Small molecule inhibition of RNA binding proteins in haematologic cancer

References

• Korobeynikov VA, Lyashchenko AK, Blanco-Redondo B, et al. Antisense oligonucleotide silencing of FUS expression as a therapeutic approach in amyotrophic lateral sclerosis. Nat Med. 2022;28(1): 104–16. doi: 10.1038/s41591-021-01615-z
   PubMed Web of Science ®Google Scholar
• Nussbacher JK, Tabet R, Yeo GW, et al. Disruption of RNA metabolism in neurological diseases and emerging therapeutic interventions. Neuron. 2019;102(2): 294–320. doi: 10.1016/j.neuron.2019.03.014
   PubMed Web of Science ®Google Scholar
• Cramer P. Multisubunit RNA polymerases. Curr Opin Struct Biol. 2002;12(1): 89–97. doi: 10.1016/S0959-440X(02)00294-4
   PubMed Web of Science ®Google Scholar
• Matera AG, Wang Z. A day in the life of the spliceosome. Nat Rev Mol Cell Biol. 2014;15(2): 108–21. doi: 10.1038/nrm3742
   PubMed Web of Science ®Google Scholar
• Herzel L, Ottoz DSM, Alpert T, et al. Splicing and transcription touch base: co-transcriptional spliceosome assembly and function. Nat Rev Mol Cell Biol. 2017;18(10): 637–50. doi: 10.1038/nrm.2017.63
   PubMed Web of Science ®Google Scholar
• Rodríguez-Molina JB, Turtola M. Birth of a poly(A) tail: mechanisms and control of mRNA polyadenylation. FEBS Open Bio. 2023;13(7): 1140–53. doi: 10.1002/2211-5463.13528
   PubMed Web of Science ®Google Scholar
• Ranji A, Boris-Lawrie K. RNA helicases: emerging roles in viral replication and the host innate response. RNA Biol. 2010;7(6): 775–87. doi: 10.4161/rna.7.6.14249
   PubMed Web of Science ®Google Scholar
• Wiener D, Schwartz S. The epitranscriptome beyond m6A. Nat Rev Genet. 2021;22(2): 119–31. doi: 10.1038/s41576-020-00295-8
   PubMed Web of Science ®Google Scholar
• Zaccara S, Ries RJ, Jaffrey SR. Reading, writing and erasing mRNA methylation. Nat Rev Mol Cell Biol. 2019;20(10): 608–24. doi: 10.1038/s41580-019-0168-5
   PubMed Web of Science ®Google Scholar
• Kadumuri RV, Janga SC. Epitranscriptomic Code and its alterations in human disease. Trends Mol Med. 2018;24(10): 886–903. doi: 10.1016/j.molmed.2018.07.010
   PubMed Web of Science ®Google Scholar
• Choi PS, Thomas-Tikhonenko A. RNA-binding proteins of COSMIC importance in cancer. J Clin Investig. 2021;131(18): 131. doi: 10.1172/JCI151627
   Web of Science ®Google Scholar
• Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell. 2011;144(5): 646–74. doi: 10.1016/j.cell.2011.02.013
   PubMed Web of Science ®Google Scholar
• Chen S, Benbarche S, Abdel-Wahab O. Splicing factor mutations in hematologic malignancies. Blood. 2021;138(8): 599–612. doi: 10.1182/blood.2019004260
   PubMed Web of Science ®Google Scholar
• Obeng EA, Chappell RJ, Seiler M, et al. Physiologic expression of Sf3b1(K700E) causes impaired erythropoiesis, aberrant splicing, and sensitivity to therapeutic spliceosome modulation. Cancer Cell. 2016;30: 404–417. doi: 10.1016/j.ccell.2016.08.006
   PubMed Web of Science ®Google Scholar
• Kim E, Ilagan JO, Liang Y, et al. SRSF2 mutations contribute to myelodysplasia by mutant-specific effects on exon recognition. Cancer Cell. 2015;27: 617–630. doi: 10.1016/j.ccell.2015.04.006
   PubMed Web of Science ®Google Scholar
• Weng H, Huang H, Wu H, et al. METTL14 inhibits hematopoietic stem/progenitor differentiation and promotes leukemogenesis via mRNA m(6)A modification. Cell Stem Cell. 2018;22: 191–205.e9. doi: 10.1016/j.stem.2017.11.016
   PubMed Web of Science ®Google Scholar
• Li Z, Weng H, Su R, et al. FTO plays an oncogenic role in acute myeloid leukemia as a N(6)-methyladenosine RNA demethylase. Cancer Cell. 2017;31: 127–141. doi: 10.1016/j.ccell.2016.11.017
   PubMed Web of Science ®Google Scholar
• Paris J, Morgan M, Campos J, et al. Targeting the RNA m(6)A Reader YTHDF2 selectively compromises cancer stem cells in acute myeloid leukemia. Cell Stem Cell. 2019;25: 137–48.e6. doi: 10.1016/j.stem.2019.03.021
   PubMed Web of Science ®Google Scholar
• Weng H, Huang F, Yu Z, et al. The m(6)A reader IGF2BP2 regulates glutamine metabolism and represents a therapeutic target in acute myeloid leukemia. Cancer Cell. 2022;40: 1566–82.e10. doi: 10.1016/j.ccell.2022.10.004
   PubMed Web of Science ®Google Scholar
• Zhou J, Bi C, Ching YQ, et al. Inhibition of LIN28B impairs leukemia cell growth and metabolism in acute myeloid leukemia. J Hematol Oncol. 2017;10: 138. doi: 10.1186/s13045-017-0507-y
   PubMed Web of Science ®Google Scholar
• Ishimaru D, Ramalingam S, Sengupta TK, et al. Regulation of bcl-2 expression by HuR in HL60 leukemia cells and A431 carcinoma cells. Mol Cancer Res. 2009;7(8): 1354. doi: 10.1158/1541-7786.MCR-08-0476
   PubMed Web of Science ®Google Scholar
• Kim HH, Kuwano Y, Srikantan S, et al. HuR recruits let-7/RISC to repress c-myc expression. Genes Dev. 2009;23(15): 1743–8. doi: 10.1101/gad.1812509
   PubMed Web of Science ®Google Scholar
• Topisirovic I, Siddiqui N, Orolicki S, et al. Stability of eukaryotic translation initiation factor 4E mRNA is regulated by HuR, and this activity is dysregulated in cancer. Mol Cell Biol. 2009;29(5): 1152–62. doi: 10.1128/MCB.01532-08
   PubMed Web of Science ®Google Scholar
• Ishimaru D, Zuraw L, Ramalingam S, et al. Mechanism of regulation of bcl-2 mRNA by nucleolin and A+U-rich element-binding factor 1 (AUF1). J Biol Chem. 2010;285(35): 27182–91. doi: 10.1074/jbc.M109.098830
   PubMed Web of Science ®Google Scholar
• Ennajdaoui H, Howard Jonathan M, Sterne-Weiler T, et al. IGF2BP3 modulates the interaction of invasion-associated transcripts with RISC. Cell Rep. 2016;15: 1876–1883. doi: 10.1016/j.celrep.2016.04.083
   PubMed Web of Science ®Google Scholar
• Palanichamy JK, Tran TM, Howard JM, et al. RNA-binding protein IGF2BP3 targeting of oncogenic transcripts promotes hematopoietic progenitor proliferation. J Clin Invest. 2016;126(4): 1495–511. doi: 10.1172/JCI80046
   PubMed Web of Science ®Google Scholar
• Tran TM, Philipp J, Bassi JS, et al. The RNA-binding protein IGF2BP3 is critical for MLL-AF4-mediated leukemogenesis. Leukemia. 2022;36(1): 68–79. doi: 10.1038/s41375-021-01346-7
   PubMed Web of Science ®Google Scholar
• Okuda H, Miyamoto R, Takahashi S, et al. RNA-binding proteins of KHDRBS and IGF2BP families control the oncogenic activity of MLL-AF4. Nat Commun. 2022;13(1): 6688. doi: 10.1038/s41467-022-34558-1
   PubMed Web of Science ®Google Scholar
• De Benedetti A, Graff JR. eIF-4E expression and its role in malignancies and metastases. Oncogene. 2004;23(18): 3189–99. doi: 10.1038/sj.onc.1207545
   PubMed Web of Science ®Google Scholar
• Song P, Yang F, Jin H, et al. The regulation of protein translation and its implications for cancer. Sig Transduct Target Ther. 2021;6: 68. doi: 10.1038/s41392-020-00444-9
   PubMed Web of Science ®Google Scholar
• Fabbri L, Chakraborty A, Robert C, et al. The plasticity of mRNA translation during cancer progression and therapy resistance. Nat Rev Cancer. 2021;21(9): 558–77. doi: 10.1038/s41568-021-00380-y
   PubMed Web of Science ®Google Scholar
• Lee LJ, Papadopoli D, Jewer M, et al. Cancer plasticity: the role of mRNA translation. Trends Cancer. 2021;7(2): 134–45. doi: 10.1016/j.trecan.2020.09.005
   PubMed Web of Science ®Google Scholar
• Gerstberger S, Hafner M, Tuschl T. A census of human RNA-binding proteins. Nat Rev Genet. 2014;15(12): 829–45. doi: 10.1038/nrg3813
   PubMed Web of Science ®Google Scholar
• Bertoldo JB, Müller S, Hüttelmaier S. RNA-binding proteins in cancer drug discovery. Drug Discovery Today. 2023;28(6): 103580. doi: 10.1016/j.drudis.2023.103580
   PubMed Web of Science ®Google Scholar
• Mohibi S, Chen X, Zhang J. Cancer the‘RBP’eutics–rNA-binding proteins as therapeutic targets for cancer. Pharmacol Ther. 2019;203: 107390. doi: 10.1016/j.pharmthera.2019.07.001
   PubMed Web of Science ®Google Scholar
• Hong S. RNA binding protein as an emerging therapeutic target for cancer prevention and treatment. J Cancer Prev. 2017;22(4): 203–10. doi: 10.15430/JCP.2017.22.4.203
   PubMedGoogle Scholar
• Gebauer F, Schwarzl T, Valcárcel J, et al. RNA-binding proteins in human genetic disease. Nat Rev Genet. 2021;22(3): 185–98. doi: 10.1038/s41576-020-00302-y
   PubMed Web of Science ®Google Scholar
• Schneider T, Hung L-H, Aziz M, et al. Combinatorial recognition of clustered RNA elements by the multidomain RNA-binding protein IMP3. Nat Commun. 2019;10(1): 2266. doi: 10.1038/s41467-019-09769-8
   PubMedGoogle Scholar
• Tian H, Ip L, Luo H, et al. A high throughput drug screen based on fluorescence resonance energy transfer (FRET) for anticancer activity of compounds from herbal medicine. Br J Pharmacol. 2007;150(3): 321–34. doi: 10.1038/sj.bjp.0706988
   PubMed Web of Science ®Google Scholar
• Rogers MS, Cryan LM, Habeshian KA, et al. A FRET-based high throughput screening assay to identify inhibitors of anthrax protective antigen binding to capillary morphogenesis gene 2 protein. PloS One. 2012;7(6): e39911. doi: 10.1371/journal.pone.0039911
   PubMed Web of Science ®Google Scholar
• Lim D, Byun WG, Koo JY, et al. Discovery of a small-molecule inhibitor of protein-MicroRNA interaction using binding assay with a site-specifically labeled Lin28. J Am Chem Soc. 2016;138: 13630–13638. doi: 10.1021/jacs.6b06965
   PubMed Web of Science ®Google Scholar
• Hall MD, Yasgar A, Peryea T, et al. Fluorescence polarization assays in high-throughput screening and drug discovery: a review. Methods Appl Fluoresc. 2016;4(2): 022001. doi: 10.1088/2050-6120/4/2/022001
   PubMed Web of Science ®Google Scholar
• Borgelt L, Li F, Hommen P, et al. Trisubstituted pyrrolinones as small-molecule inhibitors disrupting the protein-RNA interaction of LIN28 and let-7. ACS Med Chem Lett. 2021;12: 893–898. doi: 10.1021/acsmedchemlett.0c00546
   PubMed Web of Science ®Google Scholar
• Baker JD, Uhrich RL, Strovas TJ, et al. Targeting pathological tau by small molecule inhibition of the Poly(A): MSUT2 RNA-Protein interaction. ACS Chem Neurosci. 2020;11: 2277–2285. doi: 10.1021/acschemneuro.0c00214
   PubMed Web of Science ®Google Scholar
• Palacino J, Swalley SE, Song C, et al. SMN2 splice modulators enhance U1–pre-mRNA association and rescue SMA mice. Nat Chem Biol. 2015;11: 511–517. doi: 10.1038/nchembio.1837
   PubMed Web of Science ®Google Scholar
• Best MD. Click chemistry and bioorthogonal reactions: unprecedented selectivity in the labeling of biological molecules. Biochemistry. 2009;48(28): 6571–84. doi: 10.1021/bi9007726
   PubMed Web of Science ®Google Scholar
• Lorenz DA, Kaur T, Kerk SA, et al. Expansion of cat-ELCCA for the discovery of small molecule inhibitors of the pre-let-7-Lin28 RNA-Protein interaction. ACS Med Chem Lett. 2018;9: 517–521. doi: 10.1021/acsmedchemlett.8b00126
   PubMed Web of Science ®Google Scholar
• Bonnal SC, López-Oreja I, Valcárcel J. Roles and mechanisms of alternative splicing in cancer — implications for care. Nat Rev Clin Oncol. 2020;17(8): 457–74. doi: 10.1038/s41571-020-0350-x
   PubMed Web of Science ®Google Scholar
• Hershberger CE, Moyer DC, Adema V, et al. Complex landscape of alternative splicing in myeloid neoplasms. Leukemia. 2021;35(4): 1108–20. doi: 10.1038/s41375-020-1002-y
   PubMed Web of Science ®Google Scholar
• Seiler M, Peng S, Agrawal AA, et al. Somatic mutational landscape of splicing factor genes and their functional consequences across 33 cancer types. Cell Rep. 2018;23(1): 282–96.e4. doi: 10.1016/j.celrep.2018.01.088
   PubMed Web of Science ®Google Scholar
• Zhou Z, Gong Q, Wang Y, et al. The biological function and clinical significance of SF3B1 mutations in cancer. Biomark Res. 2020;8(1): 38. doi: 10.1186/s40364-020-00220-5
   PubMed Web of Science ®Google Scholar
• Folco EG, Coil KE, Reed R. The anti-tumor drug E7107 reveals an essential role for SF3b in remodeling U2 snRNP to expose the branch point-binding region. Genes Dev. 2011;25(5): 440–4. doi: 10.1101/gad.2009411
   PubMed Web of Science ®Google Scholar
• Kotake Y, Sagane K, Owa T, et al. Splicing factor SF3b as a target of the antitumor natural product pladienolide. Nat Chem Biol. 2007;3(9): 570–5. doi: 10.1038/nchembio.2007.16
   PubMed Web of Science ®Google Scholar
• Kaida D, Motoyoshi H, Tashiro E, et al. Spliceostatin a targets SF3b and inhibits both splicing and nuclear retention of pre-mRNA. Nat Chem Biol. 2007;3(9): 576–83. doi: 10.1038/nchembio.2007.18
   PubMed Web of Science ®Google Scholar
• Shi Y, Bray W, Smith AJ, et al. An exon skipping screen identifies antitumor drugs that are potent modulators of pre-mRNA splicing, suggesting new therapeutic applications. PloS One. 2020;15(5): e0233672. doi: 10.1371/journal.pone.0233672
   PubMed Web of Science ®Google Scholar
• Eskens FA, Ramos FJ, Burger H, et al. Phase I pharmacokinetic and pharmacodynamic study of the first-in-class spliceosome inhibitor E7107 in patients with advanced solid tumors. Clin Cancer Res. 2013;19: 6296–6304. doi: 10.1158/1078-0432.CCR-13-0485
   PubMed Web of Science ®Google Scholar
• Seiler M, Yoshimi A, Darman R, et al. H3B-8800, an orally available small-molecule splicing modulator, induces lethality in spliceosome-mutant cancers. Nature Med. 2018;24(4): 497–504. doi: 10.1038/nm.4493
   PubMed Web of Science ®Google Scholar
• Steensma DP, Wermke M, Klimek VM, et al. Phase I first-in-human dose escalation study of the oral SF3B1 modulator H3B-8800 in myeloid neoplasms. Leukemia. 2021;35(12): 3542–50. doi: 10.1038/s41375-021-01328-9
   PubMed Web of Science ®Google Scholar
• Lazear MR, Remsberg JR, Jaeger MG, et al. Proteomic discovery of chemical probes that perturb protein complexes in human cells. Molecular Cell. 2023;83: 1725–42.e12. doi: 10.1016/j.molcel.2023.03.026
   PubMed Web of Science ®Google Scholar
• Sidarovich A, Will CL, Anokhina MM, et al. Identification of a small molecule inhibitor that stalls splicing at an early step of spliceosome activation. Elife. 2017;6: e23533. doi: 10.7554/eLife.23533
   PubMed Web of Science ®Google Scholar
• Wang E, Lu SX, Pastore A, et al. Targeting an RNA-Binding Protein Network in acute myeloid leukemia. Cancer Cell. 2019;35(3): 369–84.e7. doi: 10.1016/j.ccell.2019.01.010
   PubMed Web of Science ®Google Scholar
• Han T, Goralski M, Gaskill N, et al. Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15. Science. 2017;356. doi: 10.1126/science.aal3755
   Web of Science ®Google Scholar
• Ozawa Y, Sugi NH, Nagasu T, et al. E7070, a novel sulphonamide agent with potent antitumour activity in vitro and in vivo. Eur J Cancer. 2001;37(17): 2275–82. doi: 10.1016/S0959-8049(01)00275-1
   PubMed Web of Science ®Google Scholar
• Pogacar Z, Groot K, Jochems F, et al. Genetic and compound screens uncover factors modulating cancer cell response to indisulam. Life Sci Alliance. 2022;5(9): e202101348. doi: 10.26508/lsa.202101348
   PubMed Web of Science ®Google Scholar
• Ledoux S, Guthrie C. Retinitis Pigmentosa mutations in bad response to refrigeration 2 (Brr2) impair ATPase and helicase activity. J Biol Chem. 2016;291(23): 11954–65. doi: 10.1074/jbc.M115.710848
   PubMed Web of Science ®Google Scholar
• Ito M, Iwatani M, Yamamoto T, et al. Discovery of spiro[indole-3,2’-pyrrolidin]-2(1H)-one based inhibitors targeting Brr2, a core component of the U5 snRNP. Bioorg Med Chem. 2017;25: 4753–4767. doi: 10.1016/j.bmc.2017.07.017
   PubMedGoogle Scholar
• Kathman SG, Koo SJ, Lindsey GL, et al. Remodeling oncogenic transcriptomes by small molecules targeting NONO. Nat Chem Biol. 2023;19(7): 825–36. doi: 10.1038/s41589-023-01270-0
   PubMed Web of Science ®Google Scholar
• Zhang X, Wu C, Xiong W, et al. Knockdown of p54nrb inhibits migration, invasion and TNF-α release of human acute monocytic leukemia THP1 cells. Oncol Rep. 2016;35(6): 3742–8. doi: 10.3892/or.2016.4756
   PubMed Web of Science ®Google Scholar
• Zhang F, Sun J, Tang X, et al. Stabilization of SAMHD1 by NONO is crucial for ara-C resistance in AML. Cell Death Dis. 2022;13(7): 590. doi: 10.1038/s41419-022-05023-0
   PubMed Web of Science ®Google Scholar
• Vu LP, Pickering BF, Cheng Y, et al. The N(6)-methyladenosine (m(6)A)-forming enzyme METTL3 controls myeloid differentiation of normal hematopoietic and leukemia cells. Nat Med. 2017;23: 1369–1376. doi: 10.1038/nm.4416
   PubMed Web of Science ®Google Scholar
• Vu LP, Cheng Y, Kharas MG. The biology of m(6)A RNA methylation in normal and malignant hematopoiesis. Cancer Discovery. 2019;9: 25–33. doi: 10.1158/2159-8290.CD-18-0959
   PubMed Web of Science ®Google Scholar
• Yankova E, Blackaby W, Albertella M, et al. Small-molecule inhibition of METTL3 as a strategy against myeloid leukaemia. Nature. 2021;593(7860): 597–601. doi: 10.1038/s41586-021-03536-w
   PubMed Web of Science ®Google Scholar
• Fiorentino F, Menna M, Rotili D, et al. METTL3 from target validation to the first Small-molecule inhibitors: a medicinal chemistry journey. J Med Chem. 2023;66(3): 1654–77. doi: 10.1021/acs.jmedchem.2c01601
   PubMed Web of Science ®Google Scholar
• Shen C, Sheng Y, Zhu AC, et al. RNA demethylase ALKBH5 selectively promotes tumorigenesis and cancer stem cell self-renewal in acute myeloid leukemia. Cell Stem Cell. 2020;27(1): 64–80.e9. doi: 10.1016/j.stem.2020.04.009
   PubMed Web of Science ®Google Scholar
• Sabnis RW. Novel small molecule RNA m6A demethylase AlkBH5 inhibitors for treating cancer. ACS Med Chem Lett. 2021;12(6): 856–7. doi: 10.1021/acsmedchemlett.1c00102
   PubMedGoogle Scholar
• Su R, Dong L, Li Y, et al. Targeting FTO suppresses cancer stem Cell maintenance and immune evasion. Cancer Cell. 2020;38(1): 79–96.e11. doi: 10.1016/j.ccell.2020.04.017
   PubMed Web of Science ®Google Scholar
• Chari A, Vogl DT, Gavriatopoulou M, et al. Oral selinexor-dexamethasone for triple-class refractory multiple myeloma. N Engl J Med. 2019;381: 727–738. doi: 10.1056/NEJMoa1903455
   PubMed Web of Science ®Google Scholar
• Kashyap T, Argueta C, Aboukameel A, et al. Selinexor, a selective inhibitor of nuclear export (SINE) compound, acts through NF-κB deactivation and combines with proteasome inhibitors to synergistically induce tumor cell death. Oncotarget. 2016;7(48): 78883–95. doi: 10.18632/oncotarget.12428
   PubMedGoogle Scholar
• Aitken MJL, Malaney P, Zhang X, et al. Heterogeneous nuclear ribonucleoprotein K is overexpressed in acute myeloid leukemia and causes myeloproliferation in mice via altered Runx1 splicing. NAR Cancer. 2022;4: zcac039. doi: 10.1093/narcan/zcac039
   PubMedGoogle Scholar
• Shu B, Zeng P, Kang S, et al. Syntheses and evaluation of new quinoline derivatives for inhibition of hnRNP K in regulating oncogene c-myc transcription. Bioorg Chem. 2019;85: 1–17. doi: 10.1016/j.bioorg.2018.12.020
   PubMed Web of Science ®Google Scholar
• Roundtree IA, Luo GZ, Zhang Z, et al. YTHDC1 mediates nuclear export of N(6)-methyladenosine methylated mRnas. Elife. 2017;6: 6. doi: 10.7554/eLife.31311
   Web of Science ®Google Scholar
• Yang S, Zhang H, Li Y, et al. Discovery of a selective YTHDC1 inhibitor that targets acute myeloid leukemia. Res Square. 2023. doi: 10.21203/rs.3.rs-2644364/v1
   Google Scholar
• Viswanathan SR, Powers JT, Einhorn W, et al. Lin28 promotes transformation and is associated with advanced human malignancies. Nature Genet. 2009;41(7): 843–8. doi: 10.1038/ng.392
   PubMed Web of Science ®Google Scholar
• Xu B, Zhang K, Huang Y. Lin28 modulates cell growth and associates with a subset of cell cycle regulator mRnas in mouse embryonic stem cells. RNA. 2009;15(3): 357–61. doi: 10.1261/rna.1368009
   PubMed Web of Science ®Google Scholar
• Yuan J, Nguyen CK, Liu X, et al. Lin28b reprograms adult bone marrow hematopoietic progenitors to mediate Fetal-Like Lymphopoiesis. Science. 2012;335: 1195. doi: 10.1126/science.1216557
   PubMed Web of Science ®Google Scholar
• Wang S, Chim B, Su Y, et al. Enhancement of LIN28B-induced hematopoietic reprogramming by IGF2BP3. Genes Dev. 2019;33(15–16): 1048–68. doi: 10.1101/gad.325100.119
   PubMed Web of Science ®Google Scholar
• Wang L, Rowe RG, Jaimes A, et al. Small-molecule inhibitors disrupt let-7 oligouridylation and release the selective blockade of let-7 processing by LIN28. Cell Rep. 2018;23(10): 3091–101. doi: 10.1016/j.celrep.2018.04.116
   PubMed Web of Science ®Google Scholar
• Roos M, Pradère U, Ngondo RP, et al. A Small-molecule inhibitor of Lin28. ACS Chem Biol. 2016;11(10): 2773–81. doi: 10.1021/acschembio.6b00232
   PubMed Web of Science ®Google Scholar
• Byun WG, Lim D, Park SB. Discovery of small-molecule modulators of protein-RNA interactions by fluorescence intensity-based binding assay. Chembiochem. 2020;21: 818–824. doi: 10.1002/cbic.201900467
   PubMed Web of Science ®Google Scholar
• Yu X, Li Z. The role of TARBP2 in the development and progression of cancers. Tumour Biol. 2016;37: 57–60. doi: 10.1007/s13277-015-4273-6
   PubMedGoogle Scholar
• Peng T, He Y, Wang T, et al. Discovery of a Novel Small-Molecule Inhibitor Disrupting TRBP-Dicer Interaction against Hepatocellular Carcinoma via the Modulation of microRNA Biogenesis. J Med Chem. 2022;65: 11010–11033. doi: 10.1021/acs.jmedchem.2c00189
   PubMedGoogle Scholar
• Huang H, Weng H, Sun W, et al. Recognition of RNA N(6)-methyladenosine by IGF2BP proteins enhances mRNA stability and translation. Nat Cell Biol. 2018;20: 285–295. doi: 10.1038/s41556-018-0045-z
   PubMed Web of Science ®Google Scholar
• Müller S, Bley N, Glaß M, et al. IGF2BP1 enhances an aggressive tumor cell phenotype by impairing miRNA-directed downregulation of oncogenic factors. Nucleic Acids Res. 2018;46(12): 6285–303. doi: 10.1093/nar/gky229
   PubMed Web of Science ®Google Scholar
• Huttelmaier S, Zenklusen D, Lederer M, et al. Spatial regulation of beta-actin translation by src-dependent phosphorylation of ZBP1. Nature. 2005;438: 512–515. doi: 10.1038/nature04115
   PubMed Web of Science ®Google Scholar
• Bell JL, Wachter K, Muhleck B, et al. Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs): post-transcriptional drivers of cancer progression? Cell Mol Life Sci. 2013;70(15): 2657–75. doi: 10.1007/s00018-012-1186-z
   PubMed Web of Science ®Google Scholar
• Mahapatra L, Andruska N, Mao C, et al. A novel IMP1 inhibitor, BTYNB, targets c-myc and inhibits melanoma and ovarian cancer Cell proliferation. Transl Oncol. 2017;10(5): 818–27. doi: 10.1016/j.tranon.2017.07.008
   PubMed Web of Science ®Google Scholar
• Wallis N, Oberman F, Shurrush K, et al. Small molecule inhibitor of Igf2bp1 represses Kras and a pro-oncogenic phenotype in cancer cells. RNA Biol. 2022;19(1): 26–43. doi: 10.1080/15476286.2021.2010983
   PubMed Web of Science ®Google Scholar
• Müller S, Bley N, Busch B, et al. The oncofetal RNA-binding protein IGF2BP1 is a druggable, post-transcriptional super-enhancer of E2F-driven gene expression in cancer. Nucleic Acids Res. 2020;48(15): 8576–90. doi: 10.1093/nar/gkaa653
   PubMed Web of Science ®Google Scholar
• Feng P, Chen D, Wang X, et al. Inhibition of the m6A reader IGF2BP2 as a strategy against T-cell acute lymphoblastic leukemia. Leukemia. 2022;36(9): 2180–8. doi: 10.1038/s41375-022-01651-9
   PubMed Web of Science ®Google Scholar
• Dahlem C, Abuhaliema A, Kessler SM, et al. First small-molecule inhibitors targeting the RNA-Binding protein IGF2BP2/IMP2 for cancer therapy. ACS Chem Biol. 2022;17(2): 361–75. doi: 10.1021/acschembio.1c00833
   PubMed Web of Science ®Google Scholar
• Li M, Zhang L, Ge C, et al. An isocorydine derivative (d-ICD) inhibits drug resistance by downregulating IGF2BP3 expression in hepatocellular carcinoma. Oncotarget. 2015;6(28): 25149–60. doi: 10.18632/oncotarget.4438
   PubMedGoogle Scholar
• Wang X, Zhao BS, Roundtree IA, et al. N(6)-methyladenosine modulates Messenger RNA translation efficiency. Cell. 2015;161: 1388–1399. doi: 10.1016/j.cell.2015.05.014
   PubMed Web of Science ®Google Scholar
• Micaelli M, Dalle Vedove A, Cerofolini L, et al. Small-molecule ebselen binds to YTHDF proteins interfering with the Recognition of N (6)-methyladenosine-modified RNAs. ACS Pharmacol Transl Sci. 2022;5: 872–891. doi: 10.1021/acsptsci.2c00008
   PubMedGoogle Scholar
• Prieto C, Kharas MG. RNA regulators in leukemia and lymphoma. Cold Spring Harb Perspect Med. 2020;10: 10. doi: 10.1101/cshperspect.a034967
   Web of Science ®Google Scholar
• Glorian V, Maillot G, Polès S, et al. HuR-dependent loading of miRNA RISC to the mRNA encoding the Ras-related small GTPase RhoB controls its translation during UV-induced apoptosis. Cell Death Diff. 2011;18(11): 1692–701. doi: 10.1038/cdd.2011.35
   PubMed Web of Science ®Google Scholar
• Meisner NC, Hintersteiner M, Mueller K, et al. Identification and mechanistic characterization of low-molecular-weight inhibitors for HuR. Nat Chem Biol. 2007;3(8): 508–15. doi: 10.1038/nchembio.2007.14
   PubMed Web of Science ®Google Scholar
• Wu X, Ramesh R, Wang J, et al. Small molecules targeting the RNA-Binding protein HuR inhibit tumor growth in xenografts. J Med Chem. 2023;66(3): 2032–53. doi: 10.1021/acs.jmedchem.2c01723
   PubMedGoogle Scholar
• Chellappan R, Guha A, Si Y, et al. SRI-42127, a novel small molecule inhibitor of the RNA regulator HuR, potently attenuates glial activation in a model of lipopolysaccharide-induced neuroinflammation. Glia. 2022;70(1): 155–72. doi: 10.1002/glia.24094
   PubMed Web of Science ®Google Scholar
• Ishii T, Hayakawa H, Sekiguchi T, et al. Role of Auf1 in elimination of oxidatively damaged messenger RNA in human cells. Free Radic Biol Med. 2015;79: 109–16. doi: 10.1016/j.freeradbiomed.2014.11.018
   PubMed Web of Science ®Google Scholar
• Li KT, Wu XZ, Sun ZY, et al. A novel strategy for regulating mRNA’s degradation via interfering the AUF1’s binding to mRNA. Molecules. 2022;27: 27. doi: 10.3390/molecules27103182
   Web of Science ®Google Scholar
• Wolfe AL, Singh K, Zhong Y, et al. RNA G-quadruplexes cause eIF4A-dependent oncogene translation in cancer. Nature. 2014;513(7516): 65–70. doi: 10.1038/nature13485
   PubMed Web of Science ®Google Scholar
• Xue C, Gu X, Li G, et al. Expression and functional roles of eukaryotic initiation factor 4A family proteins in human cancers. Front Cell Dev Biol. 2021;9: 711965. doi: 10.3389/fcell.2021.711965
   PubMed Web of Science ®Google Scholar
• Bordeleau ME, Mori A, Oberer M, et al. Functional characterization of IRESes by an inhibitor of the RNA helicase eIF4A. Nat Chem Biol. 2006;2(4): 213–20. doi: 10.1038/nchembio776
   PubMed Web of Science ®Google Scholar
• Moerke NJ, Aktas H, Chen H, et al. Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G. Cell. 2007;128(2): 257–67. doi: 10.1016/j.cell.2006.11.046
   PubMed Web of Science ®Google Scholar
• Wan X, Yang T, Cuesta A, et al. Discovery of lysine-targeted eIF4E inhibitors through covalent docking. J Am Chem Soc. 2020;142(11): 4960–4. doi: 10.1021/jacs.9b10377
   PubMed Web of Science ®Google Scholar
• Kaur T, Menon A, Garner AL. Synthesis of 7-benzylguanosine cap-analogue conjugates for eIF4E targeted degradation. Eur J Med Chem. 2019;166: 339–50. doi: 10.1016/j.ejmech.2019.01.080
   PubMed Web of Science ®Google Scholar
• Lucchesi CA, Zhang J, Gao M, et al. Identification of a first-in-class small-molecule inhibitor of the EIF4E-RBM38 complex that enhances wild-type TP53 protein translation for tumor growth suppression. Mol Cancer Ther. 2023;22(6): 726–36. doi: 10.1158/1535-7163.MCT-22-0627
   PubMed Web of Science ®Google Scholar
• Crowther-Swanepoel D, Broderick P, Di Bernardo MC, et al. Common variants at 2q37.3, 8q24.21, 15q21.3 and 16q24.1 influence chronic lymphocytic leukemia risk. Nat Genet. 2010;42(2): 132–6. doi: 10.1038/ng.510
   PubMed Web of Science ®Google Scholar
• Tyagi A, Kolluru V, Chandrasekaran B, et al. ASR488, a novel small molecule, activates an mRNA binding protein, CPEB1, and inhibits the growth of bladder cancer. Oncol Lett. 2020;20(1): 850–60. doi: 10.3892/ol.2020.11593
   PubMed Web of Science ®Google Scholar
• Han L, Huang C, Wang X, et al. The RNA-binding protein GRSF1 promotes hepatocarcinogenesis via competitively binding to YY1 mRNA with miR-30e-5p. J Exp Clin Cancer Res. 2022;41(1): 17. doi: 10.1186/s13046-021-02217-w
   PubMed Web of Science ®Google Scholar
• Tan Y, Sun X, Xu Y, et al. Small molecule targeting CELF1 RNA-binding activity to control HSC activation and liver fibrosis. Nucleic Acids Res. 2022;50(5): 2440–51. doi: 10.1093/nar/gkac139
   PubMed Web of Science ®Google Scholar
• Sakamoto KM, Kim KB, Kumagai A, et al. Protacs: chimeric molecules that target proteins to the Skp1-cullin-F box complex for ubiquitination and degradation. Proc Natl Acad Sci USA. 2001;98: 8554–8559. doi: 10.1073/pnas.141230798
   PubMed Web of Science ®Google Scholar
• Chirnomas D, Hornberger KR, Crews CM. Protein degraders enter the clinic — a new approach to cancer therapy. Nat Rev Clin Oncol. 2023;20(4): 265–78. doi: 10.1038/s41571-023-00736-3
   PubMed Web of Science ®Google Scholar
• Gama-Brambila RA, Chen J, Zhou J, et al. A PROTAC targets splicing factor 3B1. Cell Chem Biol. 2021;28(11): 1616–27.e8. doi: 10.1016/j.chembiol.2021.04.018
   PubMed Web of Science ®Google Scholar
• Ghidini A, Cléry A, Halloy F, et al. RNA-PROTACs: degraders of RNA-Binding proteins. Angew Chem Int Ed Engl. 2021;60: 3163–3169. doi: 10.1002/anie.202012330
   PubMed Web of Science ®Google Scholar
• Costales MG, Matsumoto Y, Velagapudi SP, et al. Small Molecule Targeted Recruitment of a Nuclease to RNA. J Am Chem Soc. 2018;140(22): 6741–4. doi: 10.1021/jacs.8b01233
   PubMed Web of Science ®Google Scholar
• Tong Y, Lee Y, Liu X, et al. Programming inactive RNA-binding small molecules into bioactive degraders. Nature. 2023;618(7963): 169–79. doi: 10.1038/s41586-023-06091-8
   PubMedGoogle Scholar
• Gourisankar S, Krokhotin A, Ji W, et al. Rewiring cancer drivers to activate apoptosis. Nature. 2023;620(7973): 417–25. doi: 10.1038/s41586-023-06348-2
   PubMed Web of Science ®Google Scholar