro.109 · Cited by 50 · see citing works
Self-citationZhang, L., Yang, S., & Sharrocks, A. D. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02276-06 · Cited by 47 · see citing works
Hashimoto, K., Cho, Y., Yang, I.-Y., Akagi, J., Ohashi, E., Tateishi, S., de Wind, N., Hanaoka, F., Ohmori, H., & Moriya, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.331728 · Cited by 45 · see citing works
The Transcription Factor TFII-I Promotes DNA Translesion Synthesis and Genomic Stability
Fattah, F. J., Hara, K., Fattah, K. R., Yang, C., Wu, N., Warrington, R. T., Chen, D. J., Zhou, P., Boothman, D. A., & Yu, H. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004419 · Cited by 44 · see citing works
Self-citationMurakumo, Y. (2002) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(02)00250-6 · Cited by 38 · see citing works
Rev7/Mad2B plays a critical role in the assembly of a functional mitotic spindle
Bhat, A., Wu, Z., Maher, V. M., McCormick, J. J., & Xiao, W. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1120922 · Cited by 36 · see citing works
Overlapping in short motif sequences for binding to human REV7 and MAD2 proteins
Hanafusa, T., Habu, T., Tomida, J., Ohashi, E., Murakumo, Y., & Ohmori, H. (2010) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01380.x · Cited by 32 · see citing works
Hara, K., Shimizu, T., Unzai, S., Akashi, S., Sato, M., & Hashimoto, H. (2009) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309109046181 · Cited by 28 · see citing works
Self-citationKhalaj, M., Abbasi, A., Yamanishi, H., Akiyama, K., Wakitani, S., Kikuchi, S., Hirose, M., Yuzuriha, M., Magari, M., Degheidy, H. A., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.514752 · Cited by 28 · see citing works
Self-citationREV7/MAD2L2: the multitasking maestro emerges as a barrier to recombination
Sale, J. E. (2015) · The EMBO Journal · doi:10.15252/embj.201591697 · Cited by 22 · see citing works
Destabilization of pluripotency in the absence of Mad2l2
Pirouz, M., Rahjouei, A., Shamsi, F., Eckermann, K. N., Salinas, G., Pommerenke, C., & Kessel, M. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1026485 · Cited by 19 · see citing works
Flagged first, then by citations
1 of the 39 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
A Small Molecule Targeting Mutagenic Translesion Synthesis Improves Chemotherapy
Wojtaszek, J. L., Chatterjee, N., Najeeb, J., Ramos, A., Lee, M., Bian, K., Xue, J. Y., Fenton, B. A., Park, H., Li, D., et al. (2019) · Cell · doi:10.1016/j.cell.2019.05.028 · Cited by 194 · see citing works
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 · see citing works
Inhibition of mutagenic translesion synthesis: A possible strategy for improving chemotherapy?
Yamanaka, K., Chatterjee, N., Hemann, M. T., & Walker, G. C. (2017) · PLOS Genetics · doi:10.1371/journal.pgen.1006842 · Cited by 87 · see citing works
Targeting DNA repair and replication stress in the treatment of ovarian cancer
Murai, J. (2017) · International Journal of Clinical Oncology · doi:10.1007/s10147-017-1145-7 · Cited by 75 · see citing works
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 73 · see citing works
Fanconi anemia pathway as a prospective target for cancer intervention
Liu, W., Palovcak, A., Li, F., Zafar, A., Yuan, F., & Zhang, Y. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-00401-7 · Cited by 67 · see citing works
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 · see citing works
de Krijger, I., Boersma, V., & Jacobs, J. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.04.002 · Cited by 40 · see citing works
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 · see citing works
Translesion DNA Synthesis in Cancer: Molecular Mechanisms and Therapeutic Opportunities
Zafar, M. K., & Eoff, R. L. (2017) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.7b00157 · Cited by 47 · see citing works
Beyond Kinases: Targeting Replication Stress Proteins in Cancer Therapy
Baillie, K. E., & Stirling, P. C. (2020) · Trends in cancer · doi:10.1016/j.trecan.2020.10.010 · Cited by 40 · see citing works
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 · see citing works
Targeting protein–protein interactions in the DNA damage response pathways for cancer chemotherapy
McPherson, K. S., & Korzhnev, D. M. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00101a · Cited by 33 · see citing works
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 30 · see citing works
Replication Fork Remodeling and Therapy Escape in DNA Damage Response-Deficient Cancers
Liptay, M., Barbosa, J. S., & Rottenberg, S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00670 · Cited by 29 · see citing works
Gallo, D., & Brown, G. W. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1651817 · Cited by 21 · see citing works
Ketkar, A. D., Maddukuri, L., Penthala, N. R., Reed, M. R., Zafar, M. K., Crooks, P. A., & Eoff, R. L. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00304 · Cited by 21 · see citing works
Translesion DNA Synthesis and Reinitiation of DNA Synthesis in Chemotherapy Resistance
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 · see citing works
Vanarotti, M., Evison, B. J., Actis, M. L., Inoue, A., McDonald, E. T., Shao, Y., Heath, R. J., & Fujii, N. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.03.028 · Cited by 17 · see citing works
Self-citationWang, S., Xu, Y. C., Zhao, Y. T., Zhang, S., Li, M., Li, X., He, J., Zhou, H., Ge, Z., Li, R., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113859 · Cited by 17 · see citing works
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 · see citing works
Self-citationProtein–Protein Interactions in Translesion Synthesis
Dash, R. C., & Hadden, M. K. (2021) · Molecules · doi:10.3390/molecules26185544 · Cited by 12 · see citing works
Ren, X., Zeng, R., Wang, C., Zhang, M., Liang, C., Tang, Z., & Ren, J. (2017) · RSC Advances · doi:10.1039/c7ra03716c · Cited by 11 · see citing works
Shi, T., Kaneko, L. K., Sandino, M., Busse, R., Zhang, M., Mason, D. J., Machulis, J., Ambrose, A. J., Zhang, D. D., & Chapman, E. (2018) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.8b05276 · Cited by 11 · see citing works
Tamaki, A., Kato, T., Sakurai, Y., Sato, K., Adachi, K., Tadehara, M., Kogami, T., Matsushita, M., Hoshino, A., Sanoyama, I., et al. (2023) · Cancer Science · doi:10.1111/cas.16044 · Cited by 10 · see citing works
Protein Assemblies in Translesion Synthesis
Arianna, G. A., & Korzhnev, D. M. (2024) · Genes · doi:10.3390/genes15070832 · Cited by 10 · see citing works
Tan, A., Xu, F., Yokoyama, C., Yano, S., & Konno, H. (2021) · Journal of Peptide Science · doi:10.1002/psc.3375 · Cited by 9 · see citing works
Inhibitors of the Fanconi anaemia pathway as potential antitumour agents for ovarian cancer
Taylor, S. J., Arends, M. J., & Langdon, S. P. (2020) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2020.00003 · Cited by 8 · see citing works
Coleman, K. E., Shin, D.-W., Goehring, L. J., Szeitz, B., Fenyö, D., Rothenberg, E., Poirier, J. T., & Huang, T. T. (2025) · Nature Communications · doi:10.1038/s41467-025-66068-1 · Cited by 6 · see citing works
Fujii, N. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00358 · Cited by 6 · see citing works
Self-citationStewart, J. T., Shawon, J., Ali, M., Williams, B., Shahinuzzaman, A. D. A., Rupa, S. A., Al‐Adhami, T., Jia, R., Bourque, C., Faddis, R., et al. (2023) · Journal of Peptide Science · doi:10.1002/psc.3553 · Cited by 4 · see citing works
Peptiligase, an Enzyme for Efficient Chemo-Enzymatic Peptide Synthesis (Ceps) of Aviptadil
Mahmoudzadeh, K., Habibi, Z., Yousefi, M., Mostafavi, M., & Mohammadi, M. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.127089 · Cited by 4 · see citing works
Kesen, Y., Ichinoe, M., Hayashi, S., Umezawa, A., Numata, Y., Kogami, T., Matsushita, M., Sanoyama, I., Hoshino, A., Sakurai, Y., et al. (2024) · Pathology International · doi:10.1111/pin.13504 · Cited by 1 · see citing works
Cheng, J., Sun, H., Ma, W., Yu, J., Hao, Y., Wang, F., Li, X., Wang, H., Ling, J., & Xu, F. (2023) · Research Square · doi:10.21203/rs.3.rs-3071400/v1 · Cited by 1 · see citing works
Hara, K. (2019) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.19-00092
Self-citationStudy on antibacterial activity and self-assembly of ovalbumin-derived peptides
Tan, A., & Konno, H. (2021) · E3S Web of Conferences · doi:10.1051/e3sconf/202124503056
Interview of George Toney by Dian O. Belanger
Toney, G. (2009) · The Knowledge Bank (The Ohio State University)
Ma, X., Yang, F., Ma, K., Shen, H., Han, J., Wang, K., Yang, Y., Zhu, J., An, R., Wang, Q., et al. (2023) · Food Science and Human Wellness · doi:10.26599/fshw.2022.9250241
Probing hot spots of protein-protein interactions mediated by the safety-belt region of REV7
Dash, R. C., Arianna, G. A., Patel, S. M., Rizzo, A. A., Harrahill, N. J., Korzhnev, D. M., & Hadden, M. K. (2024) · Structure · doi:10.1016/j.str.2024.09.007
Significance of REV7 Expression in p16‐Negative Oropharyngeal Squamous Cell Carcinoma
Momiyama, K., Tsutsumi, S., Sakurai, Y., Mogi, S., Miyamoto, S., Murakumo, Y., & Yamashita, T. (2024) · Head & Neck · doi:10.1002/hed.28015
Nugroho, A., Comte, S., Barrière, P., Allen, R. B., Sherwin, W. B., & Rollins, L. A. (2026) · Molecular Ecology · doi:10.1111/mec.70495
- Authors
- Actis, M. L., Ambaye, N. D., Evison, B. J., Shao, Y., Vanarotti, M., Inoue, A., McDonald, E. T., Kikuchi, S., Heath, R., Hara, K., Hashimoto, H., & Fujii, N.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Shizuoka University (JP)
- Corresponding author
- Fujii, Naoaki
- ORCID
- Venue
- Bioorganic & Medicinal Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-09
- Volume
- 24
- Issue
- 18
- Pages
- 4339-4346
- ISSN
- 0968-0896 (ISSN-L)
- PMC
- PMC5688848
- OpenAlex
- W2494938857
- Cited by
- 42
- References
- 39
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 4 · 2023: 7 · 2021: 7 · 2020: 9 · 2019: 4 · 2018: 2 · 2017: 5
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Bioorganic & Medicinal Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- American Cancer Society (CDD-120969)
- American Lebanese Syrian Associated Charities
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Oncology › Metal complexes synthesis and properties
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer therapeutics and mechanisms
- Keywords
- REV7, REV3L, DNA polymerase zeta, interstrand crosslink repair, small molecule inhibitors, protein-protein interaction inhibition, cisplatin resistance, chemosensitization, structure-activity relationship, HeLa cells, clonogenic survival
- MeSH terms
- Antineoplastic Agents, Cisplatin, DNA-Directed DNA Polymerase, DNA Repair, DNA-Binding Proteins, HeLa Cells, Humans, Protein Binding, Pyrimidinones, Structure-Activity Relationship, Thiophenes, Drug Resistance, Neoplasm, Mad2 Proteins
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