DNA damage-induced cell death relies on SLFN11-dependent cleavage of distinct type II tRNAs
Open accessAbstract
Transcriptome analysis reveals a strong positive correlation between human Schlafen family member 11 (SLFN11) expression and the sensitivity of tumor cells to DNA-damaging agents (DDAs). Here, we show that SLFN11 preferentially inhibits translation of the serine/threonine kinases ATR and ATM upon DDA treatment based on distinct codon usage without disrupting early DNA damage response signaling. Type II transfer RNAs (tRNAs), which include all serine and leucine tRNAs, are cleaved in a SLFN11-dependent manner in response to DDAs. Messenger RNAs encoded by genes with high TTA (Leu) codon usage, such as ATR, display utmost susceptibility to translational suppression by SLFN11. Specific attenuation of tRNA-Leu-TAA sufficed to ablate ATR protein expression and restore the DDA sensitivity of SLFN11-deficient cells. Our study uncovered a novel mechanism of codon-specific translational inhibition via SLFN11-dependent tRNA cleavage in the DNA damage response and supports the notion that SLFN11-deficient tumor cells can be resensitized to DDAs by targeting ATR or tRNA-Leu-TAA.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Li et al. demonstrated that genetic inhibition of SLFN11 expression caused chemoresistance.
“To functionally implicate SLFN11 in response to DNA-damaging chemotherapeutics (topoisomerase inhibitors, an anti-metabolite, and an alkylating agent), Li et al. demonstrated that genetic inhibition of SLFN11 expression caused chemoresistance [28].”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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 · see citing works
Sharp, P. M., & Li, W.-H. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.3.1281 · Cited by 3,992 · see citing works
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 1,953 · see citing works
ATR: an essential regulator of genome integrity
Cimprich, K. A., & Cortez, D. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2450 · Cited by 1,798 · see citing works
GtRNAdb 2.0: an expanded database of transfer RNA genes identified in complete and draft genomes
Chan, P. P., & Lowe, T. M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1309 · Cited by 1,035 · see citing works
GtRNAdb: a database of transfer RNA genes detected in genomic sequence
Chan, P. P., & Lowe, T. M. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn787 · Cited by 867 · see citing works
The quantitative proteome of a human cell line
Beck, M., Schmidt, A., Malmstroem, J., Claassen, M., Ori, A., Szymborska, A., Herzog, F., Rinner, O., Ellenberg, J., & Aebersold, R. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.82 · Cited by 816 · see citing works
Targeting DNA Repair in Cancer: Beyond PARP Inhibitors
Brown, J. S., O’Carrigan, B., Jackson, S. P., & Yap, T. A. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0860 · Cited by 623 · see citing works
DNA-Damaging Agents in Cancer Chemotherapy: Serendipity and Chemical Biology
Cheung-Ong, K., Giaever, G. N., & Nislow, C. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.04.007 · Cited by 585 · see citing works
Design of antisense oligonucleotides stabilized by locked nucleic acids
Kurreck, J. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.9.1911 · Cited by 576 · see citing works
CAIcal: A combined set of tools to assess codon usage adaptation
Puigbò, P., Bravo, I., & García-Vallvé, S. (2008) · Biology Direct · doi:10.1186/1745-6150-3-38 · Cited by 569 · see citing works
Efficient and quantitative high-throughput tRNA sequencing
Zheng, G., Qin, Y., Clark, W. C., Dai, Q., Yi, C., He, C., Lambowitz, A. M., & Pan, T. (2015) · Nature Methods · doi:10.1038/nmeth.3478 · Cited by 550 · see citing works
Chemosensitive Relapse in Small Cell Lung Cancer Proceeds through an EZH2-SLFN11 Axis
Gardner, E. E., Lok, B. H., Schneeberger, V. E., Desmeules, P., Miles, L. A., Arnold, P. K., Ni, A., Khodos, I., de Stanchina, E., Nguyen, T. N., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.01.006 · Cited by 516 · see citing works
Cozen, A. E., Quartley, E., Holmes, A. D., Hrabeta-Robinson, E., Phizicky, E. M., & Lowe, T. M. (2015) · Nature Methods · doi:10.1038/nmeth.3508 · Cited by 479 · see citing works
Molecular Mechanism of Scanning and Start Codon Selection in Eukaryotes
Hinnebusch, A. G. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00008-11 · Cited by 451 · see citing works
Codon-usage-based inhibition of HIV protein synthesis by human schlafen 11
Li, M., Kao, E., Gao, X., Sandig, H., Limmer, K., Pavon-Eternod, M., Jones, T. E., Landry, S., Pan, T., Weitzman, M. D., et al. (2012) · Nature · doi:10.1038/nature11433 · Cited by 375 · see citing works
Self-citationPutative DNA/RNA helicase Schlafen-11 (SLFN11) sensitizes cancer cells to DNA-damaging agents
Zoppoli, G. M., Regairaz, M., Leo, E., Reinhold, W. C., Varma, S., Ballestrero, A., Doroshow, J. H., & Pommier, Y. G. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205943109 · Cited by 364 · see citing works
SLFN11 Blocks Stressed Replication Forks Independently of ATR
Murai, J., Tang, S.-W., Leo, E., Baechler, S. A., Redon, C. E., Zhang, H., Al Abo, M., Rajapakse, V. N., Nakamura, E., Jenkins, L. M. M., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.012 · Cited by 275 · see citing works
Grünweller, A. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg409 · Cited by 269 · see citing works
Schlafen, a New Family of Growth Regulatory Genes that Affect Thymocyte Development
Schwarz, D. A., Katayama, C. D., & Hedrick, S. Μ. (1998) · Immunity · doi:10.1016/s1074-7613(00)80663-9 · Cited by 229 · see citing works
SLFN11 inhibits checkpoint maintenance and homologous recombination repair
Mu, Y., Lou, J., Srivastava, M., Zhao, B., Feng, X., Liu, T., Chen, J., & Huang, J. (2016) · The EMBO Reports · doi:10.15252/embr.201540964 · Cited by 160 · see citing works
Human cell line (COLO 357) of metastatic pancreatic adenocarcinoma
Morgan, R. T., Woods, L. K., Moore, G. E., Quinn, L. A., McGavran, L., & Gordon, S. G. (1980) · International Journal of Cancer · doi:10.1002/ijc.2910250507 · Cited by 145 · see citing works
DNA Repair: From Genome Maintenance to Biomarker and Therapeutic Target
Jalal, S. I., Earley, J. N., & Turchi, J. J. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-0761 · Cited by 130 · see citing works
Yang, J.-Y., Deng, X.-Y., Li, Y.-S., Ma, X.-C., Feng, J.-X., Yu, B., Chen, Y., Luo, Y.-L., Wang, X., Chen, M.-L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03544-x · Cited by 124 · see citing works
Bustos, O., Naik, S., Ayers, G. M., Casola, C., Perez-Lamigueiro, M. A., Chippindale, P. T., Pritham, E. J., & de la Casa‐Esperón, E. (2009) · Gene · doi:10.1016/j.gene.2009.07.006 · Cited by 117 · see citing works
Eukaryotic initiator tRNA: Finely tuned and ready for action
Kolitz, S. E., & Lorsch, J. R. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.11.047 · Cited by 64 · see citing works
Characterization of Novel Ribosome-Associated Endoribonuclease SLFN14 from Rabbit Reticulocytes
Pisareva, V. P., Muslimov, I. A., Tcherepanov, A., & Pisarev, A. V. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00302 · Cited by 53 · see citing works
Hopper, A. K., & Huang, H. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00131-15 · Cited by 42 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Noncanonical Roles of tRNAs: tRNA Fragments and Beyond
Su, Z., Wilson, B., Kumar, P., & Dutta, A. (2020) · Annual Review of Genetics · doi:10.1146/annurev-genet-022620-101840 · Cited by 241 · see citing works
Biomarker-Guided Development of DNA Repair Inhibitors
Cleary, J. M., Aguirre, A. J., Shapiro, G. I., & D’Andrea, A. D. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.04.035 · Cited by 231 · see citing works
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 · see citing works
Murai, J., Thomas, A., Miettinen, M., & Pommier, Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.05.009 · Cited by 172 · see citing works
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 152 · see citing works
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 · see citing works
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 91 · see citing works
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 87 · see citing works
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 · see citing works
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 · see citing works
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 82 · see citing works
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 79 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 69 · see citing works
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 · see citing works
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 · see citing works
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 55 · see citing works
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 · see citing works
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 · see citing works
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 51 · see citing works
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 49 · see citing works
Korniy, N., Samatova, E., Anokhina, M. M., Peske, F., & Rodnina, M. V. (2019) · FEBS Letters · doi:10.1002/1873-3468.13478 · Cited by 45 · see citing works
Shee, K., Wells, J. D., Jiang, A., & Miller, T. W. (2019) · PLOS ONE · doi:10.1371/journal.pone.0224267 · Cited by 43 · see citing works
“demonstrated that genetic inhibition of SLFN11 expression caused chemoresistance [28].”
BackgroundLee, 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 44 · see citing works
Barayan, R., Ran, X., & Lok, B. H. (2020) · Journal of Thoracic Disease · doi:10.21037/jtd.2020.03.89 · Cited by 42 · see citing works
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 43 · see citing works
Malone, D., Lardelli, R. M., Li, M., & David, M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006588 · Cited by 43 · see citing works
Self-citationThe tRNA regulome in neurodevelopmental and neuropsychiatric disease
Blaze, J., & Akbarian, S. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01585-9 · Cited by 42 · see citing works
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 41 · see citing works
Emerging translation strategies during virus–host interaction
Hoang, H.-D., Neault, S., Pelin, A., & Alain, T. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1619 · Cited by 37 · see citing works
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 40 · see citing works
Schlafens Can Put Viruses to Sleep
Kim, E. T., & Weitzman, M. D. (2022) · Viruses · doi:10.3390/v14020442 · Cited by 33 · see citing works
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 35 · see citing works
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 · see citing works
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 34 · see citing works
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 · see citing works
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 33 · see citing works
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 35 · see citing works
Self-citationKaur, 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 · see citing works
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 32 · see citing works
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 32 · see citing works
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 32 · see citing works
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 31 · see citing works
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 31 · see citing works
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 30 · see citing works
Luan, J., Gao, X., Hu, F., Zhang, Y., & Gou, X. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2019.1616746 · Cited by 24 · see citing works
Self-citationKobayashi‐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 · see citing works
Self-citationFuningana, 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 · see citing works
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 23 · see citing works
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 · see citing works
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 · see citing works
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 22 · see citing works
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 21 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationLegrand, 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 · see citing works
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 15 · see citing works
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 · see citing works
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 · see citing works
Chen, J., & Kuhn, L. A. (2019) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2019.04.003 · Cited by 14 · see citing works
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 · see citing works
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 11 · see citing works
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 · see citing works
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 13 · see citing works
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 12 · see citing works
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 11 · see citing works
“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 11 · see citing works
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 · see citing works
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 · see citing works
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 10 · see citing works
Qi, F., Alvi, E., Ogawa, M., Kobayashi, J., Mu, A., & Takata, M. (2023) · Genes to Cells · doi:10.1111/gtc.13056 · Cited by 9 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Mu, A., Okamoto, Y., Katsuki, Y., & Takata, M. (2024) · DNA repair · doi:10.1016/j.dnarep.2024.103733 · Cited by 8 · see citing works
Interpreting ribosome dynamics during mRNA translation
Uematsu, S., & Qian, S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110469 · Cited by 9 · see citing works
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. (2026) · Nature Cell Biology · doi:10.1038/s41556-025-01852-1 · Cited by 7 · see citing works
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 8 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 7 · see citing works
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 8 · see citing works
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 · 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
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 · see citing works
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 · see citing works
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 · see citing works
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 5 · see citing works
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 · see citing works
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 · see citing works
Self-citationUncovering 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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
- Authors
- Li, M., Kao, E., Malone, D., Gao, X., Wang, J. Y. J., & David, M.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Li, Manqing
- David, Michael
- Venue
- Nature Structural & Molecular Biology
- Published
- 2018-10-29
- Volume
- 25
- Issue
- 11
- Pages
- 1047-1058
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC6579113
- OpenAlex
- W2895818115
- Cited by
- 136
- References
- 28
- Citations by year
- 2026: 18 · 2025: 27 · 2024: 20 · 2023: 18 · 2022: 12 · 2021: 17 · 2020: 11 · 2019: 13
- FWCI
- 3.65
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM101982, R01GM128155)
- National Institute of Allergy and Infectious Diseases (R21AI088490, R21AI124199)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- SLFN11, DNA damage response, ATR kinase, ATM kinase, DNA-damaging agents, camptothecin, tumor cell sensitivity
- MeSH terms
- Camptothecin, Codon, DNA Damage, Humans, Nuclear Proteins, RNA, Transfer, RNA, Transfer, Leu, Protein Biosynthesis, Cell Death, RNA, Small Interfering, Cell Line, Tumor, HEK293 Cells, Topoisomerase I Inhibitors, Ataxia Telangiectasia Mutated Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review