Cited by 456RNA and protein synthesis mechanismsRNA modifications and cancerGenetics and Neurodevelopmental Disorders

The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.

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

Open access

Ishimura, Ryuta, Nagy, Gabor, Dotu, Ivan, Zhou, Huihao, Yang, Xiang-Lei, Schimmel, Paul, Senju, Satoru, Nishimura, Yasuharu, Chuang, Jeffrey H., Ackerman, Susan L.·2014·Science

DOI 10.1126/science.1249749PMC PMC4281038

Open this paper in CoChat — free account

Abstract

Problems making proteins kills nerve cells: Neurodegeneration is associated with a variety of different diseases, but its cellular roots are often obscure. Ishimura et al. find that mutant mice whose brain cells start to die rapidly soon after birth have lost the function of two vital cellular components (see the Perspective by Darnell). The first is a protein that releases stalled ribosomes stuck on messenger RNA (mRNA); the second is a transfer RNA (tRNA), which reads the code for arginine in the mRNA. This tRNA is expressed predominantly in the central nervous system. The lack of the tRNA leads to increased ribosomal stalling at arginine codons, which, when left uncorrected, blocks protein synthesis and proves fatal. Science , this issue p. 455 ; see also p. 378

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

Crossref · 10.1126/science.1249749

Cites

22 of 22 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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
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
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
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 1,280
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 561
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
Dom34 Rescues Ribosomes in 3′ Untranslated Regions
Guydosh, N. R., & Green, R. (2014) · Cell · doi:10.1016/j.cell.2014.02.006 · Cited by 370
Translational Pausing Ensures Membrane Targeting and Cytoplasmic Splicing of XBP1u mRNA
Yanagitani, K., Kimata, Y., Kadokura, H., & Kohno, K. (2011) · Science · doi:10.1126/science.1197142 · Cited by 362
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 346
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

Flagged first, then by citations

Show all 22 references

Sorted by citations

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
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 1,056
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 565
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
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 545
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
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 476
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 471
Self-citation
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
Ribosome-associated protein quality control
Brandman, O., & Hegde, R. S. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3147 · Cited by 445
Ribosomopathies: There’s strength in numbers
Mills, E. W., & Green, R. (2017) · Science · doi:10.1126/science.aan2755 · Cited by 444
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 427
Efficient Test and Visualization of Multi-Set Intersections
Wang, M., Zhao, Y., & Zhang, B. (2015) · Scientific Reports · doi:10.1038/srep16923 · Cited by 395
Modifications and functional genomics of human transfer RNA
Pan, T. (2018) · Cell Research · doi:10.1038/s41422-018-0013-y · Cited by 415
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 405
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 354
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 330
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 309
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
“The C57BL6/J (B6J)-nmf205 mouse model has mutations in both the translation GTPase GTPBP2 and the neuronal tRNAArgUCU genes that cause neurodegeneration through ribosomal stalling (Ishimura et al., 2014, 2016).”
Background
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
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
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
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 254
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
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
Proteome complexity and the forces that drive proteome imbalance
Harper, J. W., & Bennett, E. J. (2016) · Nature · doi:10.1038/nature19947 · Cited by 239
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 240
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
Self-citation
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 204
Pausing on Polyribosomes: Make Way for Elongation in Translational Control
Richter, J. D., & Coller, J. (2015) · Cell · doi:10.1016/j.cell.2015.09.041 · Cited by 207
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 201
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 208
Self-citation
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
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 186
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 193
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 185
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 193
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 193
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
Quantitative tRNA-sequencing uncovers metazoan tissue-specific tRNA regulation
Pinkard, O. W., McFarland, S., Sweet, T. J., & Coller, J. (2020) · Nature Communications · doi:10.1038/s41467-020-17879-x · Cited by 184
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
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
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 179
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
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 179
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 195
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 172
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 172
The ribosomal P-stalk couples amino acid starvation to GCN2 activation in mammalian cells
Harding, H. P., Ordóñez, A., Allen, F., Parts, L., Inglis, A. J., Williams, R. L., & Ron, D. (2019) · eLife · doi:10.7554/elife.50149 · Cited by 183
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
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 167
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 169
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 164
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
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 140
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 138
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
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 164
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 135
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 139
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
Codon optimality-mediated mRNA degradation: Linking translational elongation to mRNA stability
Bae, H., & Coller, J. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.032 · Cited by 135
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
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 132
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
Self-citation
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 134
The life and times of a tRNA
Phizicky, E. M., & Hopper, A. K. (2023) · RNA · doi:10.1261/rna.079620.123 · Cited by 122
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
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
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
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 120
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
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 118
Self-citation
Translation and mRNA Stability Control
Wu, Q., & Bazzini, A. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052621-091808 · Cited by 120
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 115
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
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
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 111
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 108
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 106
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 114
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
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 100
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 105
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 95
tRNA Metabolism and Neurodevelopmental Disorders
Schaffer, A. E., Pinkard, O. W., & Coller, J. (2019) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-083118-015334 · Cited by 95
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
Self-citation
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
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 94
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
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 99
Self-citation
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
Controlling translation via modulation of tRNA levels
Wilusz, J. E. (2015) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1287 · Cited by 101
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 86
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 87
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 92
RNA polymerase III transcription as a disease factorPreprint
Yeganeh, M., & Hernandez, N. (2020) · Genes & Development · doi:10.1101/gad.333989.119 · Cited by 85
Non-coding RNA in neural function, disease, and aging
Szafranski, K. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00087 · Cited by 86
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 88
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

Authors: Ishimura, R., Nagy, G., Dotu, I., Zhou, H., Yang, X.-L., Schimmel, P., Senju, S., Nishimura, Y., Chuang, J. H., & Ackerman, S. L.
Affiliations: Howard Hughes Medical Institute (US)
The Jackson Laboratory for Genomic Medicine, 263 Farmington Avenue, Farmington, CT 06030, USA.
Scripps Research Institute (US)
Kumamoto University (JP)
The Jackson Laboratory for Genomic Medicine (US)
Corresponding author: Ishimura, Ryuta
Nagy, Gabor
Ackerman, Susan L.
ORCID: Zhou, Huihao
Yang, Xiang-Lei
Schimmel, Paul
Chuang, Jeffrey H.
Ackerman, Susan L.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2014-07-25
Volume: 345
Issue: 6195
Pages: 455-459
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1249749
PMC: PMC4281038
OpenAlex: W1983859619
Cited by: 455
References: 22
Citations by year: 2026: 29 · 2025: 34 · 2024: 41 · 2023: 47 · 2022: 33 · 2021: 40 · 2020: 44 · 2019: 51 · 2018: 42 · 2017: 30 · 2016: 30 · 2015: 24 · 2014: 9
FWCI: 12.72
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
Funders: National Science Foundation
Howard Hughes Medical Institute
Natural Environment Research Council
National Cancer Institute (#CA34196, P30CA034196)
National Institute of Neurological Disorders and Stroke (R01NS085092)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
Keywords: ribosome stalling, tRNA mutations, pelota, ribosome recycling, neurodegeneration
MeSH terms: Animals, Cell Nucleus, Cerebellum, Endonucleases, Mice, Inbred BALB C, Mice, Inbred C57BL, Microfilament Proteins, Ribosomes, RNA, Transfer, Arg, Protein Biosynthesis, Point Mutation, Cell Cycle Proteins, GTP-Binding Proteins, Neurodegenerative Diseases, RNA Splice Sites, Mice

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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks