Specialized Ribosomes in Health and Disease

5-Fluorouracil: mechanisms of action and clinical strategies

Longley, D. B., Harkin, D. P., & Johnston, P. G. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1074 · Cited by 5,332 · see citing works

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679 · see citing works

Posttranscriptional Control of T Cell Effector Function by Aerobic Glycolysis

Chang, C.-H., Curtis, J. D., Maggi, L. B., Faubert, B., Villarino, A. V., O’Sullivan, D., Huang, S. C.-C., van der Windt, G. J. W., Blagih, J., Qiu, J., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.016 · Cited by 2,204 · see citing works

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 · see citing works

The male-specific region of the human Y chromosome is a mosaic of discrete sequence classes

Skaletsky, H., Kuroda-Kawaguchi, T., Minx, P. J., Cordum, H. S., Hillier, L., Brown, L. G., Repping, S., Pyntikova, T., Ali, J., Bieri, T. A., et al. (2003) · Nature · doi:10.1038/nature01722 · Cited by 2,098 · see citing works

The Structure of the Eukaryotic Ribosome at 3.0 Å Resolution

Shem, A. B., de Loubresse, N. G., Melnikov, S. V., Jenner, L. B., Yusupova, G. Z., & Yusupov, M. (2011) · Science · doi:10.1126/science.1212642 · Cited by 1,114 · see citing works

Four Evolutionary Strata on the Human X Chromosome

Lahn, B. T., & Page, D. C. (1999) · Science · doi:10.1126/science.286.5441.964 · Cited by 1,001 · see citing works

MYC as a regulator of ribosome biogenesis and protein synthesis

van Riggelen, J., Yetil, A., & Felsher, D. W. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2819 · Cited by 956 · see citing works

Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2

Thoms, M., Buschauer, R., Ameismeier, M., Koepke, L., Denk, T., Hirschenberger, M., Kratzat, H., Hayn, M., Mackens‐Kiani, T., Cheng, J., et al. (2020) · Science · doi:10.1126/science.abc8665 · Cited by 869 · see citing works

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 802 · see citing works

Comparative Proteomic Analysis of Eleven Common Cell Lines Reveals Ubiquitous but Varying Expression of Most Proteins

Geiger, T., Wehner, A., Schaab, C., Cox, J., & Mann, M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.014050 · Cited by 797 · see citing works

How Common Are Extraribosomal Functions of Ribosomal Proteins?

Warner, J. R., & McIntosh, K. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.03.006 · Cited by 735 · see citing works

FMRP targets distinct mRNA sequence elements to regulate protein expression

Ascano, M., Mukherjee, N., Bandaru, P., Miller, J. B., Nusbaum, J. D., Corcoran, D. L., Langlois, C., Munschauer, M., Dewell, S., Hafner, M., et al. (2012) · Nature · doi:10.1038/nature11737 · Cited by 701 · see citing works

Specialized ribosomes: a new frontier in gene regulation and organismal biology

Xue, S., & Barna, M. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3359 · Cited by 687 · see citing works

Regulation of p53 Translation and Induction after DNA Damage by Ribosomal Protein L26 and Nucleolin

Takagi, M., Absalon, M. J., McLure, K. G., & Kastan, M. B. (2005) · Cell · doi:10.1016/j.cell.2005.07.034 · Cited by 656 · see citing works

Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasisPreprint

Ruvinsky, I., Sharon, N., Lerer, T., Cohen, H., Stolovich-Rain, M., Nir, T., Dor, Y., Zisman, P., & Meyuhas, O. (2005) · Genes & Development · doi:10.1101/gad.351605 · Cited by 640 · 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

A new system for naming ribosomal proteins

Ban, N., Beckmann, R., Cate, J. H. D., Dinman, J. D., Dragon, F., Ellis, S. R., Lafontaine, D. L. J., Lindahl, L., Liljas, A., Lipton, J. M. M., et al. (2014) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.01.002 · Cited by 571 · 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

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

One core, two shells: bacterial and eukaryotic ribosomes

Melnikov, S., Ben-Shem, A., Garreau de Loubresse, N., Jenner, L., Yusupova, G., & Yusupov, M. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2313 · Cited by 477 · see citing works

The Structure and Function of the Eukaryotic RibosomePreprint

Wilson, D. N., & Cate, J. H. D. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011536 · Cited by 473 · see citing works

Pseudogenes: Pseudo-functional or key regulators in health and disease?

Pink, R. C., Wicks, K., Caley, D. P., Punch, E. K., Jacobs, L. A., & Carter, D. R. F. (2011) · RNA · doi:10.1261/rna.2658311 · Cited by 459 · see citing works

The mammalian ribo-interactome reveals ribosome functional diversity and heterogeneity

Simsek, D., Tiu, G. C., Flynn, R. A., Byeon, G. W., Leppek, K., Xu, A. F., Chang, H. Y., & Barna, M. (2017) · Cell · doi:10.1016/j.cell.2017.05.022 · Cited by 439 · 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

RNA modifications: importance in immune cell biology and related diseases

Cui, L., Ma, R., Cai, J., Guo, C., Chen, Z., Yao, L., Wang, Y., Fan, R., Wang, X., & Shi, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01175-9 · Cited by 425 · 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

A functional RNAi screen links O-GlcNAc modification of ribosomal proteins to stress granule and processing body assembly

Ohn, T., Kedersha, N., Hickman, T. T., Tisdale, S., & Anderson, P. (2008) · Nature Cell Biology · doi:10.1038/ncb1783 · Cited by 414 · see citing works

A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein

Kamitani, W., Huang, C., Narayanan, K., Lokugamage, K. G., & Makino, S. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1680 · Cited by 410 · see citing works

Postmeiotic Sex Chromatin in the Male Germline of Mice

Namekawa, S. H., Park, P. J., Zhang, L., Shima, J. E., McCarrey, J. R., Griswold, M. D., & Lee, J. T. (2006) · Current Biology · doi:10.1016/j.cub.2006.01.066 · Cited by 396 · see citing works

Homologous ribosomal protein genes on the human X and Y chromosomes: Escape from X inactivation and possible implications for turner syndrome

Fisher, E., Beer‐Romero, P., Brown, L. G., Ridley, A. J., McNeil, J. A., Lawrence, J. B., Willard, H. F., Bieber, F. R., & Page, D. C. (1990) · Cell · doi:10.1016/0092-8674(90)90416-c · Cited by 393 · see citing works

Functions of Ribosomal Proteins in Assembly of Eukaryotic Ribosomes In Vivo

de la Cruz, J., Karbstein, K., & Woolford, J. L. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033917 · Cited by 387 · see citing works

Cell signaling, the essential role of O-GlcNAc

Zachara, N. E., & Hart, G. W. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.04.007 · Cited by 386 · see citing works

Deregulation of ribosomal protein expression and translation promotes breast cancer metastasis

Ebright, R. Y., Lee, S., Wittner, B. S., Niederhoffer, K., Nicholson, B. T., Bardia, A., Truesdell, S. S., Wiley, D. F., Wesley, B., Li, S. S., et al. (2020) · Science · doi:10.1126/science.aay0939 · Cited by 365 · see citing works

Visualization of chemical modifications in the human 80S ribosome structure

Natchiar, S. K., Myasnikov, A. G., Kratzat, H., Hazemann, I., & Klaholz, B. P. (2017) · Nature · doi:10.1038/nature24482 · Cited by 364 · 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

Are all sex chromosomes created equal?

Bachtrog, D., Kirkpatrick, M. A., Mank, J. E., et al. (2011) · Trends in Genetics · doi:10.1016/j.tig.2011.05.005 · Cited by 348 · see citing works

Regulated Release of L13a from the 60S Ribosomal Subunit as A Mechanism of Transcript-Specific Translational Control

Mazumder, B., Sampath, P., Seshadri, V., Maitra, R. K., DiCorleto, P. E., & Fox, P. L. (2003) · Cell · doi:10.1016/s0092-8674(03)00773-6 · Cited by 334 · see citing works

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic ReticulumPreprint

Karagöz, G. E., Acosta‐Alvear, D., & Walter, P. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033886 · Cited by 302 · see citing works

Methylation of ribosomal RNA by NSUN5 is a conserved mechanism modulating organismal lifespan

Schosserer, M., Minois, N., Angerer, T. B., Amring, M., Dellago, H., Harreither, E., Calle-Perez, A., Pircher, A., Gerstl, M. P., Pfeifenberger, S., et al. (2015) · Nature Communications · doi:10.1038/ncomms7158 · Cited by 281 · see citing works

Ribosomal protein S6 kinase activity controls the ribosome biogenesis transcriptional program

Chauvin, C., Koka, V., Nouschi, A., Mieulet, V., Hoareau‐Aveilla, C., Dreazen, A., Cagnard, N., Carpentier, W., Kiss, T., Meyuhas, O., et al. (2013) · Oncogene · doi:10.1038/onc.2012.606 · Cited by 279 · 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

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

Eukaryotic ribosome assembly, transport and quality control

Peña, C., Hurt, E., & Panse, V. G. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3454 · Cited by 244 · see citing works

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 240 · see citing works

Patterns of ribosomal protein expression specify normal and malignant human cells

Guimaraes, J. C., & Zavolan, M. (2016) · Genome biology · doi:10.1186/s13059-016-1104-z · Cited by 233 · see citing works

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 225 · see citing works

High-resolution cryo-EM structure of the human 80S ribosome

Natchiar, S. K., Myasnikov, A. G., Kratzat, H., Hazemann, I., & Klaholz, B. P. (2017) · Worldwide Protein Data Bank · doi:10.2210/pdb6ek0/pdb · Cited by 225 · 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 217 · see citing works

Identification and Analysis of Over 2000 Ribosomal Protein Pseudogenes in the Human GenomePreprint

Zhang, Z., Harrison, P., & Gerstein, M. (2002) · Genome Research · doi:10.1101/gr.331902 · Cited by 213 · see citing works

Interferon activation and innate immunity.

Page, C. L., Génin, P., Baines, M. G., & Hiscott, J. B. (2000) · PubMed · Cited by 211 · see citing works

Ribosomal protein RPL26 is the principal target of UFMylation

Walczak, C. P., Leto, D. E., Zhang, L., Riepe, C., Muller, R. Y., DaRosa, P. A., Ingolia, N. T., Elias, J. E., & Kopito, R. R. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1816202116 · Cited by 210 · see citing works

Chromosomal Redistribution of Male-Biased Genes in Mammalian Evolution with Two Bursts of Gene Gain on the X Chromosome

Zhang, Y. E., Vibranovski, M. D., Landback, P., Marais, G. A. B., & Long, M. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000494 · Cited by 206 · see citing works

ENO1 suppresses cancer cell ferroptosis by degrading the mRNA of iron regulatory protein 1

Zhang, T., Sun, L., Hao, Y., Suo, C., Shen, S., Wei, H., Ma, W., Zhang, P., Wang, T., Gu, X., et al. (2021) · Nature Cancer · doi:10.1038/s43018-021-00299-1 · Cited by 206 · see citing works

Involvement of human ribosomal proteins in nucleolar structure and p53-dependent nucleolar stress

Nicolas, E., Parisot, P., Pinto-Monteiro, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms11390 · Cited by 202 · see citing works

UFMylation of RPL26 links translocation-associated quality control to endoplasmic reticulum protein homeostasis

Wang, L., Xu, Y., Rogers, H. M., Saidi, L. F., Noguchi, C. T., Li, H., Yewdell, J. W., Guydosh, N. R., & Ye, Y. (2019) · Cell Research · doi:10.1038/s41422-019-0236-6 · Cited by 184 · see citing works

Ribosomal proteins are targets for the NEDD8 pathway

Xirodimas, D. P., Sundqvist, A., Nakamura, A., Shen, L., Botting, C. H., & Hay, R. T. (2008) · EMBO Reports · doi:10.1038/embor.2008.10 · Cited by 171 · see citing works

A Map of 75 Human Ribosomal Protein GenesPreprint

Kenmochi, N., Kawaguchi, T., Rozen, S., et al. (1998) · Genome Research · doi:10.1101/gr.8.5.509 · Cited by 169 · see citing works

Protein synthesis, degradation, and energy metabolism in T cell immunity

Marchingo, J. M., & Cantrell, D. A. (2022) · Cellular & Molecular Immunology · doi:10.1038/s41423-021-00792-8 · Cited by 169 · see citing works

The viral protein NSP1 acts as a ribosome gatekeeper for shutting down host translation and fostering SARS-CoV-2 translation

Tidu, A., Janvier, A., Schaeffer, L., Sosnowski, P., Kühn, L., Hammann, P., Westhof, É., Eriani, G., & Martin, F. (2020) · RNA · doi:10.1261/rna.078121.120 · Cited by 162 · see citing works

Neuronal ribosomes exhibit dynamic and context-dependent exchange of ribosomal proteins

Fusco, C. M., Desch, K., Dörrbaum, A. R., Wang, M., Staab, A., Chan, I. C. W., Vail, E., Villeri, V., Langer, J. D., & Schuman, E. M. (2021) · Nature Communications · doi:10.1038/s41467-021-26365-x · Cited by 157 · see citing works

Ribosome 18S m6A Methyltransferase METTL5 Promotes Translation Initiation and Breast Cancer Cell Growth

Rong, B., Zhang, Q., Wan, J., Xing, S., Dai, R., Li, Y., Cai, J., Xie, J., Song, Y., Chen, J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108544 · Cited by 152 · see citing works

The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins

Higgins, R., Gendron, J. M., Rising, L., Mak, R., Webb, K. J., Kaiser, S. E., Zuzow, N., Riviere, P. J., Yang, B., Fenech, E. J., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.04.026 · Cited by 149 · see citing works

A missense mutation in RPS6KA3 (RSK2) responsible for non-specific mental retardation

Mérienne, K., Jacquot, S., Pannetier, S., Zeniou, M., Bankier, A., Gécz, J., Mandel, J., Mulley, J. C., Sassone‐Corsi, P., & Hanauer, A. (1999) · Nature Genetics · doi:10.1038/8719 · Cited by 148 · see citing works

N6-methyladenosine (m6A) in 18S rRNA promotes fatty acid metabolism and oncogenic transformation

Peng, H., Chen, B., Wei, W., Guo, S., Han, H., Yang, C., Ma, J., Wang, L., Peng, S., Kuang, M., et al. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00622-9 · Cited by 145 · see citing works

CDK12: an emerging therapeutic target for cancer

Lui, G. Y. L., Grandori, C., & Kemp, C. J. (2018) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2018-205356 · Cited by 136 · see citing works

A Complete Map of the Human Ribosomal Protein Genes: Assignment of 80 Genes to the Cytogenetic Map and Implications for Human Disorders

Uechi, T., Tanaka, T., & Kenmochi, N. (2001) · Genomics · doi:10.1006/geno.2000.6470 · Cited by 132 · see citing works

Transcript-Selective Translational Silencing by Gamma Interferon Is Directed by a Novel Structural Element in the Ceruloplasmin mRNA 3′ Untranslated Region

Sampath, P., Mazumder, B., Seshadri, V., & Fox, P. L. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.5.1509-1519.2003 · Cited by 130 · 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

X chromosomes, retrogenes and their role in male reproduction

Wang, P. J. (2004) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2004.01.007 · Cited by 128 · see citing works

Ribosomal Proteins Regulate MHC Class I Peptide Generation for Immunosurveillance

Wei, J., Kishton, R. J., Angel, M., Conn, C. S., Venezia, N. D., Marcel, V., Vincent, A., Catez, F., Ferré, S., Ayadi, L., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.020 · Cited by 125 · see citing works

A male germ-cell-specific ribosome controls male fertility

Li, H., Huo, Y., He, X., Yao, L., Zhang, H., Cui, Y., Xiao, H., Xie, W., Zhang, D., Wang, Y., et al. (2022) · Nature · doi:10.1038/s41586-022-05508-0 · Cited by 125 · see citing works

A Novel Ribosomal S6-Kinase (RSK4; RPS6KA6) Is Commonly Deleted in Patients with Complex X-Linked Mental Retardation

Yntema, H. G., van den Helm, B., Kissing, J., van Duijnhoven, G., Poppelaars, F. A. M., Chelly, J., Moraine, C., Fryns, J., Hamel, B. C. J., Heilbronner, H., et al. (1999) · Genomics · doi:10.1006/geno.1999.6004 · Cited by 121 · see citing works

The ribosome, (slow) beating heart of cancer (stem) cell

Bastide, A., & David, A. (2018) · Oncogenesis · doi:10.1038/s41389-018-0044-8 · Cited by 119 · see citing works

RPL10L Is Required for Male Meiotic Division by Compensating for RPL10 during Meiotic Sex Chromosome Inactivation in Mice

Jiang, L., Li, T., Zhang, X., Zhang, B., Yu, C., Li, Y., Fan, S., Jiang, X., Khan, T., Hao, Q., et al. (2017) · Current Biology · doi:10.1016/j.cub.2017.04.017 · Cited by 118 · see citing works

Quantitative analysis of Y-Chromosome gene expression across 36 human tissuesPreprint

Godfrey, A. K., Naqvi, S., Chmátal, L., Chick, J. M., Mitchell, R. N., Gygi, S. P., Skaletsky, H., & Page, D. C. (2020) · Genome Research · doi:10.1101/gr.261248.120 · Cited by 116 · see citing works

A Novel Ribosomopathy Caused by Dysfunction of RPL10 Disrupts Neurodevelopment and Causes X-Linked Microcephaly in Humans

Brooks, S. S., Wall, A. L., Golzio, C., Reid, D. W., Kondyles, A., Willer, J. R., Botti, C., Nicchitta, C. V., Katsanis, N., & Davis, E. E. (2014) · Genetics · doi:10.1534/genetics.114.168211 · Cited by 115 · see citing works

Mice Deficient in Ribosomal Protein S6 Phosphorylation Suffer from Muscle Weakness that Reflects a Growth Defect and Energy Deficit

Ruvinsky, I., Katz, M. J., Dreazen, A., Gielchinsky, Y., Saada, A., Freedman, N., Mishani, E., Zimmerman, G., Kasir, J., & Meyuhas, O. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005618 · Cited by 111 · see citing works

Pathways to Specialized Ribosomes: The Brussels Lecture

Dinman, J. D. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.12.021 · Cited by 111 · 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

The N-terminal domain of SARS-CoV-2 nsp1 plays key roles in suppression of cellular gene expression and preservation of viral gene expression

Mendez, A. S., Ly, M., González-Sánchez, A. M., Hartenian, E., Ingolia, N. T., Cate, J. H. D., & Glaunsinger, B. A. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109841 · Cited by 110 · see citing works

Escape From X-Chromosome Inactivation: An Evolutionary Perspective

Posynick, B. J., & Brown, C. J. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00241 · Cited by 109 · see citing works

An X-to-autosome retrogene is required for spermatogenesis in mice

Bradley, J., Baltus, A. E., Skaletsky, H., Royce-Tolland, M., Dewar, K., & Page, D. C. (2004) · Nature Genetics · doi:10.1038/ng1390 · Cited by 105 · see citing works

Lost in Translation: Ribosome-Associated mRNA and Protein Quality Controls

Karamyshev, A. L., & Karamysheva, Z. N. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00431 · Cited by 103 · see citing works

Structure–function insights reveal the human ribosome as a cancer target for antibiotics

Myasnikov, A. G., Natchiar, S. K., Nebout, M., Hazemann, I., Imbert, V., Khatter, H., Peyron, J., & Klaholz, B. P. (2016) · Nature Communications · doi:10.1038/ncomms12856 · Cited by 98 · see citing works

SMN-primed ribosomes modulate the translation of transcripts related to spinal muscular atrophy

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Dengue virus NS1 protein interacts with the ribosomal protein RPL18: This interaction is required for viral translation and replication in Huh-7 cells

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