DNA damage-induced cell death relies on SLFN11-dependent cleavage of distinct type II tRNAs

The Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity

Barretina, J., Caponigro, G., Stransky, N., Venkatesan, K., Margolin, A. A., Kim, S., Wilson, C. J., Lehár, J., Kryukov, G. V., Sonkin, D., et al. (2012) · Nature · doi:10.1038/nature11003 · Cited by 7,950

The codon adaptation index-a measure of directional synonymous codon usage bias, and its potential applications

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ATM, ATR, and DNA-PK: The Trinity at the Heart of the DNA Damage Response

Blackford, A. N., & Jackson, S. P. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.015 · Cited by 2,050

ATR: an essential regulator of genome integrity

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GtRNAdb 2.0: an expanded database of transfer RNA genes identified in complete and draft genomes

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GtRNAdb: a database of transfer RNA genes detected in genomic sequence

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The quantitative proteome of a human cell line

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Targeting DNA Repair in Cancer: Beyond PARP Inhibitors

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DNA-Damaging Agents in Cancer Chemotherapy: Serendipity and Chemical Biology

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Design of antisense oligonucleotides stabilized by locked nucleic acids

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Noncanonical Roles of tRNAs: tRNA Fragments and Beyond

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Biomarker-Guided Development of DNA Repair Inhibitors

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Adavosertib plus gemcitabine for platinum-resistant or platinum-refractory recurrent ovarian cancer: a double-blind, randomised, placebo-controlled, phase 2 trial

Lheureux, S., Cristea, M. C., Bruce, J. P., Garg, S., Cabanero, M., Mantia-Smaldone, G. M., Olawaiye, A. B., Ellard, S. L., Weberpals, J. I., Hendrickson, A. E. W., et al. (2021) · The Lancet · doi:10.1016/s0140-6736(20)32554-x · Cited by 214

Schlafen 11 (SLFN11), a restriction factor for replicative stress induced by DNA-targeting anti-cancer therapies

Murai, J., Thomas, A., Miettinen, M., & Pommier, Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.05.009 · Cited by 172

DNA damage induces p53-independent apoptosis through ribosome stalling

Boon, N. J., Oliveira, R. A., Körner, P.-R., Kochavi, A., Mertens, S., Malka, Y., Voogd, R., van der Horst, S. E. M., Huismans, M. A., Smabers, L. P., et al. (2024) · Science · doi:10.1126/science.adh7950 · Cited by 161

Inside the hypoxic tumour: reprogramming of the DDR and radioresistance

Begg, K., & Tavassoli, M. (2020) · Cell Death Discovery · doi:10.1038/s41420-020-00311-0 · Cited by 109

Roles and regulation of tRNA-derived small RNAs in animals

Muthukumar, S., Li, C., Liu, R., & Bellodi, C. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00690-z · Cited by 104

NONU-1 Encodes a Conserved Endonuclease Required for mRNA Translation Surveillance

Glover, M. L., Burroughs, A. M., Monem, P. C., Egelhofer, T. A., Pule, M. N., Aravind, L., & Arribere, J. A. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.023 · Cited by 88

SLFN2 protection of tRNAs from stress-induced cleavage is essential for T cell–mediated immunity

Yue, T., Zhan, X., Zhang, D., Jain, R., Wang, K.-W., Choi, J. H., Misawa, T., Su, L., Quan, J., Hildebrand, S., et al. (2021) · Science · doi:10.1126/science.aba4220 · Cited by 86

Structure of PDE3A-SLFN12 complex reveals requirements for activation of SLFN12 RNase

Garvie, C. W., Wu, X., Papanastasiou, M., Lee, S., Fuller, J., Schnitzler, G. R., Horner, S. W., Baker, A., Zhang, T., Mullahoo, J. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24495-w · Cited by 85

Chromatin Remodeling and Immediate Early Gene Activation by SLFN11 in Response to Replication Stress

Murai, J., Zhang, H., Pongor, L. S., Tang, S.-W., Jo, U., Moribe, F., Ma, Y., Tomita, M., & Pommier, Y. G. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.117 · Cited by 84

Mechanistic understanding of human SLFN11

Metzner, F. J., Wenzl, S. J., Kugler, M., Krebs, S., Hopfner, K., & Lammens, K. (2022) · Nature Communications · doi:10.1038/s41467-022-33123-0 · Cited by 80

A multiplex platform for small RNA sequencing elucidates multifaceted tRNA stress response and translational regulation

Watkins, C. P., Zhang, W., Wylder, A. C., Katanski, C. D., & Pan, T. (2022) · Nature Communications · doi:10.1038/s41467-022-30261-3 · Cited by 77

SLFN11 promotes CDT1 degradation by CUL4 in response to replicative DNA damage, while its absence leads to synthetic lethality with ATR/CHK1 inhibitors

Jo, U., Murai, Y., Chakka, S., Chen, L., Cheng, K. C.-C., Murai, J., Saha, L. K., Jenkins, L. M. M., & Pommier, Y. G. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015654118 · Cited by 76

The Role of Translation Control in Tumorigenesis and Its Therapeutic Implications

Xu, Y., & Ruggero, D. (2020) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030419-033420 · Cited by 67

Structural, molecular, and functional insights into Schlafen proteins

Jo, U., & Pommier, Y. G. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00794-0 · Cited by 72

Serum tRNA‐derived fragments (tRFs) as potential candidates for diagnosis of nontriple negative breast cancer

Huang, Y., Ge, H., Zheng, M., Cui, Y., Fu, Z., Wu, X., Xia, Y., Chen, L., Wang, Z., Wang, S., et al. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.29185 · Cited by 62

A wake-up call for cancer DNA damage: the role of Schlafen 11 (SLFN11) across multiple cancers

Zhang, B., Ramkumar, K., Cardnell, R. J., Gay, C. M., Stewart, C. A., Wang, W., Fujimoto, J., Wistuba, I. I., & Byers, L. A. (2021) · British Journal of Cancer · doi:10.1038/s41416-021-01476-w · Cited by 61

Schlafen 11 Restricts Flavivirus Replication

Valdez, F., Salvador, J., Palermo, P. M., Mohl, J. E., Hanley, K. A., Watts, D. M., & Llano, M. (2019) · Journal of Virology · doi:10.1128/jvi.00104-19 · Cited by 59

SLFN11 Inactivation Induces Proteotoxic Stress and Sensitizes Cancer Cells to Ubiquitin Activating Enzyme Inhibitor TAK-243

Murai, Y., Jo, U., Murai, J., Jenkins, L. M. M., Huang, S.-Y. N., Chakka, S., Chen, L., Cheng, K. C.-C., Fukuda, S., Takebe, N., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-2694 · Cited by 54

Schlafen 11 predicts response to platinum-based chemotherapy in gastric cancers

Takashima, T., Taniyama, D., Sakamoto, N., Yasumoto, M., Asai, R., Hattori, T., Honma, R., Phạm, Q. T., Ukai, S., Maruyama, R., et al. (2021) · British Journal of Cancer · doi:10.1038/s41416-021-01364-3 · Cited by 52

Precision Oncology with Drugs Targeting the Replication Stress, ATR, and Schlafen 11

Jo, U., Murai, Y., Takebe, N., Thomas, A., & Pommier, Y. G. (2021) · Cancers · doi:10.3390/cancers13184601 · Cited by 53

Human SAMD9 is a poxvirus-activatable anticodon nuclease inhibiting codon-specific protein synthesis

Zhang, F., Ji, Q., Chaturvedi, J., Morales, M., Mao, Y., Meng, X., Dong, L., Deng, J., Qian, S., & Xiang, Y. (2023) · Science Advances · doi:10.1126/sciadv.adh8502 · Cited by 47

Mechanisms and biomedical implications of –1 programmed ribosome frameshifting on viral and bacterial mRNAs

Korniy, N., Samatova, E., Anokhina, M. M., Peske, F., & Rodnina, M. V. (2019) · FEBS Letters · doi:10.1002/1873-3468.13478 · Cited by 46

Integrated pan-cancer gene expression and drug sensitivity analysis reveals SLFN11 mRNA as a solid tumor biomarker predictive of sensitivity to DNA-damaging chemotherapy

Shee, K., Wells, J. D., Jiang, A., & Miller, T. W. (2019) · PLOS ONE · doi:10.1371/journal.pone.0224267 · Cited by 43

Radiosensitization of head and neck squamous cell carcinoma lines by DNA-PK inhibitors is more effective than PARP-1 inhibition and is enhanced by SLFN11 and hypoxia

Lee, T. W., Wong, W. W., Dickson, B. D., Lipert, B. A., Cheng, G. J., Hunter, F. W., Hay, M. P., & Wilson, W. R. (2019) · International Journal of Radiation Biology · doi:10.1080/09553002.2019.1664787 · Cited by 46

PARP inhibitors for small cell lung cancer and their potential for integration into current treatment approaches

Barayan, R., Ran, X., & Lok, B. H. (2020) · Journal of Thoracic Disease · doi:10.21037/jtd.2020.03.89 · Cited by 43

Structural and biochemical characterization of human Schlafen 5

Metzner, F. J., Huber, E., Hopfner, K., & Lammens, K. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab1278 · Cited by 41

Dephosphorylation activates the interferon-stimulated Schlafen family member 11 in the DNA damage response

Malone, D., Lardelli, R. M., Li, M., & David, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006588 · Cited by 43

The tRNA regulome in neurodevelopmental and neuropsychiatric disease

Blaze, J., & Akbarian, S. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01585-9 · Cited by 41

Velcrin-induced selective cleavage of tRNALeu(TAA) by SLFN12 causes cancer cell death

Lee, S., Hoyt, S. H., Wu, X., Garvie, C. W., McGaunn, J. P., Shekhar, M., Tötzl, M., Rees, M. G., Cherniack, A. D., Meyerson, M. M., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01170-9 · Cited by 42

Emerging translation strategies during virus–host interaction

Hoang, H., Neault, S., Pelin, A., & Alain, T. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1619 · Cited by 39

SLFN11 captures cancer-immunity interactions associated with platinum sensitivity in high-grade serous ovarian cancer

Winkler, C., King, M., Berthe, J., Ferraioli, D., Garuti, A., Grillo, F., Rodriguez‐Canales, J., Ferrando, L., Chopin, N., Ray-Coquard, I. L., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.146098 · Cited by 43

Schlafens Can Put Viruses to Sleep

Kim, E. T., & Weitzman, M. D. (2022) · Viruses · doi:10.3390/v14020442 · Cited by 33

tsRNA modifications: An emerging layer of biological regulation in disease

Liang, Y., Ji, D., Ying, X., Ma, R., & Ji, W. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.09.010 · Cited by 40

SLFN11 promotes stalled fork degradation that underlies the phenotype in Fanconi anemia cells

Okamoto, Y., Abe, M., Mu, A., Tempaku, Y., Rogers, C. B., Mochizuki, A. L., Katsuki, Y., Kanemaki, M. T., Takaori‐Kondo, A., Sobeck, A., et al. (2020) · Blood · doi:10.1182/blood.2019003782 · Cited by 37

Reconsidering the mechanisms of action of PARP inhibitors based on clinical outcomes

Onji, H., & Murai, J. (2022) · Cancer Science · doi:10.1111/cas.15477 · Cited by 38

Resistance to Pyrrolobenzodiazepine Dimers Is Associated with SLFN11 Downregulation and Can Be Reversed through Inhibition of ATR

Mao, S., Chaerkady, R., Yu, W., D’Angelo, G., Garcia, A., Chen, H., Barrett, A. M., Phipps, S. S., Fleming, R. L., Hess, S. Y., et al. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-20-0351 · Cited by 34

tRNA ‐derived RNAs : Biogenesis and roles in translational control

Akiyama, Y., & Ivanov, P. V. (2023) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1805 · Cited by 35

Schlafen 11 triggers innate immune responses through its ribonuclease activity upon detection of single-stranded DNA

Zhang, P., Hu, X., Li, Z., Liu, Q., Liu, L., Jin, Y.-Y., Liu, S., Zhao, X., Wang, J., Hao, D., et al. (2024) · Science Immunology · doi:10.1126/sciimmunol.adj5465 · Cited by 36

Identification of Schlafen-11 as a Target of CD47 Signaling That Regulates Sensitivity to Ionizing Radiation and Topoisomerase Inhibitors

Kaur, S., Schwartz, A. L., Jordan, D. G., Soto‐Pantoja, D. R., Kuo, B., ELKAHLOUN, A. G., Griner, L. A. M., Thomas, C. J., Ferrer, M., Thomas, A., et al. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00994 · Cited by 33

SLFN11-mediated ribosome biogenesis impairment induces TP53-independent apoptosis

Ogawa, A., Izumikawa, K., Tate, S., Isoyama, S., Masaru, M., Fujiwara, K., Watanabe, S., Ohga, T., Jo, U., Taniyama, D., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.01.008 · Cited by 36

Epigenetic suppression of SLFN11 in germinal center B-cells during B-cell development

Moribe, F., Nishikori, M., Takashima, T., Taniyama, D., Onishi, N., Arima, H., Sasanuma, H., Akagawa, R., Elloumi, F., Takeda, S., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0237554 · Cited by 34

Schlafens: Emerging Proteins in Cancer Cell Biology

Al‐Marsoummi, S., Vomhof‐DeKrey, E. E., & Basson, M. D. (2021) · Cells · doi:10.3390/cells10092238 · Cited by 35

Mitochondrial tRNA-Derived Fragments and Their Contribution to Gene Expression Regulation

Shaukat, A., Kaliatsi, E. G., Stamatopoulou, V., & Stathopoulos, C. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.729452 · Cited by 33

Human cytomegalovirus protein RL1 degrades the antiviral factor SLFN11 via recruitment of the CRL4 E3 ubiquitin ligase complex

Nightingale, K., Potts, M., Hunter, L. M., Fielding, C. A., Zerbe, C. M., Fletcher-Etherington, A., Nobre, L., Wang, E. C. Y., Strang, B. L., Houghton, J. W., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2108173119 · Cited by 30

Novel therapeutic combinations with PARP inhibitors for small cell lung cancer: A bench-to-bedside review

Xiong, J., Barayan, R., Louie, A. V., & Lok, B. H. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.07.008 · Cited by 31

SLFN11 is a general target for enhancing the sensitivity of cancer to chemotherapy (DNA-damaging agents)

Luan, J., Gao, X., Hu, F., Zhang, Y., & Gou, X. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2019.1616746 · Cited by 24

Schlafen 12 restricts HIV-1 latency reversal by a codon-usage dependent post-transcriptional block in CD4+ T cells

Kobayashi‐Ishihara, M., Smutná, K. F., Alonso, F. E., Argilaguet, J. M., Esteve‐Codina, A., Geiger, K., Genescà, M., Grau-Expósito, J., Duran-Castells, C., Rogenmoser, S., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-04841-y · Cited by 25

Can integrative biomarker approaches improve prediction of platinum and PARP inhibitor response in ovarian cancer?

Funingana, I.-G., Reinius, M. A. V., Petrillo, A., Ang, J. E., & Brenton, J. D. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.02.008 · Cited by 23

Schlafen 11 further sensitizes BRCA-deficient cells to PARP inhibitors through single-strand DNA gap accumulation behind replication forks

Onji, H., Tate, S., Sakaue, T., Fujiwara, K., Nakano, S., Kawaida, M., Onishi, N., Matsumoto, T., Yamagami, W., Sugiyama, T., et al. (2024) · Oncogene · doi:10.1038/s41388-024-03094-1 · Cited by 26

SLFN5 influences proliferation and apoptosis by upregulating PTEN transcription via ZEB1 and inhibits the purine metabolic pathway in breast cancer: Am J Cancer Res. 2020; 10(9): 2832-2850

Gu, X., Wan, G., Yang, Y., Liu, Y., Yang, X., Zheng, Y., Jiang, L., Zhang, P., Liu, D., Zhao, W., et al. (2026) · American Journal of Cancer Research · doi:10.62347/noic1325 · Cited by 23

Impact of Tumour Hypoxia on Evofosfamide Sensitivity in Head and Neck Squamous Cell Carcinoma Patient-Derived Xenograft Models

Harms, J. K., Lee, T. W., Wang, T., Lai, A., Kee, D., Chaplin, J. M., McIvor, N., Hunter, F. W., Macann, A., Wilson, W. R., et al. (2019) · Cells · doi:10.3390/cells8070717 · Cited by 21

Translational quality control and reprogramming during stress adaptation

Han, N., Kelly, P., & Ibba, M. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112161 · Cited by 23

Human Schlafen 11 exploits codon preference discrimination to attenuate viral protein synthesis of prototype foamy virus (PFV)

Guo, G., Wang, Y., Hu, X., Li, Z.-R., Tan, J., & Qiao, W. (2020) · Virology · doi:10.1016/j.virol.2020.12.015 · Cited by 24

The emerging role of Schlafen-11 (SLFN11) in predicting response to anticancer treatments: Focus on small cell lung cancer

Scattolin, D., Maso, A. D., Ferro, A., Frega, S., Bonanno, L., Guarneri, V., & Pasello, G. (2024) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2024.102768 · Cited by 21

tRNA and tsRNA: From Heterogeneity to Multifaceted Regulators

Li, Y., Yu, Z., Jiang, W., Lyu, X., Guo, A., Sun, X., Yang, Y.-T., & Zhang, Y. (2024) · Biomolecules · doi:10.3390/biom14101340 · Cited by 21

Schlafen 11 expression in human acute leukemia cells with gain-of-function mutations in the interferon-JAK signaling pathway

Murai, Y., Jo, U., Murai, J., Fukuda, S., Takebe, N., & Pommier, Y. G. (2021) · iScience · doi:10.1016/j.isci.2021.103173 · Cited by 20

Epigenetic upregulation of Schlafen11 renders WNT- and SHH-activated medulloblastomas sensitive to cisplatin

Nakata, S., Murai, J., Okada, M., Takahashi, H., Findlay, T., Malebranche, K. J., Parthasarathy, A., Miyashita, S., Gabdulkhaev, R., Benkimoun, I., et al. (2022) · Neuro-Oncology · doi:10.1093/neuonc/noac243 · Cited by 23

Structural and biochemical characterization of Schlafen11 N-terminal domain

Hou, P., Hao, W., Qin, B., Li, M., Zhao, R., & Cui, S. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad509 · Cited by 20

SAMD9L acts as an antiviral factor against HIV-1 and primate lentiviruses by restricting viral and cellular translation

Legrand, A., Dahoui, C., De La Myre Mory, C., Noy, K., Guiguettaz, L., Versapuech, M., Loyer, C., Pillon, M., Wcislo, M., Guéguen, L., et al. (2024) · PLOS Biology · doi:10.1371/journal.pbio.3002696 · Cited by 18

The crucial role of single-stranded DNA binding in enhancing sensitivity to DNA-damaging agents for Schlafen 11 and Schlafen 13

Fujiwara, K., Maekawa, M., Iimori, Y., Ogawa, A., Urano, T., Kono, N., Takeda, H., Higashiyama, S., Arita, M., & Murai, J. (2023) · iScience · doi:10.1016/j.isci.2023.108529 · Cited by 19

Schlafen 11 (SLFN11) Kills Cancer Cells Undergoing Unscheduled Re-replication

Murai, J., Ceribelli, M., Fu, H., Redon, C. E., Jo, U., Murai, Y., Aladjem, M. I., Thomas, C. J., & Pommier, Y. G. (2023) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-22-0552 · Cited by 14

Human Schlafen 11 inhibits influenza A virus production

Jitobaom, K., Sirihongthong, T., Boonarkart, C., Phakaratsakul, S., Suptawiwat, O., & Auewarakul, P. (2023) · Virus Research · doi:10.1016/j.virusres.2023.199162 · Cited by 14

Deciphering the three-domain architecture in schlafens and the structures and roles of human schlafen12 and serpinB12 in transcriptional regulation

Chen, J., & Kuhn, L. A. (2019) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2019.04.003 · Cited by 15

Phosphorylation-mediated conformational change regulates human SLFN11

Kugler, M., Metzner, F. J., Witte, G., Hopfner, K.-P., & Lammens, K. (2024) · Nature Communications · doi:10.1038/s41467-024-54833-7 · Cited by 13

Expression of transgenes enriched in rare codons is enhanced by the MAPK pathway

Peterson, J. J., Li, S., Kaltenbrun, E., Roux, Ö. L., & Counter, C. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-78453-5 · Cited by 12

DNA damage response and repair genes in advanced bone and soft tissue sarcomas: An 8-gene signature as a candidate predictive biomarker of response to trabectedin and olaparib combination

Merlini, A., Centomo, M. L., Ferrero, G., Chiabotto, G., Miglio, U., Berrino, E., Giordano, G., Brusco, S., Pisacane, A. M., Maldi, E., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.844250 · Cited by 13

Mouse Slfn8 and Slfn9 genes complement human cells lacking SLFN11 during the replication stress response

Alvi, E., Mochizuki, A. L., Katsuki, Y., Ogawa, M., Qi, F., Okamoto, Y., Takata, M., & Mu, A. (2023) · Communications Biology · doi:10.1038/s42003-023-05406-9 · Cited by 16

Schlafen14 Impairs HIV-1 Expression in a Codon Usage-Dependent Manner

Valenzuela, C. A., Saucedo, S., & Llano, M. (2024) · Viruses · doi:10.3390/v16040502 · Cited by 14

Chemotherapeutic agents and leucine deprivation induce codon-biased aberrant protein production in cancer

Kochavi, A., Nagel, R., Körner, P.-R., Bleijerveld, O. B., Lin, C., Huinen, Z. R., Malka, Y., Proost, N., van de Ven, M., Feng, X., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1110 · Cited by 15

“Transfer” of power: The intersection of DNA virus infection and tRNA biology

Dremel, S. E., Jimenez, A. R., & Tucker, J. M. (2023) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2023.01.011 · Cited by 13

Epigenetic silencing schlafen-11 sensitizes esophageal cancer to ATM inhibitor

Zhou, J., Zhang, M., Gao, A., Zhu, C., He, T., Herman, J. G., & Guo, M. (2024) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v16.i5.2060 · Cited by 10

SLFN11: a pan-cancer biomarker for DNA-targeted drugs sensitivity and therapeutic strategy guidance

Zhou, K., Li, Y., Wang, W., Chen, Y., Qian, B., Liang, Y., Li, H., Xu, R., & Zhuang, L. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1582738 · Cited by 10

Men who inject opioids exhibit altered tRNA-Gly-GCC isoforms in semen

Gornalusse, G. G., Spengler, R. M., Sandford, E., Kim, Y., Levy, C., Tewari, M., Hladik, F., & Vojtech, L. N. (2023) · Molecular Human Reproduction · doi:10.1093/molehr/gaad003 · Cited by 9

The ribonuclease domain function is dispensable for SLFN11 to mediate cell fate decision during replication stress response

Qi, F., Alvi, E., Ogawa, M., Kobayashi, J., Mu, A., & Takata, M. (2023) · Genes to Cells · doi:10.1111/gtc.13056 · Cited by 10

The Typical tRNA Co-Expresses Multiple 5′ tRNA Halves Whose Sequences and Abundances Depend on Isodecoder and Isoacceptor and Change with Tissue Type, Cell Type, and Disease

Akins, R. B., Ostberg, K., Cherlin, T., Tsiouplis, N. J., Loher, P., & Rigoutsos, I. (2023) · Non-Coding RNA · doi:10.3390/ncrna9060069 · Cited by 9

tRNA‐derived fragments as new players in regulatory processes in yeast

Tyczewska, A., & Grzywacz, K. (2022) · Yeast · doi:10.1002/yea.3829 · Cited by 9

Post-Transcriptional HIV-1 Latency: A Promising Target for Therapy?

Kobayashi‐Ishihara, M., & Tsunetsugu‐Yokota, Y. (2024) · Viruses · doi:10.3390/v16050666 · Cited by 8

The role of SLFN11 in DNA replication stress response and its implications for the Fanconi anemia pathway

Mu, A., Okamoto, Y., Katsuki, Y., & Takata, M. (2024) · DNA repair · doi:10.1016/j.dnarep.2024.103733 · Cited by 8

Interpreting ribosome dynamics during mRNA translation

Uematsu, S., & Qian, S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110469 · Cited by 11

RPA exhaustion activates SLFN11 to eliminate cells with heightened replication stress

Stanage, T. H., Li, S., Segura‐Bayona, S., Idilli, A. I., Millar, R., Hewitt, G., & Boulton, S. J. (2026) · Nature Cell Biology · doi:10.1038/s41556-025-01852-1 · Cited by 9

XPOT Disruption Suppresses TNBC Growth through Inhibition of Specific tRNA Nuclear Exportation and TTC19 Expression to Induce Cytokinesis Failure

Dai, H., Yang, X., Sheng, X., Wang, Y., Zhang, S., Zhang, X., Hu, L.-P., Zhang, Z., Dong, X., Yin, W., et al. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.85006 · Cited by 9

Research progress of the SLFN family in malignant tumors

Yu, J., Guo, Z., & Zhang, J. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1468484 · Cited by 8

CryoEM structure of the SLFN14 endoribonuclease reveals insight into RNA binding and cleavage

Riper, J. M. V., Martinez-Claros, A. O., Wang, L., Schneiderman, H. E., Maheshwari, S., & Pillon, M. C. (2025) · Nature Communications · doi:10.1038/s41467-025-61091-8 · Cited by 7

SLFN11-mediated tRNA regulation induces cell death by disrupting proteostasis in response to DNA-damaging agents

Iimori, Y., Morita, T., Masuda, T., Kitajima, S., Kono, N., Kageyama, S., Galipon, J., Sasaki, A. T., & Kanai, A. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf789 · Cited by 7

Bacterial Schlafen proteins mediate phage defence

Taboada, V. P., Wu, Y., Cassidy, R., Medvedev, K. E., Loeff, L., Nemudraia, A., & Nemudryi, A. A. (2026) · Nature Microbiology · doi:10.1038/s41564-026-02277-8 · Cited by 13

Interferon-Stimulated Genes that Target Retrovirus Translation

Jäger, N., Pöhlmann, S., Rodnina, M. V., & Ayyub, S. A. (2024) · Viruses · doi:10.3390/v16060933 · Cited by 9

A rational targeted therapy for platinum-resistant small-cell lung cancer

Drapkin, B. J., & Minna, J. D. (2021) · Cancer Cell · doi:10.1016/j.ccell.2021.03.003 · Cited by 7

SLFN11 counteracts the RFWD3-PRIMPOL DNA damage tolerance axis to restrain gapped DNA synthesis in response to replication stress

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

Viral codon usage and the virus-host interactions

Sirihongthong, T., & Auewarakul, P. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1711603 · Cited by 5

Coronaviruses reprogram the tRNA epitranscriptome to favor viral protein expression

Muscolino, E., Puig-Torrents, M., Bisquert, J. B., Mendonça, D. C., Talló-Parra, M., Pérez‐Vilaró, G., Caño-Prades, O., Meehan, G. R., Kerr, K., Herder, V., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69700-w · Cited by 5

Reversing regulatory safeguards: Targeting the ATR pathway to overcome PARP inhibitor resistance

Lin, X., Qiu, Y., Soni, A., Stuschke, M., & Iliakis, G. E. (2025) · Molecular Therapy Oncology · doi:10.1016/j.omton.2025.200934 · Cited by 5

In vivo structure profiling reveals human cytosolic and mitochondrial tRNA structurome and interactome in response to stress

Peña, N., Hou, Y., Watkins, C. P., Huang, S., Zhang, W., Katanski, C. D., & Pan, T. (2025) · Nature Communications · doi:10.1038/s41467-025-59435-5 · Cited by 6

From predictive biomarker to therapeutic target: the dual role of SLFN11 in chemotherapy sensitivity

Feng, Y., Li, Y., Zhang, Z., Dai, Y., Gou, X., Lao, K., & Zhang, R. (2025) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-025-04781-w · Cited by 5

SLFN11, far from being limited to responding to cancer DNA damage

Xiao, H., Han, Z., Tang, Y., Gao, X., Xu, M., Qiu, S., Ren, N., Yi, Y., & Zhou, C. (2025) · Clinical and Experimental Medicine · doi:10.1007/s10238-025-01776-y · Cited by 5

Uncovering the evolving arms race between host immunity and HIV-1

Song, Y.-H., Kim, H., Baur, A. S., & Lee, J. (2025) · Trends in Immunology · doi:10.1016/j.it.2025.08.004 · Cited by 5

Exploiting nanopore sequencing advances for tRNA sequencing of human cancer models

Kochavi, A., Velds, A., Suzuki, M., Akichika, S., Suzuki, T., Beijersbergen, R. L., & Agami, R. (2025) · NAR Cancer · doi:10.1093/narcan/zcaf044 · Cited by 5

Progress in investigating the relationship between Schlafen5 genes and malignant tumors

Tu, T., Yuan, Y., Liu, X., Liang, X. T., Yang, X., & Yang, Y. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1248825 · Cited by 5

Evolutionary characterization of antiviral SAMD9/9L across kingdoms supports ancient convergence and lineage-specific adaptations

Legrand, A., Demeure, R., Chantharath, A., Rey, C., Baltenneck, J., Gilchrist, C. L. M., Rocha, J. L., Loyer, C., Picard, L., Cimarelli, A., et al. (2025) · Nature Ecology & Evolution · doi:10.1038/s41559-025-02845-x · Cited by 4

Abstract 2573: DNA damaging drugs stimulate tRNA cleavage through SLFN11 to inhibit protein synthesis and induce cell death

Li, M., Kao, E., Malone, D., Gao, X., Wang, J. Y., & David, M. (2019) · Molecular and Cellular Biology / Genetics · doi:10.1158/1538-7445.sabcs18-2573

Human intrinsic immunity factor SLFN11 promotes cell death upon DNA damages through cleavage of distinct type II tRNAs and inhibition of proteins syntheses related to DNA damage responses and repairs

Li, M., Kao, E., Malone, D., Gao, X., Wang, J. Y. J., & David, M. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.202.supp.194.20

SLFN11-mediated tRNA regulation induces cell death by disrupting proteostasis in response to DNA-damaging agents

Iimori, Y., Morita, T., Masuda, T., Kitajima, S., Kono, N., Kageyama, S., Galipon, J., Sasaki, A. T., & Kanai, A. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf789 · Cited by 7

The Regulation and Activity of Schlafen11

Malone, D. (2017) · eScholarship (California Digital Library)

Dephosphorylation activates the interferon-stimulated Schlafen family member 11 in the DNA damage response

Malone, D., Lardelli, R. M., Li, M., & David, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006588 · Cited by 43