The DOI matches its Crossref record; 137 of the 137 references it cites were found in a registry or an index.
Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets
Open accessAbstract
Translational control in eukaryotic cells is critical for gene regulation during nutrient deprivation and stress, development and differentiation, nervous system function, aging, and disease. We describe recent advances in our understanding of the molecular structures and biochemical functions of the translation initiation machinery and summarize key strategies that mediate general or gene-specific translational control, particularly in mammalian systems.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Both transcription and translation are strongly affected by exact DNA and mRNA sequences, respectively, as well as their cellular environments (Sonenberg and Hinnebusch, 2009; Alpert et al., 2017).”
From Evaluating Efficiencies of Dual AAV Approaches for Retinal Targeting (2017) · cites this paper as Sonenberg and Hinnebusch, 2009
Experimental — accuracy not yet measuredIn the citing paper
“Translation of a uORFs can modulate the expression of the downstream protein-coding gene in response to global (Sonenberg and Hinnebusch, 2009) or gene-specific regulatory signals (Medenbach et al., 2011).”
From Ribosome Profiling of Mouse Embryonic Stem Cells Reveals the Complexity and Dynamics of Mammalian Proteomes (2011) · cites this paper as Sonenberg and Hinnebusch, 2009
In the citing paper
“which, like NIBAN1, phosphorylates EIF4EBP1 to allow assembly of the initiation complex23”
From NEAT-seq: simultaneous profiling of intra-nuclear proteins, chromatin accessibility and gene expression in single cells (2022) · cites this paper as [23]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
(2008) · doi:10.1038/nrg2290 · Cited by 5,199 · cited 1×
“Even for those studies concluding that inhibition occurs at the level of translation initiation, the data are conflicting as in some studies translation inhibition was cap dependent and mediated by eIF4F, whereas in others it was cap independent and mediated via eIF6 (Filipowicz et al., 2008).”
Self-citationThe impact of microRNAs on protein output
Baek, D., Villén, J., Shin, C., Camargo, F. D., Gygi, S. P., & Bartel, D. P. (2008) · Nature · doi:10.1038/nature07242 · Cited by 3,592
Widespread changes in protein synthesis induced by microRNAs
Selbach, M., Schwanhäusser, B., Thierfelder, N., Fang, Z., Khanin, R., & Rajewsky, N. (2008) · Nature · doi:10.1038/nature07228 · Cited by 3,429 · cited 1×
“It is noteworthy that recent large-scale studies in cells demonstrated that the magnitude of translation inhibition of most mRNAs is moderate (~2-fold) (Baek et al., 2008; Selbach et al., 2008), and that similar results were obtained in cell-free translation extracts.”
Switching from Repression to Activation: MicroRNAs Can Up-Regulate Translation
Vasudevan, S., Tong, Y., & STEITZ, J. A. (2007) · Science · doi:10.1126/science.1149460 · Cited by 2,911 · cited 1×
“Surprisingly, it was reported recently that miRNAs can also stimulate rather than inhibit translation when cells enter quiescence (Vasudevan et al., 2007).”
Reinitiation involving upstream ORFs regulates ATF4 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
Specificity of microRNA target selection in translational repressionPreprint
Doench, J. G., & Sharp, P. A. (2004) · Genes & Development · doi:10.1101/gad.1184404 · Cited by 1,685
Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
Um, S. H., Frigerio, F., Watanabe, M., Picard, F., Joaquin, M., Sticker, M., Fumagalli, S., Allegrini, P. R., Kozma, S. C., Auwerx, J., et al. (2004) · Nature · doi:10.1038/nature02866 · Cited by 1,677
A microRNA in a Multiple-Turnover RNAi Enzyme Complex
Hutvágner, G., & Zamore, P. D. (2002) · Science · doi:10.1126/science.1073827 · Cited by 1,674
Argonaute2, a Link Between Genetic and Biochemical Analyses of RNAi
Hammond, S. M., Boettcher, S., Caudy, A. A., Kobayashi, R., & Hannon, G. J. (2001) · Science · doi:10.1126/science.1064023 · Cited by 1,580
Single-Stranded Antisense siRNAs Guide Target RNA Cleavage in RNAi
Martînez, J., Patkaniowska, A., Urlaub, H., Lührmann, R., & Tuschl, T. (2002) · Cell · doi:10.1016/s0092-8674(02)00908-x · Cited by 1,480 · cited 1×
“Once processed from its primary transcript precursor, an miRNA is then loaded into a protein complex, referred to as an RNA-induced silencing complex (RISC), which targets and inhibits protein expression from specific mRNAs (Hammond et al., 2001; Hutvagner and Zamore, 2002; Martinez et al., 2002).”
Cited by
Sorted by citations
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Ingolia, N. T., Lareau, L. F., & Weissman, J. S. (2011) · Cell · doi:10.1016/j.cell.2011.10.002 · Cited by 2,187
Extensive translation of circular RNAs driven by N6-methyladenosine
Yang, Y., Fan, X., Mao, M., Song, X., Wu, P., Zhang, Y., Jin, Y., Yang, Y., Chen, L.-L., Wang, Y., et al. (2017) · Cell Research · doi:10.1038/cr.2017.31 · Cited by 1,855
Pamudurti, N. R., Bartok, O., Jens, M., Ashwal-Fluss, R., Stottmeister, C., Ruhe, L., Hanan, M., Wyler, E., Perez-Hernandez, D., Ramberger, E., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.021 · Cited by 1,810
Cellular Adaptation to Hypoxia through Hypoxia Inducible Factors and beyond
Lee, P., Chandel, N. S., & Simon, M. C. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0227-y · Cited by 1,272
Global signatures of protein and mRNA expression levels
de Sousa Abreu, R., Penalva, L. O., Marcotte, E. M., & Vogel, C. (2009) · Molecular BioSystems · doi:10.1039/b908315d · Cited by 1,248
Mechanisms of Life Span Extension by Rapamycin in the Fruit Fly Drosophila Melanogaster
Bjedov, I., Toivonen, J. M., Kerr, F., Slack, C., Jacobson, J., Foley, A., & Partridge, L. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2009.11.010 · Cited by 1,057
Functional 5′ UTR mRNA structures in eukaryotic translation regulation and how to find them
Leppek, K., Das, R., & Barna, M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.103 · Cited by 949
Analysis of aptamer discovery and technology
Dunn, M. R., Jimenez, R. M., & Chaput, J. C. (2017) · Nature Reviews Chemistry · doi:10.1038/s41570-017-0076 · Cited by 938
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
Self-citationHigh-Resolution View of the Yeast Meiotic Program Revealed by Ribosome Profiling
Brar, G. A., Yassour, M., Friedman, N., Regev, A., Ingolia, N. T., & Weissman, J. S. (2012) · Science · doi:10.1126/science.1215110 · Cited by 533
Gene Expression Regulation by Upstream Open Reading Frames and Human Disease
Barbosa, C., Peixeiro, I., & Romão, L. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003529 · Cited by 525
Human ADAR1 Prevents Endogenous RNA from Triggering Translational Shutdown
Chung, H., Calis, J. J. A., Wu, X., Sun, T., Yu, Y., Sarbanes, S. L., Dao Thi, V. L., Shilvock, A. R., Hoffmann, H.-H., Rosenberg, B. R., et al. (2018) · Cell · doi:10.1016/j.cell.2017.12.038 · Cited by 538
Ribosome collisions trigger general stress responses to regulate cell fate
Wu, C. C.-C., Peterson, A. F., Zinshteyn, B., Regot, S., & Green, R. (2020) · Cell · doi:10.1016/j.cell.2020.06.006 · Cited by 503
“Two commonly used mechanisms for reducing initiation include the phosphorylation of eIF2a by stress-specific kinases and the phosphorylation of 4E-BPs by mTORC1 (Sonenberg and Hinnebusch, 2009).”
Life of RISC: Formation, action, and degradation of RNA-induced silencing complex
Iwakawa, H.-O., & Tomari, Y. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.11.026 · Cited by 488
Bramham, C. R., Alme, M. N., Bittins, M., Kuipers, S. D., Nair, R. R., Pai, B., Panja, D., Schubert, M., Soule, J., Tiron, A., et al. (2010) · Experimental Brain Research · doi:10.1007/s00221-009-1959-2 · Cited by 452
Dynamic profiling of the protein life cycle in response to pathogens
Jovanovic, M., Rooney, M. S., Mertins, P., Przybylski, D., Chevrier, N., Satija, R., Rodriguez, E. H., Fields, A. P., Schwartz, S., Raychowdhury, R., et al. (2015) · Science · doi:10.1126/science.1259038 · Cited by 460
Weinberg, D. E., Shah, P., Eichhorn, S. W., Hussmann, J. A., Plotkin, J. B., & Bartel, D. P. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.01.043 · Cited by 392
Signaling pathways in Parkinson’s disease: molecular mechanisms and therapeutic interventions
Xu, D.-C., Yong, C., Xu, Y., Chen-Yu, S., & Peng, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01353-3 · Cited by 528
Slobodin, B., Han, R., Calderone, V., Vrielink, J. A. F. O., Loayza-Puch, F., Elkon, R., & Agami, R. (2017) · Cell · doi:10.1016/j.cell.2017.03.031 · Cited by 434
The challenge and prospect of mRNA therapeutics landscape
Weng, Y., Li, C., Yang, T., Hu, B., Zhang, M., Guo, S., Xiao, H., Liang, X.-J., & Huang, Y. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2020.107534 · Cited by 417
mTOR complexes in neurodevelopmental and neuropsychiatric disorders
Costa-Mattioli, M., & Monteggia, L. M. (2013) · Nature Neuroscience · doi:10.1038/nn.3546 · Cited by 367
NRF2 Promotes Tumor Maintenance by Modulating mRNA Translation in Pancreatic Cancer
Chio, I. I. C., Jafarnejad, S. M., Ponz-Sarvise, M., Park, Y., Rivera, K., Palm, W., Wilson, J., Sangar, V., Hao, Y., Öhlund, D., et al. (2016) · Cell · doi:10.1016/j.cell.2016.06.056 · Cited by 378
“…cysteinemodifications, prompting us to further evaluate the functional role of Nrf2 inmRNA translation for pancreatic cancer cells. mRNA Translation Is Impeded in Nrf2-Deficient Cells mRNA translation is a vital cellular process that regulates growth and metabolism (Sonenberg and Hinnebusch, 2009).”
Self-citationNew frontiers in translational control of the cancer genome
Truitt, M. L., & Ruggero, D. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.27 · Cited by 378
Ribosomal proteins and human diseases: molecular mechanisms and targeted therapy
Kang, J., Brajanovski, N., Chan, K. T., Xuan, J., Pearson, R. B., & Sanij, E. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00728-8 · Cited by 428
Translational control in synaptic plasticity and cognitive dysfunction
Buffington, S. A., Huang, W., & Costa-Mattioli, M. (2014) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071013-014100 · Cited by 348
Impact of mRNA chemistry and manufacturing process on innate immune activation
Nelson, J., Sorensen, E. W., Mintri, S., Rabideau, A. E., Zheng, W., Besin, G., Khatwani, N., Su, S. V., Miracco, E. J., Issa, W. J., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz6893 · Cited by 354
“One possible outcome of immune activation is reduced mRNA translation due to feedback between the innate immune system and translation machinery, which will decrease the potency of therapeutic mRNA ( 18 , 19 ).”
InfluentialRNA targets of wild-type and mutant FET family proteins
Hoell, J. I., Larsson, E., Runge, S., Nusbaum, J. D., Duggimpudi, S., Farazi, T. A., Hafner, M., Borkhardt, A., Sander, C., & Tuschl, T. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2163 · Cited by 350
Translational control by changes in poly(A) tail length: recycling mRNAs
Weill, L., Belloc, E., Bava, F.-A., & Méndez, R. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2311 · Cited by 328
Dietary restriction and lifespan: lessons from invertebrate models
Kapahi, P., Kaeberlein, M., & Hansen, M. (2017) · Ageing Research Reviews · doi:10.1016/j.arr.2016.12.005 · Cited by 340
Mammalian stress granules and P bodies at a glance
Riggs, C. L., Kedersha, N., Ivanov, P. V., & Anderson, P. (2020) · Journal of Cell Science · doi:10.1242/jcs.242487 · Cited by 374
“…of translation inhibition eIF2α-P-independent Na2SeO3, aa starvation, rapamycin, H2O2 Inhibition of mTOR, leading to hypophosphorylation of 4E-BP (Sonenberg and Hinnebusch, 2009) Interference with canonical cap-dependent translation tiRNAs, pateamine A, silvestrol, hippuristanol, rocaglamide…”
BackgroundSystematic discovery of cap-independent translation sequences in human and viral genomes
Weingarten-Gabbay, S., Elias-Kirma, S., Nir, R., Gritsenko, A. A., Stern-Ginossar, N., Yakhini, Z., Weinberger, A., & Segal, E. (2016) · Science · doi:10.1126/science.aad4939 · Cited by 334
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
METTL16 exerts an m6A-independent function to facilitate translation and tumorigenesis
Su, R. J., Dong, L., Li, Y., Gao, M., He, P. C., Liu, W., Wei, J., Zhao, Z., Gao, L., Han, L., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-021-00835-2 · Cited by 350
De Rubeis, S., Pasciuto, E., Li, K. W., Fernández, E., Di Marino, D., Buzzi, A., Ostroff, L. E., Klann, E., Zwartkruis, F. J. T., Komiyama, N. H., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.06.039 · Cited by 296
Svitkin, Y. V., Cheng, Y. M., Chakraborty, T., Presnyak, V., John, M., & Sonenberg, N. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx135 · Cited by 278
Self-citationZhang, D., Liu, Y., Zhu, Y., Zhang, Q. Y., Guan, H., Liu, S., Chen, S., Chen, M., Chen, C., Liao, Z., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00894-z · Cited by 301
IRES-mediated cap-independent translation, a path leading to hidden proteome
Yang, Y., & Wang, Z. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz091 · Cited by 260
Ribosome profiling reveals post-transcriptional buffering of divergent gene expression in yeast
McManus, C. J., May, G. E., Spealman, P., & Shteyman, A. (2014) · Genome Research · doi:10.1101/gr.164996.113 · Cited by 219
Circular RNA vaccine in disease prevention and treatment
Niu, D., Wu, Y., & Lian, J. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01561-x · Cited by 281
“326,327 Hence, the requisite modi fi cation can enhance RNA vaccine stability and prevent the innate immune response.”
BackgroundBDNF activates mTOR to regulate GluR1 expression required for memory formation
Slipczuk, L., Bekinschtein, P., Katche, C., Cammarota, M., Izquierdo, I., & Medina, J. H. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006007 · Cited by 246
Synonymous but Not Silent: The Codon Usage Code for Gene Expression and Protein Folding
Liu, Y., Yang, Q., & Zhao, F. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071320-112701 · Cited by 254
“For actively translated mRNAs, translation efficiency is mainly determined by the number of ribosomes loaded at the 5′ end of the mRNA, and translation initiation—rather than elongation—was previously thought to be the main ratelimiting step and primary determinant of translation efficiency (35, 40).”
BackgroundExosome biogenesis, secretion and function of exosomal miRNAs in skeletal muscle myogenesis
Yue, B., Yang, H., Wang, J., Ru, W., Wu, J., Huang, Y., Lan, X., Lei, C., & Chen, H. (2020) · Cell Proliferation · doi:10.1111/cpr.12857 · Cited by 264
Kuhn, A. N., Diken, M., Kreiter, S., Selmi, A., Kowalska, J., Jemielity, J., Darzynkiewicz, E., Huber, C., Türeci, Ö., & Sahin, U. (2010) · Gene Therapy · doi:10.1038/gt.2010.52 · Cited by 226
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 286
Monga, A., Fulke, A. B., & Dasgupta, D. (2022) · Journal of Hazardous Materials Advances · doi:10.1016/j.hazadv.2022.100113 · Cited by 221
Saikia, M., Krokowski, D., Guan, B.-J., Ivanov, P., Parisien, M., Hu, G.-F., Anderson, P., Pan, T., & Hatzoglou, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.371799 · Cited by 214
Shi, Z., & Barna, M. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100814-125346 · Cited by 205
A stay of execution: ATF4 regulation and potential outcomes for the integrated stress response
Neill, G. W., & Masson, G. R. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1112253 · Cited by 202
What turns CREB on? And off? And why does it matter?
Steven, A., Friedrich, M., Jank, P., Heimer, N., Budczies, J., Denkert, C., & Seliger, B. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03525-8 · Cited by 220
RNA-binding proteins in regulating mRNA stability and translation: roles and mechanisms in cancer
Li, W., Deng, X., & Chen, J. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2022.03.025 · Cited by 189
Gregorio, D. D., Aguilar‐Valles, A., Preller, K. H., Heifets, B. D., Hibicke, M., Mitchell, J., & Gobbi, G. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1659-20.2020 · Cited by 279
“…mTORC1 controls numerous neuronal functions, including nucleotide and lipid synthesis, glucose metabolism, autophagy, lysosome biogenesis, proteasome assembly, and 59 cap-dependent mRNA translation (also known as protein synthesis) (Sonenberg and Hinnebusch, 2009; Saxton and Sabatini, 2017).”
Mechanisms tailoring the expression of heat shock proteins to proteostasis challenges
Boopathy, L. R. A., Jacob‐Tomas, S., Alecki, C., & Vera, M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101796 · Cited by 183
“The eIF4F complex is made of the cap recognizing factor eIF4E, the scaffold protein eIF4G, and the ATP-driven RNA helicase eIF4A that unwinds secondary structures in the 50 untranslated region (UTR) of mRNAs (75, 93).”
BackgroundThe new function of circRNA: translation
Shi, Y., Jia, X., & Xu, J. (2020) · Clinical & Translational Oncology · doi:10.1007/s12094-020-02371-1 · Cited by 181
Yan, L. L., & Zaher, H. S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.033 · Cited by 176
“Saccharomyces cerevisiae has only one eIF2α kinase, Gcn2, and the organism has proven to be an invaluable model for studying ISR (Masson, 2019), especially in response to aminoacid starvation (Sonenberg and Hinnebusch, 2009).”
BackgroundTranslational control via protein-regulated upstream open reading frames
Medenbach, J., Seiler, M., & Hentze, M. W. (2011) · Cell · doi:10.1016/j.cell.2011.05.005 · Cited by 140
Profiling SARS-CoV-2 HLA-I peptidome reveals T cell epitopes from out-of-frame ORFs
Weingarten-Gabbay, S., Klaeger, S., Sarkizova, S., Pearlman, L. R., Chen, D.-Y., Gallagher, K. M. E., Bauer, M. R., Taylor, H. B., Dunn, W. A., Tarr, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.05.046 · Cited by 147
“For example, viruses can attenuate translation of host proteins, downregulate proteasome machinery, and interfere with HLA-I expression (Hansen and Bouvier, 2009; Sonenberg and Hinnebusch, 2009).”
BackgroundAntidepressant actions of ketamine engage cell-specific translation via eIF4E
Aguilar-Valles, A., De Gregorio, D., Matta-Camacho, E., Eslamizade, M. J., Khlaifia, A., Skaleka, A., Lopez-Canul, M., Torres-Berrio, A., Bermudez, S., Rurak, G. M., et al. (2021) · Nature · doi:10.1038/s41586-020-03047-0 · Cited by 144
Self-citationChi, F., Sharpley, M. S., Nagaraj, R., Roy, S. S., & Banerjee, U. K. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.02.015 · Cited by 191
“A key phosphorylation target of mTOR is 4E-BP1, which enables CAP-dependent translation (Sonenberg and Hinnebusch, 2009).”
BackgroundChen, A. F., Parks, B., Kathiria, A. S., Ober-Reynolds, B., Goronzy, J. J., & Greenleaf, W. J. (2022) · Nature Methods · doi:10.1038/s41592-022-01461-y · Cited by 139
Small molecule cognitive enhancer reverses age-related memory decline in mice
Krukowski, K., Nolan, A., Frias, E. S., Boone, M., Ureta, G., Grue, K. A., Paladini, M. S., Elizarraras, E., Delgado, L. M., Bernales, S., et al. (2020) · eLife · doi:10.7554/elife.62048 · Cited by 167
Translational Control in the Brain in Health and Disease
Sossin, W. S., & Costa-Mattioli, M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032912 · Cited by 138
Regulation of PTEN translation by PI3K signaling maintains pathway homeostasis
Mukherjee, R., Vanaja, K. G., Boyer, J. A., Gadal, S., Solomon, H., Chandarlapaty, S., Levchenko, A., & Rosen, N. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.033 · Cited by 135
“Dephosphorylated 4E-BPs bind to eIF4E/5’capped-mRNA and, by doing so, interfere with the assembly of the pre-initiation complex (Gingras et al., 1999; Sonenberg and Hinnebusch, 2009).”
BackgroundG-Quadruplexes as pathogenic drivers in neurodegenerative disorders
Wang, E., Thombre, R., Shah, Y., Latanich, R., & Wang, J. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab164 · Cited by 152
“The roles that G4s play in the regulation of translation initiation are particularly important to elucidate because it is believed that most regulation of translation occurs at the initiation stage in eukaryotes (82).”
BackgroundClinical and immunological effects of mRNA vaccines in malignant diseases
Heine, A., Juranek, S., & Brossart, P. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01339-1 · Cited by 186
Metformin inhibits RAN translation through PKR pathway and mitigates disease in C9orf72 ALS/FTD mice
Zu, T., Guo, S., Bardhi, O., Ryskamp, D. A., Li, J., Khoramian Tusi, S., Engelbrecht, A., Klippel, K., Chakrabarty, P., Nguyen, L., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005748117 · Cited by 133
Self-citationHypoxia Dictates Metabolic Rewiring of Tumors: Implications for Chemoresistance
Belisario, D. C., Kopecka, J., Pasino, M., Akman, M., De Smaele, E., Donadelli, M., & Riganti, C. (2020) · Cells · doi:10.3390/cells9122598 · Cited by 133
“Concurrently HIF-2α activates mTOR, a sensor of the cellular energy status and of the AA availability, and a stimulator of protein translation and cell proliferation [104].”
BackgroundInsight into antibacterial mechanism of polysaccharides: A review
Wang, Z., Sun, Q., Zhang, H., Wang, J.-Q., Fu, Q.-H., Qiao, H., & Wang, Q. (2021) · LWT · doi:10.1016/j.lwt.2021.111929 · Cited by 131
Nanoplatforms for mRNA Therapeutics
Meng, C., Chen, Z., Li, G., Welte, T., & Shen, H. (2021) · Advanced Therapeutics · doi:10.1002/adtp.202000099 · Cited by 130
Plant Immune Mechanisms: From Reductionistic to Holistic Points of View
Zhang, J., Coaker, G., Zhou, J., & Dong, X. (2020) · Molecular Plant · doi:10.1016/j.molp.2020.09.007 · Cited by 176
“As PABPs link the poly(A) tail of an mRNA to its 50 cap through interactions with eIF4G and eIF3 to facilitate translation initiation (Sonenberg and Hinnebusch, 2009; Jackson et al., 2010), it is plausible that the 50 R-motif serves as a capindependent translation enhancer (CITE) (Shatsky et al.”
BackgroundThe roles of arginases and arginine in immunity
Canè, S., Geiger, R., & Bronte, V. (2024) · Nature reviews. Immunology · doi:10.1038/s41577-024-01098-2 · Cited by 140
Kwon, N. H., Kang, T., Lee, J. Y., Kim, H. H., Kim, H. R., Hong, J., Oh, Y. S., Han, J. M., Ku, M. J., Lee, S. Y., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103922108 · Cited by 120
Amino Acid Sensing in Metabolic Homeostasis and Health
Hu, X., & Guo, F. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa026 · Cited by 143
Bond, P. (2016) · Journal of the International Society of Sports Nutrition · doi:10.1186/s12970-016-0118-y · Cited by 121
Clinical delivery of circular RNA: Lessons learned from RNA drug development
Young, T. L., Wang, K. C., Varley, A., & Li, B. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.114826 · Cited by 130
eIF4A supports an oncogenic translation program in pancreatic ductal adenocarcinoma
Chan, K., Robert, F., Oertlin, C., Kapeller-Libermann, D., Avizonis, D., Gutierrez, J., Handly-Santana, A., Doubrovin, M., Park, J., Schoepfer, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13086-5 · Cited by 106
Millar, S. R., Huang, J. Q., Schreiber, K. J., Tsai, Y.-C., Won, J., Zhang, J., Moses, A. M., & Youn, J. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00608 · Cited by 133
eIF2α controls memory consolidation via excitatory and somatostatin neurons
Sharma, V. K., Sood, R., Khlaifia, A., Eslamizade, M. J., Hung, T.-Y., Lou, D., Asgarihafshejani, A., Lalzar, M., Kiniry, S. J., Stokes, M. P., et al. (2020) · Nature · doi:10.1038/s41586-020-2805-8 · Cited by 135
Self-citationTransfer RNAs: diversity in form and function
Berg, M. D., & Brandl, C. J. (2020) · RNA Biology · doi:10.1080/15476286.2020.1809197 · Cited by 151
Revolutionizing immunization: a comprehensive review of mRNA vaccine technology and applications
Leong, K. Y., Tham, S. K., & Poh, C. L. (2025) · Virology Journal · doi:10.1186/s12985-025-02645-6 · Cited by 139
“The pairing of Met-tRNAi with the AUG codon signals the binding of the 60S ribosomal subunit, thus completing the assembly of the 80S ribosome, which is ready for protein synthesis [17].”
Branched chemically modified poly(A) tails enhance the translation capacity of mRNA
Chen, H., Liu, D., Guo, J., Aditham, A. J., Zhou, Y., Tian, J., Luo, S., Ren, J., Hsu, A., Huang, J., et al. (2024) · Nature Biotechnology · doi:10.1038/s41587-024-02174-7 · Cited by 132
tRNA overexpression rescues peripheral neuropathy caused by mutations in tRNA synthetase
Zuko, A., Mallik, M., Thompson, R., Spaulding, E. L., Wienand, A., Been, M., Tadenev, A. L. D., van Bakel, N. H. M., Sijlmans, C., Santos, L. A., et al. (2021) · Science · doi:10.1126/science.abb3356 · Cited by 124
An overview of rational design of mRNA-based therapeutics and vaccines
To, K. K. W., & Cho, W. C. S. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1935859 · Cited by 110
eIF5B drives integrated stress response-dependent translation of PD-L1 in lung cancer
Suresh, S., Chen, B., Zhu, J., Golden, R. J., Lu, C., Evers, B. M., Novaresi, N., Smith, B., Zhan, X., Schmid, V., et al. (2020) · Nature Cancer · doi:10.1038/s43018-020-0056-0 · Cited by 130
Translation Regulation as a Therapeutic Target in Cancer
Grzmil, M., & Hemmings, B. A. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0026 · Cited by 103
The ribotoxic stress response drives UV-mediated cell death
Sinha, N. K., McKenney, C. D., Yeow, Z. Y., Li, J. J., Nam, K. H., Yaron, T. M., Johnson, J. L., Huntsman, E. M., Cantley, L. C., Ordureau, A., et al. (2024) · Cell · doi:10.1016/j.cell.2024.05.018 · Cited by 142
The integrated stress response in metabolic adaptation
Ryoo, H. D. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107151 · Cited by 133
“This initiates a sequence of mRNA regulatory mechanisms to induce the ISR, which has been reviewed extensively elsewhere (10, 33).”
BackgroundThe Target of Rapamycin Signalling Pathway in Ageing and Lifespan Regulation
Bjedov, I., & Rallis, C. (2020) · Genes · doi:10.3390/genes11091043 · Cited by 108
“An important feature of eIF4F complex, formed of eIF4E (cap binding), eIF4A (RNA helicase) and eIF4G (scaffolding protein), is its very low cellular concentration, which places it in a critical position to regulate translation [112].”
BackgroundProtein 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 121
Yang, G., Smibert, C. A., Kaplan, D. R., & Miller, F. D. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.022 · Cited by 98
Expanding uncapped translation and emerging function of circular RNA in carcinomas and noncarcinomas
Wang, Y., Wu, C., Du, Y., Li, Z., Li, M., Hou, P., Shen, Z., Chu, S., Zheng, J., & Bai, J. (2022) · Molecular Cancer · doi:10.1186/s12943-021-01484-7 · Cited by 112
“Canonical translation of eukaryotic mRNA depends on the m7G cap for recognition of the cap-binding protein initiation factor eIF4E complex, including eIF4E and eIF4G (a scaffold protein) and eIF4A (a helicase protein), and assembly of the 43S initiation complex to direct protein synthesis [42, 43].”
BackgroundmTORC1 promotes TOP mRNA translation through site-specific phosphorylation of LARP1
Jia, J.-J., Lahr, R. M., Solgaard, M. T., Moraes, B. J., Pointet, R., Yang, A.-D., Celucci, G., Graber, T. E., Hoang, H., Niklaus, M., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1239 · Cited by 101
“4E-BPs (of which there are three homologs in mammals: 4E-BP1, 4EBP2 and 4E-BP3) and S6Ks (S6K1 and S6K2) are the most intensively studied direct mTORC1 substrates; accordingly, these targets are frequently referred to as the most important effectors of mTORC1 in mRNA translation (50).”
BackgroundEukaryotic translation initiation factors as promising targets in cancer therapy
Hao, P., Yu, J., Ward, R. J., Liu, Y., Qiao, H., An, S., & Xu, T. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-00607-9 · Cited by 127
Determinants of genome-wide distribution and evolution of uORFs in eukaryotes
Zhang, H., Wang, Y., Wu, X., Tang, X., Wu, C., & Lü, J. (2021) · Nature Communications · doi:10.1038/s41467-021-21394-y · Cited by 105
Jeon, S., Jeon, Y., Lim, J.-Y., Kim, Y., Cha, B., & Kim, W. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02070-1 · Cited by 105
Davies, N. M., Hovdal, D., Edmunds, N. J., Nordberg, P., Dahlén, A., Dabkowska, A. P., Arteta, M. Y., Rădulescu, A., Kjellman, T., Höijer, A., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.03.008 · Cited by 93
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 93
“Originally, a long 5′-UTR, rich in secondary structures, was thought to confer mTORC1 specificity (79, 80); however, more recently, it has emerged that translation of mRNAs without a long 5′-UTR can still be sensitive to eIF4E (42, 82).”
Evaluating Efficiencies of Dual AAV Approaches for Retinal Targeting
Carvalho, L. S., Turunen, H. T., Wassmer, S. J., Luna-Velez, M. V., Xiao, R., Bennett, J., & Vandenberghe, L. H. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00503 · Cited by 86
The endoplasmic reticulum: Homeostasis and crosstalk in retinal health and disease
Zhang, S. X., Wang, J. J., Starr, C. R., Lee, E.-J., Park, K. S., Zhylkibayev, A. A., Medina, A., Lin, J. H., & Gorbatyuk, M. S. (2023) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2023.101231 · Cited by 85
FMRP phosphorylation modulates neuronal translation through YTHDF1
Zou, Z.-Y., Jiangbo, W., Chen, Y.-T., Kang, Y., Shi, H., Yang, F., Shi, Z.-Y., Chen, S.-J., Zhou, Y., Sepich-Poore, C., et al. (2022) · bioRxiv · doi:10.1101/2022.11.29.518448 · Cited by 84
Metadata
- Authors
- Sonenberg, N., & Hinnebusch, A. G.
- Affiliations
- McGill University (CA)
- National Institutes of Health (US)
- Corresponding author
- Sonenberg, Nahum
- Hinnebusch, Alan G.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 136
- Issue
- 4
- Pages
- 731-745
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3610329
- OpenAlex
- W2037313242
- Cited by
- 3,304
- References
- 137
- Citations by year
- 2026: 145 · 2025: 144 · 2024: 166 · 2023: 194 · 2022: 187 · 2021: 219 · 2020: 208 · 2019: 204 · 2018: 211 · 2017: 240 · 2016: 199 · 2015: 188 · 2014: 212 · 2013: 212 · 2012: 222
- FWCI
- 14.67
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship@McGill (McGill) (submittedVersion, cc-by-nc-nd)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health (1ziahd001004-27, ZIA HD001004)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- translation initiation, translational regulation, nutrient deprivation, stress response, nervous system function, aging, disease, mammalian cells
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Models, Molecular, Peptide Chain Initiation, Translational, Peptide Initiation Factors, Ribosomes
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
