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The Mammalian Ribo-interactome Reveals Ribosome Functional Diversity and Heterogeneity
Open accessAbstract
During eukaryotic evolution, ribosomes have considerably increased in size, forming a surface-exposed ribosomal RNA (rRNA) shell of unknown function, which may create an interface for yet uncharacterized interacting proteins. To investigate such protein interactions, we establish a ribosome affinity purification method that unexpectedly identifies hundreds of ribosome-associated proteins (RAPs) from categories including metabolism and cell cycle, as well as RNA- and protein-modifying enzymes that functionally diversify mammalian ribosomes. By further characterizing RAPs, we discover the presence of ufmylation, a metazoan-specific post-translational modification (PTM), on ribosomes and define its direct substrates. Moreover, we show that the metabolic enzyme, pyruvate kinase muscle (PKM), interacts with sub-pools of endoplasmic reticulum (ER)-associated ribosomes, exerting a non-canonical function as an RNA-binding protein in the translation of ER-destined mRNAs. Therefore, RAPs interconnect one of life's most ancient molecular machines with diverse cellular processes, providing an additional layer of regulatory potential to protein expression.
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“This is characterized by the striated muscle-specific paralog RPL3L, which is prevalent in resting tissue. Following hypertrophic overload, RPL3L expression plummets and is replaced by the ubiquitous isoform RPL3.”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [189]
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“Rather than altering mRNA selectivity for contractile proteins, this paralog switch enables the RPL3-containing ribosomes to physically anchor to mitochondria, maximizing the local ATP supply required to sustain the massive energetic cost of hypertrophy [187,189].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [189]
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Cites
The Sequence Alignment/Map format and SAMtools
Li, H., Handsaker, B., Wysoker, A., Fennell, T., Ruan, J., Homer, N., Marth, G., Abecasis, G., Durbin, R., & 1000 Genome Project Data Processing Subgroup (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp352 · Cited by 62,041
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400
STAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709
limma powers differential expression analyses for RNA-sequencing and microarray studies
Ritchie, M. E., Phipson, B., Wu, D., Hu, Y., Law, C. W., Shi, W., & Smyth, G. K. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv007 · Cited by 40,458
Cutadapt removes adapter sequences from high-throughput sequencing reads
Martin, M. (2011) · EMBnet.journal · doi:10.14806/ej.17.1.200 · Cited by 33,889
Multiplex Genome Engineering Using CRISPR/Cas Systems
Cong, L., Ran, F. A., Cox, D., Lin, S., Barretto, R., Habib, N., Hsu, P. D., Wu, X., Jiang, W., Marraffini, L. A., et al. (2013) · Science · doi:10.1126/science.1231143 · Cited by 15,339
The new frontier of genome engineering with CRISPR-Cas9
Doudna, J. A., & Charpentier, E. (2014) · Science · doi:10.1126/science.1258096 · Cited by 7,062
N6-methyladenosine Modulates Messenger RNA Translation Efficiency
Wang, X., Zhao, B. S., Roundtree, I. A., Lu, Z., Han, D., Ma, H., Weng, X., Chen, K., Shi, H., & He, C. (2015) · Cell · doi:10.1016/j.cell.2015.05.014 · Cited by 3,483
Thompson, A., Schäfer, J., Kuhn, K., Kienle, S., Schwarz, J., Schmidt, G., Neumann, T., & Hamon, C. (2003) · Analytical Chemistry · doi:10.1021/ac0262560 · Cited by 2,425
Ingolia, N. T., Lareau, L. F., & Weissman, J. S. (2011) · Cell · doi:10.1016/j.cell.2011.10.002 · Cited by 2,187
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132
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
The CRAPome: a contaminant repository for affinity purification–mass spectrometry data
Mellacheruvu, D., Wright, Z., Couzens, A. L., Lambert, J.-P., St-Denis, N. A., Li, T., Miteva, Y. V., Hauri, S., Sardiu, M. E., Low, T. Y., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2557 · Cited by 1,686
Inhibition of Translational Initiation by Let-7 MicroRNA in Human Cells
Pillai, R. S., Bhattacharyya, S. N., Artus-Revel, C. G., Zoller, T., Cougot, N., Basyuk, E. I., Bertrand, É., & Filipowicz, W. (2005) · Science · doi:10.1126/science.1115079 · Cited by 1,489
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 1,277
The dynamic N1-methyladenosine methylome in eukaryotic messenger RNA
Dominissini, D., Nachtergaele, S., Moshitch-Moshkovitz, S., Peer, E., Kol, N., Ben-Haim, M. S., Dai, Q., Segni, A. D., Salmon‐Divon, M., Clark, W. C., et al. (2016) · Nature · doi:10.1038/nature16998 · Cited by 1,047
MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics
Ting, L., Rad, R., Gygi, S. P., & Haas, W. (2011) · Nature Methods · doi:10.1038/nmeth.1714 · Cited by 1,009 · cited 7×
“For the quantification of the data, an additional peptide isolation and fragmentation event (MS3 scan), which leads to a more accurate estimate of relative protein levels than MS2-based quantification, was used (Ting et al., 2011).”
MethodInfluentialLarge-Scale Simultaneous Hypothesis Testing: The Choice of a Null Hypothesis
Efron, B. (2004) · Journal of the American Statistical Association · doi:10.1198/016214504000000089 · Cited by 1,005
Cell-type-specific isolation of ribosome-associated mRNA from complex tissues
Sanz, E., Yang, L., Su, T., Morris, D. R., McKnight, G. S., & Amieux, P. S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907143106 · Cited by 976
Lipid landscapes and pipelines in membrane homeostasis
Holthuis, J. C. M., & Menon, A. K. (2014) · Nature · doi:10.1038/nature13474 · Cited by 901
Ribosomopathies: human disorders of ribosome dysfunction
Narla, A., & Ebert, B. L. (2010) · Blood · doi:10.1182/blood-2009-10-178129 · Cited by 841
Targeting the translation machinery in cancer
Bhat, M., Robichaud, N., Hulea, L., Sonenberg, N., Pelletier, J., & Topisirovic, I. (2015) · Nature Reviews Drug Discovery · doi:10.1038/nrd4505 · Cited by 799
Jang, H. H., Lee, K. O., Chi, Y. H., Jung, B. G., Park, S. K., Park, J., Lee, J. R., Lee, S. S., Moon, J. C., Yun, J. W., et al. (2004) · Cell · doi:10.1016/j.cell.2004.05.002 · Cited by 779
Inhibitors of Ribosome Functions
Pestka, S. (1971) · Annual Review of Microbiology · doi:10.1146/annurev.mi.25.100171.002415 · Cited by 675
Structures of the human and Drosophila 80S ribosome
Anger, A. M., Armache, J., Berninghausen, O., Habeck, M., Subklewe, M. S., Wilson, D. N., & Beckmann, R. (2013) · Nature · doi:10.1038/nature12104 · Cited by 665
Serine is a natural ligand and allosteric activator of pyruvate kinase M2
Chaneton, B., Hillmann, P., Zheng, L., Martin, A. C. L., Maddocks, O. D. K., Chokkathukalam, A., Coyle, J. E., Jankevics, A., Holding, F. P., Vousden, K. H., et al. (2012) · Nature · doi:10.1038/nature11540 · Cited by 661
Pyruvate kinase: Function, regulation and role in cancer
Israelsen, W. J., & Heiden, M. G. V. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.08.004 · Cited by 608
Stem cell metabolism in tissue development and aging
Shyh‐Chang, N., Daley, G. Q., & Cantley, L. C. (2013) · Development · doi:10.1242/dev.091777 · Cited by 602
Rethinking ALS: The FUS about TDP-43
Lagier‐Tourenne, C., & Cleveland, D. W. (2009) · Cell · doi:10.1016/j.cell.2009.03.006 · Cited by 596
Structural basis for the inhibition of the eukaryotic ribosome
de Loubresse, N. G., Prokhorova, I. V., Holtkamp, W., Rodnina, M. V., Yusupova, G. Z., & Yusupov, M. (2014) · Nature · doi:10.1038/nature13737 · Cited by 589
PKM2 isoform-specific deletion reveals a differential requirement for pyruvate kinase in tumor cells
Israelsen, W. J., Dayton, T. L., Davidson, S. M., Fiske, B. P., Hosios, A. M., Bellinger, G., Li, J., Yu, Y., Sasaki, M., Horner, J. W., et al. (2013) · Cell · doi:10.1016/j.cell.2013.09.025 · Cited by 549
Translation dynamics of single mRNAs in live cells and neurons
Wu, B., Eliscovich, C., Yoon, Y. J., & Singer, R. H. (2016) · Science · doi:10.1126/science.aaf1084 · Cited by 512
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
iCLIP: Protein–RNA interactions at nucleotide resolution
Huppertz, I., Attig, J., D’Ambrogio, A., Easton, L. E., Sibley, C. R., Sugimoto, Y., Tajnik, M., König, J., & Ule, J. (2013) · Methods · doi:10.1016/j.ymeth.2013.10.011 · Cited by 449
Transcriptome-wide distribution and function of RNA hydroxymethylcytosine
Delatte, B., Wang, F., Ngoc, L. V., Collignon, É., Bonvin, E., Deplus, R., Calonne, E., Hassabi, B., Putmans, P., Awe, S., et al. (2016) · Science · doi:10.1126/science.aac5253 · Cited by 444
Size, power and false discovery rates
Efron, B. (2007) · The Annals of Statistics · doi:10.1214/009053606000001460 · Cited by 436
Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling
Jan, C. H., Williams, C. C., & Weissman, J. S. (2014) · Science · doi:10.1126/science.1257521 · Cited by 436
Smith, A. G., & Hooper, M. (1987) · Developmental Biology · doi:10.1016/0012-1606(87)90132-1 · Cited by 409
Structure of the Mammalian Ribosome-Sec61 Complex to 3.4 Å Resolution
Voorhees, R. M., Fernández, I. S., Scheres, S. H. W., & Hegde, R. S. (2014) · Cell · doi:10.1016/j.cell.2014.05.024 · Cited by 350
Florens, L. A., Carrozza, M. J., Swanson, S. K., Fournier, M. L., COLEMAN, M., Workman, J. L., & Washburn, M. P. (2006) · Methods · doi:10.1016/j.ymeth.2006.07.028 · Cited by 345
Graumann, J., Hubner, N. C., Kim, J. B., Ko, K., Moser, M., Kumar, C., Cox, J., Schöler, H., & Mann, M. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700460-mcp200 · Cited by 275
irCLIP platform for efficient characterization of protein–RNA interactions
Zarnegar, B. J., Flynn, R. A., Shen, Y., Do, B. T., Chang, H. Y., & Khavari, P. A. (2016) · Nature Methods · doi:10.1038/nmeth.3840 · Cited by 265
A Novel Type of E3 Ligase for the Ufm1 Conjugation System
Tatsumi, K., Sou, Y., Tada, N., Nakamura, E., Iemura, S.-I., Natsume, T., Kang, S. H., Chung, C. H., Kasahara, M., Kominami, E., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.036814 · Cited by 262
Fragile X Mental Retardation Protein Regulates Translation by Binding Directly to the Ribosome
Chen, E., Sharma, M. R., Shi, X., Agrawal, R. K., & Joseph, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.023 · Cited by 253
HSPC117 Is the Essential Subunit of a Human tRNA Splicing Ligase Complex
Popow, J., Englert, M., Weitzer, S., Schleiffer, A., Mierzwa, B. E., Mechtler, K., Trowitzsch, S., Will, C. L., Lührmann, R., Söll, D. G., et al. (2011) · Science · doi:10.1126/science.1197847 · Cited by 251
Structure and Assembly Pathway of the Ribosome Quality Control Complex
Shao, S., Brown, A., Santhanam, B., & Hegde, R. S. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.015 · Cited by 228
Modification of ASC1 by UFM1 Is Crucial for ERα Transactivation and Breast Cancer Development
Yoo, H. M., Kang, S. H., Kim, J. Y., Lee, J., Seong, M. W., Lee, S. W., Ka, S. H., Sou, Y., Komatsu, M., Tanaka, K., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.007 · Cited by 226
LIN28A Is a Suppressor of ER-Associated Translation in Embryonic Stem Cells
Cho, J., Chang, H., Kwon, S. C., Kim, B., Kim, Y., Choe, J., Ha, M., Kim, Y. K., & Kim, V. N. (2012) · Cell · doi:10.1016/j.cell.2012.10.019 · Cited by 223
The Translational Landscape of the Mammalian Cell Cycle
Stumpf, C. R., Moreno, M. V., Olshen, A. B., Taylor, B. S., & Ruggero, D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.09.018 · Cited by 214
Prevention of Amino Acid Conversion in SILAC Experiments with Embryonic Stem Cells
Bendall, S. C., Hughes, C. S., Stewart, M. H., Doble, B. W., Bhatia, M., & Lajoie, G. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800113-mcp200 · Cited by 213
Ribosome Assembly Factors Prevent Premature Translation Initiation by 40 S Assembly Intermediates
Strunk, B. S., Loucks, C. R., Su, M., Vashisth, H., Cheng, S., Schilling, J., Brooks, C. L., Karbstein, K., & Skiniotis, G. (2011) · Science · doi:10.1126/science.1208245 · Cited by 213
Jurkin, J., Henkel, T., Nielsen, A. F., Minnich, M., Popow, J., Kaufmann, T., Heindl, K., Hoffmann, T., Busslinger, M., & Martı̂nez, J. (2014) · The EMBO Journal · doi:10.15252/embj.201490332 · Cited by 210
Regulation of mRNA translation during mitosis
Tanenbaum, M. E., Stern‐Ginossar, N., Weissman, J. S., & Vale, R. D. (2015) · eLife · doi:10.7554/elife.07957 · Cited by 197
Conserved mRNA-binding proteomes in eukaryotic organisms
Matia‐González, A. M., Laing, E., & Gerber, A. P. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3128 · Cited by 190
The SMN Complex: An Assembly Machine for RNPsPreprint
Battle, D. J., Kasim, M., Yong, J., Lotti, F., Lau, T. C., Mouaikel, J., Zhang, Z., HAN, K., Wan, L., & Dreyfuss, G. (2006) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2006.71.001 · Cited by 187
Zhang, M., Zhu, X., Zhang, Y., Cai, Y., Chen, J., Sivaprakasam, S., Gurav, A., Pi, W., Makala, L., Wu, J., et al. (2015) · Cell Death and Differentiation · doi:10.1038/cdd.2015.51 · Cited by 186
The Ufm1-activating enzyme Uba5 is indispensable for erythroid differentiation in mice
Tatsumi, K., Yamamoto‐Mukai, H., Shimizu, R., Waguri, S., Sou, Y., Sakamoto, A., Taya, C., Shitara, H., Hara, T., Chung, C. H., et al. (2011) · Nature Communications · doi:10.1038/ncomms1182 · Cited by 180
Analyzing Protein‐Protein Interactions from Affinity Purification‐Mass Spectrometry Data with SAINT
Choi, H., Liu, G., Mellacheruvu, D., Tyers, M., Gingras, A., & Nesvizhskii, A. I. (2012) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0815s39 · Cited by 166
Coyne, A. N., Siddegowda, B. B., Estes, P. S., Johannesmeyer, J., Kovalik, T., Daniel, S. G., Pearson, A., Bowser, R. P., & Zarnescu, D. C. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2526-14.2014 · Cited by 155
Ozgur, S., Chekulaeva, M., & Stoecklin, G. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00429-10 · Cited by 143
Multifunctional roles of the mammalian CCR4–NOT complex in physiological phenomena
Shirai, Y.-T., Suzuki, T., Morita, M., Takahashi, A., & Yamamoto, T. S. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00286 · Cited by 138
The Cardiomyocyte RNA-Binding Proteome: Links to Intermediary Metabolism and Heart Disease
Liao, Y., Castelló, A., Fischer, B., Leicht, S., Föehr, S., Frese, C. K., Ragan, C., Kurscheid, S., Pagler, E., Hao, Y., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.084 · Cited by 138
An emerging role for the ribosome as a nexus for post-translational modifications
Simsek, D., & Barna, M. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.02.010 · Cited by 135
Structure and Dynamics of the Mammalian Ribosomal Pretranslocation Complex
Budkevich, T. V., Giesebrecht, J., Altman, R. B., Munro, J. B., Mielke, T., Nierhaus, K. H., Blanchard, S. C., & Spahn, C. M. T. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.040 · Cited by 131
Dissecting noncoding and pathogen RNA–protein interactomes
Flynn, R. A., Martin, L., Spitale, R. C., Do, B. T., Sagan, S. M., Zarnegar, B. J., Qu, K., Khavari, P. A., Quake, S. R., Sarnow, P., et al. (2014) · RNA · doi:10.1261/rna.047803.114 · Cited by 79
Brina, D., Miluzio, A., Ricciardi, S., & Biffo, S. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.09.010 · Cited by 72
Characterization and Analysis of the Composition and Dynamics of the Mammalian Riboproteome
Reschke, M., Clohessy, J. G., Seitzer, N., Goldstein, D. P., Breitkopf, S. B., Schmolze, D. B., Ala, U., Asara, J. M., Beck, A. H., & Pandolfi, P. P. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.014 · Cited by 69
Analyzing mRNA Localization to the Endoplasmic Reticulum via Cell Fractionation
Jagannathan, S., Nwosu, C., & Nicchitta, C. V. (2011) · Methods in Molecular Biology · doi:10.1007/978-1-61779-005-8_19 · Cited by 64
Klass, D. M., Scheibe, M., Butter, F., Hogan, G. J., Mann, M., & Brown, P. O. (2013) · Genome Research · doi:10.1101/gr.153031.112 · Cited by 63
Regulation of glycolysis by Raf protein serine/threonine kinases
Mellay, V. L., Houben, R., Troppmair, J., Hagemann, C., Mazurek, S., Frey, U. H., Beigel, J., Weber, C. K., Benz, R., EIGENBRODT, E., et al. (2002) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(01)00036-x · Cited by 47
Structural basis for protein synthesis: snapshots of the ribosome in motion
Noeske, J., & Cate, J. H. D. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.07.011 · Cited by 41
Isolation of Clathrin‐Coated Vesicles by Differential and Density Gradient Centrifugation
Girard, M., Allaire, P. D., Blondeau, F., & McPherson, P. S. (2005) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0313s26 · Cited by 22
Isolation of Centrosomes from Cultured Cells
Reber, S. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-252-6_8 · Cited by 18
Flagged first, then by citations
1 of the 74 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Functional 5′ UTR mRNA structures in eukaryotic translation regulation and how to find them
Leppek, K., Das, R., & Barna, M. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.103 · Cited by 949
Ribosome biogenesis in cancer: new players and therapeutic avenues
Pelletier, J., Thomas, G., & Volarević, S. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.104 · Cited by 837
Heterogeneous Ribosomes Preferentially Translate Distinct Subpools of mRNAs Genome-wide
Shi, Z., Fujii, K., Kovary, K. M., Genuth, N. R., Röst, H. L., Teruel, M. N., & Barna, M. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.021 · Cited by 671
The discovery of ribosome heterogeneity and its implications for gene regulation and organismal life
Genuth, N. R., & Barna, M. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.018 · Cited by 511
Stress Granules and Processing Bodies in Translational ControlPreprint
Ivanov, P. V., Kedersha, N., & Anderson, P. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032813 · Cited by 501
Metadata
- Authors
- Simsek, D., Tiu, G. C., Flynn, R. A., Byeon, G. W., Leppek, K., Xu, A. F., Chang, H. Y., & Barna, M.
- Affiliations
- Stanford University (US)
- Stanford Medicine (US)
- Corresponding author
- Barna, Maria
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 169
- Issue
- 6
- Pages
- 1051-1065.e18
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5548193
- OpenAlex
- W2621126205
- Cited by
- 439
- References
- 74
- Citations by year
- 2026: 34 · 2025: 62 · 2024: 44 · 2023: 40 · 2022: 29 · 2021: 53 · 2020: 63 · 2019: 48 · 2018: 47 · 2017: 18
- FWCI
- 19.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- New York Stem Cell Foundation (NYSCF-R-I36)
- NIH Director’s New Innovator Award (7DP2OD008509, R21HD086730)
- Alfred P. Sloan Research Fellowship (BR2014)
- Mallinckrodt Foundation Award
- Pew Scholars Award (P50-HG007735, R01-HG004361, R01-ES023168)
- 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 › Molecular Biology › RNA Research and Splicing
- Keywords
- ribosome-associated proteins, ribosome heterogeneity, UFMylation, post-translational modification, RNA-binding proteins
- MeSH terms
- Thyroid Hormone-Binding Proteins, Animals, Carrier Proteins, Endoplasmic Reticulum, Membrane Proteins, Protein Processing, Post-Translational, Ribosomal Proteins, Ribosomes, Mass Spectrometry, Thyroid Hormones, Protein Biosynthesis, Protein Interaction Mapping, Ubiquitin-Protein Ligases, Mice, Embryonic Stem Cells
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