Ribosome stalling induced by mutation of a CNS-specific tRNA causes neurodegeneration

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources

Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890 · 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

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

The ribosome profiling strategy for monitoring translation in vivo by deep sequencing of ribosome-protected mRNA fragments

Ingolia, N. T., Brar, G. A., Rouskin, S., McGeachy, A. M., & Weissman, J. S. (2012) · Nature Protocols · doi:10.1038/nprot.2012.086 · Cited by 1,240 · see citing works

The Elongation, Termination, and Recycling Phases of Translation in EukaryotesPreprint

Dever, T. E., & Green, R. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013706 · Cited by 507 · see citing works

A Novel ES Cell Line, TT2, with High Germline-Differentiating Potency

Yagi, T., Tokunaga, T., Furuta, Y., Nada, S., Yoshida, M., Tsukada, T., Saga, Y., Takeda, N., Ikawa, Y., & Aizawa, S. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1458 · Cited by 465 · see citing works

Translational Pausing Ensures Membrane Targeting and Cytoplasmic Splicing of <i>XBP1u</i> mRNA

Yanagitani, K., Kimata, Y., Kadokura, H., & Kohno, K. (2011) · Science · doi:10.1126/science.1197142 · Cited by 362 · see citing works

Dom34 Rescues Ribosomes in 3′ Untranslated Regions

Guydosh, N. R., & Green, R. (2014) · Cell · doi:10.1016/j.cell.2014.02.006 · Cited by 355 · see citing works

Dom34:Hbs1 Promotes Subunit Dissociation and Peptidyl-tRNA Drop-Off to Initiate No-Go Decay

Shoemaker, C. J., Eyler, D. E., & Green, R. (2010) · Science · doi:10.1126/science.1192430 · Cited by 335 · see citing works

Widespread Regulation of Translation by Elongation Pausing in Heat Shock

Shalgi, R., Hurt, J. A., Krykbaeva, I., Taipale, M., Lindquist, S. L., & Burge, C. B. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.11.028 · Cited by 334 · see citing works

Genome-wide ribosome profiling reveals complex translational regulation in response to oxidative stress

Gerashchenko, M. V., Lobanov, A. V., & Gladyshev, V. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120799109 · Cited by 302 · see citing works

Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes

Pisareva, V. P., Skabkin, M. A., Hellen, C. U. T., Pestova, T. V., & Pisarev, A. V. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.93 · Cited by 299 · see citing works

Diversity of tRNA genes in eukaryotes

Goodenbour, J. M., & Pan, T. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl725 · Cited by 240 · see citing works

Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP

Zhao, L., Longo-Guess, C. M., Harris, B. S., Lee, J.-W., & Ackerman, S. L. (2005) · Nature Genetics · doi:10.1038/ng1620 · Cited by 214 · see citing works

Ribosome rescue: tmRNA tagging activity and capacity in Escherichia coli

Moore, S. D., & Sauer, R. T. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04832.x · Cited by 128 · see citing works

Halting a cellular production line: responses to ribosomal pausing during translation

Buchan, J. R., & Stansfield, I. (2007) · Biology of the Cell · doi:10.1042/bc20070037 · Cited by 119 · see citing works

Ribosome profiling reveals features of normal and disease-associated mitochondrial translation

Rooijers, K., Loayza‐Puch, F., Nijtmans, L. G. J., & Agami, R. (2013) · Nature Communications · doi:10.1038/ncomms3886 · Cited by 97 · see citing works

Large-scale mutagenesis of the mouse to understand the genetic bases of nervous system structure and function

Goldowitz, D., Frankel, W. N., Takahashi, J. S., Vitaterna, M. H., Bult, C. J., Kibbe, W. A., Snoddy, J. R., Li, Y., Pretel, S., Yates, J., et al. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.09.016 · Cited by 72 · see citing works

Sequence and Structure Requirements for Drosophila tRNA 5′- and 3′-End Processing

Levinger, L., Vasisht, V., Greene, V., Bourne, R., Birk, A. V., & Kolla, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18903 · Cited by 37 · see citing works

Mouse and human GTPBP2, newly identified members of the GP-1 family of GTPase.

Kudo, H., Senju, S., Mitsuya, H., & Nishimura, Y. (2000) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1006/bbrc.2000.2763 · Cited by 24 · see citing works

Cloning, expression analysis, and chromosomal mapping of GTPBP2, a novel member of the G protein family.

Watanabe, M., Yoshida, K.-I., Hida, M., Kato, H., Uchida, K., Yamaguchi, R., Tateyama, S., & Sugano, S. (2000) · Gene · doi:10.1016/s0378-1119(00)00346-2 · Cited by 18 · see citing works

Pathogenesis-related mutations in the T-loops of human mitochondrial tRNAs affect 3′ end processing and tRNA structure

Levinger, L., & Serjanov, D. (2012) · RNA Biology · doi:10.4161/rna.19025 · Cited by 17 · see citing works

A large-scale binding and functional map of human RNA-binding proteins

Van Nostrand, E. L., Freese, P., Pratt, G. A., Wang, X., Wei, X., Xiao, R., Blue, S. M., Chen, J.-Y., Cody, N. A. L., Dominguez, D., et al. (2020) · Nature · doi:10.1038/s41586-020-2077-3 · Cited by 1,317 · see citing works

GtRNAdb 2.0: an expanded database of transfer RNA genes identified in complete and draft genomes

Chan, P. P., & Lowe, T. M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1309 · Cited by 1,035 · see citing works

Optimization of Codon Translation Rates via tRNA Modifications Maintains Proteome Integrity

Nedialkova, D. D., & Leidel, S. A. (2015) · Cell · doi:10.1016/j.cell.2015.05.022 · Cited by 546 · see citing works

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 · see citing works

Emerging roles of tRNA in adaptive translation, signalling dynamics and disease

Kirchner, S., & Ignatova, Z. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3861 · Cited by 524 · 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

Modulated Expression of Specific tRNAs Drives Gene Expression and Cancer Progression

Goodarzi, H., Nguyen, H. C. B., Zhang, S., Dill, B. D., Molina, H., & Tavazoie, S. F. (2016) · Cell · doi:10.1016/j.cell.2016.05.046 · Cited by 454 · see citing works

The emerging complexity of the tRNA world: mammalian tRNAs beyond protein synthesis

SCHIMMEL, P. R. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.77 · Cited by 463 · see citing works

Mechanisms and functions of ribosome-associated protein quality control

Joazeiro, C. A. P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0118-2 · Cited by 456 · see citing works

Ribosome-associated protein quality control

Brandman, O., & Hegde, R. S. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3147 · Cited by 443 · see citing works

Ribosomopathies: There’s strength in numbers

Mills, E. W., & Green, R. (2017) · Science · doi:10.1126/science.aan2755 · Cited by 424 · see citing works

ZNF598 Is a Quality Control Sensor of Collided Ribosomes

Juszkiewicz, S., Chandrasekaran, V., Lin, Z., Kraatz, S. H. W., Ramakrishnan, V., & Hegde, R. S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.037 · Cited by 429 · see citing works

Efficient Test and Visualization of Multi-Set Intersections

Wang, M., Zhao, Y., & Zhang, B. (2015) · Scientific Reports · doi:10.1038/srep16923 · Cited by 395 · see citing works

Modifications and functional genomics of human transfer RNA

Pan, T. (2018) · Cell Research · doi:10.1038/s41422-018-0013-y · Cited by 399 · see citing works

Sex hormone-dependent tRNA halves enhance cell proliferation in breast and prostate cancers

Honda, S., Loher, P., Shigematsu, M., Palazzo, J., Suzuki, R., Imoto, I., Rigoutsos, I., & Kirino, Y. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510077112 · Cited by 386 · see citing works

METTL1-mediated m7G modification of Arg-TCT tRNA drives oncogenic transformation

Orellana, E. A., Liu, Q., Yankova, E., Pirouz, M., Braekeleer, E. D., Zhang, W. C., Lim, J., Aspris, D., Sendinc, E., Garyfallos, D. A., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.06.031 · Cited by 352 · see citing works

Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use

Atkins, J. F., Loughran, G., Bhatt, P. R., Firth, A. E., & Baranov, P. V. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw530 · Cited by 320 · see citing works

Codon identity regulates mRNA stability and translation efficiency during the maternal‐to‐zygotic transition

Bazzini, A., Viso, F. D., Moreno-Mateos, M. A., Johnstone, T. G., Vejnar, C. E., Qin, Y., Yao, J., Khokha, M. K., & Giráldez, A. J. (2016) · The EMBO Journal · doi:10.15252/embj.201694699 · Cited by 307 · see citing works

Meta-Analysis of the Alzheimer’s Disease Human Brain Transcriptome and Functional Dissection in Mouse Models

Wan, Y.-W., Al-Ouran, R., Mangleburg, C. G., Perumal, T. M., Lee, T. V., Allison, K., Swarup, V., Funk, C. C., Gaiteri, C., Allen, M., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107908 · Cited by 295 · see citing works

Rqc2p and 60 S ribosomal subunits mediate mRNA-independent elongation of nascent chains

Shen, P. S., Park, J. H., Qin, Y., Li, X., Parsawar, K., Larson, M. H., Cox, J. E., Cheng, Y., Lambowitz, A. M., Weissman, J. S., et al. (2015) · Science · doi:10.1126/science.1259724 · Cited by 295 · see citing works

Translation affects mRNA stability in a codon-dependent manner in human cells

Wu, Q., Medina, S. G., Kushawah, G., DeVore, M. L., Castellano, L. A., Hand, J. M., Wright, M., & Bazzini, A. A. (2019) · eLife · doi:10.7554/elife.45396 · Cited by 283 · see citing works

Tunable protein synthesis by transcript isoforms in human cells

Floor, S. N., & Doudna, J. A. (2016) · eLife · doi:10.7554/elife.10921 · Cited by 265 · see citing works

High-resolution quantitative profiling of tRNA abundance and modification status in eukaryotes by mim-tRNAseq

Behrens, A., Rodschinka, G., & Nedialkova, D. D. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.028 · Cited by 248 · see citing works

Roadblocks and resolutions in eukaryotic translation

Schuller, A. P., & Green, R. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0011-4 · Cited by 245 · see citing works

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 242 · see citing works

Proteome complexity and the forces that drive proteome imbalance

Harper, J. W., & Bennett, E. J. (2016) · Nature · doi:10.1038/nature19947 · Cited by 234 · see citing works

Ageing exacerbates ribosome pausing to disrupt cotranslational proteostasis

Stein, K. C., Morales-Polanco, F., van der Lienden, J. C., Rainbolt, T. K., & Frydman, J. (2022) · Nature · doi:10.1038/s41586-021-04295-4 · Cited by 239 · see citing works

Activation of GCN2 kinase by ribosome stalling links translation elongation with translation initiation

Ishimura, R., Nagy, G., Dotu, I., Chuang, J. H., & Ackerman, S. L. (2016) · eLife · doi:10.7554/elife.14295 · Cited by 221 · see citing works

The endonuclease Cue2 cleaves mRNAs at stalled ribosomes during No Go Decay

D’Orazio, K. N., Wu, C. C., Sinha, N. K., Loll‐Krippleber, R., Brown, G. W., & Green, R. (2019) · eLife · doi:10.7554/elife.49117 · Cited by 196 · see citing works

Pausing on Polyribosomes: Make Way for Elongation in Translational Control

Richter, J. D., & Coller, J. M. (2015) · Cell · doi:10.1016/j.cell.2015.09.041 · Cited by 204 · see citing works

Ribosomal Stalling During Translation: Providing Substrates for Ribosome-Associated Protein Quality Control

Joazeiro, C. A. P. (2017) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-111315-125249 · Cited by 198 · see citing works

Regulation of mRNA Translation in Neurons—A Matter of Life and Death

Kapur, M., Monaghan, C. E., & Ackerman, S. L. (2017) · Neuron · doi:10.1016/j.neuron.2017.09.057 · Cited by 200 · see citing works

Recent Advances in Mitochondrial Aminoacyl-tRNA Synthetases and Disease

Sissler, M., González-Serrano, L. E., & Westhof, É. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.06.002 · Cited by 197 · see citing works

Ribosome pausing, arrest and rescue in bacteria and eukaryotes

Buskirk, A. R., & Green, R. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0183 · Cited by 188 · see citing works

Disome and Trisome Profiling Reveal Genome-wide Targets of Ribosome Quality Control

Meydan, S., & Guydosh, N. R. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.010 · Cited by 187 · see citing works

Differential expression of human tRNA genes drives the abundance of tRNA-derived fragments

Torres, A. G., Reina, Ó., Attolini, C. S., & de Pouplana, L. R. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821120116 · Cited by 182 · see citing works

Ribosomopathies: Old Concepts, New Controversies

Farley‐Barnes, K. I., Ogawa, L. M., & Baserga, S. J. (2019) · Trends in Genetics · doi:10.1016/j.tig.2019.07.004 · Cited by 183 · see citing works

How do cells cope with RNA damage and its consequences?

Yan, L. L., & Zaher, H. S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.006513 · Cited by 185 · see citing works

UFMylation of RPL26 links translocation-associated quality control to endoplasmic reticulum protein homeostasis

Wang, L., Xu, Y., Rogers, H. M., Saidi, L. F., Noguchi, C. T., Li, H., Yewdell, J. W., Guydosh, N. R., & Ye, Y. (2019) · Cell Research · doi:10.1038/s41422-019-0236-6 · Cited by 184 · see citing works

Quantitative tRNA-sequencing uncovers metazoan tissue-specific tRNA regulation

Pinkard, O. W., McFarland, S., Sweet, T. J., & Coller, J. M. (2020) · Nature Communications · doi:10.1038/s41467-020-17879-x · Cited by 178 · see citing works

Regional protein expression in human Alzheimer’s brain correlates with disease severity

Xu, J., Patassini, S., Rustogi, N., Riba‐Garcia, I., Hale, B. D., Phillips, A. M., Waldvogel, H. J., Haines, R., Bradbury, P., Stevens, A., et al. (2019) · Communications Biology · doi:10.1038/s42003-018-0254-9 · Cited by 182 · see citing works

tRNA dysregulation and disease

Orellana, E. A., Siegal, E. Z., & Gregory, R. I. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00501-9 · Cited by 175 · see citing works

EDF1 coordinates cellular responses to ribosome collisions

Sinha, N. K., Ordureau, A., Best, K., Saba, J. A., Zinshteyn, B., Sundaramoorthy, E., Fulzele, A., Garshott, D. M., Denk, T., Thoms, M., et al. (2020) · eLife · doi:10.7554/elife.58828 · Cited by 174 · see citing works

Ribosome-associated quality-control mechanisms from bacteria to humans

Filbeck, S., Cerullo, F., Pfeffer, S., & Joazeiro, C. A. P. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.038 · Cited by 175 · see citing works

Emerging mechanisms of aminoacyl-tRNA synthetase mutations in recessive and dominant human disease

Meyer‐Schuman, R., & Antonellis, A. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx231 · Cited by 180 · see citing works

Translational Control through Differential Ribosome Pausing during Amino Acid Limitation in Mammalian Cells

Darnell, A. M., Subramaniam, A. R., & O’Shea, E. K. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.06.041 · Cited by 183 · see citing works

A novel class of microRNA-recognition elements that function only within open reading frames

Zhang, K., Zhang, X., Cai, Z., Zhou, J., Cao, R., Zhao, Y., Chen, Z., Wang, D., Ruan, W., Zhao, Q. C., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0136-3 · Cited by 169 · see citing works

Ribosomal stress-surveillance: three pathways is a magic number

Vind, A., Genzor, A. V., & Bekker‐Jensen, S. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa757 · Cited by 166 · see citing works

The ribosomal P-stalk couples amino acid starvation to GCN2 activation in mammalian cells

Harding, H. P., Ordóñez, A., Allen, F. R., Parts, L., Inglis, A. J., Williams, R. L., & Ron, D. (2019) · eLife · doi:10.7554/elife.50149 · Cited by 176 · see citing works

Matching tRNA modifications in humans to their known and predicted enzymes

de Crécy‐Lagard, V., Boccaletto, P., Mangleburg, C. G., Sharma, P., Lowe, T. M., Leidel, S. A., & Bujnicki, J. M. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz011 · Cited by 170 · see citing works

The role of RNA modifications in the regulation of tRNA cleavage

Lyons, S. M., Fay, M. M., & Ivanov, P. V. (2018) · FEBS Letters · doi:10.1002/1873-3468.13205 · Cited by 159 · see citing works

The stop-and-go traffic regulating protein biogenesis: How translation kinetics controls proteostasis

Stein, K. C., & Frydman, J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002814 · Cited by 160 · see citing works

Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis

Shang, Y., & Huang, E. J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.036 · Cited by 154 · see citing works

Ribosome states signal RNA quality control

D’Orazio, K. N., & Green, R. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.02.022 · Cited by 147 · see citing works

Defects in tRNA Anticodon Loop 2′-O-Methylation Are Implicated in Nonsyndromic X-Linked Intellectual Disability due to Mutations inFTSJ1

Guy, M. P., Shaw, M. A., Weiner, C. L., Hobson, L., Stark, Z., Rose, K., Kalscheuer, V. M., Gécz, J., & Phizicky, E. M. (2015) · Human Mutation · doi:10.1002/humu.22897 · Cited by 142 · see citing works

RNA metabolism in neurodegenerative disease

Liu, E. Y., Cali, C. P., & Lee, E. B. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.028613 · Cited by 137 · see citing works

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 · see citing works

Protein translation: biological processes and therapeutic strategies for human diseases

Jia, X., He, X., Huang, C., Li, J., Dong, Z., & Liu, K. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01749-9 · Cited by 143 · see citing works

A Ribosomal Perspective on Proteostasis and Aging

Steffen, K. K., & Dillin, A. G. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.013 · Cited by 136 · see citing works

Alteration of protein function by a silent polymorphism linked to tRNA abundance

Kirchner, S., Cai, Z., Rauscher, R., Kastelić, N., Anding, M., Czech, A., Kleizen, B., Ostedgaard, L. S., Braakman, I., Sheppard, D. N., et al. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2000779 · Cited by 137 · see citing works

The integrated stress response contributes to tRNA synthetase–associated peripheral neuropathy

Spaulding, E. L., Hines, T. J., Bais, P., Tadenev, A. L. D., Schneider, R., Jewett, D., Pattavina, B., Pratt, S. L., Morelli, K. H., Stum, M., et al. (2021) · Science · doi:10.1126/science.abb3414 · Cited by 135 · see citing works

Codon optimality-mediated mRNA degradation: Linking translational elongation to mRNA stability

Bae, H., & Coller, J. M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.032 · Cited by 128 · see citing works

Asc1, Hel2, and Slh1 couple translation arrest to nascent chain degradation

Sitron, C. S., Park, J. H., & Brandman, O. (2017) · RNA · doi:10.1261/rna.060897.117 · Cited by 128 · see citing works

Connections Underlying Translation and mRNA Stability

Radhakrishnan, A., & Green, R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.05.025 · Cited by 131 · see citing works

Impaired protein translation in Drosophila models for Charcot–Marie–Tooth neuropathy caused by mutant tRNA synthetases

Niehues, S., Bussmann, J., Steffes, G., Erdmann, I., Köhrer, C., Sun, L., Wagner, M., Schäfer, K. J., Wang, G., Koerdt, S. N., et al. (2015) · Nature Communications · doi:10.1038/ncomms8520 · Cited by 122 · see citing works

Emerging roles of tRNA-derived fragments in cancer

Fu, M., Gu, J., Wang, M., Zhang, J., Chen, Y., Jiang, P., Zhu, T., & Zhang, X. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01739-5 · Cited by 127 · see citing works

The life and times of a tRNA

Phizicky, E. M., & Hopper, A. K. (2023) · RNA · doi:10.1261/rna.079620.123 · Cited by 120 · see citing works

Alanine Tails Signal Proteolysis in Bacterial Ribosome-Associated Quality Control

Lytvynenko, I., Paternoga, H., Thrun, A., Balke, A., Müller, T., Chiang, C. H., Nagler, K., Tsaprailis, G., Anders, S., Bischofs, I. B., et al. (2019) · Cell · doi:10.1016/j.cell.2019.05.002 · Cited by 119 · see citing works

tRNA overexpression rescues peripheral neuropathy caused by mutations in tRNA synthetase

Zuko, A., Mallik, M., Thompson, R., Spaulding, E., Wienand, A., Been, M., Tadenev, A., van Bakel, N., Sijlmans, C., Santos, L. A., et al. (2021) · Science · doi:10.1126/science.abb3356 · Cited by 111 · see citing works

The integrated stress response in metabolic adaptation

Ryoo, H. D. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107151 · Cited by 120 · see citing works

Ribosomopathies and the paradox of cellular hypo- to hyperproliferation

Keersmaecker, K. D., Sulima, S. O., & Dinman, J. D. (2015) · Blood · doi:10.1182/blood-2014-10-569616 · Cited by 119 · see citing works

Determination of tRNA aminoacylation levels by high-throughput sequencing

Evans, M., Clark, W. C., Zheng, G., & Pan, T. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx514 · Cited by 116 · see citing works

mRNA Translation Gone Awry: Translation Fidelity and Neurological Disease

Kapur, M., & Ackerman, S. L. (2018) · Trends in Genetics · doi:10.1016/j.tig.2017.12.007 · Cited by 112 · see citing works

Translation and mRNA Stability Control

Wu, Q., & Bazzini, A. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052621-091808 · Cited by 117 · see citing works

Glutamyl-Prolyl-tRNA Synthetase Regulates Proline-Rich Pro-Fibrotic Protein Synthesis During Cardiac Fibrosis

Wu, J., Subbaiah, K. C. V., Xie, L. H., Jiang, F., Khor, E.-S., Mickelsen, D. M., Myers, J. R., Tang, W. H. W., & Yao, P. (2020) · Circulation Research · doi:10.1161/circresaha.119.315999 · Cited by 111 · see citing works

Ribosome‐based quality control of mRNA and nascent peptides

Simms, C. L., Thomas, E. N., & Zaher, H. S. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1366 · Cited by 108 · see citing works

Detection of Cyanotoxins, β-N-methylamino-L-alanine and Microcystins, from a Lake Surrounded by Cases of Amyotrophic Lateral Sclerosis

Banack, S. A., Caller, T. A., Henegan, P. L., Haney, J. F., Murby, A., Metcalf, J. S., Powell, J. T., Cox, P. A., & Stommel, E. W. (2015) · Toxins · doi:10.3390/toxins7020322 · Cited by 108 · see citing works

RNA-binding proteins balance brain function in health and disease

Schieweck, R., Ninkovic, J., & Kiebler, M. A. (2020) · Physiological Reviews · doi:10.1152/physrev.00047.2019 · Cited by 104 · see citing works

Effects of Acute Aerobic Exercise on Rats Serum Extracellular Vesicles Diameter, Concentration and Small RNAs Content

de Oliveira, G. P., Porto, W. F., Palu, C. C., Pereira, L. M., Petriz, B. A., de Almeida, J. A., Viana, J., Filho, N. N. A., Franco, O. L., & Pereira, R. W. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00532 · Cited by 104 · see citing works

Systematic Review of Plant Ribosome Heterogeneity and Specialization

Martínez-Seidel, F., Beine-Golovchuk, O., Hsieh, Y.-C., & Kopka, J. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00948 · Cited by 104 · see citing works

Mutant Huntingtin stalls ribosomes and represses protein synthesis in a cellular model of Huntington disease

Eshraghi, M., Karunadharma, P. P., Blin, J., Shahani, N., Ricci, E. P., Michel, A. M., Urban, N. T., Galli, N., Sharma, M., Ramírez-Jarquín, U. N., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21637-y · Cited by 110 · see citing works

MISTERMINATE Mechanistically Links Mitochondrial Dysfunction with Proteostasis Failure

Wu, Z., Tantray, I., Lim, J., Chen, S., Li, Y., Davis, Z. H., Sitron, C. S., Dong, J., Gispert, S., Auburger, G. W. J., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.031 · Cited by 106 · see citing works

Detection and Degradation of Stalled Nascent Chains via Ribosome-Associated Quality Control

Sitron, C. S., & Brandman, O. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-110729 · Cited by 101 · see citing works

NEMF mutations that impair ribosome-associated quality control are associated with neuromuscular disease

Martin, P. B., Kigoshi-Tansho, Y., Sher, R. B., Ravenscroft, G., Stauffer, J. E., Kumar, R., Yonashiro, R., Müller, T., Griffith, C. B., Allen, W., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18327-6 · Cited by 100 · see citing works

Accurate design of translational output by a neural network model of ribosome distribution

Tunney, R. J., McGlincy, N. J., Graham, M. E., Naddaf, N., Pachter, L. S., & Lareau, L. F. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0080-2 · Cited by 96 · see citing works

tRNA Metabolism and Neurodevelopmental Disorders

Schaffer, A. E., Pinkard, O. W., & Coller, J. M. (2019) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-083118-015334 · Cited by 92 · see citing works

Neurodegenerative Charcot–Marie–Tooth disease as a case study to decipher novel functions of aminoacyl-tRNA synthetases

Wei, N., Zhang, Q., & Yang, X. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002955 · Cited by 94 · see citing works

Detecting and Rescuing Stalled Ribosomes

Yip, M. C. J., & Shao, S. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.03.008 · Cited by 94 · see citing works

Translation stress and collided ribosomes are co-activators of cGAS

Wan, L., Juszkiewicz, S., Blears, D., Bajpe, P. K., Han, Z., Faull, P. A., Mitter, R., Stewart, A., Snijders, A. P., Hegde, R. S., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.05.018 · Cited by 92 · see citing works

RNA Polymerase III Advances: Structural and tRNA Functional Views

Arimbasseri, G. A., & Maraia, R. J. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.03.003 · Cited by 94 · see citing works

SmProt: A Reliable Repository with Comprehensive Annotation of Small Proteins Identified from Ribosome Profiling

Li, Y., Zhou, H., Chen, X., Zheng, Y., Kang, Q., Hao, D., Zhang, L., Song, T., Luo, H., Hao, Y., et al. (2021) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2021.09.002 · Cited by 93 · see citing works

Neurodegeneration with Brain Iron Accumulation Disorders: Valuable Models Aimed at Understanding the Pathogenesis of Iron Deposition

Levi, S., & Tiranti, V. (2019) · Pharmaceuticals · doi:10.3390/ph12010027 · Cited by 90 · see citing works

Controlling translation via modulation of tRNA levels

Wilusz, J. E. (2015) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1287 · Cited by 91 · see citing works

Recent Progress on the Molecular Mechanism of Quality Controls Induced by Ribosome Stalling

Ikeuchi, K., Izawa, T., & Inada, T. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2018.00743 · Cited by 89 · see citing works

Ubiquitination of ABCE1 by NOT4 in Response to Mitochondrial Damage Links Co-translational Quality Control to PINK1-Directed Mitophagy

Wu, Z., Wang, Y., Lim, J., Liu, B., Li, Y., Vartak, R. S., Stankiewicz, T. R., Montgomery, S. B., & Lu, B. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.05.007 · Cited by 84 · see citing works

Heterogeneity of the translational machinery: Variations on a common theme

Sauert, M., Temmel, H., & Moll, I. (2014) · Biochimie · doi:10.1016/j.biochi.2014.12.011 · Cited by 87 · see citing works

RNA polymerase III transcription as a disease factorPreprint

Yeganeh, M., & Hernandez, N. (2020) · Genes & Development · doi:10.1101/gad.333989.119 · Cited by 85 · see citing works

Non-coding RNA in neural function, disease, and aging

Szafranski, K. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00087 · Cited by 85 · see citing works

tRNA Deregulation and Its Consequences in Cancer

Santos, M., Varanda, A. S., Varanda, A. S., Oliveira, C. R. A. D., & Santos, M. A. S. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.05.011 · Cited by 85 · see citing works

Mechanism for recycling tRNAs on stalled ribosomes

Yip, M. C. J., Keszei, A. F. A., Feng, Q., Chu, V., McKenna, M. J., & Shao, S. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0211-4 · Cited by 79 · see citing works

Loss of rescue factor unmasks epistatic mutation

Koch, L. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3807

Ribosome rescue and neurodegeneration

Darnell, J. C. (2014) · Science · doi:10.1126/science.1257193 · Cited by 14 · see citing works

GTPBP1 resolves paused ribosomes to maintain neuronal homeostasis

Terrey, M., Adamson, S. I., Gibson, A. L., Deng, T. Z., Ishimura, R., Chuang, J. H., & Ackerman, S. L. (2020) · eLife · doi:10.7554/elife.62731 · Cited by 47 · see citing works

Structural basis for impaired 5′ processing of a mutant tRNA associated with defects in neuronal homeostasis

Lai, L. B., Lai, S. M., Szymanski, E. S., Kapur, M., Choi, E. K., Al‐Hashimi, H. M., Ackerman, S. L., & Gopalan, V. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2119529119 · Cited by 16 · see citing works

Defective tRNA Processing by RNase P Contributes to Neurodegeneration in Mice

Lai, S. M. (2017) · OhioLink ETD Center (Ohio Library and Information Network)