Translational control of gene expression

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., Sadri, N., Yun, C., Popko, B., Paules, R., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,323

Regulation of mRNA Translation and Stability by microRNAs

Fabian, M. R., Sonenberg, N., & Filipowicz, W. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060308-103103 · Cited by 3,214

The mechanism of eukaryotic translation initiation and principles of its regulation

Jackson, R. J., Hellen, C. U. T., & Pestova, T. V. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2838 · Cited by 2,759

Molecular mechanisms of mTOR-mediated translational control

Ma, X. M., & Blenis, J. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2672 · Cited by 2,558

Listening to silence and understanding nonsense: exonic mutations that affect splicing

Cartegni, L., Chew, S. L., & Krainer, A. R. (2002) · Nature Reviews Genetics · doi:10.1038/nrg775 · Cited by 2,209

TRANSLATIONAL REGULATION OF GCN4 AND THE GENERAL AMINO ACID CONTROL OF YEAST

Hinnebusch, A. G. (2005) · Annual Review of Microbiology · doi:10.1146/annurev.micro.59.031805.133833 · Cited by 1,251

Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics

Maquat, L. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1310 · Cited by 1,214

The eIF2α/ATF4 pathway is essential for stress-induced autophagy gene expression

B’chir, W., Maurin, A.-C., Carraro, V., Averous, J., Jousse, C., Muranishi, Y., Parry, L., Stepien, G., Fafournoux, P., & Bruhat, A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt563 · Cited by 1,162

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 1,082

Molecular mechanisms of translational control

Gebauer, F., & Hentze, M. W. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1488 · Cited by 991

Translational control of long-lasting synaptic plasticity and memory

Costa-Mattioli, M., Sossin, W. S., Klann, E., & Sonenberg, N. (2009) · Neuron · doi:10.1016/j.neuron.2008.10.055 · Cited by 944

A nutrient sensor mechanism controls Drosophila growth

Colombani, J., Raisin, S., Pantalacci, S., Radimerski, T., Montagne, J., & Léopold, P. (2003) · Cell · doi:10.1016/s0092-8674(03)00713-x · Cited by 809

The Scanning Mechanism of Eukaryotic Translation Initiation

Hinnebusch, A. G. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035802 · Cited by 798

Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae

Arava, Y., Wang, Y., Storey, J. D., Liu, C. L., Brown, P. O., & Herschlag, D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0635171100 · Cited by 663

Translational Regulatory Mechanisms in Persistent Forms of Synaptic Plasticity

Kelleher, R. J., Govindarajan, A., & Tonegawa, S. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.013 · Cited by 592

The power of the 3′ UTR: translational control and development.

Kuersten, S., & Goodwin, E. B. (2003) · Nature Reviews Genetics · doi:10.1038/nrg1125 · Cited by 530

Signalling to translation: How signal transduction pathways control the protein synthetic machinery

Proud, C. G. (2007) · Biochemical Journal · doi:10.1042/bj20070024 · Cited by 520

Activating Transcription Factor 3 Is Integral to the Eukaryotic Initiation Factor 2 Kinase Stress Response

Jiang, H.-Y., Wek, S. A., McGrath, B. C., Lu, D., Hai, T., Harding, H. P., Wang, X., Ron, D., Cavener, D. R., & Wek, R. C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.1365-1377.2004 · Cited by 503

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

Leukodystrophies: a proposed classification system based on pathological changes and pathogenetic mechanisms

van der Knaap, M. S., & Bugiani, M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1739-1 · Cited by 403

Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398

Browne, G. J., Finn, S. G., & Proud, C. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309773200 · Cited by 353

Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein

Sawicka, K., Bushell, M., Spriggs, K. A., & Willis, A. E. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360641 · Cited by 332

Messenger RNA Turnover in Eukaryotes: Pathways and Enzymes

Meyer, S., Temme, C., & Wahle, E. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490513991 · Cited by 342

The implications of structured 5′ untranslated regions on translation and disease

Pickering, B. M., & Willis, A. E. (2005) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2004.11.006 · Cited by 339

Leucine Regulates Translation Initiation of Protein Synthesis in Skeletal Muscle after Exercise

Norton, L. E., & Layman, D. K. (2006) · The Journal of Nutrition · doi:10.1093/jn/136.2.533s · Cited by 333

Structure and function of poly(A) binding proteins

Kühn, U., & Wahle, E. (2004) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2004.03.008 · Cited by 323

Opposing Polymerase-Deadenylase Activities Regulate Cytoplasmic Polyadenylation

Kim, J. H., & Richter, J. D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.08.016 · Cited by 300

Silent Substitutions Predictably Alter Translation Elongation Rates and Protein Folding Efficiencies

Spencer, P. S., Siller, E., Anderson, J. F., & Barral, J. M. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.06.010 · Cited by 278

New functions for amino acids: effects on gene transcription and translation

Kimball, S. R., & Jefferson, L. S. (2006) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/83.2.500s · Cited by 276

Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2α) dephosphorylation in mammalian development

Harding, H. P., Zhang, Y., Scheuner, D., Chen, J.-J., Kaufman, R. J., & Ron, D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809632106 · Cited by 267

Dimerization and Release of Molecular Chaperone Inhibition Facilitate Activation of Eukaryotic Initiation Factor-2 Kinase in Response to Endoplasmic Reticulum Stress

Ma, K., Vattem, K. M., & Wek, R. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200903200 · Cited by 265

Altered Machinery of Protein Synthesis in Alzheimer's: From the Nucleolus to the Ribosome

Hernández‐Ortega, K., Garcia‐Esparcia, P., Gil, L., Lucas, J. J., & Ferrer, I. (2016) · Brain Pathology · doi:10.1111/bpa.12335 · Cited by 245

Starting the protein synthesis machine: eukaryotic translation initiation

Preiss, T., & W. Hentze, M. (2003) · BioEssays · doi:10.1002/bies.10362 · Cited by 216

Genome-wide Identification and Quantitative Analysis of Cleaved tRNA Fragments Induced by Cellular Stress

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

Human Interferon-γ mRNA Autoregulates Its Translation through a Pseudoknot that Activates the Interferon-Inducible Protein Kinase PKR

Ben-Asouli, Y., Banai, Y., Pel-Or, Y., Shir, A., & Kaempfer, R. (2002) · Cell · doi:10.1016/s0092-8674(02)00616-5 · Cited by 206

A Network of Multiple Regulatory Layers Shapes Gene Expression in Fission Yeast

Lackner, D. H., Beilharz, T. H., Marguerat, S., Mata, J., Watt, S., Schubert, F., Preiss, T., & Bähler, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.002 · Cited by 204

Translation factors promote the formation of two states of the closed-loop mRNP

Amrani, N., Ghosh, S., Mangus, D. A., & Jacobson, A. (2008) · Nature · doi:10.1038/nature06974 · Cited by 200

Exogenous Amino Acids Regulate Trophectoderm Differentiation in the Mouse Blastocyst through an mTOR-Dependent Pathway

Martin, P. M., & Sutherland, A. E. (2001) · Developmental Biology · doi:10.1006/dbio.2001.0461 · Cited by 196

mTOR signaling: implications for cancer and anticancer therapy

Petroulakis, E., Mamane, Y., Le Bacquer, O., Shahbazian, D., & Sonenberg, N. (2006) · British Journal of Cancer · doi:10.1038/sj.bjc.6602902 · Cited by 170

The role of c-myc in regulation of translation initiation

Schmidt, E. V. (2004) · Oncogene · doi:10.1038/sj.onc.1207548 · Cited by 166

Response of rat muscle to acute resistance exercise defined by transcriptional and translational profiling

Chen, Y., Nader, G. A., Baar, K. R., Fedele, M. J., Hoffman, E. P., & Esser, K. A. (2002) · The Journal of Physiology · doi:10.1113/jphysiol.2002.021220 · Cited by 158

Compulsive exercise acutely upregulates rat hippocampal brain-derived neurotrophic factor

Huang, A. M., Jen, C. J., Chen, H. F., Yu, L., Kuo, Y. M., & Chen, H. I. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-005-0359-4 · Cited by 155

Mechanisms of Food Intake Repression in Indispensable Amino Acid Deficiency

Gietzen, D. W., Hao, S., & Anthony, T. G. (2007) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.27.061406.093726 · Cited by 143

Intracellular translation initiation factor levels in Saccharomyces cerevisiae and their role in cap‐complex function

von der Haar, T., & McCarthy, J. E. G. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03172.x · Cited by 137

Glucagon Represses Signaling through the Mammalian Target of Rapamycin in Rat Liver by Activating AMP-activated Protein Kinase

Kimball, S. R., Siegfried, B. A., & Jefferson, L. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410755200 · Cited by 133

TOPs and their regulation

Hamilton, T. L., Stoneley, M., Spriggs, K. A., & Bushell, M. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340012 · Cited by 91

Global analyses of mRNA translational control during early Drosophila embryogenesis

Qin, X., Ahn, S., Speed, T. P., & Rubin, G. M. (2007) · Genome Biology · doi:10.1186/gb-2007-8-4-r63 · Cited by 86

The role of the TOR pathway in mediating the link between nutrition and longevity

Lushchak, O., Strilbytska, O., Piskovatska, V., Storey, K. B., Koliada, A., & Vaiserman, A. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2017.03.005 · Cited by 73

Tools and targets: the dual role of plant viruses in CRISPR–Cas genome editing

Uranga, M., & Daròs, J. (2023) · The Plant Genome · doi:10.1002/tpg2.20220 · Cited by 68

The nicotinic receptor antagonists abolish pathobiologic effects of tobacco-derived nitrosamines on BEP2D cells

Arredondo, J., Chernyavsky, A. I., & Grando, S. A. (2006) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-006-0113-9 · Cited by 57

The immunosuppressant rapamycin exacerbates neurotoxicity of Aβ peptide

Lafay‐Chebassier, C., Pérault‐Pochat, M. C., Page, G., Bilan, A. R., Damjanac, M., Pain, S., Houeto, J., Gil, R., & Hugon, J. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.21039 · Cited by 52

Eukaryotic Translation Initiation Factor 5 Is Critical for Integrity of the Scanning Preinitiation Complex and Accurate Control of GCN4 Translation

Singh, C. R., Curtis, C., Yamamoto, Y., Hall, N. S., Kruse, D. S., He, H., Hannig, E. M., & Asano, K. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5480-5491.2005 · Cited by 52

Human Gene Profiling in Response to the Active Protein Kinase, Interferon-induced Serine/threonine Protein Kinase (PKR), in Infected Cells

Guerra, S., López-Fernández, L. A., García, M. A., Zaballos, A., & Esteban, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511983200 · Cited by 40

Profiling of genes associated with transcriptional responses in mouse hippocampus after transient forebrain ischemia using high-density oligonucleotide DNA array

Nagata, T., Takahashi, Y., Sugahara, M., Murata, A., Nishida, Y., Ishikawa, K., & Asai, S. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2003.10.023 · Cited by 37