New frontiers in translational control of the cancer genome

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351 · see citing works

MicroRNA expression profiles classify human cancers

Lü, J., Getz, G. A., Miska, E. A., Alvarez-Saavedra, E., Lamb, J., Peck, D., Sweet-Cordero, A., Ebert, B. L., Mak, R. H., Ferrando, A. A., et al. (2005) · Nature · doi:10.1038/nature03702 · Cited by 9,497 · see citing works

The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation

Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,893 · see citing works

An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs

Kozak, M. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.20.8125 · Cited by 5,090 · see citing works

Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq

Dominissini, D., Moshitch-Moshkovitz, S., Schwartz, S., Salmon-Divon, M., Ungar, L., Osenberg, S., Cesarkas, K., Jacob-Hirsch, J., Amariglio, N., Kupiec, M., et al. (2012) · Nature · doi:10.1038/nature11112 · Cited by 4,884 · see citing works

Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons

Meyer, K. D., Saletore, Y., Zumbo, P., Elemento, O., Mason, C. E., & Jaffrey, S. R. (2012) · Cell · doi:10.1016/j.cell.2012.05.003 · Cited by 4,223 · see citing works

Insights into the regulation of protein abundance from proteomic and transcriptomic analyses

Vogel, C., & Marcotte, E. M. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3185 · Cited by 4,195 · see citing works

mTOR: from growth signal integration to cancer, diabetes and ageing

Zoncu, R., Efeyan, A., & Sabatini, D. M. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3025 · Cited by 3,941 · see citing works

Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling

Ingolia, N. T., Ghaemmaghami, S., Newman, J. R. S., & Weissman, J. S. (2009) · Science · doi:10.1126/science.1168978 · Cited by 3,853 · see citing works

RAS Is Regulated by the let-7 MicroRNA Family

Johnson, S., Großhans, H., Shingara, J., Byrom, M., JARVIS, R., Cheng, A., Labourier, E., Reinert, K. L., Brown, D., & Slack, F. J. (2005) · Cell · doi:10.1016/j.cell.2005.01.014 · Cited by 3,662 · see citing works

Modulation of oxidative stress as an anticancer strategy

Gorrini, C., Harris, I. S., & Mak, T. W. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4002 · Cited by 3,579 · see citing works

An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress

Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336 · see citing works

Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets

Sonenberg, N., & Hinnebusch, A. G. (2009) · Cell · doi:10.1016/j.cell.2009.01.042 · Cited by 3,304 · see citing works

Transcriptome-wide Identification of RNA-Binding Protein and MicroRNA Target Sites by PAR-CLIP

Hafner, M., Landthaler, M., Burger, L., Khorshid, M., Hausser, J., Berninger, P., Rothballer, A., Ascano, M., Jungkamp, A.-C., Munschauer, M., et al. (2010) · Cell · doi:10.1016/j.cell.2010.03.009 · Cited by 2,873 · see citing works

The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1

Sancak, Y., Peterson, T. R., Shaul, Y. D., Lindquist, R. A., Thoreen, C. C., Bar-Peled, L., & Sabatini, D. M. (2008) · Science · doi:10.1126/science.1157535 · Cited by 2,773 · see citing works

Characterization of Mammalian Selenoproteomes

Kryukov, G. V., Castellano, S., Novoselov, S. V., Lobanov, A. V., Zehtab, O., Guigó, R., & Gladyshev, V. N. (2003) · Science · doi:10.1126/science.1083516 · Cited by 2,353 · see citing works

Ribosome Profiling of Mouse Embryonic Stem Cells Reveals the Complexity and Dynamics of Mammalian Proteomes

Ingolia, N. T., Lareau, L. F., & Weissman, J. S. (2011) · Cell · doi:10.1016/j.cell.2011.10.002 · Cited by 2,187 · see citing works

Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins

Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132 · see citing works

A census of human RNA-binding proteins

Gerstberger, S., Hafner, M., & Tuschl, T. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3813 · Cited by 2,032 · see citing works

Towards a molecular understanding of microRNA-mediated gene silencing

Jonas, S., & Izaurralde, E. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3965 · Cited by 1,872 · see citing works

5′ UTR m6A Promotes Cap-Independent Translation

Meyer, K. D., Patil, D. P., Zhou, J. L., Zinoviev, A., Skabkin, M. A., Elemento, O., Pestova, T. V., Qian, S., & Jaffrey, S. R. (2015) · Cell · doi:10.1016/j.cell.2015.10.012 · Cited by 1,812 · see citing works

An ATP-competitive Mammalian Target of Rapamycin Inhibitor Reveals Rapamycin-resistant Functions of mTORC1

Thoreen, C. C., Kang, S. A., Chang, J. W., Liu, Q., Zhang, J., Gao, Y., Reichling, L. J., Sim, T., Sabatini, D. M., & Gray, N. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900301200 · Cited by 1,803 · see citing works

Principles of cancer therapy: oncogene and non-oncogene addiction

Luo, J., Solimini, N. L., & Elledge, S. J. (2009) · Cell · doi:10.1016/j.cell.2009.02.024 · Cited by 1,765 · see citing works

Reinitiation involving upstream ORFs regulates <i>ATF4</i> mRNA translation in mammalian cells

Vattem, K. M., & Wek, R. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400541101 · Cited by 1,696 · see citing works

Mitochondrial ROS in cancer: initiators, amplifiers or an Achilles' heel?

Sabharwal, S. S., & Schumacker, P. T. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3803 · Cited by 1,643 · see citing works

Widespread Shortening of 3′UTRs by Alternative Cleavage and Polyadenylation Activates Oncogenes in Cancer Cells

Mayr, C., & Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.06.016 · Cited by 1,613 · see citing works

A compendium of RNA-binding motifs for decoding gene regulation

Ray, D., Kazan, H., Cook, K. B., Weirauch, M. T., Najafabadi, H. S., Li, X., Gueroussov, S., Albu, M., Zheng, H., Yang, A., et al. (2013) · Nature · doi:10.1038/nature12311 · Cited by 1,480 · see citing works

A unifying model for mTORC1-mediated regulation of mRNA translation

Thoreen, C. C., Chantranupong, L., Keys, H. R., Wang, T., Gray, N. S., & Sabatini, D. M. (2012) · Nature · doi:10.1038/nature11083 · Cited by 1,477 · see citing works

RNA‐binding proteins and post‐transcriptional gene regulation

Glisovic, T., Bachorik, J. L., Yong, J., & Dreyfuss, G. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.004 · Cited by 1,398 · see citing works

Regulation of mTOR function in response to hypoxia by REDD1 and the TSC1/TSC2 tumor suppressor complex

Brugarolas, J., Lei, K., Hurley, R. L., Manning, B. D., Reiling, J. H., Hafen, E., Witters, L. A., Ellisen, L. W., & Kaelin, W. G. (2004) · Genes &amp; Development · doi:10.1101/gad.1256804 · Cited by 1,384 · see citing works

HITS-CLIP yields genome-wide insights into brain alternative RNA processing

Licatalosi, D. D., Mele, A., Fak, J. J., Ule, J., Kayikci, M., Chi, S. W., Clark, T. A., Schweitzer, A. C., Blume, J. E., Wang, X., et al. (2008) · Nature · doi:10.1038/nature07488 · Cited by 1,352 · see citing works

Proliferating Cells Express mRNAs with Shortened 3' Untranslated Regions and Fewer MicroRNA Target Sites

Sandberg, R., Neilson, J. R., Sarma, A., Sharp, P. A., & Burge, C. B. (2008) · Science · doi:10.1126/science.1155390 · Cited by 1,349 · see citing works

The translational landscape of mTOR signalling steers cancer initiation and metastasis

Hsieh, A. C., Liu, Y., Edlind, M. P., Ingolia, N. T., Janes, M. R., Sher, A., Shi, E. Y., Stumpf, C. R., Christensen, C., Bonham, M. J., et al. (2012) · Nature · doi:10.1038/nature10912 · Cited by 1,313 · see citing works

Dynamic m6A mRNA methylation directs translational control of heat shock response

Zhou, J. L., Wan, J., Gao, X., Zhang, X., Jaffrey, S. R., & Qian, S. (2015) · Nature · doi:10.1038/nature15377 · Cited by 1,228 · see citing works

The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts

Baltz, A. G., Munschauer, M., Schwanhäußer, B., Vasile, A. I., Murakawa, Y., Schueler, M., Youngs, N., Penfold-Brown, D., Drew, K., Milek, M., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.021 · Cited by 1,175 · see citing works

The Xist lncRNA interacts directly with SHARP to silence transcription through HDAC3

McHugh, C. A., Chen, C., Chow, A. Y., Surka, C., Tran, C., McDonel, P. E., Pandya‐Jones, A., Blanco, M. R., Burghard, C. P., Moradian, A., et al. (2015) · Nature · doi:10.1038/nature14443 · Cited by 1,163 · see citing works

iCLIP reveals the function of hnRNP particles in splicing at individual nucleotide resolution

König, J., Zarnack, K., Rot, G., Curk, T., Kayikci, M., Zupan, B., Turner, D. J., Luscombe, N. M., & Ule, J. (2010) · Nature Structural &amp; Molecular Biology · doi:10.1038/nsmb.1838 · Cited by 1,126 · see citing works

Systematic Discovery of Xist RNA Binding Proteins

Chu, C., Zhang, Q. C., da Rocha, S. T., Flynn, R. A., Bharadwaj, M. C., Calabrese, J. M., Magnuson, T., Heard, É., & Chang, H. Y. (2015) · Cell · doi:10.1016/j.cell.2015.03.025 · Cited by 1,103 · see citing works

Active-Site Inhibitors of mTOR Target Rapamycin-Resistant Outputs of mTORC1 and mTORC2

Feldman, M. E., Apsel, B., Uotila, A., Loewith, R., Knight, Z. A., Ruggero, D., & Shokat, K. M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000038 · Cited by 1,080 · see citing works

Replication stress and cancer

Gaillard, H., García‐Muse, T., & Aguilera, A. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3916 · Cited by 1,077 · see citing works

Widespread occurrence of 5-methylcytosine in human coding and non-coding RNA

Squires, J. E., Patel, H. R., Nousch, M., Sibbritt, T., Humphreys, D. T., Parker, B. J., Suter, C. M., & Preiß, T. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks144 · Cited by 1,011 · see citing works

Pseudouridine profiling reveals regulated mRNA pseudouridylation in yeast and human cells

Carlile, T. M., Rojas-Durán, M. F., Zinshteyn, B., Shin, H., Bartoli, K. M., & Gilbert, W. V. (2014) · Nature · doi:10.1038/nature13802 · Cited by 1,004 · see citing works

Transcriptome-wide Mapping Reveals Widespread Dynamic-Regulated Pseudouridylation of ncRNA and mRNA

Schwartz, S., Bernstein, D. A., Mumbach, M. R., Jovanović, M., Herbst, R. H., León-Ricardo, B. X., Engreitz, J., Guttman, M., Satija, R., Lander, E. S., et al. (2014) · Cell · doi:10.1016/j.cell.2014.08.028 · Cited by 988 · see citing works

Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5' cap

Lazaris-Karatzas, A., Montine, K. S., & Sonenberg, N. (1990) · Nature · doi:10.1038/345544a0 · Cited by 965 · see citing works

Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2

Waskiewicz, A. J., Flynn, A., Proud, C. G., & Cooper, J. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.8.1909 · Cited by 951 · see citing works

A large-scale analysis of mRNA polyadenylation of human and mouse genes

Tian, B. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki158 · Cited by 944 · see citing works

Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans

Calvo, S. E., Pagliarini, D. J., & Mootha, V. K. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810916106 · Cited by 914 · see citing works

miRNA-Mediated Gene Silencing by Translational Repression Followed by mRNA Deadenylation and Decay

Djuranović, S., Nahvi, A., & Green, R. (2012) · Science · doi:10.1126/science.1215691 · Cited by 866 · see citing works

Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase

Wang, X.-M., Li, W., Williams, M. R., Terada, N., Alessi, D., & Proud, C. G. (2001) · EMBO Journal · doi:10.1093/emboj/20.16.4370 · Cited by 862 · see citing works

PKR; a sentinel kinase for cellular stress

Williams, B. R. (1999) · Oncogene · doi:10.1038/sj.onc.1203127 · Cited by 820 · see citing works

Translational control in cancer

Silvera, D., Formenti, S. C., & Schneider, R. J. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2824 · Cited by 820 · see citing works

Alternative cleavage and polyadenylation: extent, regulation and function

Elkon, R., Ugalde, A. P., & Agami, R. (2013) · Nature Reviews Genetics · doi:10.1038/nrg3482 · Cited by 805 · see citing works

Targeting 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

Genome-wide measurement of RNA secondary structure in yeast

Kertesz, M., Wan, Y., Mazor, E., Rinn, J. L., Nutter, R. C., Chang, H. Y., & Segal, E. (2010) · Nature · doi:10.1038/nature09322 · Cited by 765 · see citing works

tRNA biology charges to the frontPreprint

Phizicky, E. M., & Hopper, A. K. (2010) · Genes & Development · doi:10.1101/gad.1956510 · Cited by 764 · see citing works

Extensive post-transcriptional regulation of microRNAs and its implications for cancer

Thomson, J. M., Newman, M., Parker, J. S., Morin-Kensicki, E. M., Wright, T., & Hammond, S. M. (2006) · Genes &amp; Development · doi:10.1101/gad.1444406 · Cited by 755 · see citing works

Structural imprints in vivo decode RNA regulatory mechanisms

Spitale, R. C., Flynn, R. A., Zhang, Q. C., Crisalli, P., Lee, B., Jung, J., Kuchelmeister, H. Y., Batista, P. J., Torre, E. A., Kool, E. T., et al. (2015) · Nature · doi:10.1038/nature14263 · Cited by 745 · see citing works

S6K1 −/− / S6K2 −/− Mice Exhibit Perinatal Lethality and Rapamycin-Sensitive 5′-Terminal Oligopyrimidine mRNA Translation and Reveal a Mitogen-Activated Protein Kinase-Dependent S6 Kinase Pathway

Pende, M., Um, S. H., Mieulet, V., Sticker, M., Goss, V. L., Mestan, J., Mueller, M., Fumagalli, S., Kozma, S. C., & Thomas, G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3112-3124.2004 · Cited by 743 · see citing works

The Functions of MicroRNAs: mRNA Decay and Translational Repression

Iwakawa, H., & Tomari, Y. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.07.011 · Cited by 732 · see citing works

S6K1- and ßTRCP-Mediated Degradation of PDCD4 Promotes Protein Translation and Cell Growth

Dorrello, N. V., Peschiaroli, A., Guardavaccaro, D., Colburn, N. H., Sherman, N. E., & Pagano, M. (2006) · Science · doi:10.1126/science.1130276 · Cited by 731 · see citing works

Ribosome Profiling Shows That miR-430 Reduces Translation Before Causing mRNA Decay in Zebrafish

Bazzini, A. A., Lee, M. T., & Giraldez, A. J. (2012) · Science · doi:10.1126/science.1215704 · Cited by 709 · see citing works

Influences of mRNA secondary structure on initiation by eukaryotic ribosomes.

Kozak, M. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.9.2850 · Cited by 687 · see citing works

Specialized ribosomes: a new frontier in gene regulation and organismal biology

Xue, S., & Barna, M. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3359 · Cited by 687 · see citing works

Poly(A)-tail profiling reveals an embryonic switch in translational control

Subtelny, A. O., Eichhorn, S. W., Chen, G. R., Sive, H., & Bartel, D. P. (2014) · Nature · doi:10.1038/nature13007 · Cited by 664 · see citing works

c-Myc binds to human ribosomal DNA and stimulates transcription of rRNA genes by RNA polymerase I

Grandori, C., Gomez-Roman, N., Felton-Edkins, Z. A., Ngouenet, C., Galloway, D. A., Eisenman, R. N., & White, R. J. (2005) · Nature Cell Biology · doi:10.1038/ncb1224 · Cited by 659 · see citing works

Ribosome Profiling Reveals Pervasive Translation Outside of Annotated Protein-Coding Genes

Ingolia, N. T., Brar, G. A., Stern‐Ginossar, N., Harris, M. S., Talross, G. J. S., Jackson, S. E., Wills, M. R., & Weissman, J. S. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.045 · Cited by 644 · see citing works

Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasisPreprint

Ruvinsky, I., Sharon, N., Lerer, T., Cohen, H., Stolovich-Rain, M., Nir, T., Dor, Y., Zisman, P., & Meyuhas, O. (2005) · Genes & Development · doi:10.1101/gad.351605 · Cited by 640 · see citing works

MicroRNA Inhibition of Translation Initiation in Vitro by Targeting the Cap-Binding Complex eIF4F

Mathonnet, G., Fabian, M., Svitkin, Y., Parsyan, A., Huck, L., Murata, T., Biffo, S., Merrick, W., Darżynkiewicz, E., Pillai, R., et al. (2007) · Science · doi:10.1126/science.1146067 · Cited by 636 · see citing works

RNA 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

Bidirectional RNA Helicase Activity of Eucaryotic Translation Initiation Factors 4A and 4F

Rozen, F., Edery, I., Meerovitch, K., Dever, T. E., Merrick, W. C., & Sonenberg, N. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.3.1134 · Cited by 632 · see citing works

Rapamycin selectively represses translation of the "polypyrimidine tract" mRNA family.

Jefferies, H. B. J., Reinhard, C., Kozma, S. C., & Thomas, G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.10.4441 · Cited by 623 · see citing works

Targeting RNA Polymerase I with an Oral Small Molecule CX-5461 Inhibits Ribosomal RNA Synthesis and Solid Tumor Growth

Drygin, D., Lin, A. H., Bliesath, J., Ho, C., O’Brien, S., Proffitt, C., Omori, M., Haddach, M., Schwaebe, M. K., Siddiqui-Jain, A., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1728 · Cited by 622 · see citing works

Repression of cap‐dependent translation by 4E‐binding protein 1: competition with p220 for binding to eukaryotic initiation factor‐4E.

Haghighat, A., Mader, S., Pause, A., & Sonenberg, N. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00257.x · Cited by 615 · see citing works

Insertion mutagenesis to increase secondary structure within the 5′ noncoding region of a eukaryotic mRNA reduces translational efficiency

Pelletier, J., & Sonenberg, N. (1985) · Cell · doi:10.1016/0092-8674(85)90200-4 · Cited by 610 · see citing works

Tissue-Specific Differences in Human Transfer RNA Expression

Dittmar, K. A., Goodenbour, J. M., & Pan, T. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020221 · Cited by 601 · see citing works

Global mapping of translation initiation sites in mammalian cells at single-nucleotide resolution

Lee, S., Liu, B., Lee, S., Huang, S., Shen, B., & Qian, S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207846109 · Cited by 595 · see citing works

The translation factor eIF-4E promotes tumor formation and cooperates with c-Myc in lymphomagenesis

Ruggero, D., Montanaro, L., Ma, L., Xu, W. G., Londei, P., Cordon‐Cardo, C., & Pandolfi, P. P. (2004) · Nature Medicine · doi:10.1038/nm1042 · Cited by 592 · see citing works

Ribosome-Mediated Specificity in Hox mRNA Translation and Vertebrate Tissue Patterning

Kondrashov, N., Pusic, A. D., Stumpf, C. R., Shimizu, K., Hsieh, A. C., Xue, S., Ishijima, J., Shiroishi, T., & Barna, M. (2011) · Cell · doi:10.1016/j.cell.2011.03.028 · Cited by 581 · see citing works

NSun2-Mediated Cytosine-5 Methylation of Vault Noncoding RNA Determines Its Processing into Regulatory Small RNAs

Hussain, S., Sajini, A. A., Blanco, S., Dietmann, S., Lombard, P., Sugimoto, Y., Paramor, M., Gleeson, J. G., Odom, D. T., Ule, J., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.029 · Cited by 569 · see citing works

Inhibition of RNA Polymerase I as a Therapeutic Strategy to Promote Cancer-Specific Activation of p53

Bywater, M. J., Poortinga, G., Sanij, E., Hein, N., Peck, A., Cullinane, C. M., Wall, M., Cluse, L. A., Drygin, D., Anderes, K. L., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.05.019 · Cited by 561 · see citing works

Chemical pulldown reveals dynamic pseudouridylation of the mammalian transcriptome

Li, X., Zhu, P., Ma, S., Song, J., Bai, J., Sun, F., & Yi, C. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1836 · Cited by 554 · see citing works

Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

Bah, A., Vernon, R. M., Siddiqui, Z., Krzeminski, M., Muhandiram, R., Zhao, C. W., Sonenberg, N., Kay, L. E., & Forman-Kay, J. D. (2014) · Nature · doi:10.1038/nature13999 · Cited by 554 · 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

Uncharged tRNA Activates GCN2 by Displacing the Protein Kinase Moiety from a Bipartite tRNA-Binding Domain

Dong, J., Qiu, H., Garcia-Barrio, M., Anderson, J., & Hinnebusch, A. G. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00028-9 · Cited by 545 · see citing works

eIF4E phosphorylation promotes tumorigenesis and is associated with prostate cancer progression

Furic, L., Rong, L., Larsson, O. S., Koumakpayi, I. H., Yoshida, K., Brueschke, A., Petroulakis, E., Robichaud, N., Pollak, M., Gaboury, L. A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005320107 · Cited by 528 · see citing works

mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availabilityPreprint

Mayer, C., Zhao, J., Yuan, X., & Grummt, I. (2004) · Genes & Development · doi:10.1101/gad.285504 · Cited by 506 · see citing works

mRNA Destabilization Is the Dominant Effect of Mammalian MicroRNAs by the Time Substantial Repression Ensues

Eichhorn, S. W., Guo, H., McGeary, S. E., Rodríguez‐Mias, R. A., Shin, C., Baek, D., Hsu, S., Ghoshal, K., Villén, J., & Bartel, D. P. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.028 · Cited by 491 · see citing works

A Dual Program for Translation Regulation in Cellular Proliferation and Differentiation

Gingold, H., Tehler, D., Christoffersen, N. R., Nielsen, M. M., Asmar, F., Kooistra, S. M., Christophersen, N. S., Christensen, L. L., Borre, M., Sørensen, K. D., et al. (2014) · Cell · doi:10.1016/j.cell.2014.08.011 · Cited by 487 · see citing works

Identification of direct targets and modified bases of RNA cytosine methyltransferases

Khoddami, V., & Cairns, B. R. (2013) · Nature Biotechnology · doi:10.1038/nbt.2566 · Cited by 484 · see citing works

Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F.

Duncan, R., Milburn, S. C., & Hershey, J. W. B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75938-9 · Cited by 483 · see citing works

ARM-seq: AlkB-facilitated RNA methylation sequencing reveals a complex landscape of modified tRNA fragments

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

The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 5′ secondary structure

Svitkin, 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

mTOR-Dependent Regulation of Ribosomal Gene Transcription Requires S6K1 and Is Mediated by Phosphorylation of the Carboxy-Terminal Activation Domain of the Nucleolar Transcription Factor UBF†

Hannan, K., Brandenburger, Y., Jenkins, A., Sharkey, K., Cavanaugh, A., Rothblum, L., Moss, T., Poortinga, G., McArthur, G., Pearson, R., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8862-8877.2003 · Cited by 473 · see citing works

Phosphorylation of eucaryotic translation initiation factor 4B Ser422 is modulated by S6 kinases

Raught, B., Peiretti, F., Gingras, A., Livingstone, M., Shahbazian, D., Mayeur, G. L., Polakiewicz, R. D., Sonenberg, N., & Hershey, J. W. B. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600193 · Cited by 473 · see citing works

c-Myc associates with ribosomal DNA and activates RNA polymerase I transcription

Arabi, A., Wu, S., Ridderstråle, K., Bierhoff, H., Shiue, C.-N., Fátyol, K., Fahlén, S., Hydbring, P., Söderberg, O., Grummt, I., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1225 · Cited by 471 · see citing works

A Quantitative Systems Approach Reveals Dynamic Control of tRNA Modifications during Cellular Stress

Chan, C. T. Y., Dyavaiah, M., DeMott, M. S., Taghizadeh, K., Dedon, P. C., & Begley, T. J. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001247 · Cited by 466 · see citing works

Genetic Dissection of the Oncogenic mTOR Pathway Reveals Druggable Addiction to Translational Control via 4EBP-eIF4E

Hsieh, A. C., Costa, M. D., Zollo, O., Davis, C. B., Feldman, M. E., Testa, J. R., Meyuhas, O., Shokat, K. M., & Ruggero, D. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.01.021 · Cited by 464 · see citing works

Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation

Ryazanov, A. G., Shestakova, E. A., & Natapov, P. G. (1988) · Nature · doi:10.1038/334170a0 · Cited by 459 · see citing works

The RNA-binding protein repertoire of embryonic stem cells

Kwon, S. C., Yi, H., Eichelbaum, K., Föehr, S., Fischer, B., You, K. T., Castelló, A., Krijgsveld, J., Hentze, M. W., & Kim, V. N. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2638 · Cited by 451 · see citing works

CFIm25 links alternative polyadenylation to glioblastoma tumour suppression

Masamha, C. P., Xia, Z., Yang, J., Albrecht, T. R., Li, M., Shyu, A., Li, W., & Wagner, E. J. (2014) · Nature · doi:10.1038/nature13261 · Cited by 449 · see citing works

RNA-binding protein HuR enhances p53 translation in response to ultraviolet light irradiation

Mazan-Mamczarz, K., Galbán, S., de Silanes, I. L., Martindale, J. L., Atasoy, U., Keene, J. D., & Gorospe, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1432104100 · Cited by 445 · see citing works

Altered expression of the mRNA stability factor HuR promotes cyclooxygenase-2 expression in colon cancer cells

Dixon, D. A., Tolley, N. D., King, P. H., Nabors, B., McIntyre, T. M., Zimmerman, G. A., & Prescott, S. M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12973 · Cited by 443 · see citing works

RNA SHAPE analysis in living cells

Spitale, R. C., Crisalli, P., Flynn, R. A., Torre, E. A., Kool, E. T., & Chang, H. Y. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1131 · Cited by 442 · see citing works

Reprogramming of tRNA modifications controls the oxidative stress response by codon-biased translation of proteins

Chan, C. T. Y., Pang, Y. L. J., Deng, W., Babu, I. R., Dyavaiah, M., Begley, T. J., & Dedon, P. C. (2012) · Nature Communications · doi:10.1038/ncomms1938 · Cited by 442 · see citing works

N‐myc enhances the expression of a large set of genes functioning in ribosome biogenesis and protein synthesis

Boon, K., Caron, H. N., van Asperen, R., Valentijn, L. J., Hermus, M.-C., Sluis, P. V., Roobeek, I., Weis, I., Voûte, P. A., Schwab, M., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.6.1383 · Cited by 439 · see citing works

ER stress–mediated autophagy promotes Myc-dependent transformation and tumor growth

Hart, L. S., Cunningham, J. T., Datta, T., Dey, S., Tameire, F., Lehman, S. L., Qiu, B., Zhang, H., Cerniglia, G. J., Bi, M., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci62973 · Cited by 436 · see citing works

Dyskeratosis Congenita and Cancer in Mice Deficient in Ribosomal RNA Modification

Ruggero, D., Grisendi, S., Piazza, F., Rego, E. M., Mari, F., Rao, P. H., Cordon‐Cardo, C., & Pandolfi, P. P. (2003) · Science · doi:10.1126/science.1079447 · Cited by 435 · see citing works

Suppression of Myc oncogenic activity by ribosomal protein haploinsufficiency

Barna, M., Pusic, A., Zollo, O., Costa, M. J., Kondrashov, N., Rego, E., Rao, P., & Ruggero, D. (2008) · Nature · doi:10.1038/nature07449 · Cited by 434 · see citing works

Direct activation of RNA polymerase III transcription by c-Myc

Gomez-Roman, N., Grandori, C., Eisenman, R. N., & White, R. J. (2003) · Nature · doi:10.1038/nature01327 · Cited by 434 · see citing works

Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling

Jan, C. H., Williams, C. C., & Weissman, J. S. (2014) · Science · doi:10.1126/science.1257521 · Cited by 431 · see citing works

eIF3 targets cell-proliferation messenger RNAs for translational activation or repression

Lee, A. S. Y., Kranzusch, P. J., & Cate, J. H. D. (2015) · Nature · doi:10.1038/nature14267 · Cited by 429 · see citing works

Impaired Control of IRES-Mediated Translation in X-Linked Dyskeratosis Congenita

Yoon, A., Peng, G., Brandenburg, Y., Zollo, O., Xu, W. G., Rego, E. M., & Ruggero, D. (2006) · Science · doi:10.1126/science.1123835 · Cited by 423 · see citing works

mRNAs containing extensive secondary structure in their 5′ non‐coding region translate efficiently in cells overexpressing initiation factor eIF‐4E.

Koromilas, A. E., Lazaris-Karatzas, A., & Sonenberg, N. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05508.x · Cited by 422 · see citing works

Oncogenic Ras and Akt signaling contribute to glioblastoma formation by differential recruitment of existing mRNAs to polysomes.

Rajasekhar, V. K., Viale, A., Socci, N. D., Wiedmann, M., Hu, X., & Holland, E. C. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00395-2 · Cited by 420 · see citing works

Musashi-2 regulates normal hematopoiesis and promotes aggressive myeloid leukemia

Kharas, M., Lengner, C., Al-Shahrour, F., Bullinger, L., Ball, B., Zaidi, S., Morgan, K. J., Tam, W. F., Paktinat, M., Okabe, R., et al. (2010) · Nature Medicine · doi:10.1038/nm.2187 · Cited by 417 · see citing works

The eEF2 Kinase Confers Resistance to Nutrient Deprivation by Blocking Translation Elongation

Leprivier, G., Remke, M., Rotblat, B., Dubuc, A. M., Mateo, A.-R. F., Kool, M., Agnihotri, S., El-Naggar, A. M., Yu, B., Somasekharan, S. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.04.055 · Cited by 412 · see citing works

4E-BP1 Is a Key Effector of the Oncogenic Activation of the AKT and ERK Signaling Pathways that Integrates Their Function in Tumors

She, Q.-B., Halilovic, E., Ye, Q., Zhen, W., Shirasawa, S., Sasazuki, T., Solit, D. B., & Rosen, N. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.05.023 · Cited by 400 · see citing works

ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors.

Ray, B. K., Lawson, T. G., Kramer, J. C., Hadzopoulou‐Cladaras, M., GRIFO, J. A., Abramson, R. D., Merrick, W. C., & Thach, R. E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39658-8 · Cited by 399 · see citing works

Identification of eukaryotic mRNAs that are translated at reduced cap binding complex eIF4F concentrations using a cDNA microarray

Johannes, G., Carter, M. S., Eisen, M. B., Brown, P. O., & Sarnow, P. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13118 · Cited by 394 · see citing works

Therapeutic suppression of translation initiation factor eIF4E expression reduces tumor growth without toxicity.

Graff, J., Konicek, B., Vincent, T. M., Lynch, R. L., Monteith, D., Weir, S., Schwier, P., Capen, A., Goode, R., Dowless, M., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32044 · Cited by 393 · see citing works

Multiplexed RNA structure characterization with selective 2′-hydroxyl acylation analyzed by primer extension sequencing (SHAPE-Seq)

Lucks, J. B., Mortimer, S., Trapnell, C., Luo, S. J., Aviran, S., Schroth, G. P., Pachter, L. S., Doudna, J. A., & Arkin, A. P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106501108 · Cited by 390 · see citing works

Transcriptome-Wide Mapping of Pseudouridines: Pseudouridine Synthases Modify Specific mRNAs in S. cerevisiae

Lovejoy, A. F., Riordan, D. P., & Brown, P. O. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110799 · Cited by 381 · see citing works

Differential Requirements for eIF4E Dose in Normal Development and Cancer

Truitt, M., Conn, C. S., Shi, Z., Pang, X., Tokuyasu, T. A., Coady, A. M., Seo, Y., Barna, M., & Ruggero, D. (2015) · Cell · doi:10.1016/j.cell.2015.05.049 · Cited by 374 · 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

p53 Acts as a Safeguard of Translational Control by Regulating Fibrillarin and rRNA Methylation in Cancer

Marcel, V., Ghayad, S. E., Belin, S., Thérizols, G., Morel, A., Solano-Gonzàlez, E., Vendrell, J. A., Hacot, S., Mertani, H. C., Albaret, M. A., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.08.013 · Cited by 361 · see citing works

Regulation of myeloid leukaemia by the cell-fate determinant Musashi

Ito, T., Kwon, H. Y., Zimdahl, B., Congdon, K. L., Blum, J. M., Lento, W. E., Zhao, C., Lagoo, A. S., Gerrard, G., Foroni, L., et al. (2010) · Nature · doi:10.1038/nature09171 · Cited by 357 · see citing works

Oligopyrimidine tract at the 5' end of mammalian ribosomal protein mRNAs is required for their translational control.

Levy, S., Avni, D., Hariharan, N., Perry, R. P., & Meyuhas, O. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.8.3319 · Cited by 344 · see citing works

Translation of 5′ leaders is pervasive in genes resistant to eIF2 repression

Andreev, D. E., O’Connor, P. B. F., Fahey, C., Kenny, E. M., Terenin, I. M., Dmitriev, S. E., Cormican, P., Morris, D. W., Shatsky, I. N., & Baranov, P. V. (2015) · eLife · doi:10.7554/elife.03971 · Cited by 338 · see citing works

Therapeutic suppression of translation initiation modulates chemosensitivity in a mouse lymphoma model

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

ELAV/Hu proteins inhibit p27 translation via an IRES element in the p27 5′UTR

Kullmann, M., Göpfert, U., Siewe, B., & Hengst, L. (2002) · Genes &amp; Development · doi:10.1101/gad.248902 · Cited by 327 · see citing works

Translational Repression and eIF4A2 Activity Are Critical for MicroRNA-Mediated Gene Regulation

Meijer, H. A., Kong, Y. W., Lu, W. T., Wilczynska, A., Spriggs, R. V., Robinson, S. W., Godfrey, J. D., Willis, A. E., & Bushell, M. (2013) · Science · doi:10.1126/science.1231197 · Cited by 326 · see citing works

A Secreted PTEN Phosphatase That Enters Cells to Alter Signaling and Survival

Hopkins, B. D., Fine, B. M., Steinbach, N., Dendy, M., Rapp, Z., Shaw, J. M., Pappas, K., Yu, J. S., Hodakoski, C., Mense, S. M., et al. (2013) · Science · doi:10.1126/science.1234907 · Cited by 325 · see citing works

Trm9-Catalyzed tRNA Modifications Link Translation to the DNA Damage Response

Begley, U., Dyavaiah, M., Patil, A., Rooney, J. P., DiRenzo, D. M., Young, C. M., Conklin, D. S., Zitomer, R. S., & Begley, T. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.09.021 · Cited by 325 · see citing works

mRNA helicases: the tacticians of translational control

Parsyan, A., Svitkin, Y., Shahbazian, D., Gkogkas, C., Lasko, P., Merrick, W. C., & Sonenberg, N. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3083 · Cited by 323 · see citing works

A hypoxia-controlled cap-dependent to cap-independent translation switch in breast cancer.

Braunstein, S., Karpisheva, K., Pola, C., Goldberg, J., Hochman, T., Yee, H., Cangiarella, J., Arju, R., Formenti, S., & Schneider, R. (2007) · Molecules and Cells · doi:10.1016/j.molcel.2007.10.019 · Cited by 320 · see citing works

RNA regulons in Hox 5′ UTRs confer ribosome specificity to gene regulation

Xue, S., Tian, S., Fujii, K., Kladwang, W., Das, R., & Barna, M. (2014) · Nature · doi:10.1038/nature14010 · Cited by 319 · see citing works

An oxygen-regulated switch in the protein synthesis machinery

Uniacke, J., Holterman, C. E., Lachance, G., Franovic, A., Jacob, M. D., Fabian, M. R., Payette, J., Holcik, M., Pause, A., & Lee, S. (2012) · Nature · doi:10.1038/nature11055 · Cited by 319 · see citing works

FragSeq: transcriptome-wide RNA structure probing using high-throughput sequencing

Underwood, J. G., Uzilov, A. V., Katzman, S. J., Onodera, C. S., Mainzer, J. E., Mathews, D. H., Lowe, T. M., Salama, S. R., & Haussler, D. H. (2010) · Nature Methods · doi:10.1038/nmeth.1529 · Cited by 315 · see citing works

Drosophila miR2 induces pseudo-polysomes and inhibits translation initiation

Thermann, R., & Hentze, M. W. (2007) · Nature · doi:10.1038/nature05878 · Cited by 314 · see citing works

Cross-linking, ligation, and sequencing of hybrids reveals RNA–RNA interactions in yeast

Kudla, G., Granneman, S., Hahn, D., Beggs, J. D., & Tollervey, D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017386108 · Cited by 308 · see citing works

Regulation of protein synthesis by the heme-regulated eIF2α kinase: relevance to anemias

Chen, J.-J. (2006) · Blood · doi:10.1182/blood-2006-08-041830 · Cited by 306 · see citing works

TGF-β-mediated phosphorylation of hnRNP E1 induces EMT via transcript-selective translational induction of Dab2 and ILEI

Chaudhury, A., Hussey, G. S., Ray, P. S., Jin, G., Fox, P. L., & Howe, P. H. (2010) · Nature Cell Biology · doi:10.1038/ncb2029 · Cited by 305 · see citing works

mTORC1-mediated translational elongation limits intestinal tumour initiation and growth

Faller, W. J., Jackson, T. J., Knight, J. R. P., Ridgway, R. A., Jamieson, T. J., Karim, S. A., Jones, C., Radulescu, S., Huels, D. J., Myant, K., et al. (2014) · Nature · doi:10.1038/nature13896 · Cited by 302 · see citing works

A new internal-ribosome-entry-site motif potentiates XIAP- mediated cytoprotection

Holčı́k, M., Lefebvre, C. A., Yeh, C., Chow, T. Y.-K., & Korneluk, R. G. (1999) · Nature Cell Biology · doi:10.1038/11109 · Cited by 302 · see citing works

Antitumor Activity and Mechanism of Action of the Cyclopenta[b]benzofuran, Silvestrol

Cencic, R., Carrier, M., Galicia-Vázquez, G., Bordeleau, M.-E., Sukarieh, R., Bourdeau, A., Brem, B., Teodoro, J. G., Greger, H., Tremblay, M. L., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005223 · Cited by 302 · see citing works

tRNA over-expression in breast cancer and functional consequences

Pavon-Eternod, M., Gomes, S., Geslain, R., Dai, Q., Rosner, M. R., & Pan, T. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp787 · Cited by 296 · see citing works

Myc and mTOR converge on a common node in protein synthesis control that confers synthetic lethality in Myc-driven cancers

Pourdehnad, M., Truitt, M., Siddiqi, I. N., Ducker, G. S., Shokat, K. M., & Ruggero, D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310230110 · Cited by 288 · see citing works

A new paradigm for translational control: inhibition via 5'-3' mRNA tethering by Bicoid and the eIF4E cognate 4EHP.

Cho, P. F., Poulin, F., Yoon, A. C.-P., Cho-Park, I. B., Chicoine, J., Lasko, P., & Sonenberg, N. (2005) · Cell · doi:10.1016/j.cell.2005.02.024 · Cited by 279 · see citing works

Mutation of the CDKN2A 5' UTR creates an aberrant initiation codon and predisposes to melanoma

Liu, L., Dilworth, D., Gao, L., Monzon, J. G., Summers, A., Lassam, N. J., & Hogg, D. (1999) · Nature Genetics · doi:10.1038/5082 · Cited by 276 · see citing works

Diagnostic and prognostic signatures from the small non-coding RNA transcriptome in prostate cancer

Martens‐Uzunova, E. S., Jalava, S. E., Dits, N. F. J., van Leenders, G. J. L. H., Møller, S., Trapman, J., Bangma, C. H., Litman, T., Visakorpi, T., & Jenster, G. W. (2011) · Oncogene · doi:10.1038/onc.2011.304 · Cited by 271 · see citing works

C/EBPβ at the core of the TGFβ cytostatic response and its evasion in metastatic breast cancer cells

Gomis, R. R., Alarcón, C. R., Nadal, C., Poznak, C. H. V., & Massagué, J. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.07.019 · Cited by 270 · see citing works

hiCLIP reveals the in vivo atlas of mRNA secondary structures recognized by Staufen 1

Sugimoto, Y., Vigilante, A., Darbo, É., Zirra, A., Militti, C., D’Ambrogio, A., Luscombe, N. M., & Ule, J. (2015) · Nature · doi:10.1038/nature14280 · Cited by 270 · see citing works

La-related Protein 1 (LARP1) Represses Terminal Oligopyrimidine (TOP) mRNA Translation Downstream of mTOR Complex 1 (mTORC1)

Fonseca, B. D., Zakaria, C., Jia, J.-J., Graber, T. E., Svitkin, Y. V., Tahmasebi, S., Healy, D., Hoang, H., Jensen, J. M., Diao, I. T., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.621730 · Cited by 264 · see citing works

Protein and nucleotide biosynthesis are coupled by a single rate-limiting enzyme, PRPS2, to drive cancer

Cunningham, J. T., Moreno, M. V., Lodi, A., Ronen, S. M., & Ruggero, D. (2014) · Cell · doi:10.1016/j.cell.2014.03.052 · Cited by 260 · see citing works

ERK-Dependent Phosphorylation of the Transcription Initiation Factor TIF-IA Is Required for RNA Polymerase I Transcription and Cell Growth

Zhao, J., Yuan, X., Frödin, M., & Grummt, I. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00036-4 · Cited by 259 · see citing works

Phosphorylation of eIF4E promotes EMT and metastasis via translational control of SNAIL and MMP-3

Robichaud, N., Rincon, S. V. D., Huor, B., Alain, T., Petruccelli, L. A., Hearnden, J., Gonçalves, C., Grotegut, S., Spruck, C., Furic, L., et al. (2014) · Oncogene · doi:10.1038/onc.2014.146 · Cited by 259 · see citing works

Increased expression of eukaryotic translation initiation factors eIF-4E and eIF-2 alpha in response to growth induction by c-myc.

Rosenwald, I. B., Rhoads, D. B., Callanan, L., Isselbacher, K. J., & Schmidt, E. V. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.13.6175 · Cited by 256 · see citing works

A Novel mTOR-Regulated Phosphorylation Site in Elongation Factor 2 Kinase Modulates the Activity of the Kinase and Its Binding to Calmodulin

Browne, G. J., & Proud, C. G. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.2986-2997.2004 · Cited by 256 · see citing works

Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5′TOP mRNA translationPreprint

Tcherkezian, J., Cargnello, M., Roméo, Y., Huttlin, E. L., Lavoie, G., Gygi, S. P., & Roux, P. P. (2014) · Genes & Development · doi:10.1101/gad.231407.113 · Cited by 255 · see citing works

An Immediate Response of Ribosomal Transcription to Growth Factor Stimulation in Mammals Is Mediated by ERK Phosphorylation of UBF

Stefanovsky, V. Y., Pelletier, G., Hannan, R. D., Gagnon-Kugler, T., Rothblum, L. I., & Moss, T. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00384-7 · Cited by 242 · see citing works

Dissecting the expression landscape of RNA-binding proteins in human cancers

Kechavarzi, B., & Janga, S. C. (2014) · Genome biology · doi:10.1186/gb-2014-15-1-r14 · Cited by 242 · see citing works

Alternative Translation of the Proto-oncogene c-mycby an Internal Ribosome Entry Site

Nanbru, C., Lafon, I., Audigier, S., Gensac, M.-C., Vagner, S., Huez, G. A., & Prats, A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.32061 · Cited by 242 · see citing works

Mammalian ALKBH8 Possesses tRNA Methyltransferase Activity Required for the Biogenesis of Multiple Wobble Uridine Modifications Implicated in Translational Decoding

Songe-Møller, L., van den Born, E., Leihne, V., Vågbø, C. B., Andersstuen, T. K., Krokan, H. E., Kirpekar, F., Falnes, P. Ø., & Klungland, A. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01602-09 · Cited by 238 · see citing works

Programmed Translational Readthrough Generates Antiangiogenic VEGF-Ax

Eswarappa, S. M., Potdar, A. A., Koch, W. J., Fan, Y., Vasu, K. I., Lindner, D. J., Willard, B. B., Graham, L. M., DiCorleto, P. E., & Fox, P. L. (2014) · Cell · doi:10.1016/j.cell.2014.04.033 · Cited by 237 · see citing works

An Essential E Box in the Promoter of the Gene Encoding the mRNA Cap-Binding Protein (Eukaryotic Initiation Factor 4E) Is a Target for Activation by c-myc

Jones, R. M., Branda, J. A., Johnston, K. A., Polymenis, M., Gadd, M. A., Rustgi, A. K., Callanan, L., & Schmidt, E. V. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4754 · Cited by 237 · see citing works

Tissue-specific codon usage and the expression of human genes

Plotkin, J. B., Robins, H. S., & Levine, A. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404957101 · Cited by 235 · see citing works

Hypoxia Inhibits Protein Synthesis through a 4E-BP1 and Elongation Factor 2 Kinase Pathway Controlled by mTOR and Uncoupled in Breast Cancer Cells

Connolly, E., Braunstein, S., Formenti, S., & Schneider, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.10.3955-3965.2006 · Cited by 233 · see citing works

mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1

Kantidakis, T., Ramsbottom, B. A., Birch, J. L., Dowding, S. N., & White, R. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1005188107 · Cited by 218 · see citing works

The GAIT system: a gatekeeper of inflammatory gene expression

Mukhopadhyay, R., Jia, J., Arif, A., Ray, P. S., & Fox, P. L. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.03.004 · Cited by 216 · see citing works

PI3K-targeted therapy can be evaded by gene amplification along the MYC-eukaryotic translation initiation factor 4E (eIF4E) axis

Ilić, N., Utermark, T., Widlund, H. R., & Roberts, T. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108237108 · Cited by 213 · see citing works

Translational enhancement of mdm2 oncogene expression in human tumor cells containing a stabilized wild-type p53 protein.

Landers, J. E., Cassel, S., & George, D. L. (1997) · PubMed · Cited by 210 · see citing works

Two internal ribosome entry sites mediate the translation of p53 isoforms

Ray, P. S., Grover, R., & Das, S. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400623 · Cited by 209 · see citing works

Repression of RNA polymerase III transcription by the retinoblastoma protein

White, R. J., Trouche, D., Martin, K., Jackson, S. P., & Kouzarides, T. (1996) · Nature · doi:10.1038/382088a0 · Cited by 205 · see citing works

Human AlkB Homolog ABH8 Is a tRNA Methyltransferase Required for Wobble Uridine Modification and DNA Damage Survival

Fu, D., Brophy, J. A. N., Chan, C. T. Y., Atmore, K. A., Begley, U., Paules, R. S., Dedon, P. C., Begley, T. J., & Samson, L. D. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01604-09 · Cited by 204 · see citing works

Immunological detection of the messenger RNA cap-binding protein.

Hiremath, L., Webb, N. R., & Rhoads, R. E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39529-7 · Cited by 202 · see citing works

Kinetic analysis reveals successive steps leading to miRNA‐mediated silencing in mammalian cells

Béthune, J., Artus-Revel, C. G., & Filipowicz, W. (2012) · EMBO Reports · doi:10.1038/embor.2012.82 · Cited by 201 · see citing works

Transcriptome-wide characterization of the eIF4A signature highlights plasticity in translation regulation

Rubio, C. A., Weisburd, B., Holderfield, M., Arias, C., Fang, E., DeRisi, J. L., & Fanidi, A. (2014) · Genome Biology · doi:10.1186/s13059-014-0476-1 · Cited by 200 · see citing works

A perspective on mammalian upstream open reading frame function

Somers, J., Pöyry, T. A. A., & Willis, A. E. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.020 · Cited by 199 · see citing works

Initiation of Apaf-1 translation by internal ribosome entry

Coldwell, M. J., Mitchell, S. A., Stoneley, M., MacFarlane, M., & Willis, A. E. (2000) · Oncogene · doi:10.1038/sj.onc.1203407 · Cited by 199 · see citing works

A Novel 4EHP-GIGYF2 Translational Repressor Complex Is Essential for Mammalian Development

Morita, M., Ler, L. W., Fabian, M. R., Siddiqui, N., Mullin, M. J., Henderson, V. C., Alain, T., Fonseca, B. D., Karashchuk, G., Bennett, C. F., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00455-12 · Cited by 198 · see citing works

Identification of an mRNP Complex Regulating Tumorigenesis at the Translational Elongation Step

Hussey, G. S., Chaudhury, A., Dawson, A. E., Lindner, D. J., Knudsen, C. R., Wilce, M. C. J., Merrick, W. C., & Howe, P. H. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.003 · Cited by 193 · see citing works

p53 is a general repressor of RNA polymerase III transcription

Cairns, C. A., & White, R. J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.11.3112 · Cited by 190 · see citing works

Induction of ribosomal genes and hepatocyte hypertrophy by adenovirus-mediated expression of c-Myc in vivo

Kim, S., Li, Q., Dang, C. V., & Lee, L. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.200372597 · Cited by 187 · see citing works

Eukaryotic elongation factor 2 kinase, an unusual enzyme with multiple roles

Kenney, J. W., Moore, C. E., Xuemin, W., & Proud, C. G. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.04.003 · Cited by 182 · see citing works

Regulation of XIAP Translation and Induction by MDM2 following Irradiation

Gu, L., Zhu, N., Zhang, H., Durden, D. L., Feng, Y., & Zhou, M. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.03.002 · Cited by 178 · see citing works

Mitotic cell-cycle progression is regulated by CPEB1 and CPEB4-dependent translational control

Novoa, I., Gallego, J. G., Ferreira, P. G., & Méndez, R. (2010) · Nature Cell Biology · doi:10.1038/ncb2046 · Cited by 177 · see citing works

APC Is an RNA-Binding Protein, and Its Interactome Provides a Link to Neural Development and Microtubule Assembly

Preitner, N., Quan, J., Nowakowski, D. W., Hancock, M., Shi, J., Tcherkezian, J., Young‐Pearse, T. L., & Flanagan, J. G. (2014) · Cell · doi:10.1016/j.cell.2014.05.042 · Cited by 174 · see citing works

ALKBH8-mediated formation of a novel diastereomeric pair of wobble nucleosides in mammalian tRNA

van den Born, E., Vågbø, C. B., Songe-Møller, L., Leihne, V., Lien, G. F., Leszczyńska, G., Małkiewicz, A. J., Krokan, H. E., Kirpekar, F., Klungland, A., et al. (2011) · Nature Communications · doi:10.1038/ncomms1173 · Cited by 174 · see citing works

Loss of Function of the Tumor Suppressor DKC1 Perturbs p27 Translation Control and Contributes to Pituitary Tumorigenesis

Bellodi, C., Krasnykh, O., Haynes, N., Theodoropoulou, M., Peng, G., Montanaro, L., & Ruggero, D. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4730 · Cited by 173 · see citing works

The mRNA 5 ' Cap-Binding Protein, eIF-4E, Cooperates with v-myc or E1A in the Transformation of Primary Rodent Fibroblasts

Lazaris-Karatzas, A., & Sonenberg, N. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.3.1234 · Cited by 171 · see citing works

Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity

Feoktistova, K., Tuvshintogs, E., Do, A., & Fraser, C. S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303781110 · Cited by 169 · see citing works

Deregulation of oncogene‐induced senescence and p53 translational control in X‐linked dyskeratosis congenita

Bellodi, C., Kopmar, N. E., & Ruggero, D. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.83 · Cited by 168 · see citing works

CPEB1 coordinates alternative 3′-UTR formation with translational regulation

Bava, F.-A., Eliscovich, C., Ferreira, P. G., Miñana, B., Ben-Dov, C., Guigó, R., Valcárcel, J., & Méndez, R. (2013) · Nature · doi:10.1038/nature11901 · Cited by 164 · see citing works

Preferential Translation of Internal Ribosome Entry Site-containing mRNAs during the Mitotic Cycle in Mammalian Cells

Qin, X., & Sarnow, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312854200 · Cited by 160 · see citing works

Mechanisms of regulation of RNA polymerase III‐dependent transcription by TORC1

Wei, Y., Tsang, C. K., & Zheng, X.-F. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.179 · Cited by 156 · see citing works

Hu Antigen R (HuR) Functions as an Alternative Pre-mRNA Splicing Regulator of Fas Apoptosis-promoting Receptor on Exon Definition

Izquierdo, J. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800017200 · Cited by 156 · see citing works

BCL-2 Translation Is Mediated via Internal Ribosome Entry during Cell Stress

Sherrill, K. W., Byrd, M. P., Eden, M. E. V., & Lloyd, R. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402727200 · Cited by 155 · see citing works

Regulation of rat ornithine decarboxylase mRNA translation by its 5'-untranslated region.

Manzella, J. M., & Blackshear, P. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38471-6 · Cited by 154 · see citing works

Rare Codons Regulate KRas Oncogenesis

Lampson, B. L., Pershing, N. L., Prinz, J. A., Lacsina, J. R., Marzluff, W. F., Nicchitta, C. V., MacAlpine, D. M., & Counter, C. M. (2012) · Current Biology · doi:10.1016/j.cub.2012.11.031 · Cited by 150 · see citing works

Ribosome biogenesis in cancer: new players and therapeutic avenues

Pelletier, J., Thomas, G., & Volarević, S. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.104 · Cited by 802 · see citing works

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 765 · see citing works

The m6A reader YTHDF1 promotes ovarian cancer progression via augmenting EIF3C translation

Liu, T., Wei, Q., Jin, J., Luo, Q., Liu, Y., Yu, Y., Cheng, C., Li, L., Pi, J., Si, Y., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa048 · Cited by 751 · see citing works

Pseudouridylation of tRNA-Derived Fragments Steers Translational Control in Stem Cells

Guzzi, N., Cieśla, M., Ngoc, P. C. T., Lang, S., Arora, S., Dimitriou, M., Pimková, K., Sommarin, M. N. E., Munita, R., Lubas, M., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.008 · Cited by 521 · see citing works

Translational Control in CancerPreprint

Robichaud, N., Sonenberg, N., Ruggero, D., & Schneider, R. J. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032896 · Cited by 309 · see citing works

Erratum: New frontiers in translational control of the cancer genome

Truitt, M., & Ruggero, D. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.30 · Cited by 306 · see citing works

Alpha-foetoprotein (AFP): A multi-purpose marker in hepatocellular carcinoma

Sauzay, C., Petit, A., Bourgeois, A.-M., Barbare, J., Chauffert, B., Galmiche, A., & Houessinon, A. (2016) · Clinica Chimica Acta · doi:10.1016/j.cca.2016.10.006 · Cited by 293 · see citing works

The plasticity of mRNA translation during cancer progression and therapy resistance

Fabbri, L., Chakraborty, A., Robert, C., & Vagner, S. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00380-y · Cited by 273 · see citing works

Codon-specific translation reprogramming promotes resistance to targeted therapy

Rapino, F., Delaunay, S., Rambow, F., Zhou, Z., Tharun, L., De Tullio, P., Sin, O., Shostak, K., Schmitz, S., Piepers, J., et al. (2018) · Nature · doi:10.1038/s41586-018-0243-7 · Cited by 271 · see citing works

Translation deregulation in human disease

Tahmasebi, S., Khoutorsky, A., Mathews, M. B., & Sonenberg, N. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0034-x · Cited by 255 · see citing works

Translational control of tumor immune escape via the eIF4F–STAT1–PD-L1 axis in melanoma

Cerezo, M., Guemiri, R., Druillennec, S., Girault, I., Malka-Mahieu, H., Shen, S., Allard, D., Martineau, S., Welsch, C., Agoussi, S., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0217-1 · Cited by 249 · see citing works

Hallmarks of ribosomopathies

Kampen, K. R., Sulima, S. O., Vereecke, S., & Keersmaecker, K. D. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz637 · Cited by 217 · see citing works

METTL13 methylation of eEF1A increases translational output to promote tumorigenesis

Liu, S., Hausmann, S., Carlson, S. M., Fuentes, M. E., Francis, J., Pillai, R., Lofgren, S. M., Hulea, L., Tandoc, K. V., Lu, J.-W., et al. (2019) · Cell · doi:10.1016/j.cell.2018.11.038 · Cited by 175 · see citing works

METTL1 promotes hepatocarcinogenesis via m 7 G tRNA modification‐dependent translation control

Chen, Z., Zhu, W., Zhu, S., Sun, K., Liao, J., Liu, H., Dai, Z., Han, H., Ren, X., Yang, Q., et al. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.661 · Cited by 204 · see citing works

Neat1 is a p53-inducible lincRNA essential for transformation suppressionPreprint

Mello, S. S., Sinow, C., Raj, N., Mazur, P. K., Bieging-Rolett, K. T., Brož, D. K., Conklin, J. F., Vogel, H. S., Wood, L. D., Sage, J., et al. (2017) · Genes & Development · doi:10.1101/gad.284661.116 · Cited by 203 · see citing works

Structure-based Design of Pyridone–Aminal eFT508 Targeting Dysregulated Translation by Selective Mitogen-activated Protein Kinase Interacting Kinases 1 and 2 (MNK1/2) Inhibition

Reich, S., Sprengeler, P. A., Chiang, G. G., Appleman, J. R., Chen, J. W., Clarine, J., Eam, B., Ernst, J. T., Han, Q., Goel, V., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01795 · Cited by 185 · see citing works

RNA-binding Proteins in Regulating mRNA Stability and Translation: Roles and Mechanisms in Cancer

Li, W., Deng, X., & Chen, J.-J. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.03.025 · Cited by 168 · see citing works

How Ribosomes Translate Cancer

Sulima, S. O., Hofman, I. J., Keersmaecker, K. D., & Dinman, J. D. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-0550 · Cited by 174 · see citing works

RNA-binding proteins and cancer metastasis

Wang, S., Sun, Z., Lei, Z., & Zhang, H. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.03.018 · Cited by 175 · see citing works

Development of a stress response therapy targeting aggressive prostate cancer

Nguyen, H. G., Conn, C. S., Kye, Y., Xue, L., Forester, C. M., Cowan, J. E., Hsieh, A. C., Cunningham, J. T., Truillet, C., Tameire, F., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aar2036 · Cited by 164 · see citing works

Ribosomal DNA copy number loss and sequence variation in cancer

Xu, B., Li, H., Perry, J. M., Singh, V. P., Unruh, J. R., Yu, Z., Zakari, M., McDowell, W., Li, L., & Gerton, J. L. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006771 · Cited by 148 · see citing works

Design of Development Candidate eFT226, a First in Class Inhibitor of Eukaryotic Initiation Factor 4A RNA Helicase

Ernst, J. T., Thompson, P. A., Nilewski, C., Sprengeler, P. A., Sperry, S., Packard, G., Michels, T., Xiang, A., Tran, C., Wegerski, C. J., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00182 · Cited by 150 · see citing works

Polyamine synthesis as a target of MYC oncogenes

Bachmann, A. S., & Geerts, D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.003336 · Cited by 148 · see citing works

A single H/ACA small nucleolar RNA mediates tumor suppression downstream of oncogenic RAS

McMahon, M. E., Contreras, A., Holm, M., Uechi, T., Forester, C. M., Pang, X., Jackson, C. B., Calvert, M., Chen, B., Quigley, D. A., et al. (2019) · eLife · doi:10.7554/elife.48847 · Cited by 137 · see citing works

Transfer RNA-Derived Small RNAs: Another Layer of Gene Regulation and Novel Targets for Disease Therapeutics

Kim, H. K., Yeom, J., & Kay, M. A. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.09.013 · Cited by 134 · see citing works

Ribosomal DNA copy number amplification and loss in human cancers is linked to tumor genetic context, nucleolus activity, and proliferation

Wang, M., & Lemos, B. (2017) · PLoS Genetics · doi:10.1371/journal.pgen.1006994 · Cited by 129 · see citing works

Translational Control Mechanisms in Persistent Pain

Khoutorsky, A., & Price, T. J. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.11.006 · Cited by 127 · see citing works

The oncomicropeptide APPLE promotes hematopoietic malignancy by enhancing translation initiation

Sun, L.-Y., Wang, W., Han, C., Huang, W., Sun, Y., Fang, K., Zeng, Z., Yang, Q., Pan, Q., Chen, T., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.033 · Cited by 126 · see citing works

The ribosome, (slow) beating heart of cancer (stem) cell

Bastide, A., & David, A. (2018) · Oncogenesis · doi:10.1038/s41389-018-0044-8 · Cited by 119 · see citing works

Pseudouridine-modified tRNA fragments repress aberrant protein synthesis and predict leukaemic progression in myelodysplastic syndrome

Guzzi, N., Muthukumar, S., Cieśla, M., Todisco, G., Ngoc, P. C. T., Madej, M., Munita, R., Fazio, S., Ekström, S., Blanco, T. M., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00852-9 · Cited by 124 · see citing works

Protein synthesis control in cancer: selectivity and therapeutic targeting

Kovalski, J. R., Kuzuoğlu‐Öztürk, D., & Ruggero, D. (2022) · The EMBO Journal · doi:10.15252/embj.2021109823 · Cited by 120 · see citing works

PM2.5 promotes NSCLC carcinogenesis through translationally and transcriptionally activating DLAT-mediated glycolysis reprograming

Chen, Q., Wang, Y., Yang, L. T., Sun, L., Wen, Y., Huang, Y., Gao, K., Yang, W., Bai, F., Ling, L., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02437-8 · Cited by 120 · see citing works

CDK1 couples proliferation with protein synthesis

Haneke, K., Schott, J., Lindner, D., Hollensen, A. K., Damgaard, C. K., Mongis, C., Knop, M., Palm, W., Ruggieri, A., & Stoecklin, G. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201906147 · Cited by 109 · see citing works

Molecular Pathways: The eIF4F Translation Initiation Complex—New Opportunities for Cancer Treatment

Malka-Mahieu, H., Newman, M., Désaubry, L., Robert, C., & Vagner, S. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2362 · Cited by 105 · see citing works

Translational control of aberrant stress responses as a hallmark of cancer

El-Naggar, A. M., & Sorensen, P. H. B. (2018) · The Journal of Pathology · doi:10.1002/path.5030 · Cited by 102 · see citing works

Quantitative time-resolved chemoproteomics reveals that stable O -GlcNAc regulates box C/D snoRNP biogenesis

Qin, W., Lv, P., Fan, X., Quan, B., Zhu, Y., Qin, K., Chen, Y., Wang, C., & Chen, X. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702688114 · Cited by 98 · see citing works

Ribosome ADP-ribosylation inhibits translation and maintains proteostasis in cancers

Challa, S., Khulpateea, B. R., Nandu, T. S., Camacho, C. V., Ryu, K. W., Chen, H., Peng, Y. S., Lea, J. S., & Kraus, W. L. (2021) · Cell · doi:10.1016/j.cell.2021.07.005 · Cited by 97 · see citing works

MNK Inhibition Sensitizes <i>KRAS</i> -Mutant Colorectal Cancer to mTORC1 Inhibition by Reducing eIF4E Phosphorylation and c-MYC Expression

Knight, J. R. P., Alexandrou, C., Skalka, G. L., Vlahov, N., Pennel, K., Officer, L., Teodosio, A., Kanellos, G., Gay, D. M., May-Wilson, S., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0652 · Cited by 96 · see citing works

Translation elongation rate varies among organs and decreases with age

Gerashchenko, M. V., Péterfi, Z., Yim, S. H., & Gladyshev, V. N. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1103 · Cited by 95 · see citing works

A MYC–GCN2–eIF2α negative feedback loop limits protein synthesis to prevent MYC-dependent apoptosis in colorectal cancer

Schmidt, S., Gay, D. M., Uthe, F. W., Denk, S., Paauwe, M., Matthes, N., Diefenbacher, M. E., Bryson, S., Warrander, F., Erhard, F., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0408-0 · Cited by 94 · see citing works

Ribosomal RNA 2′O-methylation as a novel layer of inter-tumour heterogeneity in breast cancer

Marcel, V., Kielbassa, J., Marchand, V., Natchiar, K., Paraqindes, H., Long, F. N. V., Ayadi, L., Bourguignon‐Igel, V., Monaco, P. L., Monchiet, D., et al. (2020) · NAR Cancer · doi:10.1093/narcan/zcaa036 · Cited by 94 · see citing works

Linking the YTH domain to cancer: the importance of YTH family proteins in epigenetics

Shi, R., Ying, S., Li, Y., Zhu, L., Wang, X., & Jin, H. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03625-8 · Cited by 93 · see citing works

Spatial proteomic characterization of HER2-positive breast tumors through neoadjuvant therapy predicts response

(2021) · doi:10.1038/s43018-021-00190-z · Cited by 92 · see citing works

Glucocorticoids and the cytokines IL-12, IL-15, and IL-18 present in the tumor microenvironment induce PD-1 expression on human natural killer cells

Quatrini, L., Vacca, P., Tumino, N., Besi, F., Pace, A. L. D., Scordamaglia, F., Martini, S., Munari, E., Mingari, M. C., Ugolini, S., et al. (2020) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2020.04.044 · Cited by 90 · see citing works

Targeting RNA helicases in cancer: The translation trap

van Voss, M. R. H., van Diest, P. J., & Raman, V. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.09.006 · Cited by 87 · see citing works

The T-cell leukemia-associated ribosomal RPL10 R98S mutation enhances JAK-STAT signaling

Girardi, T., Vereecke, S., Sulima, S. O., Khan, Y. A., Fancello, L., Briggs, J., Schwab, C. J., de Beeck, J. O., Verbeeck, J., Royaert, J., et al. (2017) · Leukemia · doi:10.1038/leu.2017.225 · Cited by 86 · see citing works

mTOR-dependent translation amplifies microglia priming in aging mice

Keane, L., Antignano, I., Riechers, S., Zollinger, R., Dumas, A. A., Offermann, N., Bernis, M. E., Russ, J., Graelmann, F. J., McCormick, P. N., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci132727 · Cited by 86 · see citing works

SWI/SNF component <i>ARID1A</i> restrains pancreatic neoplasia formation

Wang, S. C., Nassour, I., Xiao, S., Zhang, S., Luo, X., Lee, J., Li, L., Sun, X., Nguyen, L. H., Chuang, J.-C., et al. (2019) · Gut · doi:10.1136/gutjnl-2017-315490 · Cited by 85 · see citing works

The homeostatic regulation of ribosome biogenesis

Ni, C., & Buszczak, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.043 · Cited by 82 · see citing works

Nutrient Deprivation Elicits a Transcriptional and Translational Inflammatory Response Coupled to Decreased Protein Synthesis

Gameiro, P. A., & Struhl, K. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.021 · Cited by 84 · see citing works

Global analysis of tRNA and translation factor expression reveals a dynamic landscape of translational regulation in human cancers

Zhang, Z., Ye, Y., Gong, J., Ruan, H., Liu, C., Xiang, Y., Cai, C. C., Guo, A., Ling, J., Diao, L., et al. (2018) · Communications Biology · doi:10.1038/s42003-018-0239-8 · Cited by 81 · see citing works

Emerging Role of Eukaryote Ribosomes in Translational Control

Venezia, N. D., Vincent, A., Marcel, V., Catez, F., & Diaz, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20051226 · Cited by 77 · see citing works

Coordinated Control of mRNA and rRNA Processing Controls Embryonic Stem Cell Pluripotency and Differentiation

Corsini, N. S., Peer, A. M., Möseneder, P., Roiuk, M., Burkard, T. R., Theussl, H., Moll, I., & Knoblich, J. A. (2018) · Cell stem cell · doi:10.1016/j.stem.2018.03.002 · Cited by 79 · see citing works

Suppression of Ribosomal Pausing by eIF5A Is Necessary to Maintain the Fidelity of Start Codon Selection

Manjunath, H., Zhang, H., Rehfeld, F., Han, J., Chang, T.-C., & Mendell, J. T. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.129 · Cited by 74 · see citing works

Cancer cells employ an evolutionarily conserved polyploidization program to resist therapy

Pienta, K. J., Hammarlund, E. U., Austin, R. H., Axelrod, R., Brown, J. S., & Amend, S. R. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.11.016 · Cited by 77 · see citing works

Desmosomes as Signaling Hubs in the Regulation of Cell Behavior

Müller, L., Hatzfeld, M., & Keil, R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.745670 · Cited by 78 · see citing works

Novel insights into the emerging roles of tRNA-derived fragments in mammalian development

Guzzi, N., & Bellodi, C. (2020) · RNA Biology · doi:10.1080/15476286.2020.1732694 · Cited by 77 · see citing works

Role of Cyclin-Dependent Kinase 1 in Translational Regulation in the M-Phase

Kalous, J., Jansová, D., & Šušor, A. (2020) · Cells · doi:10.3390/cells9071568 · Cited by 54 · see citing works

Driver mutations of the adenoma-carcinoma sequence govern the intestinal epithelial global translational capacity

Smit, W. L., Spaan, C. N., de Boer, R. J., Ramesh, P., Garcia, T. M., Meijer, B. J., Vermeulen, J. L. M., Lezzerini, M., MacInnes, A. W., Köster, J., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912772117 · Cited by 77 · see citing works

eIF4E-Dependent Translational Control: A Central Mechanism for Regulation of Pain Plasticity

Uttam, S., Wong, C., Price, T. J., & Khoutorsky, A. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00470 · Cited by 75 · see citing works

Translational Dysregulation in Cancer: Molecular Insights and Potential Clinical Applications in Biomarker Development

Vaklavas, C., Blume, S. W., & Grizzle, W. E. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00158 · Cited by 71 · see citing works

Regulators of cardiac fibroblast cell state

Bretherton, R. C., Bugg, D., Olszewski, E., & Davis, J. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.04.002 · Cited by 71 · see citing works

Dysfunctional tRNA reprogramming and codon-biased translation in cancer

Dedon, P., & Begley, T. J. (2022) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2022.09.007 · Cited by 66 · see citing works

Inhibiting the oncogenic translation program is an effective therapeutic strategy in multiple myeloma

Manier, S., Huynh, D., Shen, Y. J., Zhou, J., Yusufzai, T. M., Salem, K. Z., Ebright, R. Y., Shi, J., Park, J., Glavey, S. V., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aal2668 · Cited by 71 · see citing works

Translational control and the cancer cell response to stress

Robichaud, N., & Sonenberg, N. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.05.007 · Cited by 72 · see citing works

Human eIF3: from ‘blobology’ to biological insight

Cate, J. H. D. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0176 · Cited by 68 · see citing works

Ribosome Biogenesis Alterations in Colorectal Cancer

Nait-Slimane, S., Marcel, V., Fenouil, T., Catez, F., Saurin, J., Bouvet, P., Diaz, J., & Mertani, H. C. (2020) · Cells · doi:10.3390/cells9112361 · Cited by 68 · see citing works

Lineage-specific roles of the cytoplasmic polyadenylation factor CPEB4 in the regulation of melanoma drivers

Pérez‐Guijarro, E., Karras, P., Cifdaloz, M., Martínez-Herranz, R., Cañón, E., Graña‐Castro, O., Horcajada‐Reales, C., Alonso‐Curbelo, D., Calvo, T. G., Goméz-López, G., et al. (2016) · Nature Communications · doi:10.1038/ncomms13418 · Cited by 67 · see citing works

Breast Cancer Suppression by Progesterone Receptors Is Mediated by Their Modulation of Estrogen Receptors and RNA Polymerase III

Finlay-Schultz, J., Gillen, A. E., Brechbuhl, H. M., Ivie, J., Matthews, S. B., Jacobsen, B. M., Bentley, D. L., Kabos, P., & Sartorius, C. A. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-3541 · Cited by 66 · see citing works

The integrated stress response in cancer progression: a force for plasticity and resistance

Lines, C. L., McGrath, M. J., Dorwart, T. J., & Conn, C. S. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1206561 · Cited by 69 · see citing works

Targeting the Human 80S Ribosome in Cancer: From Structure to Function and Drug Design for Innovative Adjuvant Therapeutic Strategies

Gilles, A., Fréchin, L., Natchiar, K., Biondani, G., von Loeffelholz, O., Holvec, S., Malaval, J., Winum, J., Klaholz, B. P., & Peyron, J. (2020) · Cells · doi:10.3390/cells9030629 · Cited by 66 · see citing works

The EZH2–PHACTR2–AS1–Ribosome Axis induces Genomic Instability and Promotes Growth and Metastasis in Breast Cancer

Chu, W., Zhang, X., Qi, L., Fu, Y., Wang, P., Zhao, W., Du, J., Zhang, J., Zhan, J., Wang, Y., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3326 · Cited by 65 · see citing works

A Closer Look at Estrogen Receptor Mutations in Breast Cancer and Their Implications for Estrogen and Antiestrogen Responses

Clusan, L., Goff, P. L., Flouriot, G., & Pakdel, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020756 · Cited by 65 · see citing works

RNA-binding protein FXR1 drives cMYC translation by recruiting eIF4F complex to the translation start site

George, J., Li, Y., Kadamberi, I. P., Parashar, D., Tsaih, S.-W., Gupta, P., Geethadevi, A., Chen, C., Ghosh, C., Sun, Y., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109934 · Cited by 65 · see citing works

Revealing nascent proteomics in signaling pathways and cell differentiation

Forester, C. M., Zhao, Q. C., Phillips, N. J., Urisman, A., Chalkley, R. J., Osés-Prieto, J. A., Zhang, L., Ruggero, D., & Burlingame, A. L. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707514115 · Cited by 67 · see citing works

mTORC1-Mediated Inhibition of 4EBP1 Is Essential for Hedgehog Signaling-Driven Translation and Medulloblastoma

Wu, C., Hou, S., Orr, B. A., Kuo, B., Youn, Y. H., Ong, T., Roth, F., Eberhart, C. G., Robinson, G. W., Solecki, D. J., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.10.011 · Cited by 58 · see citing works

uORF-mediated translational control: recently elucidated mechanisms and implications in cancer

Chen, H.-H., & Tarn, W. (2019) · RNA Biology · doi:10.1080/15476286.2019.1632634 · Cited by 58 · see citing works

40 Years of Research Put p53 in Translation

Marcel, V., Long, F. N. V., & Diaz, J. (2018) · Cancers · doi:10.3390/cancers10050152 · Cited by 60 · see citing works

RNA binding motif protein 10 suppresses lung cancer progression by controlling alternative splicing of eukaryotic translation initiation factor 4H

Zhang, S., Bao, Y., Shen, X., Pan, Y., Sun, Y., Xiao, M., Chen, K., Wei, H., Zuo, J., Saffen, D., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.103067 · Cited by 59 · see citing works

tRNA-derived small RNAs: Mechanisms and potential roles in cancers

Wang, Y., Weng, Q., Ge, J., Zhang, X., Guo, J., & Ye, G. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2021.12.009 · Cited by 60 · see citing works

Stress Granules in Cancer

Song, M., & Grabocka, E. (2020) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2020_37 · Cited by 59 · see citing works

Genetically encoded bioorthogonal tryptophan decaging in living cells

Zhu, Y., Ding, W., Chen, Y., Shan, Y., Liu, C., Fan, X., Lin, S., & Chen, P. R. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01463-7 · Cited by 59 · see citing works

Oncogenic translation directs spliceosome dynamics revealing an integral role for SF3A3 in breast cancer

Cieśla, M., Ngoc, P. C. T., Cordero, E., Martínez, Á. S., Morsing, M., Muthukumar, S., Beneventi, G., Madej, M., Munita, R., Jönsson, T., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.034 · Cited by 59 · see citing works

METTL16 Promotes Translation and Lung Tumorigenesis by Sequestering Cytoplasmic eIF4E2

Wang, F., Zhang, J., Lin, X., Yang, L., Zhou, Q., Mi, X., Li, Q., Wang, S., Li, D., Liu, X., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2023.112150 · Cited by 57 · see citing works

Role of hypoxia in Diffuse Large B-cell Lymphoma: Metabolic repression and selective translation of HK2 facilitates development of DLBCL

Bhalla, K., Jaber, S. M., Nanaji, N. M., Underwood, K. F., Beheshti, A., Landon, A. L., Bhandary, B., Bastian, P., Evens, A. M., Haley, J. D., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-19182-8 · Cited by 56 · see citing works

Transcriptional-translational conflict is a barrier to cellular transformation and cancer progression

Jana, S., Brahma, S., Arora, S., Wladyka, C. L., Hoang, P., Blinka, S. M., Hough, R. P., Horn, J. L., Liu, Y., Wang, L., et al. (2023) · Cancer Cell · doi:10.1016/j.ccell.2023.03.021 · Cited by 56 · see citing works

tRNA Modification: Is Cancer Having a Wobble?

Rapino, F. A., Delaunay, S., Zhou, Z., Chariot, A., & Close, P. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.02.004 · Cited by 56 · see citing works

mTORC1 regulates cell survival under glucose starvation through 4EBP1/2-mediated translational reprogramming of fatty acid metabolism

Levy, T., Voeltzke, K., Hruby, L. A., Alasad, K., Bas, Z., Snaebjornsson, M. T., Marciano, R., Scharov, K., Planque, M., Vriens, K., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48386-y · Cited by 53 · see citing works

Alteration of ribosome function upon 5-fluorouracil treatment favors cancer cell drug-tolerance

Thérizols, G., Bash-Imam, Z., Panthu, B., Machon, C., Vincent, A., Ripoll, J., Nait-Slimane, S., Chalabi‐Dchar, M., Gaucherot, A., Garcia, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-021-27847-8 · Cited by 52 · see citing works

Errors in translational decoding: tRNA wobbling or misincorporation?

Ou, X., Cao, J., Cheng, A., Peppelenbosch, M. P., & Pan, Q. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008017 · Cited by 51 · see citing works

Nucleoporin Nup155 is part of the p53 network in liver cancer

Hölzer, K., Ori‬‬, A., Cooke, A. M., Dauch, D., Drucker, E., Riemenschneider, P., Andrés‐Pons, A., DiGuilio, A. L., Mackmull, M., Baßler, J., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10133-z · Cited by 50 · see citing works

Prognostic role of METTL1 in glioma

Li, L., Yang, Y., Wang, Z., Xu, C., Huang, J., & Li, G. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02346-4 · Cited by 49 · see citing works

SMYD5 methylation of rpL40 links ribosomal output to gastric cancer

Park, J.-H., Wu, J., Szkop, K. J., Jeong, J., Jovanovic, P., Husmann, D., Flores, N. M., Francis, J. W., Chen, Y.-J. C., Benitez, A. M., et al. (2024) · Nature · doi:10.1038/s41586-024-07718-0 · Cited by 45 · see citing works

RNA m6A methylation regulators in ovarian cancer

Guo, J., Zheng, J., Zhang, H., & Tong, J. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02318-8 · Cited by 47 · see citing works

Translational offsetting as a mode of estrogen receptor α‐dependent regulation of gene expression

Lorent, J., Kusnadi, E. P., van Hoef, V., Rebello, R. J., Leibovitch, M., Ristau, J., Chen, S., Lawrence, M. G., Szkop, K. J., Samreen, B., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018101323 · Cited by 46 · see citing works

Estrogen receptor alpha controls gene expression via translational offsetting

Lorent, J., Rebello, R. J., Hoef, V. V., Lawrence, M. G., Szkop, K. J., Kusnadi, E., Samreen, B., Balanathan, P., Scharmann, K., Takizawa, I., et al. (2018) · doi:10.1101/507574 · Cited by 46 · see citing works

Translating the Game: Ribosomes as Active Players

Calamita, P., Gatti, G., Miluzio, A., Scagliola, A., & Biffo, S. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00533 · Cited by 45 · see citing works

tRNA Modification and Cancer: Potential for Therapeutic Prevention and Intervention

Endres, L., Fasullo, M., & Rose, R. E. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0404 · Cited by 45 · see citing works

Survey of the translation shifts in hepatocellular carcinoma with ribosome profiling

Zou, Q., Xiao, Z., Huang, R., Wang, X., Wang, X., Zhao, H., & Yang, X. (2019) · Theranostics · doi:10.7150/thno.35033 · Cited by 44 · see citing works

Targeting translation: a promising strategy for anticancer metallodrugs

Ortega, E., Vigueras, G., Ballester, F. J., & Ruiz, J. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214129 · Cited by 44 · 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

Translational Dysregulation in Cancer: Molecular Insights and Potential Clinical Applications in Biomarker Development

Vaklavas, C., Blume, S. W., & Grizzle, W. E. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00158 · Cited by 71 · see citing works

The cancerous translation apparatus

Stumpf, C. R., & Ruggero, D. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.03.007 · Cited by 116 · see citing works

Translational control and the cancer cell response to stress

Robichaud, N., & Sonenberg, N. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.05.007 · Cited by 72 · see citing works

Translational Control in CancerPreprint

Robichaud, N., Sonenberg, N., Ruggero, D., & Schneider, R. J. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032896 · Cited by 309 · see citing works