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Codon and amino acid content are associated with mRNA stability in mammalian cells
Open accessAbstract
Messenger RNA (mRNA) degradation plays a critical role in regulating transcript levels in the cell and is a major control point for modulating gene expression. In yeast and other model organisms, codon identity is a powerful determinant of transcript stability, contributing broadly to impact half-lives. General principles governing mRNA stability are poorly understood in mammalian systems. Importantly, however, the degradation machinery is highly conserved, thus it seems logical that mammalian transcript half-lives would also be strongly influenced by coding determinants. Herein we characterize the contribution of coding sequence towards mRNA decay in human and Chinese Hamster Ovary cells. In agreement with previous studies, we observed that synonymous codon usage impacts mRNA stability in mammalian cells. Surprisingly, however, we also observe that the amino acid content of a gene is an additional determinant correlating with transcript stability. The impact of codon and amino acid identity on mRNA decay appears to be associated with underlying tRNA and intracellular amino acid concentrations. Accordingly, genes of similar physiological function appear to coordinate their mRNA stabilities in part through codon and amino acid content. Together, these results raise the possibility that intracellular tRNA and amino acid levels interplay to mediate coupling between translational elongation and mRNA degradation rate in mammals.
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“Prior work has demonstrated strong relationships between codon usage and mRNA half-life23,78.”
From Predicting RNA-seq coverage from DNA sequence as a unifying model of gene regulation (2025) · cites this paper as [78]
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“Although we generally do not find determinants of mRNA half-life in the 3′ UTR attributions, we do observe a correlation between codon-aggregated gradient saliencies of gene exon coverage and MPRA measurements from a previous publication78 (Pearson’ R = 0.59) (Supplementary Fig. 11a).”
From Predicting RNA-seq coverage from DNA sequence as a unifying model of gene regulation (2025) · cites this paper as [78]
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Cites
R: A Language and Environment for Statistical Computing
R Core Team (2000) · doi:10.32614/r.manuals · Cited by 355,893
Transcript-level expression analysis of RNA-seq experiments with HISAT, StringTie and Ballgown
Pertea, M., Kim, D., Pertea, G. M., Leek, J. T., & Salzberg, S. L. (2016) · Nature Protocols · doi:10.1038/nprot.2016.095 · Cited by 6,783
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Interactive Tree Of Life (iTOL) v4: recent updates and new developments
Letunić, I., & Peer Bork, B. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz239 · Cited by 5,988
Tight control of gene expression in mammalian cells by tetracycline-responsive promoters.
Gossen, M., & Bujard, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5547 · Cited by 4,943 · cited 1×
“…test whether changes in mRNA levels reflect changes in stability, we shut off transcription of reporter mRNAs by doxy-cycline treatment in HEK293 Tet-off cells, which express a tetracycline-regulated transcription activator that is inactive in the presence of tetracycline or doxycycline [50].”
Liao, Y., Smyth, G. K., & Shi, W. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz114 · Cited by 2,927
Post-transcriptional gene regulation by mRNA modifications
Zhao, B. S., Roundtree, I. A., & He, C. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.132 · Cited by 2,469
MODOMICS: a database of RNA modification pathways. 2017 update
Boccaletto, P., Machnicka, M. A., Purta, E., Piątkowski, P., Bagiński, B., Wirecki, T. K., de Crécy‐Lagard, V., Ross, R. L., Limbach, P. A., Kötter, A., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1030 · Cited by 1,767
Serine, glycine and one-carbon units: cancer metabolism in full circle
Locasale, J. W. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3557 · Cited by 1,727
The highways and byways of mRNA decay
Garneau, N. L., Wilusz, J., & Wilusz, C. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2104 · Cited by 1,294
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
Codon Optimality Is a Major Determinant of mRNA Stability
Presnyak, V., Alhusaini, N., Chen, Y.-H., Martin, S., Morris, N., Kline, N., Olson, S., Weinberg, D., Baker, K. E., Graveley, B. R., et al. (2015) · Cell · doi:10.1016/j.cell.2015.02.029 · Cited by 1,078
Self-citationThe mechanics of miRNA-mediated gene silencing: a look under the hood of miRISC
Fabian, M. R., & Sonenberg, N. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2296 · Cited by 1,066
Serine and one-carbon metabolism in cancer
Yang, M., & Vousden, K. H. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.81 · Cited by 992
Acetylation of Cytidine in mRNA Promotes Translation Efficiency
Arango, D., Sturgill, D., Alhusaini, N., Dillman, A. A., Sweet, T. J., Hanson, G., Hosogane, M., Sinclair, W. R., Nanan, K. K., Mandler, M. D., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.030 · Cited by 862
Self-citationCodon optimality, bias and usage in translation and mRNA decay
Hanson, G., & Coller, J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.91 · Cited by 825
Self-citationRegulation of cytoplasmic mRNA decay
Schoenberg, D. R., & Maquat, L. E. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3160 · Cited by 656
Anderson, J. S. J., & Parker, R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1497 · Cited by 652
Tissue-Specific Differences in Human Transfer RNA Expression
Dittmar, K. A., Goodenbour, J. M., & Pan, T. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020221 · Cited by 601
Regulation by 3′-Untranslated Regions
Mayr, C. (2017) · Annual Review of Genetics · doi:10.1146/annurev-genet-120116-024704 · Cited by 588
Efficient and quantitative high-throughput tRNA sequencing
Zheng, G., Qin, Y., Clark, W. C., Dai, Q., Yi, C., He, C., Lambowitz, A. M., & Pan, T. (2015) · Nature Methods · doi:10.1038/nmeth.3478 · Cited by 550
A Dual Program for Translation Regulation in Cellular Proliferation and Differentiation
Gingold, H., Tehler, D., Christoffersen, N. R., Nielsen, M. M., Asmar, F., Kooistra, S. M., Christophersen, N. S., Christensen, L. L., Borre, M., Sørensen, K. D., et al. (2014) · Cell · doi:10.1016/j.cell.2014.08.011 · Cited by 513
Muhlrad, D., Decker, C. J., & Parker, R. (1994) · Genes & Development · doi:10.1101/gad.8.7.855 · Cited by 507
Evolutionary conservation of codon optimality reveals hidden signatures of cotranslational folding
Pechmann, S., & Frydman, J. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2466 · Cited by 504
Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover
Yamashita, A., Chang, T.-C., Yamashita, Y., Zhu, W., Zhong, Z., Chen, C. A., & Shyu, A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1016 · Cited by 504
Dynamics of Translation of Single mRNA Molecules In Vivo
Yan, X., Hoek, T. A., Vale, R. D., & Tanenbaum, M. E. (2016) · Cell · doi:10.1016/j.cell.2016.04.034 · Cited by 503
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
Mammalian miRNA RISC Recruits CAF1 and PABP to Affect PABP-Dependent Deadenylation
Fabian, M. R., Mathonnet, G., Sundermeier, T. R., Mathys, H., Zipprich, J. T., Svitkin, Y. V., Rivas, F. V., Jínek, M., Wohlschlegel, J. A., Doudna, J. A., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.004 · Cited by 427
Modifications and functional genomics of human transfer RNA
Pan, T. (2018) · Cell Research · doi:10.1038/s41422-018-0013-y · Cited by 415
Eulálio, A., Huntzinger, E., & Izaurralde, E. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1405 · Cited by 414
Xu, N., Chen, C. A., & Shyu, A. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4611 · Cited by 350
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
Decoding the genome: a modified view
Agris, P. F. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh185 · Cited by 341
An essential component of the decapping enzyme required for normal rates of mRNA turnover
Beelman, C. A., Stevens, A., Caponigro, G., LaGrandeur, T. E., Hatfield, L., Fortner, D. M., & Parker, R. (1996) · Nature · doi:10.1038/382642a0 · Cited by 327
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
Balanced Codon Usage Optimizes Eukaryotic Translational Efficiency
Qian, W., Yang, J.-R., Pearson, N. M., Maclean, C. J., & Zhang, J. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002603 · Cited by 308
The MECP2 duplication syndrome
Ramocki, M. B., Tavyev, Y. J., & Peters, S. U. (2010) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.33184 · Cited by 308
Chen, Y., Boland, A., Kuzuoğlu‐Öztürk, D., Bawankar, P., Loh, B., Chang, C.-T., Weichenrieder, O., & Izaurralde, E. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.034 · Cited by 306
l-Serine in disease and development
de Koning, T. J., Snell, K., Durán, M., Berger, R., Poll‐The, B. T., & Surtees, R. A. H. (2003) · Biochemical Journal · doi:10.1042/bj20021785 · Cited by 304
Amino acid regulation of gene expression
Fafournoux, P., Bruhat, A., & Jousse, C. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510001 · Cited by 299
Positively Charged Residues Are the Major Determinants of Ribosomal Velocity
Charneski, C. A., & Hurst, L. D. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001508 · Cited by 299
Wu, C. C., Zinshteyn, B., Wehner, K. A., & Green, R. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.009 · Cited by 298
The DEAD-Box Protein Dhh1p Couples mRNA Decay and Translation by Monitoring Codon Optimality
Radhakrishnan, A., Chen, Y.-H., Martin, S., Alhusaini, N., Green, R., & Coller, J. (2016) · Cell · doi:10.1016/j.cell.2016.08.053 · Cited by 297
Self-citationtRNA over-expression in breast cancer and functional consequences
Pavon-Eternod, M., Gomes, S., Geslain, R., Dai, Q., Rosner, M. R., & Pan, T. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp787 · Cited by 296
Codon Usage and 3′ UTR Length Determine Maternal mRNA Stability in Zebrafish
Mishima, Y., & Tomari, Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.027 · Cited by 288
Schaffer, A. E., Eggens, V. R., Çağlayan, A. O., Reuter, M. S., Scott, E., Coufal, N. G., Silhavy, J. L., Xue, Y., Kayserili, H., Yasuno, K., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.049 · Cited by 283
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
Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast.Preprint
Caponigro, G., & Parker, R. (1995) · Genes & Development · doi:10.1101/gad.9.19.2421 · Cited by 279
Functional Link between the Mammalian Exosome and mRNA Decapping
Wang, Z., & Kiledjian, M. (2001) · Cell · doi:10.1016/s0092-8674(01)00592-x · Cited by 263
Webster, M. W., Chen, Y.-H., Stowell, J. A. W., Alhusaini, N., Sweet, T. J., Graveley, B. R., Coller, J., & Passmore, L. A. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.033 · Cited by 258
Self-citationThe mRNA cap-binding protein eIF4E in post-transcriptional gene expression
von der Haar, T., Gross, J. D., Wagner, G., & McCarthy, J. E. G. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb779 · Cited by 234
Conserved principles of mammalian transcriptional regulation revealed by RNA half-life
Friedel, C. C., Dölken, L., Ruzsics, Z., Koszinowski, U. H., & Zimmer, R. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp542 · Cited by 230
Spies, N., Burge, C. B., & Bartel, D. P. (2013) · Genome Research · doi:10.1101/gr.156919.113 · Cited by 217
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
Self-citationSchwartz, D. C., & Parker, R. (2000) · Molecular and Cellular Biology · doi:10.1128/.20.21.7933-7942.2000 · Cited by 187
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 183
Liyanage, V. R. B., & Rastegar, M. (2014) · NeuroMolecular Medicine · doi:10.1007/s12017-014-8295-9 · Cited by 182
Gossmann, T. I., Keightley, P. D., & Eyre‐Walker, A. (2012) · Genome Biology and Evolution · doi:10.1093/gbe/evs027 · Cited by 178
Endres, L., Dedon, P. C., & Begley, T. J. (2015) · RNA Biology · doi:10.1080/15476286.2015.1031947 · Cited by 173
Colombo, S. L., Palacios‐Callender, M., Frakich, N., Carcamo, S., Kovacs, I., Tudzarova, S., & Moncada, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117500108 · Cited by 171
Codon bias confers stability to human mRNAs
Hia, F., Yang, S. F., Shichino, Y., Yoshinaga, M., Murakawa, Y., Vandenbon, A., Fukao, A., Fujiwara, T., Landthaler, M., Natsume, T., et al. (2019) · EMBO Reports · doi:10.15252/embr.201948220 · Cited by 171
The chemical diversity of RNA modifications
Ontiveros, R. J., Stoute, J., & Liu, K. F. (2019) · Biochemical Journal · doi:10.1042/bcj20180445 · Cited by 164
Rezgui, V. A. N., Tyagi, K., Ranjan, N., Konevega, A. L., Mittelstaet, J., Rodnina, M. V., Peter, M., & Pedrioli, P. G. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300781110 · Cited by 163
Cancer Metabolism: Is Glutamine Sweeter than Glucose?
Lu, W., Pelicano, H., & Huang, P. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.08.017 · Cited by 146
Artieri, C. G., & Fraser, H. B. (2014) · Genome Research · doi:10.1101/gr.175893.114 · Cited by 136
Modelling the Efficiency of Codon–tRNA Interactions Based on Codon Usage Bias
Sabi, R., & Tuller, T. (2014) · DNA Research · doi:10.1093/dnares/dsu017 · Cited by 135
Structural and molecular mechanisms for the control of eukaryotic 5′–3′ mRNA decay
Mugridge, J. S., Coller, J., & Gross, J. D. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0164-z · Cited by 133
Self-citationHuman DDX6 effects miRNA-mediated gene silencing via direct binding to CNOT1
Rouya, C., Siddiqui, N., Morita, M., Duchaine, T., Fabian, M., & Sonenberg, N. (2014) · RNA: A publication of the RNA Society · doi:10.1261/rna.045302.114 · Cited by 133
Coding regions affect mRNA stability in human cells
Narula, A., Ellis, J., Taliaferro, J. M., & Rissland, O. S. (2019) · RNA · doi:10.1261/rna.073239.119 · Cited by 127
YAMAT-seq: an efficient method for high-throughput sequencing of mature transfer RNAs
Shigematsu, M., Honda, S., Loher, P., Telonis, A. G., Rigoutsos, I., & Kirino, Y. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx005 · Cited by 126
Genome-wide technology for determining RNA stability in mammalian cells
Tani, H., & Akimitsu, N. (2012) · RNA Biology · doi:10.4161/rna.22036 · Cited by 120
Metformin reverses early cortical network dysfunction and behavior changes in Huntington’s disease
Arnoux, I., Willam, M., Griesche, N., Krummeich, J., Watari, H., Offermann, N., Weber, S. S., Dey, P. N., Chen, C., Monteiro, O., et al. (2018) · eLife · doi:10.7554/elife.38744 · Cited by 117
Dana, A., & Tuller, T. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002755 · Cited by 112
Lü, H., Ash, R. T., He, L.-J., Kee, S. E., Wang, W., Yu, D., Hao, S., Meng, X., Ure, K., Ito, A., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.07.018 · Cited by 108
Assessing the Disease-Liability of Mutations in CFTRPreprint
Férec, C., & Cutting, G. R. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009480 · Cited by 107
Variation and selection on codon usage bias across an entire subphylum
LaBella, A. L., Opulente, D. A., Steenwyk, J. L., Hittinger, C. T., & Rokas, A. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008304 · Cited by 106
Wilusz, C. J., Gao, M., Jones, C. L., Wilusz, J., & Peltz, S. W. (2001) · PubMed Central · Cited by 97
miRISC recruits decapping factors to miRNA targets to enhance their degradation
Nishihara, T., Zekri, L., Braun, J. E., & Izaurralde, E. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt619 · 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
Self-citationmiRISC and the CCR4–NOT complex silence mRNA targets independently of 43S ribosomal scanning
Kuzuoğlu‐Öztürk, D., Bhandari, D., Huntzinger, E., Fauser, M., Helms, S., & Izaurralde, E. (2016) · The EMBO Journal · doi:10.15252/embj.201592901 · Cited by 91
Zhang, Z., Ye, Y., Gong, J., Ruan, H., Liu, C., Xiang, Y., Cai, C. C., Guo, A., Ling, J., Diao, L., et al. (2018) · Communications Biology · doi:10.1038/s42003-018-0239-8 · Cited by 84
Mammalian Mitochondrial Ribosomal Proteins (4)
O’Brien, T. W., Liu, J., Sylvester, J. E., Mougey, E. B., Fischel‐Ghodsian, N., Thiede, B., Wittmann‐Liebold, B., & Graack, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909762199 · Cited by 84
BRIC-seq: A genome-wide approach for determining RNA stability in mammalian cells
Imamachi, N., Tani, H., Onoguchi‐Mizutani, R., Imamura, K., Irie, T., Suzuki, Y., & Akimitsu, N. (2013) · Methods · doi:10.1016/j.ymeth.2013.07.014 · Cited by 82
mRNA deadenylation by Pan2–Pan3
Wolf, J., & Passmore, L. A. (2014) · Biochemical Society Transactions · doi:10.1042/bst20130211 · Cited by 78
Codon choice directs constitutive mRNA levels in trypanosomes
Nascimento, J. D. F., Kelly, S. L., Sunter, J. D., & Carrington, M. (2018) · eLife · doi:10.7554/elife.32467 · Cited by 77
Analysis of the association between codon optimality and mRNA stability in Schizosaccharomyces pombe
Harigaya, Y., & Parker, R. (2016) · BMC Genomics · doi:10.1186/s12864-016-3237-6 · Cited by 76
Chen, S., Li, K., Cao, W., Wang, J., Zhao, T., Huan, Q., Yang, Y., Wu, S., & Qian, W. (2017) · Molecular Biology and Evolution · doi:10.1093/molbev/msx229 · Cited by 75
The organization and regulation of mRNA –protein complexes
Rissland, O. S. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1369 · Cited by 73
Attenuated Codon Optimality Contributes to Neural-Specific mRNA Decay in Drosophila
Burow, D. A., Martin, S., Quail, J. F., Alhusaini, N., Coller, J., & Cleary, M. D. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.039 · Cited by 68
Self-citationMammalian Mitochondrial Ribosomal Proteins
Goldschmidt‐Reisin, S., Kitakawa, M., Herfurth, E., Wittmann‐Liebold, B., Grohmann, L., & Graack, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34828 · Cited by 68
Ribothrypsis, a novel process of canonical mRNA decay, mediates ribosome-phased mRNA endonucleolysis
Ibrahim, F., Maragkakis, M., Alexiou, P., & Mourelatos, Z. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0042-8 · Cited by 63
Purification of RNA by SDS Solubilization and Phenol ExtractionPreprint
Rio, D. C., Ares, M., Hannon, G. J., & Nilsen, T. W. (2010) · Cold Spring Harbor Protocols · doi:10.1101/pdb.prot5438 · Cited by 63
Amino acid regulation of gene expression
Jousse, C., Bruhat, A., & Fafournoux, P. (1999) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-199907000-00008 · Cited by 61
The influence of microRNAs and poly(A) tail length on endogenous mRNA–protein complexes
Rissland, O. S., Subtelny, A. O., Wang, M., Lugowski, A., Nicholson, B. L., Laver, J. D., Sidhu, S. S., Smibert, C. A., Lipshitz, H. D., & Bartel, D. P. (2017) · Genome biology · doi:10.1186/s13059-017-1330-z · Cited by 52
Leung‐Pineda, V., Pan, Y., Chen, H., & Kilberg, M. S. (2004) · Biochemical Journal · doi:10.1042/bj20031383 · Cited by 51
Translation elongation and mRNA stability are coupled through the ribosomal A-site
Hanson, G. K., Alhusaini, N., Morris, N. J., Sweet, T. J., & Coller, J. (2018) · RNA · doi:10.1261/rna.066787.118 · Cited by 51
Self-citationMattijssen, S., Arimbasseri, G. A., Iben, J., Gaidamakov, S., Lee, J., Hafner, M., & Maraia, R. J. (2017) · eLife · doi:10.7554/elife.28889 · Cited by 50
Emerging Themes in Regulation of Global mRNA Turnover in cis
Chen, C. A., & Shyu, A. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.014 · Cited by 42
Mammalian Mitochondrial Ribosomal Proteins (2)
O’Brien, T. W., Fiesler, S. E., Denslow, N. D., Thiede, B., Wittmann‐Liebold, B., Mougey, E. B., Sylvester, J. E., & Graack, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.51.36043 · Cited by 35
Single Amino Acid Repeats in the Proteome World: Structural, Functional, and Evolutionary Insights
Kumar, A. S., Sowpati, D. T., & Mishra, R. K. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166854 · Cited by 31
Promoter architecture determines cotranslational regulation of mRNAPreprint
Espinar, L., Schikora-Tamarit, M. À., Domingo, J., & Carey, L. B. (2018) · Genome Research · doi:10.1101/gr.230458.117 · Cited by 22
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Kami, D., Kitani, T., Nakamura, A., Wakui, N., Onoguchi‐Mizutani, R., Ohue, M., Kametani, F., Akimitsu, N., & Gojo, S. (2018) · PLoS ONE · doi:10.1371/journal.pone.0203708 · Cited by 13
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Roles of mRNA poly(A) tails in regulation of eukaryotic gene expression
Passmore, L. A., & Coller, J. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00417-y · Cited by 590
Self-citationPredicting RNA-seq coverage from DNA sequence as a unifying model of gene regulation
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Theoretical basis for stabilizing messenger RNA through secondary structure design
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Metadata
- Authors
- Forrest, M. E., Pinkard, O., Martin, S., Sweet, T. J., Hanson, G., & Coller, J.
- Affiliations
- Case Western Reserve University (US)
- Corresponding author
- Coller, Jeff
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2020-02-13
- Volume
- 15
- Issue
- 2
- Pages
- e0228730
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC7018022
- OpenAlex
- W3006243445
- Cited by
- 116
- References
- 104
- Citations by year
- 2026: 15 · 2025: 23 · 2024: 25 · 2023: 15 · 2022: 12 · 2021: 15 · 2020: 9
- FWCI
- 4.14
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- National Institutes of Health (GM125086)
- National Institute of General Medical Sciences (GM118018, T32GM136570)
- 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
- mRNA stability, mRNA degradation, codon usage, synonymous codons, amino acid content, transcript half-life, translation elongation, gene expression regulation, mammalian cells, CHO cells
- MeSH terms
- Amino Acids, Animals, Codon, Cricetulus, Half-Life, Cricetinae, HeLa Cells, Humans, RNA, Messenger, RNA, Transfer, Open Reading Frames, CHO Cells, RNA Stability
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.
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