Therapeutic targeting of splicing in cancer

Comprehensive molecular profiling of lung adenocarcinoma

The Cancer Genome Atlas Research Network (2014) · Nature · doi:10.1038/nature13385 · Cited by 5,732

Alternative isoform regulation in human tissue transcriptomes

Wang, E. T., Sandberg, R., Luo, S., Khrebtukova, I., Zhang, L., Mayr, C., Kingsmore, S. F., Schroth, G. P., & Burge, C. B. (2008) · Nature · doi:10.1038/nature07509 · Cited by 5,181

Comprehensive genomic characterization of squamous cell lung cancers

The Cancer Genome Atlas Research Network (2012) · Nature · doi:10.1038/nature11404 · Cited by 3,994

Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing

Pan, Q., Shai, O., Lee, L. J., Frey, B. J., & Blencowe, B. J. (2008) · Nature Genetics · doi:10.1038/ng.259 · Cited by 3,951

The Spliceosome: Design Principles of a Dynamic RNP Machine

Wahl, M. C., Will, C. L., & Lührmann, R. (2009) · Cell · doi:10.1016/j.cell.2009.02.009 · Cited by 2,665

Frequent pathway mutations of splicing machinery in myelodysplasia

Yoshida, K., Sanada, M., Shiraishi, Y., Nowak, D., Nagata, Y., Yamamoto, R., Sato, Y., Sato-Otsubo, A., Kon, A., Nagasaki, M., et al. (2011) · Nature · doi:10.1038/nature10496 · Cited by 2,029

Mapping the Hallmarks of Lung Adenocarcinoma with Massively Parallel Sequencing

Imielinski, M., Berger, A. H., Hammerman, P. S., Hernandez, B., Pugh, T. J., Hodis, E., Cho, J., Suh, J., Capelletti, M., Sivachenko, A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.08.029 · Cited by 1,789

RAF inhibitor resistance is mediated by dimerization of aberrantly spliced BRAF(V600E)

Poulikakos, P. I., Persaud, Y., Janakiraman, M., Kong, X., Ng, C., Moriceau, G., Shi, H., Atefi, M., Titz, B., Gabay, M. T., et al. (2011) · Nature · doi:10.1038/nature10662 · Cited by 1,454

Convergence of Acquired Mutations and Alternative Splicing of CD19 Enables Resistance to CART-19 Immunotherapy

Sotillo, E., Barrett, D. M., Black, K. L., Bagashev, A., Oldridge, D., Wu, G., Sussman, R., Lanauze, C., Ruella, M., Gazzara, M. R., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-1020 · Cited by 1,254

Somatic SF3B1 Mutation in Myelodysplasia with Ring Sideroblasts

Papaemmanuil, E., Cazzola, M., Boultwood, J., Malcovati, L., Vyas, P., Bowen, D., Pellagatti, A., Wainscoat, J. S., Hellstrom-Lindberg, E., Gambacorti-Passerini, C., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1103283 · Cited by 1,222

HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer

David, C. J., Chen, M., Assanah, M., Canoll, P., & Manley, J. L. (2010) · Nature · doi:10.1038/nature08697 · Cited by 1,179

RNA therapeutics: beyond RNA interference and antisense oligonucleotides

Kole, R., Krainer, A. R., & Altman, S. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3625 · Cited by 1,152

Splicing regulation: From a parts list of regulatory elements to an integrated splicing code

Wang, Z., & Burge, C. B. (2008) · RNA · doi:10.1261/rna.876308 · Cited by 1,086

Protein arginine methyltransferases and cancer

Yang, Y., & Bedford, M. T. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3409 · Cited by 1,083

SF3B1 and Other Novel Cancer Genes in Chronic Lymphocytic Leukemia

Wang, L., Lawrence, M. S., Wan, Y., Stojanov, P., Sougnez, C., Stevenson, K., Werner, L., Sivachenko, A., DeLuca, D. S., Zhang, L., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1109016 · Cited by 1,080

A day in the life of the spliceosome

Matera, A. G., & Wang, Z. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3742 · Cited by 1,074

Context-dependent control of alternative splicing by RNA-binding proteins

Fu, X.-D., & Ares, M. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3778 · Cited by 1,044

Exome sequencing identifies recurrent mutations of the splicing factor SF3B1 gene in chronic lymphocytic leukemia

Quesada, V., Conde, L., Villamor, N., Ordóñez, G. R., Jares, P., Bassaganyas, L., Ramsay, A. J., Beà, S., Pinyol, M., Martínez-Trillos, A., et al. (2012) · Nature Genetics · doi:10.1038/ng.1032 · Cited by 996

The gene encoding the splicing factor SF2/ASF is a proto-oncogene

Karni, R., de Stanchina, E., Lowe, S. W., Sinha, R., Mu, D., & Krainer, A. R. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1209 · Cited by 934

Exon skipping and dystrophin restoration in patients with Duchenne muscular dystrophy after systemic phosphorodiamidate morpholino oligomer treatment: an open-label, phase 2, dose-escalation study

Cirak, S., Arechavala-Gomeza, V., Guglieri, M., Feng, L., Torelli, S., Anthony, K., Abbs, S., Garralda, M. E., Bourke, J., Wells, D. J., et al. (2011) · The Lancet · doi:10.1016/s0140-6736(11)60756-3 · Cited by 878

Non-coding recurrent mutations in chronic lymphocytic leukaemia

Puente, X. S., Beà, S., Valdés-Mas, R., Villamor, N., Gutiérrez-Abril, J., Martín-Subero, J. I., Munar, M., Rubio-Pérez, C., Jares, P., Aymerich, M., et al. (2015) · Nature · doi:10.1038/nature14666 · Cited by 829

MTAP deletion confers enhanced dependency on the PRMT5 arginine methyltransferase in cancer cells

Kryukov, G. V., Wilson, F. H., Ruth, J. R., Paulk, J., Tsherniak, A., Marlow, S. E., Vazquez, F., Weir, B. A., Fitzgerald, M. E., Tanaka, M., et al. (2016) · Science · doi:10.1126/science.aad5214 · Cited by 688

RNA splicing factors as oncoproteins and tumour suppressors

Dvinge, H., Kim, E., Abdel-Wahab, O., & Bradley, R. K. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.51 · Cited by 687

Splicing factor SF3b as a target of the antitumor natural product pladienolide

Kotake, Y., Sagane, K., Owa, T., Mimori-Kiyosue, Y., Shimizu, H., Uesugi, M., Ishihama, Y., Iwata, M., & Mizui, Y. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.16 · Cited by 657

Spliceostatin A targets SF3b and inhibits both splicing and nuclear retention of pre-mRNA

Kaida, D., Motoyoshi, H., Tashiro, E., Nojima, T., Hagiwara, M., Ishigami, K., Watanabe, H., Kitahara, T., Yoshida, T., Nakajima, H., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.18 · Cited by 650

Disordered methionine metabolism in MTAP/CDKN2A-deleted cancers leads to dependence on PRMT5

Mavrakis, K. J., McDonald, E. R., Schlabach, M. R., Billy, E., Hoffman, G. R., deWeck, A., Ruddy, D. A., Venkatesan, K., Yu, J., McAllister, G., et al. (2016) · Science · doi:10.1126/science.aad5944 · Cited by 607

The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution.

Colwill, K., Pawson, T., Andrews, B., Prasad, J., Manley, J. L., Bell, J. C., & Duncan, P. I. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00357.x · Cited by 580

Recurrent mutations in the U2AF1 splicing factor in myelodysplastic syndromes

Graubert, T. A., Shen, D., Ding, L., Okeyo-Owuor, T., Lunn, C. L., Shao, J., Krysiak, K., Harris, C. C., Koboldt, D. C., Larson, D. E., et al. (2012) · Nature Genetics · doi:10.1038/ng.1031 · Cited by 580

SRSF2 Mutations Contribute to Myelodysplasia by Mutant-Specific Effects on Exon Recognition

Kim, E., Ilagan, J. O., Liang, Y., Daubner, G. M., Lee, S. C.-W., Ramakrishnan, A., Li, Y., Chung, Y. R., Micol, J.-B., Murphy, M. E., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.04.006 · Cited by 575

Response to MET Inhibitors in Patients with Stage IV Lung Adenocarcinomas Harboring MET Mutations Causing Exon 14 Skipping

Paik, P. K., Drilon, A., Fan, P.-D., Yu, H., Rekhtman, N., Ginsberg, M. S., Borsu, L., Schultz, N., Berger, M. F., Rudin, C. M., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-1467 · Cited by 575

Antisense Masking of an hnRNP A1/A2 Intronic Splicing Silencer Corrects SMN2 Splicing in Transgenic Mice

Hua, Y., Vickers, T. A., Okunola, H. L., Bennett, C. F., & Krainer, A. R. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.01.014 · Cited by 574

A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models

Chan-Penebre, E., Kuplast, K. G., Majer, C. R., Boriack-Sjodin, P. A., Wigle, T. J., Johnston, L. D., Rioux, N., Munchhof, M. J., Jin, L., Jacques, S. L., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1810 · Cited by 569

Synonymous Mutations Frequently Act as Driver Mutations in Human Cancers

Supek, F., Miñana, B., Valcárcel, J., Gabaldón, T., & Lehner, B. (2014) · Cell · doi:10.1016/j.cell.2014.01.051 · Cited by 557

Non-coding recurrent mutations in chronic lymphocytic leukaemia

Puente, X. S., Beà, S., Valdés-Mas, R., Villamor, N., Gutiérrez-Abril, J., Martín-Subero, J. I., Munar, M., Rubio-Pérez, C., Jares, P., Aymerich, M., et al. (2016) · Nature · doi:10.1038/nature18910 · Cited by 546

Exome sequencing identifies recurrent somatic mutations in EIF1AX and SF3B1 in uveal melanoma with disomy 3

Martin, M., Maßhöfer, L., Temming, P., Rahmann, S., Metz, C., Bornfeld, N., van de Nes, J., Klein-Hitpass, L., Hinnebusch, A. G., Horsthemke, B., et al. (2013) · Nature Genetics · doi:10.1038/ng.2674 · Cited by 542

Recurrent mutations at codon 625 of the splicing factor SF3B1 in uveal melanoma

Harbour, J. W., Roberson, E. D. O., Anbunathan, H., Onken, M. D., Worley, L. A., & Bowcock, A. M. (2013) · Nature Genetics · doi:10.1038/ng.2523 · Cited by 516

The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond

Stopa, N., Krebs, J. E., & Shechter, D. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1847-9 · Cited by 513

Rescue of Dystrophic Muscle Through U7 snRNA-Mediated Exon Skipping

Goyenvalle, A., Vulin, A., Fougerousse, F., Leturcq, F., Kaplan, J.-C., Garcia, L., & Danos, O. (2004) · Science · doi:10.1126/science.1104297 · Cited by 506

The spliceosome is a therapeutic vulnerability in MYC-driven cancer

Hsu, T. Y.-T., Simon, L. M., Neill, N. J., Marcotte, R., Sayad, A., Bland, C. S., Echeverria, G. V., Sun, T., Kurley, S. J., Tyagi, S., et al. (2015) · Nature · doi:10.1038/nature14985 · Cited by 492

Somatic Mutations Lead to an Oncogenic Deletion of Met in Lung Cancer

Kong-Beltran, M., Seshagiri, S., Zha, J., Zhu, W., Bhawe, K., Mendoza, N., Holcomb, T., Pujara, K., Stinson, J., Fu, L., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2749 · Cited by 490

Regulation of splicing by SR proteins and SR protein-specific kinases

Zhou, Z., & Fu, X.-D. (2013) · Chromosoma · doi:10.1007/s00412-013-0407-z · Cited by 478

c-MET mutational analysis in small cell lung cancer: novel juxtamembrane domain mutations regulating cytoskeletal functions.

Ma, P. C., Kijima, T., Maulik, G., Fox, E. A., Sattler, M., Griffin, J. D., Johnson, B. E., & Salgia, R. (2003) · PubMed · Cited by 454

Cancer-Associated SF3B1 Hotspot Mutations Induce Cryptic 3′ Splice Site Selection through Use of a Different Branch Point

Darman, R. B., Seiler, M., Agrawal, A. A., Lim, K. H., Peng, S., Aird, D., Bailey, S. L., Bhavsar, E. B., Chan, B., Colla, S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.053 · Cited by 453

The splicing factor SRSF1 regulates apoptosis and proliferation to promote mammary epithelial cell transformation

Anczuków, O., Rosenberg, A. Z., Akerman, M., Das, S., Zhan, L., Karni, R., Muthuswamy, S. K., & Krainer, A. R. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2207 · Cited by 447

The SR protein family

Shepard, P. J., & Hertel, K. J. (2009) · Genome Biology · doi:10.1186/gb-2009-10-10-242 · Cited by 416

The spliceosome as a target of novel antitumour drugs

Bonnal, S., Vigevani, L., & Valcárcel, J. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3823 · Cited by 405

Functional amounts of dystrophin produced by skipping the mutated exon in the mdx dystrophic mouse

Lu, Q. L., Mann, C. J., Lou, F., Bou-Gharios, G., Morris, G. E., Xue, S.-A., Fletcher, S., Partridge, T. A., & Wilton, S. D. (2003) · Nature Medicine · doi:10.1038/nm897 · Cited by 398

Evolution of SR protein and hnRNP splicing regulatory factors

Busch, A., & Hertel, K. J. (2012) · WIREs RNA · doi:10.1002/wrna.100 · Cited by 394

Cancer-associated SF3B1 mutations affect alternative splicing by promoting alternative branchpoint usage

Alsafadi, S., Houy, A., Battistella, A., Popova, T., Wassef, M., Henry, E., Tirode, F., Constantinou, A., Piperno-Neumann, S., Roman-Roman, S., et al. (2016) · Nature Communications · doi:10.1038/ncomms10615 · Cited by 386

MYC regulates the core pre-mRNA splicing machinery as an essential step in lymphomagenesis

Koh, C. M., Bezzi, M., Low, D. H. P., Ang, W. X., Teo, S. X., Gay, F. P. H., Al-Haddawi, M., Tan, S. Y., Osato, M., Sabò, A., et al. (2015) · Nature · doi:10.1038/nature14351 · Cited by 380

SRSF1-Regulated Alternative Splicing in Breast Cancer

Anczuków, O., Akerman, M., Cléry, A., Wu, J., Shen, C., Shirole, N. H., Raimer, A., Sun, S., Jensen, M. A., Hua, Y., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.005 · Cited by 367

Modulation of splicing catalysis for therapeutic targeting of leukemia with mutations in genes encoding spliceosomal proteins

Lee, S. C.-W., Dvinge, H., Kim, E., Cho, H., Micol, J.-B., Chung, Y. R., Durham, B. H., Yoshimi, A., Kim, Y. J., Thomas, M., et al. (2016) · Nature Medicine · doi:10.1038/nm.4097 · Cited by 347

Widespread intron retention diversifies most cancer transcriptomes

Dvinge, H., & Bradley, R. K. (2015) · Genome Medicine · doi:10.1186/s13073-015-0168-9 · Cited by 344

Intron retention is a widespread mechanism of tumor-suppressor inactivation

Jung, H., Lee, D., Lee, J., Park, D., Kim, Y. J., Park, W.-Y., Hong, D., Park, P. J., & Lee, E. (2015) · Nature Genetics · doi:10.1038/ng.3414 · Cited by 339

Structure of a yeast spliceosome at 3.6-angstrom resolution

Yan, C., Hang, J., Wan, R., Huang, M., Wong, C. C. L., & Shi, Y. (2015) · Science · doi:10.1126/science.aac7629 · Cited by 334

Genome-wide Analysis Reveals SR Protein Cooperation and Competition in Regulated Splicing

Pandit, S., Zhou, Y., Shiue, L., Coutinho-Mansfield, G., Li, H., Qiu, J., Huang, J., Yeo, G. W., Ares, M., & Fu, X.-D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.001 · Cited by 321

Manipulation of Alternative Splicing by a Newly Developed Inhibitor of Clks

Muraki, M., Ohkawara, B., Hosoya, T., Onogi, H., Koizumi, J., Koizumi, T., Sumi, K., Yomoda, J.-I., Murray, M. V., Kimura, H., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314298200 · Cited by 308

Misregulation of Pre-mRNA Alternative Splicing in Cancer

Zhang, J., & Manley, J. L. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0253 · Cited by 307

Regulation of constitutive and alternative splicing by PRMT5 reveals a role for Mdm4 pre-mRNA in sensing defects in the spliceosomal machinery

Bezzi, M., Teo, S. X., Muller, J., Mok, W. C., Sahu, S. K., Vardy, L. A., Bonday, Z. Q., & Guccione, E. (2013) · Genes & Development · doi:10.1101/gad.219899.113 · Cited by 300

U2AF1 mutations alter splice site recognition in hematological malignancies

Ilagan, J. O., Ramakrishnan, A., Hayes, B., Murphy, M. E., Zebari, A. S., Bradley, P., & Bradley, R. K. (2015) · Genome Research · doi:10.1101/gr.181016.114 · Cited by 287

Reduced fidelity of branch point recognition and alternative splicing induced by the anti-tumor drug spliceostatin A

Corrionero, A., Miñana, B., & Valcárcel, J. (2011) · Genes & Development · doi:10.1101/gad.2014311 · Cited by 263

Phase I Pharmacokinetic and Pharmacodynamic Study of the First-in-Class Spliceosome Inhibitor E7107 in Patients with Advanced Solid Tumors

Eskens, F. A. L. M., Ramos, F. J., Burger, H., O'Brien, J. P., Piera, A., de Jonge, M. J. A., Mizui, Y., Wiemer, E. A. C., Carreras, M. J., Baselga, J., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0485 · Cited by 259

The architecture of the spliceosomal U4/U6.U5 tri-snRNP

Nguyen, T. H. D., Galej, W. P., Bai, X.-C., Savva, C. G., Newman, A. J., Scheres, S. H. W., & Nagai, K. (2015) · Nature · doi:10.1038/nature14548 · Cited by 238

The Protein Kinase Clk/Sty Directly Modulates SR Protein Activity: Both Hyper- and Hypophosphorylation Inhibit Splicing

Prasad, J., Colwill, K., Pawson, T., & Manley, J. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.6991 · Cited by 235

Disease-associated mutation in SRSF2 misregulates splicing by altering RNA-binding affinities

Zhang, J., Lieu, Y. K., Ali, A. M., Penson, A., Reggio, K. S., Rabadán, R., Raza, A., Mukherjee, S., & Manley, J. L. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514105112 · Cited by 234

A phase I, open-label, single-arm, dose-escalation study of E7107, a precursor messenger ribonucleic acid (pre-mRNA) splicesome inhibitor administered intravenously on days 1 and 8 every 21 days to patients with solid tumors

Hong, D. S., Kurzrock, R., Naing, A., Wheler, J. J., Falchook, G. S., Schiffman, J. S., Faulkner, N., Pilat, M. J., O’Brien, J. P., & LoRusso, P. M. (2013) · Investigational New Drugs · doi:10.1007/s10637-013-0046-5 · Cited by 232

Utilization of host SR protein kinases and RNA-splicing machinery during viral replication

Fukuhara, T., Hosoya, T., Saki, S., Sumi, K., Oshiro, T., Yoshinaka, Y., Suzuki, M., Yamamoto, N., Herzenberg, L. A., Herzenberg, L. A., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604616103 · Cited by 231

New Antitumor Substances, FR901463, FR901464 and FR901465. II. Activities against Experimental Tumors in Mice and Mechanism of Action.

NAKAJIMA, H., HORI, Y., TERANO, H., OKUHARA, M., MANDA, T., MATSUMOTO, S., & SHIMOMURA, K. (1996) · The Journal of Antibiotics · doi:10.7164/antibiotics.49.1204 · Cited by 216

Cryo-EM structure of the yeast U4/U6.U5 tri-snRNP at 3.7 Å resolution

Nguyen, T. H. D., Galej, W. P., Bai, X., Oubridge, C., Newman, A. J., Scheres, S. H. W., & Nagai, K. (2016) · Nature · doi:10.1038/nature16940 · Cited by 215

Transcriptome Sequencing Reveals Potential Mechanism of Cryptic 3’ Splice Site Selection in SF3B1-mutated Cancers

DeBoever, C., Ghia, E. M., Shepard, P. J., Rassenti, L., Barrett, C. L., Jepsen, K., Jamieson, C. H. M., Carson, D., Kipps, T. J., & Frazer, K. A. (2015) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004105 · Cited by 211

Oncogenic Splicing Factor SRSF1 Is a Critical Transcriptional Target of MYC

Das, S., Anczuków, O., Akerman, M., & Krainer, A. R. (2012) · Cell Reports · doi:10.1016/j.celrep.2011.12.001 · Cited by 202

The inhibition of DRB (5,6-dichloro-1-β-d-ribofuranosylbenzimidazole) of hnRNA and mRNA production in HeLa cells

Sehgal, P. B., Darnell Jr., J. E., & Tamm, I. (1976) · Cell · doi:10.1016/0092-8674(76)90092-1 · Cited by 200

Variation in chromatin accessibility in human kidney cancer links H3K36 methyltransferase loss with widespread RNA processing defects

Simon, J. M., Hacker, K. E., Singh, D., Brannon, A. R., Parker, J. S., Weiser, M., Ho, T. H., Kuan, P.-F., Jonasch, E., Furey, T. S., et al. (2014) · Genome Research · doi:10.1101/gr.158253.113 · Cited by 189

Serine-arginine protein kinases: a small protein kinase family with a large cellular presence

Giannakouros, T., Nikolakaki, E., Mylonis, I., & Georgatsou, E. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07987.x · Cited by 188

Pladienolides, New Substances from Culture of Streptomyces platensis Mer-11107 III. In Vitro and In Vivo Antitumor Activities

MIZUI, Y., SAKAI, T., IWATA, M., UENAKA, T., OKAMOTO, K., SHIMIZU, H., YAMORI, T., YOSHIMATSU, K., & ASADA, M. (2004) · The Journal of Antibiotics · doi:10.7164/antibiotics.57.188 · Cited by 185

Biological validation that SF3b is a target of the antitumor macrolide pladienolide

Yokoi, A., Kotake, Y., Takahashi, K., Kadowaki, T., Matsumoto, Y., Minoshima, Y., Sugi, N. H., Sagane, K., Hamaguchi, M., Iwata, M., et al. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08387.x · Cited by 177

New Antitumor Substances, FR901463, FR901464 and FR901465. I. Taxonomy, Fermentation, Isolation, Physico-chemical Properties and Biological Activities.

NAKAJIMA, H., SATO, B., FUJITA, T., TAKASE, S., TERANO, H., & OKUHARA, M. (1996) · The Journal of Antibiotics · doi:10.7164/antibiotics.49.1196 · Cited by 174

Sudemycins, Novel Small Molecule Analogues of FR901464, Induce Alternative Gene Splicing

Fan, L., Lagisetti, C., Edwards, C. C., Webb, T. R., & Potter, P. M. (2011) · ACS Chemical Biology · doi:10.1021/cb100356k · Cited by 167

The anti-tumor drug E7107 reveals an essential role for SF3b in remodeling U2 snRNP to expose the branch point-binding region

Folco, E. G., Coil, K. E., & Reed, R. (2011) · Genes & Development · doi:10.1101/gad.2009411 · Cited by 162

The 3.8 Å structure of the U4/U6.U5 tri-snRNP: Insights into spliceosome assembly and catalysis

Wan, R., Yan, C., Bai, R., Wang, L., Huang, M., Wong, C. C. L., & Shi, Y. (2016) · Science · doi:10.1126/science.aad6466 · Cited by 159

Total Syntheses, Fragmentation Studies, and Antitumor/Antiproliferative Activities of FR901464 and Its Low Picomolar Analogue

Albert, B. J., Sivaramakrishnan, A., Naka, T., Czaicki, N. L., & Koide, K. (2007) · Journal of the American Chemical Society · doi:10.1021/ja067870m · Cited by 157

Identification of recurrent regulated alternative splicing events across human solid tumors

Danan-Gotthold, M., Golan‐Gerstl, R., Eisenberg, E., Meir, K., Karni, R., & Levanon, E. Y. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv210 · Cited by 155

Identification of SAP155 as the Target of GEX1A (Herboxidiene), an Antitumor Natural Product

Hasegawa, M., Miura, T., Kuzuya, K., Inoue, A., Ki, S. W., Horinouchi, S., Yoshida, T., Kunoh, T., Koseki, K., Mino, K., et al. (2010) · ACS Chemical Biology · doi:10.1021/cb100248e · Cited by 153

Splicing factor SRSF6 promotes hyperplasia of sensitized skin

Jensen, M. A., Wilkinson, J. E., & Krainer, A. R. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2756 · Cited by 150

FR901464: Total Synthesis, Proof of Structure, and Evaluation of Synthetic Analogues

Thompson, C. F., Jamison, T. F., & Jacobsen, E. N. (2001) · Journal of the American Chemical Society · doi:10.1021/ja016615t · Cited by 142

Genomics-Guided Discovery of Thailanstatins A, B, and C As Pre-mRNA Splicing Inhibitors and Antiproliferative Agents from Burkholderia thailandensis MSMB43

Liu, X., Biswas, S., Berg, M. G., Antapli, C. M., Xie, F., Wang, Q., Tang, M.-C., Tang, G.-L., Zhang, L., Dreyfuss, G., et al. (2013) · Journal of Natural Products · doi:10.1021/np300913h · Cited by 138

Genome-wide RNAi screens in human brain tumor isolates reveal a novel viability requirement for PHF5APreprint

Hubert, C. G., Bradley, R. K., Ding, Y., Toledo, C. M., Herman, J., Skutt-Kakaria, K., Girard, E. J., Davison, J., Berndt, J. D., Corrin, P. D., et al. (2013) · Genes & Development · doi:10.1101/gad.212548.112 · Cited by 135

Pladienolides, New Substances from Culture of Streptomyces platensis Mer-11107 I. Taxonomy, Fermentation, Isolation and Screening

SAKAI, T., Sameshima, T., Matsufuji, M., Kawamura, N., Dobashi, K., & Mizui, Y. (2004) · The Journal of Antibiotics · doi:10.7164/antibiotics.57.173 · Cited by 131

An overview of the clinical application of antisense oligonucleotides for RNA-targeting therapies

McClorey, G., & Wood, M. J. A. (2015) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2015.07.005 · Cited by 130

Specific inhibition of serine- and arginine-rich splicing factors phosphorylation, spliceosome assembly, and splicing by the antitumor drug NB-506.

Pilch, B., Allemand, E., Facompré, M., et al. (2001) · PubMed · Cited by 130

Spliceostatin A inhibits spliceosome assembly subsequent to prespliceosome formation

Roybal, G. A., & Jurica, M. S. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq494 · Cited by 126

The splicing-factor oncoprotein SF2/ASF activates mTORC1

Karni, R., Hippo, Y., Lowe, S. W., & Krainer, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801376105 · Cited by 122

Inhibition of vemurafenib-resistant melanoma by interference with pre-mRNA splicing

Salton, M., Kasprzak, W. K., Voss, T. C., Shapiro, B. A., Poulikakos, P. I., & Misteli, T. (2015) · Nature Communications · doi:10.1038/ncomms8103 · Cited by 114

Spliceosomal gene mutations in myelodysplasia: molecular links to clonal abnormalities of hematopoiesisPreprint

Inoue, D., Bradley, R. K., & Abdel-Wahab, O. I. (2016) · Genes & Development · doi:10.1101/gad.278424.116 · Cited by 113

Identification of a Novel Function of CX-4945 as a Splicing Regulator

Kim, H., Choi, K., Kang, H., Lee, S., Chi, S., Lee, M., Jaehyoung, S., Donghwa, I., Choi, Y., & Cho, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094978 · Cited by 99

The development and application of small molecule modulators of SF3b as therapeutic agents for cancer

Webb, T. R., Joyner, A. S., & Potter, P. M. (2012) · Drug Discovery Today · doi:10.1016/j.drudis.2012.07.013 · Cited by 99

Potential Antileukemia Effect and Structural Analyses of SRPK Inhibition by N-(2-(Piperidin-1-yl)-5-(Trifluoromethyl)Phenyl)Isonicotinamide (SRPIN340)

Siqueira, R. P., Barbosa, É. D. A. A., Polêto, M. D., Righetto, G. L., Seraphim, T. V., Salgado, R. L., Ferreira, J. G., Barros, M. V. D. A., de Oliveira, L. L., Laranjeira, A. B. A., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134882 · Cited by 95

Interchangeable SF3B1 inhibitors interfere with pre-mRNA splicing at multiple stages

Effenberger, K. A., Urabe, V. K., Prichard, B. E., Ghosh, A. K., & Jurica, M. S. (2016) · RNA · doi:10.1261/rna.053108.115 · Cited by 89

A Chemical Genetics Approach for the Functional Assessment of Novel Cancer Genes

Zhou, Q., Derti, A., Ruddy, D. A., Rakiec, D. P., Kao, I., Lira, M., Gibaja, V., Chan, H., Yang, Y., Min, J., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2930 · Cited by 85

Targeting the spliceosome in chronic lymphocytic leukemia with the macrolides FD-895 and pladienolide-B

Kashyap, M. K., Kumar, D., Villa, R., Clair, J. J. L., Benner, C. W., Sasik, R., Jones, H., Ghia, E. M., Rassenti, L. Z., Kipps, T. J., et al. (2015) · Haematologica · doi:10.3324/haematol.2014.122069 · Cited by 83

Pre-mRNA Splicing-Modulatory Pharmacophores: The Total Synthesis of Herboxidiene, a Pladienolide–Herboxidiene Hybrid Analog and Related Derivatives

Lagisetti, C., Yermolina, M. V., Sharma, L. K., Palacios, G. F., Prigaro, B. J., & Webb, T. R. (2013) · ACS Chemical Biology · doi:10.1021/cb400695j · Cited by 65

Distinct iron architecture in SF3B1-mutant myelodysplastic syndrome patients is linked to an SLC25A37 splice variant with a retained intron

Visconte, V., Avishai, N., Mahfouz, R. Z., Tabarroki, A., Cowen, J., Sharghi-Moshtaghin, R., Hitomi, M., Rogers, H. J., Hasrouni, E., Phillips, J., et al. (2014) · Leukemia · doi:10.1038/leu.2014.170 · Cited by 64

Optimization of Antitumor Modulators of Pre-mRNA Splicing

Lagisetti, C., Palacios, G. F., Goronga, T., Freeman, B. B., Caufield, W. V., & Webb, T. R. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401370h · Cited by 64

Increased levels of noisy splicing in cancers, but not for oncogene-derived transcripts

Chen, L., Tovar-Corona, J. M., & Urrutia, A. O. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr370 · Cited by 40

A Quantitative High-Throughput In Vitro Splicing Assay Identifies Inhibitors of Spliceosome Catalysis

Berg, M. G., Wan, L., Younis, I., Diem, M. D., Soo, M., Wang, C., & Dreyfuss, G. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.05788-11 · Cited by 40

A High-Throughput Splicing Assay Identifies New Classes of Inhibitors of Human and Yeast Spliceosomes

Effenberger, K. A., Perriman, R., Bray, W. M., Lokey, R. S., Ares, M., & Jurica, M. S. (2013) · SLAS DISCOVERY · doi:10.1177/1087057113493117 · Cited by 34

The Natural Product N-Palmitoyl-l-leucine Selectively Inhibits Late Assembly of Human Spliceosomes

Effenberger, K. A., James, R. C., Urabe, V. K., Dickey, B. J., Linington, R. G., & Jurica, M. S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.673210 · Cited by 24

Total Synthesis of 6-Deoxypladienolide D and Assessment of Splicing Inhibitory Activity in a Mutant SF3B1 Cancer Cell Line

Arai, K., Buonamici, S., Chan, B., Corson, L., Endo, A., Gerard, B., Hao, M., Karr, C. D., Kira, K., Lee, L., et al. (2014) · Organic Letters · doi:10.1021/ol502556c · Cited by 23

Small Molecule Inhibitors of Yeast Pre-mRNA Splicing

Aukema, K. G., Chohan, K. K., Plourde, G. L., Reimer, K. B., & Rader, S. D. (2009) · ACS Chemical Biology · doi:10.1021/cb900090z · Cited by 22

Preclinical Activity of Splicing Modulators in U2AF1 Mutant MDS/AML

Shirai, C. L., Tripathi, M., Ley, J. N., Ndonwi, M., White, B. S., TAPIA-CONYER, R. C., Sáez, B., Bertino, A. M., Shao, J., Kim, S., et al. (2015) · Blood · doi:10.1182/blood.v126.23.1653.1653 · Cited by 8

Alternative Splicing Regulatory Networks: Functions, Mechanisms, and Evolution

Ule, J., & Blencowe, B. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.017 · Cited by 780

RNA-Binding Proteins in Cancer: Old Players and New Actors

Pereira, B., Billaud, M., & Almeida, R. (2017) · Trends in Cancer · doi:10.1016/j.trecan.2017.05.003 · Cited by 773

Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15

Han, T., Goralski, M., Gaskill, N., Capota, E., Kim, J., Ting, T. C., Xie, Y., Williams, N. S., & Nijhawan, D. (2017) · Science · doi:10.1126/science.aal3755 · Cited by 762

Somatic mutations precede acute myeloid leukemia years before diagnosis

Desai, P., Mencia-Trinchant, N., Savenkov, O., Simon, M. S., Cheang, G., Lee, S., Samuel, M., Ritchie, E. K., Guzman, M. L., Ballman, K. V., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0081-z · Cited by 619

Alternative‐splicing defects in cancer: Splicing regulators and their downstream targets, guiding the way to novel cancer therapeutics

Urbanski, L. M., Leclair, N., & Anczuków, O. (2018) · WIREs RNA · doi:10.1002/wrna.1476 · Cited by 389