A cellular handbook for collided ribosomes: Surveillance pathways and collision types
Open accessAbstract
Translating ribosomes slow down or completely stall when they encounter obstacles on mRNAs. Such events can lead to ribosomes colliding with each other and forming complexes of two (disome), three (trisome) or more ribosomes. While these events can activate surveillance pathways, it has been unclear if collisions are common on endogenous mRNAs and whether they are usually detected by these cellular pathways. Recent genome-wide surveys of collisions revealed widespread distribution of disomes and trisomes across endogenous mRNAs in eukaryotic cells. Several studies further hinted that the recognition of collisions and response to them by multiple surveillance pathways depend on the context and duration of the ribosome stalling. This review considers recent efforts in the identification of endogenous ribosome collisions and cellular pathways dedicated to sense their severity. We further discuss the potential role of collided ribosomes in modulating co-translational events and contributing to cellular homeostasis.
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
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?
If anabolic signaling drives high rates of translation without sufficient recovery or quality control, resulting translational errors may activate stress responses that impair protein synthesis efficiency.
“If anabolic signaling drives high rates of translation without sufficient recovery or quality control, the resulting increase in translational errors may activate stress responses that ultimately impair protein synthesis efficiency [208,209,210].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [209]
In “Multiple surveillance pathways detect ribosome collisions” (page not provided), the paper describes ribosome stalling or collisions activating an integrated stress response that blocks translation initiation. It does not connect that response to anabolic signaling, insufficient recovery, or an increase in translational errors, so it supports only the stress-response and translation-inhibition portion of the claim. (LLM, conf=0.86)
Experimental — accuracy not yet measuredRibosome collisions are detected by surveillance mechanisms including the E3 ubiquitin ligase ZNF598, which marks defective translational complexes for resolution and degradation.
“These events are detected by surveillance mechanisms that include the E3 ubiquitin ligase ZNF598, which helps mark defective translational complexes for resolution and degradation [208,209].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [209]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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
FMRP Stalls Ribosomal Translocation on mRNAs Linked to Synaptic Function and Autism
Darnell, J. C., Van Driesche, S. J., Zhang, C., Hung, K. Y. S., Mele, A., Fraser, C. E., Stone, E. F., Chen, C., Fak, J. J., Chi, S. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.013 · Cited by 2,072 · see citing works
TRANSLATIONAL REGULATION OFGCN4AND 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 1,258 · see citing works
Dever, T. E., Feng, L., Wek, R. C., Cigan, A. M., Donahue, T. F., & Hinnebusch, A. G. (1992) · Cell · doi:10.1016/0092-8674(92)90193-g · Cited by 776 · see citing works
Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation
Doma, M. K., & Parker, R. (2006) · Nature · doi:10.1038/nature04530 · Cited by 764 · see citing works
Brandman, O., Stewart-Ornstein, J., Wong, D., Larson, A. G., Williams, C. C., Li, G., Zhou, S., King, D., Shen, P. S., Weibezahn, J., et al. (2012) · Cell · doi:10.1016/j.cell.2012.10.044 · Cited by 631 · 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 profiling reveals the what, when, where and how of protein synthesis
Brar, G. A., & Weissman, J. S. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4069 · Cited by 535 · 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
Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
Bengtson, M. H., & Joazeiro, C. A. P. (2010) · Nature · doi:10.1038/nature09371 · Cited by 470 · 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
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
Sundaramoorthy, E., Leonard, M., Mak, R., Liao, J., Fulzele, A., & Bennett, E. J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.026 · Cited by 375 · 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
Self-citationJuszkiewicz, S., & Hegde, R. S. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.11.039 · Cited by 339 · see citing works
Ribosome Collision Is Critical for Quality Control during No-Go Decay
Simms, C. L., Yan, L. L., & Zaher, H. S. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.08.019 · Cited by 321 · see citing works
Collided ribosomes form a unique structural interface to induce Hel2-driven quality control pathways
Ikeuchi, K., Tesina, P., Matsuo, Y., Sugiyama, T., Cheng, J., Saeki, Y., Tanaka, K., Becker, T., Beckmann, R., & Inada, T. (2019) · The EMBO Journal · doi:10.15252/embj.2018100276 · Cited by 315 · see citing works
Ubiquitination of stalled ribosome triggers ribosome-associated quality control
Matsuo, Y., Ikeuchi, K., Saeki, Y., Iwasaki, S., Schmidt, C. M., Udagawa, T., Sato, F., Tsuchiya, H., Becker, T. A., Tanaka, K., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00188-1 · Cited by 314 · see citing works
Ribosome Profiling: Global Views of TranslationPreprint
Ingolia, N. T., Hussmann, J. A., & Weissman, J. S. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032698 · Cited by 285 · see citing works
Cho, P. F., Poulin, F., Yoon, A. C.-P., Cho-Park, I. B., Chicoine, J., Lasko, P., & Sonenberg, N. (2005) · Cell · doi:10.1016/j.cell.2005.02.024 · Cited by 279 · see citing works
Dimitrova-Paternoga, L., Kuroha, K., Tatematsu, T., & Inada, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808840200 · Cited by 252 · see citing works
Chu, J., Hong, N. A., Masuda, C. A., Jenkins, B., Nelms, K. A., Goodnow, C. C., Glynne, R. J., Wu, H., Masliah, E., Joazeiro, C. A. P., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812819106 · Cited by 238 · see citing works
Failure of RQC machinery causes protein aggregation and proteotoxic stress
Choe, Y., Park, S.-H., Hassemer, T., Körner, R., Vincenz‐Donnelly, L., Hayer-Hartl, M. K., & Hartl, F. U. (2016) · Nature · doi:10.1038/nature16973 · Cited by 237 · see citing works
Marton, M. J., de Aldana, C. R. V., Qiu, H., Chakraburtty, K., & Hinnebusch, A. G. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4474 · Cited by 223 · see citing works
Adjacent Codons Act in Concert to Modulate Translation Efficiency in Yeast
Gamble, C. E., Brule, C. E., Dean, K., Fields, S., & Grayhack, E. J. (2016) · Cell · doi:10.1016/j.cell.2016.05.070 · Cited by 222 · see citing works
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
An Active Role for the Ribosome in Determining the Fate of Oxidized mRNA
Simms, C. L., Hudson, B. H., Mosior, J., Rangwala, A. S., & Zaher, H. S. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.042 · Cited by 211 · see citing works
Garzia, A., Jafarnejad, S. M., Meyer, C., Chapat, C., Gogakos, T., Morozov, P. S., Amiri, M., Shapiro, M., Molina, H., Tuschl, T., et al. (2017) · Nature Communications · doi:10.1038/ncomms16056 · Cited by 209 · see citing works
The ASC-1 complex disassembles collided ribosomes
Juszkiewicz, S., Speldewinde, S. H., Wan, L., Svejstrup, J. Q., & Hegde, R. S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.006 · Cited by 206 · see citing works
Activation of GCN2 by the ribosomal P-stalk
Inglis, A. J., Masson, G. R., Shao, S., Perišić, O., McLaughlin, S. H., Hegde, R. S., & Williams, R. L. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1813352116 · Cited by 203 · see citing works
A Novel 4EHP-GIGYF2 Translational Repressor Complex Is Essential for Mammalian Development
Morita, M., Ler, L. W., Fabian, M. R., Siddiqui, N., Mullin, M. J., Henderson, V. C., Alain, T., Fonseca, B. D., Karashchuk, G., Bennett, C. F., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00455-12 · Cited by 198 · see citing works
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
Genome-wide Survey of Ribosome Collision
Han, P., Shichino, Y., Schneider‐Poetsch, T., Mito, M., Hashimoto, S., Udagawa, T., Kohno, K., Yoshida, M., Mishima, Y., Inada, T., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107610 · Cited by 187 · 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
Self-citationThe 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
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
Mechanism of ribosome stalling during translation of a poly(A) tail
Chandrasekaran, V., Juszkiewicz, S., Choi, J., Puglisi, J. D., Brown, A., Shao, S., Ramakrishnan, V., & Hegde, R. S. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0331-x · Cited by 173 · see citing works
ZAKα Recognizes Stalled Ribosomes through Partially Redundant Sensor Domains
Vind, A., Snieckute, G., Blasius, M., Tiedje, C., Krogh, N., Bekker‐Jensen, D. B., Andersen, K. L., Nordgaard, C., Tollenaere, M. A. X., Lund, A. H., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.03.021 · Cited by 171 · see citing works
Ribosome collisions trigger cis-acting feedback inhibition of translation initiation
Juszkiewicz, S., Slodkowicz, G., Lin, Z., Freire-Pritchett, P., Peak‐Chew, S., & Hegde, R. S. (2020) · eLife · doi:10.7554/elife.60038 · Cited by 170 · see citing works
Hickey, K. L., Dickson, K., Cogan, J. Z., Replogle, J. M., Schoof, M., D’Orazio, K. N., Sinha, N. K., Hussmann, J. A., Jost, M., Frost, A. S., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.007 · Cited by 162 · see citing works
CAT-tailing as a fail-safe mechanism for efficient degradation of stalled nascent polypeptides
Kostova, K. K., Hickey, K. L., Osuna, B. A., Hussmann, J. A., Frost, A. S., Weinberg, D. E., & Weissman, J. S. (2017) · Science · doi:10.1126/science.aam7787 · Cited by 160 · see citing works
Garcia-Barrio, M. T., Dong, J., Ufano, S., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.8.1887 · Cited by 159 · see citing works
Meyer, C., Garzia, A., Morozov, P. S., Molina, H., & Tuschl, T. (2020) · Molecular Cell · doi:10.1016/j.molcel.2019.12.024 · Cited by 159 · see citing works
RQT complex dissociates ribosomes collided on endogenous RQC substrate SDD1
Matsuo, Y., Tesina, P., Nakajima, S., Mizuno, M., Endo, A., Buschauer, R., Cheng, J., Shounai, O., Ikeuchi, K., Saeki, Y., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0393-9 · Cited by 150 · see citing works
Ribosome pausing, a dangerous necessity for co-translational events
Collart, M. A., & Weiss, B. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz763 · Cited by 149 · see citing works
Yonashiro, R., Tahara, E. B., Bengtson, M. H., et al. (2016) · eLife · doi:10.7554/elife.11794 · Cited by 147 · see citing works
Ivanov, I. P., Shin, B., Loughran, G., Tzani, I., Young, S. K., Cao, C., Atkins, J. F., & Dever, T. E. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.015 · Cited by 138 · see citing works
Transcriptome-wide sites of collided ribosomes reveal principles of translational pausingPreprint
Arpat, A. B., Liechti, A., Matos, M. D., Dreos, R., Janich, P., & Gatfield, D. (2020) · Genome Research · doi:10.1101/gr.257741.119 · Cited by 136 · 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
Letzring, D. P., Wolf, A. S., Brule, C. E., & Grayhack, E. J. (2013) · RNA · doi:10.1261/rna.039446.113 · Cited by 115 · see citing works
CAT tails drive degradation of stalled polypeptides on and off the ribosome
Sitron, C. S., & Brandman, O. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0230-1 · Cited by 107 · see citing works
Hashimoto, S., Sugiyama, T., Yamazaki, R., Nobuta, R., & Inada, T. (2020) · Scientific Reports · doi:10.1038/s41598-020-60241-w · Cited by 102 · see citing works
Dinkova, T. D., Keiper, B. D., Korneeva, N. L., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.100-113.2005 · Cited by 97 · see citing works
Translation of poly(A) tails leads to precise mRNA cleavage
Guydosh, N. R., & Green, R. (2017) · RNA · doi:10.1261/rna.060418.116 · Cited by 93 · see citing works
Self-citationShah, S., Molinaro, G., Liu, B., Wang, R., Huber, K. M., & Richter, J. D. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.02.076 · Cited by 91 · see citing works
Guydosh, N. R., Kimmig, P., Walter, P., & Green, R. (2017) · eLife · doi:10.7554/elife.29216 · Cited by 89 · see citing works
Self-citationNONU-1 Encodes a Conserved Endonuclease Required for mRNA Translation Surveillance
Glover, M. L., Burroughs, A. M., Monem, P. C., Egelhofer, T. A., Pule, M. N., Aravind, L., & Arribere, J. A. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.023 · Cited by 87 · see citing works
Expression of the Neuronal tRNA n-Tr20 Regulates Synaptic Transmission and Seizure Susceptibility
Kapur, M., Ganguly, A., Nagy, G., Adamson, S. I., Chuang, J. H., Frankel, W. N., & Ackerman, S. L. (2020) · Neuron · doi:10.1016/j.neuron.2020.07.023 · Cited by 75 · see citing works
In vitro analysis of RQC activities provides insights into the mechanism and function of CAT tailing
Osuna, B. A., Howard, C. J., Subheksha, K. C., Frost, A. S., & Weinberg, D. E. (2017) · eLife · doi:10.7554/elife.27949 · Cited by 73 · see citing works
Distinct regulatory ribosomal ubiquitylation events are reversible and hierarchically organized
Garshott, D. M., Sundaramoorthy, E., Leonard, M., et al. (2020) · eLife · doi:10.7554/elife.54023 · Cited by 72 · see citing works
Widespread Alterations in Translation Elongation in the Brain of Juvenile Fmr1 Knockout Mice
Sharma, S. D., Metz, J. B., Li, H., Hobson, B. D., Hornstein, N. J., Sulzer, D., Tang, G., & Sims, P. A. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.086 · Cited by 71 · see citing works
Eisenberg, A., Higdon, A. L., Hollerer, I., Fields, A. P., Jungreis, I., Diamond, P. D., Kellis, M., Jovanović, M., & Brar, G. A. (2020) · Cell Systems · doi:10.1016/j.cels.2020.06.011 · Cited by 71 · see citing works
Tollenaere, M. A. X., Tiedje, C., Rasmussen, S. H., Nielsen, J. C., Vind, A., Blasius, M., Batth, T. S., Mailand, N., Olsen, J. V., Gaestel, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.006 · Cited by 67 · see citing works
Ribosome Collisions Result in +1 Frameshifting in the Absence of No-Go Decay
Simms, C. L., Yan, L. L., Qiu, J., & Zaher, H. S. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.046 · Cited by 64 · see citing works
Ribosome collisions alter frameshifting at translational reprogramming motifs in bacterial mRNAs
Smith, A. M., Costello, M. S., Kettring, A. H., Wingo, R. J., & Moore, S. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1910613116 · Cited by 59 · see citing works
No-Go Decay mRNA cleavage in the ribosome exit tunnel produces 5′-OH ends phosphorylated by Trl1
Navickas, A., Chamois, S., Saint‐Fort, R., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13991-9 · Cited by 59 · see citing works
A proximity-dependent biotinylation map of a human cell: an interactive web resourcePreprint
Go, C. D., Knight, J. D. R., Rajasekharan, A., Rathod, B., Hesketh, G. G., Abe, K. T., Youn, J.-Y., Samavarchi-Tehrani, P., Zhang, H., Zhu, L. Y., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/796391 · Cited by 57 · see citing works
The extent of ribosome queuing in budding yeast
Diament, A., Feldman, A., Schochet, E., Kupiec, M., Arava, Y., & Tuller, T. (2018) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005951 · Cited by 56 · see citing works
Multi-protein bridging factor 1(Mbf1), Rps3 and Asc1 prevent stalled ribosomes from frameshifting
Wang, J., Zhou, J., Yang, Q., & Grayhack, E. J. (2018) · eLife · doi:10.7554/elife.39637 · Cited by 51 · see citing works
Jung, Y., Kim, H. D., Yang, H. W., Kim, H. J., Jang, C., & Kim, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.128 · Cited by 50 · see citing works
Inverted translational control of eukaryotic gene expression by ribosome collisions
Park, H., & Subramaniam, A. R. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000396 · Cited by 50 · see citing works
Hildebrandt, A., Brüggemann, M., Rücklé, C., Boerner, S., Heidelberger, J. B., Busch, A., Hänel, H., Voigt, A., Möckel, M. M., Ebersberger, S., et al. (2019) · Genome biology · doi:10.1186/s13059-019-1814-0 · Cited by 47 · see citing works
Simms, C. L., Kim, K. Q., Yan, L. L., et al. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007818 · Cited by 31 · see citing works
Overexpression of Eukaryotic Translation Elongation Factor 3 Impairs Gcn2 Protein Activation
Visweswaraiah, J., Lee, S. J., Hinnebusch, A. G., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.368266 · Cited by 23 · see citing works
FMRP ribonucleoprotein complexes and RNA homeostasis
Suardi, G. A. M., & Haddad, L. A. (2020) · Advances in genetics · doi:10.1016/bs.adgen.2020.01.001 · Cited by 17 · see citing works
Two Ribosomes Are Better Than One... Sometimes
Olson, A. N., & Dinman, J. D. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.022 · Cited by 3 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Muñoz López, M., López-Gil, J. F., Ramírez de la piscina Viúdez, X., Baz-Valle, E., & Tornero Aguilera, J. F. (2026) · Cells · doi:10.3390/cells15111041 · Cited by 1 · see citing works
“These events are detected by surveillance mechanisms that include the E3 ubiquitin ligase ZNF598, which helps mark defective translational complexes for resolution and degradation [208,209].”
- Authors
- Meydan, S., & Guydosh, N. R.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Guydosh, Nicholas R.
- Venue
- Current Genetics
- Published
- 2020-10-12
- Volume
- 67
- Issue
- 1
- Pages
- 19-26
- ISSN
- 0172-8083 (ISSN-L)
- 1432-0983
- PMC
- PMC7887001
- OpenAlex
- W3092101222
- Cited by
- 87
- References
- 77
- Citations by year
- 2026: 12 · 2025: 14 · 2024: 20 · 2023: 21 · 2022: 12 · 2021: 8
- FWCI
- 0.98
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Current Genetics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (DK075132)
- National Institute of General Medical Sciences (1FI2GM137845)
- 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 Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- ribosome collisions, ribosome stalling, endogenous mRNA, ribosome-associated quality control, eukaryotic translation
- MeSH terms
- Ribosomes, RNA, Messenger, Saccharomyces cerevisiae, Protein Biosynthesis, Saccharomyces cerevisiae Proteins, Ubiquitination
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