Translational control through ribosome heterogeneity and functional specialization

Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae

Kellis, M., Birren, B. W., & Lander, E. S. (2004) · Nature · doi:10.1038/nature02424 · Cited by 1,500 · see citing works

On protein synthesis.

Crick, F. (1958) · PubMed · Cited by 1,188 · see citing works

Tuning the ribosome: The influence of rRNA modification on eukaryotic ribosome biogenesis and function

Sloan, K. E., Warda, A. S., Sharma, S., Entian, K.-D., Lafontaine, D. L. J., & Bohnsack, M. T. (2017) · RNA Biology · doi:10.1080/15476286.2016.1259781 · Cited by 707 · see citing works

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 638 · see citing works

Ribosome profiling: new views of translation, from single codons to genome scale

Ingolia, N. T. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3645 · Cited by 636 · see citing works

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 629 · see citing works

Ribosome-Mediated Specificity in Hox mRNA Translation and Vertebrate Tissue Patterning

Kondrashov, N., Pusic, A. D., Stumpf, C. R., Shimizu, K., Hsieh, A. C., Xue, S., Ishijima, J., Shiroishi, T., & Barna, M. (2011) · Cell · doi:10.1016/j.cell.2011.03.028 · Cited by 581 · see citing works

Structure of the human 80S ribosome

Khatter, H., Myasnikov, A. G., Natchiar, S. K., & Klaholz, B. P. (2015) · Nature · doi:10.1038/nature14427 · Cited by 546 · see citing works

Accurate detection of m6A RNA modifications in native RNA sequences

Liu, H., Begik, O., Lucas, M. C., Ramírez, J. M., Mason, C. E., Wiener, D., Schwartz, S., Mattick, J. S., Smith, M. A., & Novoa, E. M. (2019) · Nature Communications · doi:10.1038/s41467-019-11713-9 · Cited by 516 · see citing works

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 · see citing works

DMS-MaPseq for genome-wide or targeted RNA structure probing in vivo

Zubradt, M., Gupta, P., Persad, S., Lambowitz, A. M., Weissman, J. S., & Rouskin, S. (2016) · Nature Methods · doi:10.1038/nmeth.4057 · Cited by 442 · see citing works

Local protein synthesis is a ubiquitous feature of neuronal pre- and postsynaptic compartments

Hafner, A.-S., Donlin-Asp, P. G., Leitch, B., Herzog, E., & Schuman, E. M. (2019) · Science · doi:10.1126/science.aau3644 · Cited by 431 · see citing works

Ribosomopathies: There’s strength in numbers

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

Eukaryotic Ribosome Assembly

Baßler, J., & Hurt, E. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-110817 · Cited by 423 · see citing works

Ribosome Levels Selectively Regulate Translation and Lineage Commitment in Human Hematopoiesis

Khajuria, R. K., Munschauer, M., Ulirsch, J. C., Fiorini, C., Ludwig, L. S., McFarland, S. K., Abdulhay, N. J., Specht, H., Keshishian, H., Mani, D. R., et al. (2018) · Cell · doi:10.1016/j.cell.2018.02.036 · Cited by 416 · see citing works

The ribosomal protein genes and Minute loci of Drosophila melanogaster

Marygold, S. J., Roote, J., Reuter, G., Lambertsson, A., Ashburner, M., Millburn, G., Harrison, P. M., Yu, Z., Kenmochi, N., Kaufman, T. C., et al. (2007) · Genome biology · doi:10.1186/gb-2007-8-10-r216 · Cited by 398 · see citing works

Transcriptome-Wide Mapping of Pseudouridines: Pseudouridine Synthases Modify Specific mRNAs in S. cerevisiae

Lovejoy, A. F., Riordan, D. P., & Brown, P. O. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110799 · Cited by 381 · see citing works

Mutations in genes encoding subunits of RNA polymerases I and III cause Treacher Collins syndrome

Dauwerse, J. G., Dixon, J., Seland, S., Ruivenkamp, C. A. L., van Haeringen, A., Hoefsloot, L. H., Peters, D. J. M., Boers, A. C.-D., Daumer‐Haas, C., Maiwald, R., et al. (2010) · Nature Genetics · doi:10.1038/ng.724 · Cited by 369 · see citing works

Landscape of the complete RNA chemical modifications in the human 80S ribosome

Taoka, M., Nobe, Y., Yamaki, Y., Sato, K., Ishikawa, H., Izumikawa, K., Yamauchi, Y., Hirota, K., Nakayama, H., Takahashi, N., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky811 · Cited by 357 · see citing works

Dynamic RNA acetylation revealed by quantitative cross-evolutionary mapping

Sas‐Chen, A., Thomas, J. M., Matzov, D., Taoka, M., Nance, K. D., Nir, R., Bryson, K. M., Shachar, R., Liman, G. L. S., Burkhart, B. W., et al. (2020) · Nature · doi:10.1038/s41586-020-2418-2 · Cited by 328 · see citing works

RNA regulons in Hox 5′ UTRs confer ribosome specificity to gene regulation

Xue, S., Tian, S., Fujii, K., Kladwang, W., Das, R., & Barna, M. (2014) · Nature · doi:10.1038/nature14010 · Cited by 319 · see citing works

rRNA Pseudouridylation Defects Affect Ribosomal Ligand Binding and Translational Fidelity from Yeast to Human Cells

Jack, K. D., Bellodi, C., Landry, D. M., Niederer, R. O., Meškauskas, A., Musalgaonkar, S., Kopmar, N. E., Krasnykh, O., Dean, A. M., Thompson, S. R., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.017 · Cited by 318 · see citing works

Evidence for rRNA 2′-O-methylation plasticity: Control of intrinsic translational capabilities of human ribosomes

Erales, J., Marchand, V., Panthu, B., Gillot, S., Belin, S., Ghayad, S. E., Garcia, M., Laforêts, F., Marcel, V., Baudin‐Baillieu, A., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707674114 · Cited by 291 · see citing works

Ribosomal protein L24 defect in Belly spot and tail (<i>Bst</i>), a mouse<i>Minute</i>

Oliver, E. R., Saunders, T. L., Tarlé, S. A., & Glaser, T. (2004) · Development · doi:10.1242/dev.01268 · Cited by 288 · see citing works

Profiling of Ribose Methylations in RNA by High‐Throughput Sequencing

Birkedal, U., Christensen‐Dalsgaard, M., Krogh, N., Sabarinathan, R., Gorodkin, J., & Nielsen, H. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201408362 · Cited by 274 · see citing works

Diagnostic and prognostic signatures from the small non-coding RNA transcriptome in prostate cancer

Martens‐Uzunova, E. S., Jalava, S. E., Dits, N. F. J., van Leenders, G. J. L. H., Møller, S., Trapman, J., Bangma, C. H., Litman, T., Visakorpi, T., & Jenster, G. W. (2011) · Oncogene · doi:10.1038/onc.2011.304 · Cited by 271 · see citing works

Monosomes actively translate synaptic mRNAs in neuronal processes

Biever, A., Glock, C., Tushev, G., Ciirdaeva, E., Dalmay, T., Langer, J. D., & Schuman, E. M. (2020) · Science · doi:10.1126/science.aay4991 · Cited by 266 · see citing works

Profiling of 2′- O -Me in human rRNA reveals a subset of fractionally modified positions and provides evidence for ribosome heterogeneity

Krogh, N., Jansson, M., Häfner, S. J., Tehler, D., Birkedal, U., Christensen‐Dalsgaard, M., Lund, A. H., & Nielsen, H. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw482 · Cited by 264 · see citing works

The ribosome filter hypothesis

Mauro, V. P., & Edelman, G. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192442499 · Cited by 260 · see citing works

Variant ribosomal RNA alleles are conserved and exhibit tissue-specific expression

Parks, M. M., Kurylo, C. M., Dass, R. A., Bojmar, L., Lyden, D., Vincent, C. T., & Blanchard, S. C. (2018) · Science Advances · doi:10.1126/sciadv.aao0665 · Cited by 260 · see citing works

Ribosomal Protein S6 Phosphorylation: Four Decades of Research.

Meyuhas, O. (2015) · International Review of Cell and Molecular Biology · doi:10.1016/bs.ircmb.2015.07.006 · Cited by 259 · see citing works

The ribosomal basis of diamond-blackfan anemia: mutation and database update

Boria, I., Garelli, E., Gazda, H. T., Aspesi, A., Quarello, P., Pavesi, E., Ferrante, D., Meerpohl, J. J., Kartal, M., Da Costa, L., et al. (2010) · Human Mutation · doi:10.1002/humu.21383 · Cited by 233 · see citing works

Detection of internal N7-methylguanosine (m7G) RNA modifications by mutational profiling sequencing

Enroth, C., Poulsen, L. D., Iversen, S., Kirpekar, F., Albrechtsen, A., & Vinther, J. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz736 · Cited by 228 · see citing works

Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution

Armache, J., Jarasch, A., Anger, A. M., Villa, E., Becker, T. A., Bhushan, S., Jossinet, F., Habeck, M., Dindar, G., Franckenberg, S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009999107 · Cited by 226 · see citing works

Heterogeneity and specialized functions of translation machinery: from genes to organisms

Genuth, N. R., & Barna, M. (2018) · Nature Reviews Genetics · doi:10.1038/s41576-018-0008-z · Cited by 221 · see citing works

Hallmarks of ribosomopathies

Kampen, K. R., Sulima, S. O., Vereecke, S., & Keersmaecker, K. D. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz637 · Cited by 213 · see citing works

Root of the Tree: The Significance, Evolution, and Origins of the Ribosome

Bowman, J. C., Petrov, A. S., Frenkel-Pinter, M., Penev, P. I., & Williams, L. D. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00742 · Cited by 197 · see citing works

Differential Stoichiometry among Core Ribosomal Proteins

Slavov, N., Semrau, S., Airoldi, E. M., Budnik, B., & van Oudenaarden, A. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.056 · Cited by 188 · see citing works

Ribosomal deficiencies in Diamond-Blackfan anemia impair translation of transcripts essential for differentiation of murine and human erythroblasts

Horos, R., IJspeert, H., Pospı́šilová, D., Sendtner, R., Andrieu‐Soler, C., Taskesen, E., Nieradka, A., Čmejla, R., Sendtner, M., Touw, I. P., et al. (2011) · Blood · doi:10.1182/blood-2011-06-358200 · Cited by 186 · see citing works

Epigenetic loss of RNA-methyltransferase NSUN5 in glioma targets ribosomes to drive a stress adaptive translational program

Janin, M., Ortiz-Barahona, V., de Moura, M. C., Martínez‐Cardús, A., Llinàs‐Arias, P., Soler, M., Nachmani, D., Pelletier, J., Schümann, U., Calleja-Cervantes, M. E., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02062-4 · Cited by 184 · see citing works

On-Site Ribosome Remodeling by Locally Synthesized Ribosomal Proteins in Axons

Shigeoka, T., Koppers, M., Wong, H. H., Lin, J. Q., Cagnetta, R., Dwivedy, A., Nascimento, J. D. F., van Tartwijk, F. W., Ströhl, F., Cioni, J.-M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.11.025 · Cited by 180 · see citing works

Rps26 directs mRNA-specific translation by recognition of Kozak sequence elements

Ferretti, M., Ghalei, H., Ward, E. A., Potts, E. L., & Karbstein, K. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3442 · Cited by 172 · see citing works

Secondary Structures of rRNAs from All Three Domains of Life

Petrov, A. S., Bernier, C. R., Gulen, B., Waterbury, C. C., Hershkovits, E., Hsiao, C., Harvey, S. C., Hud, N. V., Fox, G. E., Wartell, R. M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088222 · Cited by 162 · see citing works

Severe Zinc Depletion of Escherichia coli

Graham, A. I., Hunt, S., Stokes, S. L., Bramall, N., Bunch, J., Cox, A. G., McLeod, C. W., & Poole, R. K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.001503 · Cited by 156 · see citing works

Profiling of Ribose Methylations in RNA by High‐Throughput Sequencing

Birkedal, U., Christensen‐Dalsgaard, M., Krogh, N., Sabarinathan, R., Gorodkin, J., & Nielsen, H. (2014) · Angewandte Chemie · doi:10.1002/ange.201408362 · Cited by 154 · see citing works

A Dual Protein-mRNA Localization Screen Reveals Compartmentalized Translation and Widespread Co-translational RNA Targeting

Chouaib, R., Safieddine, A., Pichon, X., Imbert, A., Kwon, O. S., Samacoïts, A., Traboulsi, A.-M., Robert, M.-C., Tsanov, N., Coleno, E., et al. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.07.010 · Cited by 150 · see citing works

HydraPsiSeq: a method for systematic and quantitative mapping of pseudouridines in RNA

Marchand, V., Pichot, F., Neybecker, P., Ayadi, L., Bourguignon‐Igel, V., Wacheul, L., Lafontaine, D. L. J., Pinzano, A., Helm, M., & Motorin, Y. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa769 · Cited by 145 · see citing works

Systematic Detection of Amino Acid Substitutions in Proteomes Reveals Mechanistic Basis of Ribosome Errors and Selection for Translation Fidelity

Mordret, E., Dahan, O., Asraf, O., Rak, R., Yehonadav, A., Barnabas, G. D., Cox, J., Geiger, T., Lindner, A. B., & Pilpel, Y. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.041 · Cited by 144 · see citing works

Loss of the ribosomal RNA methyltransferase NSUN5 impairs global protein synthesis and normal growth

Heissenberger, C., Liendl, L., Nagelreiter, F., Gonskikh, Y., Yang, G., Stelzer, E. M., Krammer, T. L., Mičutková, L., Vogt, S., Kreil, D. P., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1043 · Cited by 138 · see citing works

A single H/ACA small nucleolar RNA mediates tumor suppression downstream of oncogenic RAS

McMahon, M. E., Contreras, A., Holm, M., Uechi, T., Forester, C. M., Pang, X., Jackson, C. B., Calvert, M., Chen, B., Quigley, D. A., et al. (2019) · eLife · doi:10.7554/elife.48847 · Cited by 137 · see citing works

Germline NPM1 mutations lead to altered rRNA 2′-O-methylation and cause dyskeratosis congenita

Nachmani, D., Bothmer, A., Grisendi, S., Mele, A., Bothmer, D., Lee, J. D., Monteleone, E., Cheng, K., Zhang, Y., Bester, A. C., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0502-z · Cited by 133 · see citing works

Does functional specialization of ribosomes really exist?

Ferretti, M., & Karbstein, K. (2019) · RNA · doi:10.1261/rna.069823.118 · Cited by 130 · see citing works

Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy

Loenarz, C., Sekirnik, R., Thalhammer, A., Ge, W., Spivakovsky, E., Mackeen, M. M., McDonough, M. A., Cockman, M. E., Kessler, B. M., Ratcliffe, P. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311750111 · Cited by 127 · see citing works

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 125 · see citing works

OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation

Singleton, R. S., Liu-Yi, P., Formenti, F., Ge, W., Sekirnik, R., Fischer, R., Adam, J., Pollard, P. J., Wolf, A., Thalhammer, A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314482111 · Cited by 122 · see citing works

Expression of distinct maternal and somatic 5.8S, 18S, and 28S rRNA types during zebrafish development

Locati, M. D., Pagano, J. F. B., Girard, G., Ensink, W. A., van Olst, M. F., van Leeuwen, S. M., Nehrdich, U., Spaink, H. P., Rauwerda, H., Jonker, M. J., et al. (2017) · RNA · doi:10.1261/rna.061515.117 · Cited by 121 · see citing works

Three Forms of the 5.8‐S Ribosomal RNA Species in Saccharomyces cerevisiae

Rubin, G. M. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03260.x · Cited by 119 · see citing works

Endogenous rRNA Sequence Variation Can Regulate Stress Response Gene Expression and Phenotype

Kurylo, C. M., Parks, M. M., Juette, M. F., Zinshteyn, B., Altman, R. B., Thibado, J. K., Vincent, C. T., & Blanchard, S. C. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.08.093 · Cited by 117 · see citing works

Rare ribosomopathies: insights into mechanisms of cancer

Aspesi, A., & Ellis, S. R. (2019) · Nature reviews. Cancer · doi:10.1038/s41568-019-0105-0 · Cited by 114 · see citing works

Ribosome–NatA architecture reveals that rRNA expansion segments coordinate N-terminal acetylation

Knorr, A. G., Schmidt, C. M., Těšina, P., Berninghausen, O., Becker, T. A., Beatrix, B., & Beckmann, R. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0165-y · Cited by 113 · see citing works

Loss of m1acp3Ψ Ribosomal RNA Modification Is a Major Feature of Cancer

Babaian, A., Rothe, K., Girodat, D. J., Minia, I., Djondovic, S., Milek, M., Miko, S. E. S., Wieden, H., Landthaler, M., Morin, G. B., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107611 · Cited by 110 · see citing works

Phosphorylation of the Ribosomal Protein RPL12/uL11 Affects Translation during Mitosis

Imami, K., Milek, M., Bogdanow, B., Yasuda, T., Kastelić, N., Zauber, H., Ishihama, Y., Landthaler, M., & Selbach, M. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.019 · Cited by 109 · see citing works

The complete chemical structure ofSaccharomyces cerevisiaerRNA: partial pseudouridylation of U2345 in 25S rRNA by snoRNA snR9

Taoka, M., Nobe, Y., Yamaki, Y., Yamauchi, Y., Ishikawa, H., Takahashi, N., Nakayama, H., & Isobe, T. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw564 · Cited by 108 · see citing works

RiboVision suite for visualization and analysis of ribosomes

Bernier, C. R., Petrov, A. S., Waterbury, C. C., Jett, J. R., Li, F., Freil, L., Xiong, X., Wang, L., Migliozzi, B. L. R., Hershkovits, E., et al. (2014) · Faraday Discussions · doi:10.1039/c3fd00126a · Cited by 107 · see citing works

Decoding the Function of Expansion Segments in Ribosomes

Fujii, K., Susanto, T. T., Saurabh, S., & Barna, M. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.11.023 · Cited by 106 · see citing works

Secondary structure and domain architecture of the 23S and 5S rRNAs

Petrov, A. S., Bernier, C. R., Hershkovits, E., Xue, Y., Waterbury, C. C., Hsiao, C., Stepanov, V. G., Gaucher, E. A., Grover, M. A., Harvey, S. C., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt513 · Cited by 105 · see citing works

The Ribosome Filter Redux

Mauro, V. P., & Edelman, G. M. (2007) · Cell Cycle · doi:10.4161/cc.6.18.4739 · Cited by 98 · see citing works

Ribosome Stoichiometry: From Form to Function

Emmott, E., Jovanović, M., & Slavov, N. (2018) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.10.009 · Cited by 95 · see citing works

Ribosomal RNA 2′O-methylation as a novel layer of inter-tumour heterogeneity in breast cancer

Marcel, V., Kielbassa, J., Marchand, V., Natchiar, K., Paraqindes, H., Long, F. N. V., Ayadi, L., Bourguignon‐Igel, V., Monaco, P. L., Monchiet, D., et al. (2020) · NAR Cancer · doi:10.1093/narcan/zcaa036 · Cited by 94 · see citing works

Small nucleolar RNAs as new biomarkers in chronic lymphocytic leukemia

Ronchetti, D., Mosca, L., Cutrona, G., Tuana, G., Gentile, M., Fabris, S., Agnelli, L., Ciceri, G., Matis, S., Massucco, C., et al. (2013) · BMC Medical Genomics · doi:10.1186/1755-8794-6-27 · Cited by 91 · see citing works

Functional Dynamics within the Human Ribosome Regulate the Rate of Active Protein Synthesis

Ferguson, A., Wang, L., Altman, R. B., Terry, D. S., Juette, M. F., Burnett, B. J., Alejo, J. L. P., Dass, R. A., Parks, M., Vincent, C. T., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.013 · Cited by 84 · see citing works

Differential expression of duplicated ribosomal protein genes modifies ribosome composition in response to stress

Ghulam, M. M., Catala, M., & Elela, S. A. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1183 · Cited by 84 · see citing works

Novel and known ribosomal causes of Diamond-Blackfan anaemia identified through comprehensive genomic characterisation

Mirabello, L. J., Khincha, P. P., Ellis, S. R., Giri, N., Brodie, S. A., Chandrasekharappa, S. C., Donovan, F. X., Zhou, W., Hicks, B. D., Boland, J. F., et al. (2017) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2016-104346 · Cited by 82 · see citing works

Characterizing RNA structures in vitro and in vivo with selective 2′-hydroxyl acylation analyzed by primer extension sequencing (SHAPE-Seq)

Watters, K. E., Yu, A. M., Strobel, E. J., Settle, A. H., & Lucks, J. B. (2016) · Methods · doi:10.1016/j.ymeth.2016.04.002 · Cited by 81 · see citing works

In vitro ribosome synthesis and evolution through ribosome display

Hammerling, M. J., Fritz, B. R., Yoesep, D. J., Kim, D. S., Carlson, E. D., & Jewett, M. C. (2020) · Nature Communications · doi:10.1038/s41467-020-14705-2 · Cited by 78 · see citing works

Developmental changes of rRNA ribose methylations in the mouse

Hebras, J., Krogh, N., Marty, V., Nielsen, H., & Cavaillé, J. (2019) · RNA Biology · doi:10.1080/15476286.2019.1670598 · Cited by 74 · see citing works

Pseudo-Seq

Carlile, T. M., Rojas-Durán, M. F., & Gilbert, W. V. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.03.011 · Cited by 70 · see citing works

Ribosome reactivation by replacement of damaged proteins

Pulk, A., Liiv, A., Peil, L., Maiväli, Ü., Nierhaus, K. H., & Rèmme, J. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.07002.x · Cited by 67 · see citing works

Time-Resolved Proteomics Extends Ribosome Profiling-Based Measurements of Protein Synthesis Dynamics

Liu, T., Huang, H. H., Wheeler, D., Xu, Y., Wells, J. A., Song, Y. S., & Wiita, A. P. (2017) · Cell Systems · doi:10.1016/j.cels.2017.05.001 · Cited by 66 · see citing works

Functional importance of individual rRNA 2′-O-ribose methylations revealed by high-resolution phenotyping

Esguerra, J. L. S., Warringer, J., & Blomberg, A. (2008) · RNA · doi:10.1261/rna.845808 · Cited by 65 · see citing works

MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments

Wild, K., Aleksić, M., Lapouge, K., Juaire, K. D., Flemming, D., Pfeffer, S., & Sinning, I. (2020) · Nature Communications · doi:10.1038/s41467-020-14603-7 · Cited by 63 · see citing works

An efficient factor-depleted mammalian in vitro translation system

Rakotondrafara, A. M., & Hentze, M. W. (2011) · Nature Protocols · doi:10.1038/nprot.2011.314 · Cited by 62 · see citing works

Bacterial ribosome heterogeneity: Changes in ribosomal protein composition during transition into stationary growth phase

Lilleorg, S., Reier, K., Pulk, A., Liiv, A., Tammsalu, T., Peil, L., Cate, J. H. D., & Rèmme, J. (2018) · Biochimie · doi:10.1016/j.biochi.2018.10.013 · Cited by 57 · see citing works

Divergent rRNAs as regulators of gene expression at the ribosome level

Song, W., Joo, M., Yeom, J., Shin, E., Lee, M., Choi, H., Hwang, J., Kim, Y., Seo, R., Lee, J. E., et al. (2019) · Nature Microbiology · doi:10.1038/s41564-018-0341-1 · Cited by 57 · see citing works

Gene- and Species-Specific Hox mRNA Translation by Ribosome Expansion Segments

Leppek, K., Fujii, K., Quade, N., Susanto, T. T., Boehringer, D., Lenarčič, T., Xue, S., Genuth, N. R., Ban, N., & Barna, M. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.10.023 · Cited by 56 · see citing works

Profiling of ribose methylations in ribosomal RNA from diffuse large B-cell lymphoma patients for evaluation of ribosomes as drug targets

Krogh, N., Asmar, F., Côme, C., Munch‐Petersen, H. F., Grønbæk, K., & Nielsen, H. (2020) · NAR Cancer · doi:10.1093/narcan/zcaa035 · Cited by 54 · see citing works

In vitro reconstitution of functional small ribosomal subunit assembly for comprehensive analysis of ribosomal elements in E. coli

Shimojo, M., Amikura, K., Masuda, K., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-0874-8 · Cited by 53 · see citing works

N6-adenosine methylation of ribosomal RNA affects lipid oxidation and stress resistance

Liberman, N., O’Brown, Z. K., Earl, A., Boulias, K., Gerashchenko, M. V., Wang, S. Y., Fritsche, C. M., Fady, P.-E., Dong, A., Gladyshev, V. N., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz4370 · Cited by 53 · see citing works

Spinocerebellar ataxia type 17: Report of a family with reduced penetrance of an unstable Gln49TBP allele, haplotype analysis supporting a founder effect for unstable alleles and comparative analysis of SCA17 genotypes

Zühlke, C., Dalski, A., SCHWINGER, E., et al. (2005) · BMC Medical Genetics · doi:10.1186/1471-2350-6-27 · Cited by 50 · see citing works

Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth

Katz, M. J., Acevedo, J. M., Loenarz, C., Galagovsky, D., Liu-Yi, P., Pérez-Pepe, M., Thalhammer, A., Sekirnik, R., Ge, W., Melani, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314485111 · Cited by 50 · see citing works

Protein Synthesis in the Developing Neocortex at Near-Atomic Resolution Reveals Ebp1-Mediated Neuronal Proteostasis at the 60S Tunnel Exit

Kraushar, M. L., Krupp, F., Harnett, D., Turko, P., Ambrozkiewicz, M. C., Sprink, T., Imami, K., Günnigmann, M., Zinnall, U., Vieira-Vieira, C. H., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.11.037 · Cited by 49 · see citing works

Ribosome biogenesis factor Ltv1 chaperones the assembly of the small subunit head

Collins, J. C., Ghalei, H., Doherty, J. R., et al. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201804163 · Cited by 48 · see citing works

Expression of ribosomal protein L22e family members in Drosophila melanogaster: rpL22-like is differentially expressed and alternatively spliced

Kearse, M. G., Chen, A. S., & Ware, V. C. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1218 · Cited by 47 · see citing works

Nol9 is a novel polynucleotide 5′‐kinase involved in ribosomal RNA processing

Heindl, K., & Martı̂nez, J. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.275 · Cited by 45 · see citing works

A mass spectrometry-based method for direct determination of pseudouridine in RNA

Yamauchi, Y., Nobe, Y., Izumikawa, K., Higo, D., Yamagishi, Y., Takahashi, N., Nakayama, H., Isobe, T., & Taoka, M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1462 · Cited by 45 · see citing works

Specialized eRpL22 paralogue-specific ribosomes regulate specific mRNA translation in spermatogenesis inDrosophila melanogaster

Mageeney, C. M., & Ware, V. C. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-02-0086 · Cited by 45 · see citing works

H/ACA snoRNA levels are regulated during stem cell differentiation

McCann, K. L., Kavari, S. L., Burkholder, A., Phillips, B., & Hall, T. M. T. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa612 · Cited by 43 · see citing works

rRNA expansion segment 27Lb modulates the factor recruitment capacity of the yeast ribosome and shapes the proteome

Shankar, V. G., Rauscher, R., Reuther, J., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa003 · Cited by 39 · see citing works

Methylation of yeast ribosomal protein Rpl3 promotes translational elongation fidelity

Al‐Hadid, Q., Roy, K. R., Chanfreau, G., et al. (2016) · RNA · doi:10.1261/rna.054569.115 · Cited by 38 · see citing works

Sequencing-based methods for detection and quantitation of ribose methylations in RNA

Krogh, N., & Nielsen, H. (2018) · Methods · doi:10.1016/j.ymeth.2018.11.017 · Cited by 37 · see citing works

Ribosomopathies: New Therapeutic Perspectives

Orgebin, E., Lamoureux, F., Isidor, B., Charrier, C., Ory, B., Lézot, F., & Baud’huin, M. (2020) · Cells · doi:10.3390/cells9092080 · Cited by 36 · see citing works

Invariable stoichiometry of ribosomal proteins in mouse brain tissues with aging

Amirbeigiarab, S., Kiani, P., Sanchez, A. K. V., Krisp, C., Kazantsev, A., Fester, L., Schlüter, H., & Ignatova, Z. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912060116 · Cited by 33 · see citing works

Ribosomes and cryo-EM: a duet

Brown, A., & Shao, S. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.07.001 · Cited by 32 · see citing works

An evolutionary conserved pattern of 18S rRNA sequence complementarity to mRNA 5′ UTRs and its implications for eukaryotic gene translation regulation

Pánek, J., Kolář, M., Vohradský, J., & Valášek, L. S. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt548 · Cited by 29 · see citing works

Specialized Yeast Ribosomes: A Customized Tool for Selective mRNA Translation

Bauer, J. W., Brandl, C., Haubenreisser, O., Wimmer, B., Weber, M., Karl, T., Klausegger, A., Breitenbach, M., Hintner, H., von der Haar, T., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067609 · Cited by 27 · see citing works

The Expansion Segments of 28S Ribosomal RNA Extensively Match Human Messenger RNAs

Parker, M. S., Balasubramaniam, A., Sallee, F. R., & Parker, S. L. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00066 · Cited by 26 · see citing works

The shift from early to late types of ribosomes in zebrafish development involves changes at a subset of rRNA 2′-O-Me sites

Ramachandran, S., Krogh, N., Jørgensen, T. E., Johansen, S., Nielsen, H., & Babiak, I. (2020) · RNA · doi:10.1261/rna.076760.120 · Cited by 25 · see citing works

Phenotypic effects of paralogous ribosomal proteins bL31A and bL31B in E. coli

Lilleorg, S., Reier, K., Volõnkin, P., Remme, J., & Liiv, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-68582-2 · Cited by 23 · see citing works

VELCRO-IP RNA-seq reveals ribosome expansion segment function in translation genome-wide

Leppek, K., Byeon, G. W., Fujii, K., & Barna, M. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108629 · Cited by 18 · see citing works

The Expanding Riboverse

Sulima, S. O., & Dinman, J. D. (2019) · Cells · doi:10.3390/cells8101205 · Cited by 17 · see citing works

How Does the Alarmone ppGpp Change Bacterial Cell Metabolism? From Genome-wide Approaches to Structure to Physiology

Petchiappan, A., & Gottesman, S. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.09.019 · Cited by 17 · see citing works

Ribosome Biogenesis and Translational Control in Skeletal Muscle Atrophy and Hypertrophy: Mechanisms and Therapeutic Perspectives

Xu, M., & Liu, X. (2026) · Biomolecules · doi:10.3390/biom16030406 · Cited by 6 · see citing works

Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators

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

ИСПОЛЬЗОВAНИЕ ПОТЕНЦИAЛA СОЦИAЛЬНЫХ ПAРТНЕРОВ В ПОДГОТОВКЕ БУДУЩИХ ПЕДAГОГОВ

Атабекова, Б. Б. (2024) · Habaršy. Pedagogika ġylymdary seriâsy · doi:10.51889/2959-5762.2023.80.4.019

Cloning and Characterization of Rat BAT3 cDNA

Ozaki, T., Hanaoka, E., Naka, M., et al. (1999) · DNA and Cell Biology · doi:10.1089/104454999315222 · Cited by 22 · see citing works

EFFECT OF THE NEMATODE PHASMARHABDITIS HERMAPHRODITA ON YOUNG STAGES OF THE PEST SLUG ARION LUSITANICUS

Grimm, B. (2002) · Journal of Molluscan Studies · doi:10.1093/mollus/68.1.25 · Cited by 41 · see citing works

HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53Preprint

Sasaki, T., Gan, E. C., Wakeham, A. C., Kornbluth, S. A., Mak, T. W., & Okada, H. (2007) · Genes & Development · doi:10.1101/gad.1534107 · Cited by 127 · see citing works

Anthoxanthum Mosaic Virus

Catherall, P. L. (1970) · Plant Pathology · doi:10.1111/j.1365-3059.1970.tb00999.x · Cited by 6 · see citing works