Amidino-Rocaglates: A Potent Class of eIF4A Inhibitors
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Rocaglates share a common cyclopenta[b]benzofuran core that inhibits eukaryotic translation initiation by modifying the behavior of the RNA helicase, eIF4A. Working as interfacial inhibitors, rocaglates stabilize the association between eIF4A and RNA, which can lead to the formation of steric barriers that block initiating ribosomes. There is significant interest in the development and expansion of rocaglate derivatives, as several members of this family have been shown to possess potent anti-neoplastic activity in vitro and in vivo. To further our understanding of rocaglate diversity and drug design, herein we explore the RNA clamping activity of >200 unique rocaglate derivatives. Through this, we report on the identification and characterization of a potent class of synthetic rocaglates called amidino-rocaglates. These compounds are among the most potent rocaglates documented to date and, taken together, this work offers important information that will guide the future design of rocaglates with improved biological properties.
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eIF4A1 and eIF4A2 share approximately 90% sequence similarity and both can integrate into the eIF4F complex.
“The eIF4A gene encodes 2 isoforms, eIF4A1 and eIF4A2, which share approximately 90% sequence similarity and can both integrate into the eIF4F complex.”
From Targeting eIF4A-dependent translation in genetically complex sarcoma (2026) · cites this paper as [34]
The Introduction states that eIF4A2 shares 90% amino acid identity with eIF4A1 and participates in translation initiation. It describes eIF4A as a component of eIF4F, but does not explicitly say that both paralogs can integrate into that complex. Page numbers are unavailable in our copy. (LLM, conf=0.83)
Experimental — accuracy not yet measuredInhibition of both eIF4A isoforms by rocaglates may contribute to their efficacy.
“This supports the idea that increased expression of eIF4A2 may protect cells from the effects of eIF4A1 inhibition; rocaglates such as [-]CR-1-31B inhibit both isoforms, which may contribute to their efficacy (21, 34).”
From Targeting eIF4A-dependent translation in genetically complex sarcoma (2026) · cites this paper as [34]
Rocaglates such as [-]CR-1-31B inhibit both eIF4A1 and eIF4A2 isoforms.
“This supports the idea that increased expression of eIF4A2 may protect cells from the effects of eIF4A1 inhibition; rocaglates such as [-]CR-1-31B inhibit both isoforms, which may contribute to their efficacy (21, 34).”
From Targeting eIF4A-dependent translation in genetically complex sarcoma (2026) · cites this paper as [34]
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Survival signalling by Akt and eIF4E in oncogenesis and cancer therapy
Wendel, H., de Stanchina, E., Fridman, J. S., Malina, A., Ray, S., Kogan, S. C., Cordon‐Cardo, C., Pelletier, J., & Lowe, S. W. (2004) · Nature · doi:10.1038/nature02369 · Cited by 956 · see citing works
Self-citationTargeting the translation machinery in cancer
Bhat, M., Robichaud, N., Hulea, L., Sonenberg, N., Pelletier, J., & Topisirovic, I. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4505 · Cited by 799 · see citing works
Self-citationRNA G-quadruplexes cause eIF4A-dependent oncogene translation in cancer
Wolfe, A. L., Singh, K., Zhong, Y., Drewe, P., Rajasekhar, V. K., Sanghvi, V. R., Mavrakis, K. J., Jiang, M., Roderick, J. E., Van der Meulen, J., et al. (2014) · Nature · doi:10.1038/nature13485 · Cited by 635 · see citing works
Self-citationSvitkin, Y. V., Pause, A., Haghighat, A., Pyronnet, S., Witherell, G. W., Belsham, G. J., & Sonenberg, N. (2001) · RNA · doi:10.1017/s135583820100108x · Cited by 477 · see citing works
eIF4F is a nexus of resistance to anti-BRAF and anti-MEK cancer therapies
Boussemart, L., Malka-Mahieu, H., Girault, I., Allard, D., Hemmingsson, O., Tomasic, G., Thomas, M., Basmadjian, C., Ribeiro, N., Thuaud, F., et al. (2014) · Nature · doi:10.1038/nature13572 · Cited by 373 · see citing works
Bordeleau, M.-È., Robert, F., Gerard, B., Lindqvist, L., Chen, S. M. H., Wendel, H., Brem, B., Greger, H., Lowe, S. W., Porco, J. A. J., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34753 · Cited by 335 · see citing works
Self-citationRocaglates convert DEAD-box protein eIF4A into a sequence-selective translational repressor
Iwasaki, S., Floor, S. N., & Ingolia, N. T. (2016) · Nature · doi:10.1038/nature17978 · Cited by 304 · see citing works
eIF4A: The godfather of the DEAD box helicases
Rogers, G. W., Komar, A. A., & Merrick, W. C. (2002) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(02)72073-4 · Cited by 274 · see citing works
The Organizing Principles of Eukaryotic Ribosome Recruitment
Pelletier, J., & Sonenberg, N. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111042 · Cited by 261 · see citing works
Self-citationNielsen, P. J., & Trachsel, H. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb03049.x · Cited by 237 · see citing works
Bordeleau, M.-È., Matthews, J., Wojnar, J. M., Lindqvist, L., Novac, O., Jankowsky, E., Sonenberg, N., Northcote, P. T., Teesdale‐Spittle, P. H., & Pelletier, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504249102 · Cited by 229 · see citing works
Self-citationThe ATP-dependent interaction of eukaryotic initiation factors with mRNA.
Abramson, R. D., Dever, T. E., Lawson, T. G., Ray, B. K., Thach, R. E., & Merrick, W. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61430-9 · Cited by 208 · see citing works
The Translation Inhibitor Rocaglamide Targets a Bimolecular Cavity between eIF4A and Polypurine RNA
Iwasaki, S., Iwasaki, W., Takahashi, M., Sakamoto, A., Watanabe, C., Shichino, Y., Floor, S. N., Fujiwara, K., Mito, M., Dodo, K., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.11.026 · Cited by 193 · see citing works
King, M., Chiang, C. M., Ling, H.-C., Fujita, E., Ochiai, M., & McPhail, A. T. (1982) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c39820001150 · Cited by 187 · see citing works
Inhibitors of protein synthesis identified by a high throughput multiplexed translation screen
Novac, O. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh235 · Cited by 141 · see citing works
The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges with eIF-4A.
Yoder-Hill, J., Pause, A., Sonenberg, N., & Merrick, W. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53358-5 · Cited by 140 · see citing works
Rocaglamide, silvestrol and structurally related bioactive compounds from Aglaia species
Li, P., Woodard, J. L., Lucas, D. M., Fuchs, J. R., & Kinghorn, A. D. (2014) · Natural Product Reports · doi:10.1039/c4np00006d · Cited by 133 · see citing works
A cellular response linking eIF4AI activity to eIF4AII transcription
Galicia-Vázquez, G., Cencic, R., Robert, F., Agenor, A., & Pelletier, J. (2012) · RNA · doi:10.1261/rna.033209.112 · Cited by 119 · see citing works
Self-citationChu, J., Galicia-Vázquez, G., Cencic, R., Mills, J. R., Katigbak, A., Porco, J. A. J., & Pelletier, J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.005 · Cited by 100 · see citing works
Self-citationRodrigo, C. M., Cencic, R., Roche, S. P., Pelletier, J., & Porco, J. A. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201263k · Cited by 99 · see citing works
Self-citationEbada, S. S., Lajkiewicz, N. J., Porco, J. A. J., Li‐Weber, M., & Proksch, P. (2011) · Fortschritte der Chemie Organischer Naturstoffe/Fortschritte der Chemie organischer Naturstoffe/Progress in the chemistry of organic natural products · doi:10.1007/978-3-7091-0748-5_1 · Cited by 92 · see citing works
Self-citationA helicase-independent activity of eIF4A in promoting mRNA recruitment to the human ribosome
Sokabe, M., & Fraser, C. S. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620426114 · Cited by 91 · see citing works
Roche, S. P., Cencic, R., Pelletier, J., & Porco, J. A. J. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201003212 · Cited by 76 · see citing works
Self-citationTranslation initiation factor eIF4F modifies the dexamethasone response in multiple myeloma
Robert, F., Roman, W., Bramoullé, A., Fellmann, C., Roulston, A., Shustik, C., Porco, J. A., Shore, G. C., Sebag, M., & Pelletier, J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402650111 · Cited by 64 · see citing works
Self-citationChen, Z., Qi, J.-J., Wu, Q., Lu, J., Liu, Z., Wang, Y., Hu, P., Li, T., Lin, J., Wu, X., et al. (2019) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-019-1178-z · Cited by 63 · see citing works
Recent advances in the biology and chemistry of the flavaglines
Ribeiro, N., Thuaud, F., Nebigil, C. G., & Désaubry, L. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.10.048 · Cited by 58 · see citing works
Tecle, H., Shao, J., Li, Y., Kothe, M., Kazmirski, S. L., Penzotti, J. E., Ding, Y., Ohren, J. F., Moshinsky, D., Coli, R., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.10.108 · Cited by 45 · see citing works
Zhao, Q., Abou‐Hamdan, H., & Désaubry, L. (2016) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201600437 · Cited by 36 · see citing works
Zhang, W., Chu, J., Cyr, A. M., Yueh, H., Brown, L. E., Wang, T. T., Pelletier, J., & Porco, J. A. J. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06446 · Cited by 33 · see citing works
Self-citation
Flagged first, then by citations
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Sorted by citations
Cellular functions of eukaryotic RNA helicases and their links to human diseases
Bohnsack, K. E., Yi, S., Venus, S., Jankowsky, E., & Bohnsack, M. T. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00628-5 · Cited by 131 · see citing works
Dual targeting of DDX3 and eIF4A by the translation inhibitor rocaglamide A
Chen, M., Asanuma, M., Takahashi, M., Shichino, Y., Mito, M., Fujiwara, K., Saito, H., Floor, S. N., Ingolia, N. T., Sodeoka, M., et al. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.11.008 · Cited by 90 · see citing works
Mill, C. P., Fiskus, W. C., Dinardo, C. D., Birdwell, C. E., Davis, J. A., Kadia, T. M., Takahashi, K., Short, N. J., Daver, N. G., Ohanian, M. N., et al. (2021) · Blood · doi:10.1182/blood.2021013156 · Cited by 83 · see citing works
Rocaglates Induce Gain-of-Function Alterations to eIF4A and eIF4F
Chu, J., Zhang, W., Cencic, R., O’Connor, P. B. F., Robert, F., Devine, W. G., Selznick, A., Henkel, T. O., Merrick, W. C., Brown, L. E., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.002 · Cited by 74 · see citing works
Self-citationGeneral and Target-Specific DExD/H RNA Helicases in Eukaryotic Translation Initiation
Shen, L. L., & Pelletier, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124402 · Cited by 63 · see citing works
Self-citationExpression and Functional Roles of Eukaryotic Initiation Factor 4A Family Proteins in Human Cancers
Xue, C., Gu, X.-Y., Li, G., Bao, Z., & Li, L.-J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.711965 · Cited by 40 · see citing works
Nebigil, C. G., Moog, C., Vagner, S., Benkirane-Jessel, N., Smith, D. R., & Désaubry, L. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112653 · Cited by 46 · see citing works
RNA-binding proteins in cancer drug discovery
Bertoldo, J. B., Müller, S., & Hüttelmaier, S. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103580 · Cited by 44 · see citing works
Iyer, K. R., Whitesell, L. J., Porco, J. A. J., Henkel, T. O., Brown, L. E., Robbins, N., & Cowen, L. E. (2020) · mBio · doi:10.1128/mbio.03329-19 · Cited by 41 · see citing works
Self-citationNishida, Y., Zhao, R., Heese, L. E., Akiyama, H., Patel, S., Jaeger, A. M., Jacamo, R. O., Kojima, K., Ma, M. C. J., Ruvolo, V. R., et al. (2021) · Leukemia · doi:10.1038/s41375-021-01308-z · Cited by 37 · see citing works
Self-citationSteinberger, J., Shen, L. L., Kiniry, S. J., Naineni, S. K., Cencic, R., Amiri, M., Aboushawareb, S. A. E., Chu, J., Maïga, R. I., Yachnin, B. J., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa662 · Cited by 39 · see citing works
Self-citationTaroncher‐Oldenburg, G., Müller, C., Obermann, W., Ziebuhr, J., Hartmann, R. K., & Grünweller, A. (2021) · Microorganisms · doi:10.3390/microorganisms9030540 · Cited by 38 · see citing works
Wilmore, S., Rogers-Broadway, K.-R., Taylor, J., Lemm, E., Fell, R., Stevenson, F., Forconi, F., Steele, A., Coldwell, M. J., Packham, G., et al. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03910-x · Cited by 29 · see citing works
Fooks, K., Galicia-Vázquez, G., Gife, V., Schcolnik-Cabrera, A., Nouhi, Z., Poon, W. W. L., Luo, V. M., Rys, R., Aloyz, R., Orthwein, A., et al. (2022) · Journal of experimental & clinical cancer research : CR · doi:10.1186/s13046-022-02542-8 · Cited by 23 · see citing works
Greger, H. (2021) · Phytochemistry Reviews · doi:10.1007/s11101-021-09761-5 · Cited by 33 · see citing works
Gupta, I., & Gaykalova, D. A. (2024) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2024.08.004 · Cited by 31 · see citing works
Howard, C. M., Estrada, M. D., Terrero, D., Tiwari, A. K., & Raman, D. (2020) · Cancers · doi:10.3390/cancers12082169 · Cited by 31 · see citing works
Inhibitors of Eukaryotic Translational Machinery as Therapeutic Agents
Fan, A. P., & Sharp, P. P. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01746 · Cited by 29 · see citing works
Ho, J. J. D., Cunningham, T. A., Manara, P., Coughlin, C. A., Arumov, A., Roberts, E. R., Osteen, A., Kumar, P., Bilbao, D., Krieger, J. R., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109806 · Cited by 27 · see citing works
Cencic, R., Im, Y. K., Naineni, S. K., Moustafa-Kamal, M., Jovanovic, P., Sabourin, V., Annis, M. G., Robert, F., Schmeing, T. M., Koromilas, A. E., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318093121 · Cited by 27 · see citing works
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Kayastha, F. B., Herrington, N. B., Kapadia, B. B., Roychowdhury, A., Nanaji, N. M., Kellogg, G. E., & Gartenhaus, R. B. (2022) · Molecular Medicine · doi:10.1186/s10020-022-00534-0 · Cited by 23 · see citing works
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Li, S., Chen, J., Li, X., bai, X., & Shi, D. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115781 · Cited by 22 · see citing works
Herzog, L.-O., Walters, B., Buono, R., Lee, J. S., Mallya, S., Fung, A., Chiu, H., Nguyen, N., Li, B., Pinkerton, A. B., et al. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-01205-9 · Cited by 21 · see citing works
A parasitic fungus employs mutated eIF4A to survive on rocaglate-synthesizing Aglaia plants
Chen, M., Kumakura, N., Saito, H., Muller, R. Y., Nishimoto, M., Mito, M., Gan, P., Ingolia, N. T., Shirasu, K., Ito, T., et al. (2023) · eLife · doi:10.7554/elife.81302 · Cited by 21 · see citing works
Obermann, W., Friedrich, A., Madhugiri, R., Klemm, P., Mengel, J. P., Hain, T., Pleschka, S., Wendel, H., Hartmann, R. K., Schiffmann, S., et al. (2022) · Viruses · doi:10.3390/v14030519 · Cited by 19 · see citing works
Pesce, E., Miluzio, A., Turcano, L., Minici, C., Cirino, D., Calamita, P., Manfrini, N., Oliveto, S., Ricciardi, S., Grifantini, R., et al. (2020) · Cells · doi:10.3390/cells9010172 · Cited by 18 · see citing works
Ribosome Biogenesis and Function in Cancer: From Mechanisms to Therapy
Gitareja, K., Chelliah, S. S., Sanij, E., Sandhu, S. K., Kang, J., & Khot, A. S. (2025) · Cancers · doi:10.3390/cancers17152534 · Cited by 18 · see citing works
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Lizardo, M. M., Hughes, C. S., Huang, Y. Z., Shyp, T., Delaidelli, A., Zhang, H., Shaool, S. S., Renner, A. F., Burwag, F., Sayles, L. C., et al. (2024) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-24-1317 · Cited by 18 · see citing works
Victoria, C., Schulz, G., Klöhn, M., Weber, S., Holicki, C. M., Brüggemann, Y., Becker, M., Gerold, G., Eiden, M., Groschup, M. H., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01357 · Cited by 15 · see citing works
Eukaryotic Translation Initiation Factor 4AI: A Potential Novel Target in Neuroblastoma
Skofler, C., Kleinegger, F., Krassnig, S., Birkl-Toeglhofer, A. M., Singer, G., Till, H., Benesch, M., Cencic, R., Porco, J. A. J., Pelletier, J., et al. (2021) · Cells · doi:10.3390/cells10020301 · Cited by 15 · see citing works
Self-citationSaito, H., Handa, Y., Chen, M., Schneider‐Poetsch, T., Shichino, Y., Takahashi, M., Romo, D., Yoshida, M., Fürstner, A., Ito, T., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51635-9 · Cited by 14 · see citing works
Boyer, J. A., Rosen, E. Y., Sharma, M., Dorso, M. A., Mai, N., Amor, C., Reiter, J., Kannan, R., Gadal, S., Xu, J., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2424286122 · Cited by 14 · see citing works
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Cai, Z., Ma, H., Ye, F., Lei, D., Deng, Z., Li, Y., Gu, R., & Wen, H. (2025) · MedComm · doi:10.1002/mco2.70342 · Cited by 14 · see citing works
Compounds for selective translational inhibition
Shichino, Y., & Iwasaki, S. (2022) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2022.102158 · Cited by 13 · see citing works
Praditya, D., Klöhn, M., Brüggemann, Y., Brown, L. E., Porco, J. A. J., Zhang, W., Kinast, V., Kirschning, A., Vondran, F. W. R., Tödt, D., et al. (2022) · Antiviral Research · doi:10.1016/j.antiviral.2022.105359 · Cited by 13 · see citing works
Self-citationProtein–RNA interactions mediated by silvestrol—insight into a unique molecular clamp
Naineni, S. K., Bhatt, G., Jiramongkolsiri, E., Robert, F., Cencic, R., Huang, S., Nagar, B., & Pelletier, J. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae824 · Cited by 12 · see citing works
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Naineni, S. K., Cencic, R., Robert, F., Brown, L. E., Haque, M., Scott-Talib, J., Sénéchal, P., Schmeing, T. M., Porco, J. A. J., & Pelletier, J. (2023) · RNA · doi:10.1261/rna.079318.122 · Cited by 11 · see citing works
Self-citationDiscovery of an eIF4A Inhibitor with a Novel Mechanism of Action
Zerio, C. J., Cunningham, T. A., Tulino, A. S., Alimusa, E. A., Buckley, T. M., Moore, K. T., Dodson, M. B., Wilson, N. C., Ambrose, A. J., Shi, T., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01014 · Cited by 11 · see citing works
Cao, Y., He, Y., Yang, L., & Luan, Z. (2020) · Oncology Reports · doi:10.3892/or.2020.7856 · Cited by 10 · see citing works
Schiffmann, S., Henke, M., Seifert, M., Ulshöfer, T., Roser, L. A., Magari, F., Wendel, H., Grünweller, A., & Parnham, M. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24065872 · Cited by 10 · see citing works
Oblinger, J. L., Wang, J., Wetherell, G. D., Agarwal, G., Wilson, T. A., Benson, N., Fenger, J. M., Fuchs, J. R., Kinghorn, A. D., & Chang, L. (2024) · Scientific Reports · doi:10.1038/s41598-024-69171-3 · Cited by 9 · see citing works
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Wang, Z., Thakare, R., Chitale, S., Mishra, A., Goldstein, S. I., Fan, A. C., Li, R., Zhu, L. J., Brown, L. E., Cencic, R., et al. (2024) · ACS Central Science · doi:10.1021/acscentsci.4c01073 · Cited by 7 · see citing works
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Webb, T. E., Davies, M., Maher, J. F., & Sarker, D. (2020) · Clinical and Translational Radiation Oncology · doi:10.1016/j.ctro.2020.07.002 · Cited by 7 · see citing works
DiVita, D. J., & Kearse, M. G. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.03.014 · Cited by 7 · see citing works
Grindheim, A., Patil, S. S., Nebigil, C., Désaubry, L., & Vedeler, A. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094941 · Cited by 6 · see citing works
Sieber‐Frank, J., Stark, H., Kalteis, S., Prigge, E., Köhler, R. M., Andresen, C., Henkel, T. O., Casari, G., Schubert, T., Fischl, W., et al. (2021) · Cancer Medicine · doi:10.1002/cam4.4212 · Cited by 4 · see citing works
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Goldstein, S. I., Fan, A. C., Wang, Z., Naineni, S. K., Cencic, R., Garcia-Gutierrez, S. B., Patel, K., Huang, S., Brown, L. E., Emili, A., et al. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.4c01129 · Cited by 5 · see citing works
Self-citationKeiser, P. T., Zhang, W., Ricca, M., Wacquiez, A., Grimins, A. O., Cencic, R., Patten, J. J., Shah, P., Padilha, E. C., Connor, J. H., et al. (2024) · Antiviral Research · doi:10.1016/j.antiviral.2024.105976 · Cited by 4 · see citing works
Self-citationEukaryotic translation initiation factor 4A1 in the pathogenesis and treatment of cancers
Huang, J., Zhang, L., Yang, R. X., Yao, L., Gou, J., Cao, D., Pan, Z., Li, D., Pan, Y., & Zhang, W. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1289650 · Cited by 4 · see citing works
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Thirman, H. L., Hayes, M., Geben, L. C., Ihrie, R. A., Brown, L. E., Porco, J. A. J., & Irish, J. M. (2025) · Communications Biology · doi:10.1038/s42003-025-08545-3 · Cited by 3 · see citing works
Self-citationVo, D.-K. H., Engler, A., Stoimenovski, D., Hartig, R., Kaehne, T., Kalinski, T., Naumann, M., Haybaeck, J., & Naß, N. (2021) · Cancers · doi:10.3390/cancers13061293 · Cited by 3 · see citing works
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Conley, J. F., Brown, L. E., McNeely, J. H., Pelletier, J., Porco, J. A. J., & Allen, K. N. (2025) · ACS Omega · doi:10.1021/acsomega.4c09421 · Cited by 2 · see citing works
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Mi, W., Cigliano, A., Galleri, G., Gigante, I., Steinmann, S. M., Cibali, E., Serra, M., Pes, G. M., Schlösser, D., Pizzuto, E., et al. (2025) · JHEP Reports · doi:10.1016/j.jhepr.2025.101416 · Cited by 2 · see citing works
Broad-acting antivirals: the pursuit of pan-viral therapeutics in the era of pandemics
Олеговна, Б. Е., Kostyushev, D. S., Tikhonov, A., Chulanov, V. P., & Gordeychuk, I. V. (2026) · Journal of Virology · doi:10.1128/jvi.00077-26 · Cited by 2 · see citing works
eIF4A1 is essential for reprogramming the translational landscape of Wnt-driven colorectal cancersPreprint
Waldron, J. A., Kanellos, G., Smith, R. C. L., Knight, J. R. P., Munro, J., Alexandrou, C., Vlahov, N., Pardo, L., Moore, M. H., Gillen, S. L., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.10.566546 · Cited by 2 · see citing works
Zhao, J.-G., Liu, T., Jiao, Y., Du, Z., Fu, B., Zhang, W.-J., Fan, Z., Qin, Y., Fan, Z., Wang, J.-H., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c06480 · Cited by 1 · see citing works
Self-citationPaediatric therapeutic development workshop on osteosarcoma
Baxter, J. S., Montiel-Equihua, C., Molenaar, J. J., Berlanga, P., Bishop, M. W., Blanc, P., Campbell-Hewson, Q., Casanova, M., Cortés‐Ciriano, I., Crompton, B. D., et al. (2026) · British Journal of Cancer · doi:10.1038/s41416-026-03572-1 · Cited by 1 · see citing works
A specific eIF4A paralog facilitates LARP1-mediated translation repression during mTORC1 inhibitionPreprint
Shichino, Y., Mito, M., Kashiwagi, K., Takahashi, M., Ito, T., Ingolia, N. T., & Iwasaki, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.18.460932 · Cited by 1 · see citing works
New Rocaglate Derivatives Tip the Scale against Brain Tumors
Iwasaki, S. (2024) · ACS Central Science · doi:10.1021/acscentsci.4c01524 · Cited by 1 · see citing works
Programmable translational inhibition by a molecular glue-oligonucleotide conjugatePreprint
Wang, S., Kovalski, J. R., Belinchón, F. J. Z., Bennett, M., Kuzuoğlu‐Öztürk, D., Li, Q., Stevenson, E. J., Liu, J., Krogan, N. J., Ott, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.15.664547 · Cited by 1 · see citing works
Targeting eIF4A-dependent translation in genetically complex sarcoma
Kim, Y.-M., Mohan, P., Sehrawat, U., Seffar, E., De Queiroz, R. M., Chadalavada, K., Persaud, N., Okada, T., Kulkarni, A., Lin, J., et al. (2026) · JCI Insight · doi:10.1172/jci.insight.192936
Fooks, K., Galicia-Vázquez, G., Schcolnik‐Cabrera, A., Gife, V., Nouhi, Z., Poon, W. W. L., Luo, V. M., Aloyz, R. S., Orthwein, A., Hulea, L., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1696855/v1
Saito, H., Handa, Y., Chen, M., Schneider‐Poetsch, T., Shichino, Y., Takahashi, M., Romo, D., Yoshida, M., Fürstner, A., Ito, T., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.21.558742
Santos, D., Christopoulou, V., Taning, C. N. T., Avgeris, S. N., Papadopoulou, A., Kletsas, D., Voutsinas, G. E., Labropoulou, V., & Swevers, L. (2025) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.70028
Fooks, K., Galicia-Vázquez, G., Gife, V., Schcolnik‐Cabrera, A., Nouhi, Z., Poon, W. W. L., Luo, V. M., Rys, R. N., Aloyz, R. S., Orthwein, A., et al. (2023) · Figshare · doi:10.6084/m9.figshare.22614635
Identification and optimization of first-in-class RNA helicase inhibitors of DDX1, LGP2, and MDA5
Wang, X., Wang, F., Kong, D., Uredi, D., Li, F., Li, F., Rayadurgam, J., Li, H., Wolf, E., Chan, U. H., et al. (2026) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2026.118724
Ren, X., Shan, W., Salman, M., Ren, J., Gao, X., & Liu, X. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118060
SARS-CoV-2 3CL protease interaction with host factors – identifying novel drug targets
Sanyal, D., & Chaubey, B. (2026) · Archives of Virology · doi:10.1007/s00705-026-06667-5
Schcolnik‐Cabrera, A., Takdenti, M., Nejad, A. S. H., Nouhi, Z., St-Amand, S., Capdevielle, C., Issa, D., Riaud, M., Rose, A. A. N., Khacho, M., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.03.749206
Halting translation by the letter with sequence-selective small molecules
Schneider‐Poetsch, T., Yoshida, M., Ito, T., & Iwasaki, S. (2026) · Nature Chemical Biology · doi:10.1038/s41589-026-02318-7
BindingDB Entry 50018392: Inhibitors of Eukaryotic Translational Machinery as Therapeutic Agents.
BindingDB (2024) · UC San Diego · doi:10.7270/q2t43z96
BindingDB Entry 50018671: Discovery of an eIF4A Inhibitor with a Novel Mechanism of Action.
BindingDB (2024) · UC San Diego · doi:10.7270/q22j6h3k
Manara, P., & Schatz, J. H. (2026) · Current Oncology Reports · doi:10.1007/s11912-026-01848-6
- Authors
- Chu, J., Zhang, W., Cencic, R., Devine, W. G., Beglov, D., Henkel, T., Brown, L. E., Vajda, S., Porco, J. A., & Pelletier, J.
- Affiliations
- McGill University (CA)
- Boston University (US)
- Institut du cancer Rosalind & Morris Goodman (CA)
- Corresponding author
- Porco, John A.
- Pelletier, Jerry
- ORCID
- Venue
- Cell Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2019-11
- Volume
- 26
- Issue
- 11
- Pages
- 1586-1593.e3
- ISSN
- 2451-9448 (ISSN-L)
- 2451-9456
- PMC
- PMC6874763
- OpenAlex
- W2973112770
- Cited by
- 74
- References
- 29
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 12 · 2023: 12 · 2022: 6 · 2021: 13 · 2020: 11
- FWCI
- 2.46
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell chemical biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- OpenBU (Boston University) (submittedVersion)
- Funders
- National Institutes of Health (R35 GM-118173, R01 GM-067041, R24 GM-111625, R35 GM-118078)
- Canadian Institutes of Health Research (FDN- 148366)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- rocaglates, RNA helicase, eukaryotic translation initiation, anticancer drug design
- MeSH terms
- Amidines, Animals, Antineoplastic Agents, Benzofurans, Cell Survival, Female, Humans, Lymphoma, Mice, Inbred C57BL, Recombinant Proteins, Ribosomes, RNA, Structure-Activity Relationship, Protein Biosynthesis, Drug Design, Eukaryotic Initiation Factor-4A, Mice, DEAD-box RNA Helicases
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