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

Gene expression regulation mediated through reversible m6A RNA methylation

Fu, Y., Dominissini, D., Rechavi, G., & He, C. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3724 · Cited by 1,961

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 1,187

Pseudouridine profiling reveals regulated mRNA pseudouridylation in yeast and human cells

Carlile, T. M., Rojas-Durán, M. F., Zinshteyn, B., Shin, H., Bartoli, K. M., & Gilbert, W. V. (2014) · Nature · doi:10.1038/nature13802 · Cited by 1,042

Transcriptome-wide Mapping Reveals Widespread Dynamic-Regulated Pseudouridylation of ncRNA and mRNA

Schwartz, S., Bernstein, D. A., Mumbach, M. R., Jovanović, M., Herbst, R. H., León-Ricardo, B. X., Engreitz, J., Guttman, M., Satija, R., Lander, E. S., et al. (2014) · Cell · doi:10.1016/j.cell.2014.08.028 · Cited by 1,013

MODOMICS: a database of RNA modification pathways—2013 update

Machnicka, M. A., Milanowska, K., Oglou, O. O., Purta, E., Kurkowska, M., Olchowik, A., Januszewski, W., Kalinowski, S., Dunin-Horkawicz, S., Rother, K. M., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1007 · Cited by 1,003

X-linked dyskeratosis congenita is caused by mutations in a highly conserved gene with putative nucleolar functions

Heiss, N. S., Knight, S. W., Vulliamy, T. J., Klauck, S. M., Wiemann, S., Mason, P. J., Poustka, A., & Dokal, I. (1998) · Nature Genetics · doi:10.1038/ng0598-32 · Cited by 976

Site-Specific Ribose Methylation of Preribosomal RNA: A Novel Function for Small Nucleolar RNAs

Kiss-László, Z., Henry, Y. A. L., Bachellerie, J., Caizergues‐Ferrer, M., & Kiss, T. (1996) · Cell · doi:10.1016/s0092-8674(00)81308-2 · Cited by 855

The RNA modification database, RNAMDB: 2011 update

Cantara, W. A., Crain, P. F., Rozenski, J., McCloskey, J. A., Harris, K. A., Zhang, X., Vendeix, F. A. P., Fabris, D., & Agris, P. F. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1028 · Cited by 822

Ribosome Biogenesis in the Yeast Saccharomyces cerevisiae

Woolford, J. L., & Baserga, S. J. (2013) · Genetics · doi:10.1534/genetics.113.153197 · Cited by 780

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 730

rRNA modifications and ribosome function

Decatur, W. A., & Fournier, M. J. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02109-6 · Cited by 703

An overview of pre‐ribosomal RNA processing in eukaryotes

Henras, A. K., Plisson‐Chastang, C., O’Donohue, M.-F., Chakraborty, A., & Gleizes, P. (2014) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1269 · Cited by 644

Site-Specific Pseudouridine Formation in Preribosomal RNA Is Guided by Small Nucleolar RNAs

Ganot, P., Bortolin‐Cavaillé, M., & Kiss, T. (1997) · Cell · doi:10.1016/s0092-8674(00)80263-9 · Cited by 643

Messenger RNA modifications: Form, distribution, and function

Gilbert, W. V., Bell, T. A., & Schaening-Burgos, C. (2016) · Science · doi:10.1126/science.aad8711 · Cited by 630

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 591

The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA

Watkins, N. J., & Bohnsack, M. T. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.117 · Cited by 520

Small Nucleolar RNAs Direct Site-Specific Synthesis of Pseudouridine in Ribosomal RNA

Ni, J., Tien, A. L., & Fournier, M. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80238-x · Cited by 519

snoRNA-LBME-db, a comprehensive database of human H/ACA and C/D box snoRNAs

Lestrade, L. (2005) · Nucleic Acids Research · doi:10.1093/nar/gkj002 · Cited by 518

Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly

Tollervey, D. W., Lehtonen, H., Jansen, R., Kern, H., & Hurt, E. C. (1993) · Cell · doi:10.1016/0092-8674(93)90120-f · Cited by 516

The Complexity of Human Ribosome Biogenesis Revealed by Systematic Nucleolar Screening of Pre-rRNA Processing Factors

Tafforeau, L., Zorbas, C., Langhendries, J.-L., Mullineux, S.-T., Stamatopoulou, V., Mullier, R., Wacheul, L., & Lafontaine, D. L. J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.011 · Cited by 492

A Computational Screen for Methylation Guide snoRNAs in Yeast

Lowe, T. M., & Eddy, S. R. (1999) · Science · doi:10.1126/science.283.5405.1168 · Cited by 467

Dyskeratosis Congenita and Cancer in Mice Deficient in Ribosomal RNA Modification

Ruggero, D., Grisendi, S., Piazza, F., Rego, E. M., Mari, F., Rao, P. H., Cordon‐Cardo, C., & Pandolfi, P. P. (2003) · Science · doi:10.1126/science.1079447 · Cited by 450

RNA nucleotide methylation

Motorin, Y., & Helm, M. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.79 · Cited by 441

Impaired Control of IRES-Mediated Translation in X-Linked Dyskeratosis Congenita

Yoon, A., Peng, G., Brandenburg, Y., Zollo, O., Xu, W. G., Rego, E. M., & Ruggero, D. (2006) · Science · doi:10.1126/science.1123835 · Cited by 423

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 405

Yeast Kre33 and human NAT10 are conserved 18S rRNA cytosine acetyltransferases that modify tRNAs assisted by the adaptor Tan1/THUMPD1

Sharma, S., Langhendries, J.-L., Watzinger, P., Kötter, P., Entian, K., & Lafontaine, D. L. J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv075 · Cited by 394

p53 Acts as a Safeguard of Translational Control by Regulating Fibrillarin and rRNA Methylation in Cancer

Marcel, V., Ghayad, S. E., Belin, S., Thérizols, G., Morel, A., Solano-Gonzàlez, E., Vendrell, J. A., Hacot, S., Mertani, H. C., Albaret, M. A., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.08.013 · Cited by 394

Global Mapping of Human RNA-RNA Interactions

Sharma, E., Sterne‐Weiler, T., O’Hanlon, D., & Blencowe, B. J. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.030 · Cited by 394

Post-transcriptional nucleotide modification and alternative folding of RNA

Helm, M. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj471 · Cited by 373

The box H + ACA snoRNAs carry Cbf5p, the putative rRNA pseudouridine synthase.Preprint

Lafontaine, D., Bousquet-Antonelli, C., Henry, Y., Caizergues-Ferrer, M., & Tollervey, D. (1998) · Genes & Development · doi:10.1101/gad.12.4.527 · Cited by 371

Are snoRNAs and snoRNA host genes new players in cancer?

Williams, G. T., & Farzaneh, F. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3195 · Cited by 363

Four newly located pseudouridylate residues in Escherichia coli 23S ribosomal RNA are all at the peptidyltransferase center: Analysis by the application of a new sequencing technique

Bakin, A. V., & Ofengand, J. (1993) · Biochemistry · doi:10.1021/bi00088a030 · Cited by 335

Eukaryotic ribosome biogenesis at a glance

Thomson, E., Ferreira-Cerca, S., & Hurt, E. (2013) · Journal of Cell Science · doi:10.1242/jcs.111948 · Cited by 324

Transfer RNA modifications: nature's combinatorial chemistry playground

Jackman, J. E., & Alfonzo, J. D. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1144 · Cited by 323

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

Yeast Pre-rRNA Processing and Modification Occur Cotranscriptionally

Koš, M., & Tollervey, D. W. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.024 · Cited by 310

Cross-linking, ligation, and sequencing of hybrids reveals RNA–RNA interactions in yeast

Kudla, G., Granneman, S., Hahn, D., Beggs, J. D., & Tollervey, D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017386108 · Cited by 308

The 5S RNP Couples p53 Homeostasis to Ribosome Biogenesis and Nucleolar Stress

Sloan, K. E., Bohnsack, M. T., & Watkins, N. J. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.049 · Cited by 298

Human NAT10 Is an ATP-dependent RNA Acetyltransferase Responsible for N4-Acetylcytidine Formation in 18 S Ribosomal RNA (rRNA)

Ito, S., Horikawa, S., Suzuki, T., Kawauchi, H., Tanaka, Y., Suzuki, T., & Suzuki, T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.c114.602698 · Cited by 297

Small nucleolar RNA signatures as biomarkers for non-small-cell lung cancer

Liao, J., Yu, L., Mei, Y., Guarnera, M., Shen, J., Li, R., Liu, Z., & Jiang, F. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-198 · Cited by 293

Ribosome Structure and Activity Are Altered in Cells Lacking snoRNPs that Form Pseudouridines in the Peptidyl Transferase Center

King, T. H., Liu, B., McCully, R. R., & Fournier, M. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00040-6 · Cited by 292

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 288

Noncoding RNAs in eukaryotic ribosome biogenesis and function

Lafontaine, D. L. J. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2939 · Cited by 285

The small-nucleolar RNAs commonly used for microRNA normalisation correlate with tumour pathology and prognosis

Gee, H. E., Buffa, F. M., Camps, C., Ramachandran, A., Leek, R., Taylor, M., Patil, M., Sheldon, H., Betts, G. N. J., Homer, J. J., et al. (2011) · British Journal of Cancer · doi:10.1038/sj.bjc.6606076 · Cited by 285

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 283

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

Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly

Polikanov, Y. S., Melnikov, S. V., Söll, D. G., & Steitz, T. A. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2992 · Cited by 275

Loss of rRNA modifications in the decoding center of the ribosome impairs translation and strongly delays pre-rRNA processing

Liang, X., Liu, Q., & Fournier, M. J. (2009) · RNA · doi:10.1261/rna.1724409 · Cited by 263

An updated human snoRNAome

Jorjani, H., Kehr, S., Jedlinski, D. J., Gumienny, R., Hertel, J., Stadler, P. F., Zavolan, M., & Gruber, A. R. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw386 · Cited by 257

‘View From A Bridge’: A New Perspective on Eukaryotic rRNA Base Modification

Sharma, S., & Lafontaine, D. L. J. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.07.008 · Cited by 255

Illumina-based RiboMethSeq approach for mapping of 2′-O-Me residues in RNA

Marchand, V., Blanloeil-Oillo, F., Helm, M., & Motorin, Y. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw547 · Cited by 246

Architecture of the 90S Pre-ribosome: A Structural View on the Birth of the Eukaryotic Ribosome

Kornprobst, M., Turk, M., Kellner, N., Cheng, J., Flemming, D., Kos‐Braun, I. C., Koš, M., Thoms, M., Berninghausen, O., Beckmann, R., et al. (2016) · Cell · doi:10.1016/j.cell.2016.06.014 · Cited by 239

Mutual protection of ribosomal proteins L5 and L11 from degradation is essential for p53 activation upon ribosomal biogenesis stress

Bursać, S., Brdovčak, M. C., Pfannkuchen, M. A., Oršolić, I., Golomb, L., Zhu, Y. Y., Katz, C., Daftuar, L., Grabušić, K., Vukelić, I., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218535109 · Cited by 237

Dual function of C/D box small nucleolar RNAs in rRNA modification and alternative pre-mRNA splicing

Falaleeva, M., Pagès, A., Matuszek, Ż., Hidmi, S., Agranat-Tamir, L., Korotkov, K. V., Nevo, Y., Eyras, E., Sperling, R., & Stamm, S. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519292113 · Cited by 229

rRNA Modifications in an Intersubunit Bridge of the Ribosome Strongly Affect Both Ribosome Biogenesis and Activity

Liang, X., Liu, Q., & Fournier, M. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.012 · Cited by 226

Point Mutations in Yeast CBF5 Can Abolish In Vivo Pseudouridylation of rRNA

Zebarjadian, Y., King, T., Fournier, M. J., Clarke, L., & Carbon, J. A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7461 · Cited by 224

Evolution of the ribosome at atomic resolution

Petrov, A. S., Bernier, C. R., Hsiao, C., Norris, A., Kovacs, N. A., Waterbury, C. C., Stepanov, V. G., Harvey, S. C., Fox, G. E., Wartell, R. M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1407205111 · Cited by 222

Structural Snapshots of Actively Translating Human Ribosomes

Behrmann, E., Loerke, J., Budkevich, T. V., Yamamoto, K., Schmidt, A., Penczek, P. A., Vos, M. R. J., Bürger, J., Mielke, T., Scheerer, P., et al. (2015) · Cell · doi:10.1016/j.cell.2015.03.052 · Cited by 220

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 220

Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively

Sharma, S., Yang, J., Watzinger, P., Kötter, P., & Entian, K. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt679 · Cited by 219

The 3D rRNA modification maps database: with interactive tools for ribosome analysis

Piekna‐Przybylska, D., Decatur, W. A., & Fournier, M. J. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm855 · Cited by 215

Elevated snoRNA biogenesis is essential in breast cancer

Su, H., Teng, X., Ganapathy, S., Shadfan, M., Long, M., Huang, T. H. ‐., Thompson, I. M., & Yuan, Z.-M. (2013) · Oncogene · doi:10.1038/onc.2013.89 · Cited by 209

Translating the genome in time and space: Specialized ribosomes, RNA regulons, and RNA-binding proteins

Shi, Z., & Barna, M. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100814-125346 · Cited by 205

The 18S rRNA dimethylase Dim1p is required for pre-ribosomal RNA processing in yeast.Preprint

Lafontaine, D. L. J., Vandenhaute, J., & Tollervey, D. W. (1995) · Genes & Development · doi:10.1101/gad.9.20.2470 · Cited by 204

Classical and novel approaches to the detection and localization of the numerous modified nucleotides in eukaryotic ribosomal RNA

Maden, B. E. H., Corbett, M., Heeney, P. A., Pugh, K., & Ajuh, P. (1995) · Biochimie · doi:10.1016/0300-9084(96)88100-4 · Cited by 192

Beyond microRNA – Novel RNAs derived from small non-coding RNA and their implication in cancer

Martens‐Uzunova, E. S., Olvedy, M., & Jenster, G. W. (2013) · Cancer Letters · doi:10.1016/j.canlet.2012.11.058 · Cited by 191

The human 18S rRNA base methyltransferases DIMT1L and WBSCR22-TRMT112 but not rRNA modification are required for ribosome biogenesis

Zorbas, C., Nicolas, É., Wacheul, L., Huvelle, E., Heurgué‐Hamard, V., & Lafontaine, D. L. J. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-02-0073 · Cited by 184

When ribosomes go bad: diseases of ribosome biogenesis

Freed, E. F., Bleichert, F., Dutca, L. M., & Baserga, S. J. (2010) · Molecular BioSystems · doi:10.1039/b919670f · Cited by 181

Deregulation of oncogene‐induced senescence and p53 translational control in X‐linked dyskeratosis congenita

Bellodi, C., Kopmar, N. E., & Ruggero, D. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.83 · Cited by 177

Prp43 Bound at Different Sites on the Pre-rRNA Performs Distinct Functions in Ribosome Synthesis

Bohnsack, M. T., Martin, R., Granneman, S., Ruprecht, M., Schleiff, E., & Tollervey, D. W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.039 · Cited by 175

Loss of Function of the Tumor Suppressor DKC1 Perturbs p27 Translation Control and Contributes to Pituitary Tumorigenesis

Bellodi, C., Krasnykh, O., Haynes, N., Theodoropoulou, M., Peng, G., Montanaro, L., & Ruggero, D. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4730 · Cited by 173

Activation of the tumor suppressor p53 upon impairment of ribosome biogenesis

Bursać, S., Brdovčak, M. C., Donati, G., & Volarević, S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.014 · Cited by 166

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 162

Small nucleolar RNAs in cancer

Mannoor, K., Liao, J., & Jiang, F. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.03.005 · Cited by 161

Yeast 18S rRNA Dimethylase Dim1p: a Quality Control Mechanism in Ribosome Synthesis?

Lafontaine, D. L. J., Preiß, T., & Tollervey, D. W. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.4.2360 · Cited by 160

Nucleotide modifications in three functionally important regions of the Saccharomyces cerevisiae ribosome affect translation accuracy

Baudin‐Baillieu, A., Fabret, C., Liang, X., Piekna‐Przybylska, D., Fournier, M. J., & Rousset, J. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp816 · Cited by 159

Genome-wide searching for pseudouridylation guide snoRNAs: analysis of the Saccharomyces cerevisiae genome

Schattner, P. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh768 · Cited by 158

WBSCR22/Merm1 is required for late nuclear pre-ribosomal RNA processing and mediates N 7 -methylation of G1639 in human 18S rRNA

Haag, S., Kretschmer, J., & Bohnsack, M. T. (2014) · RNA · doi:10.1261/rna.047910.114 · Cited by 158

The Treacher Collins syndrome (TCOF1) gene product is involved in pre-rRNA methylation

Gonzales, B. N., Henning, D., So, R. B., Dixon, J., Dixon, M. J., & Valdez, B. C. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi208 · Cited by 155

H/ACA Small RNA Dysfunctions in Disease Reveal Key Roles for Noncoding RNA Modifications in Hematopoietic Stem Cell Differentiation

Bellodi, C., McMahon, M. E., Contreras, A., Juliano, D., Kopmar, N. E., Nakamura, T., Maltby, D. A., Burlingame, A. L., Savage, S. A., Shimamura, A., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.04.030 · Cited by 154

Nob1p Is Required for Cleavage of the 3′ End of 18S rRNA

Fatica, A., Oeffinger, M., Dlakić, M., & Tollervey, D. W. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.5.1798-1807.2003 · Cited by 153

U2 snRNA is inducibly pseudouridylated at novel sites by Pus7p and snR81 RNP

Wu, G., Xiao, M., Yang, C., & Yu, Y. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.316 · Cited by 152

Posttranscriptional Modifications in 16S and 23S rRNAs of the Archaeal Hyperthermophile Sulfolobus solfataricus

Noon, K. R., Bruenger, E., & McCloskey, J. A. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.11.2883-2888.1998 · Cited by 147

High-throughput single-base resolution mapping of RNA 2΄-O-methylated residues

Incarnato, D., Anselmi, F., Morandi, E., Neri, F., Maldotti, M., Rapelli, S., Parlato, C., Basile, G., & Oliviero, S. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw810 · Cited by 145

Df31 Protein and snoRNAs Maintain Accessible Higher-Order Structures of Chromatin

Schubert, T. E. O., Pusch, M. C., Diermeier, S. D., Beneš, V., Kremmer, E., Imhof, A., & Längst, G. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.08.021 · Cited by 144

Bud23 Methylates G1575 of 18S rRNA and Is Required for Efficient Nuclear Export of Pre-40S Subunits

White, J., Li, Z., Sardana, R., Bujnicki, J. M., Marcotte, E. M., & Johnson, A. M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01674-07 · Cited by 139

Optimization of Ribosome Structure and Function by rRNA Base Modification

Baxter-Roshek, J. L., Petrov, A. N., & Dinman, J. D. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000174 · Cited by 138

RNA-guided isomerization of uridine to pseudouridine—pseudouridylation

Yu, Y., & Meier, U. T. (2014) · RNA Biology · doi:10.4161/15476286.2014.972855 · Cited by 135

The Bowen–Conradi syndrome protein Nep1 (Emg1) has a dual role in eukaryotic ribosome biogenesis, as an essential assembly factor and in the methylation of Ψ1191 in yeast 18S rRNA

Meyer, B., Wurm, J. P., Kötter, P., Leisegang, M. S., Schilling, V., Buchhaupt, M., Held, M., Bahr, U., Karas, M., Heckel, A., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq931 · Cited by 133

Structural basis for site-specific ribose methylation by box C/D RNA protein complexes

Lin, J., Lai, S., Jia, R., Xu, A., Zhang, L., Lu, J., & Ye, K. (2011) · Nature · doi:10.1038/nature09688 · Cited by 131

The ribosome assembly factor Nep1 responsible for Bowen–Conradi syndrome is a pseudouridine-N1-specific methyltransferase

Wurm, J. P., Meyer, B., Bahr, U., Held, M., Frolow, O., Kötter, P., Engels, J. W., Heckel, A., Karas, M., Entian, K., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1189 · Cited by 131

Mutation of a Gene Essential for Ribosome Biogenesis, EMG1, Causes Bowen-Conradi Syndrome

Armistead, J., Khatkar, S., Meyer, B., Mark, B. L., Patel, N., Coghlan, G., Lamont, R. E., Liu, S., Wiechert, J., Cattini, P. A., et al. (2009) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.04.017 · Cited by 129

Functional specialization of ribosomes?

Gilbert, W. V. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.12.002 · Cited by 122

Cracking pre‐40S ribosomal subunit structure by systematic analyses of RNA–protein cross‐linking

Granneman, S., Petfalski, E., Świątkowska, A., & Tollervey, D. W. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.86 · Cited by 122

The cancerous translation apparatus

Stumpf, C. R., & Ruggero, D. (2011) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2011.03.007 · Cited by 122

Identification of the locations of the methyl groups in 18 S ribosomal RNA from Xenopus laevis and man

Maden, B. E. H. (1986) · Journal of Molecular Biology · doi:10.1016/0022-2836(86)90498-5 · Cited by 120

Yeast Rrp8p, a novel methyltransferase responsible for m1A 645 base modification of 25S rRNA

Peifer, C., Sharma, S., Watzinger, P., Lamberth, S., Kötter, P., & Entian, K. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1102 · Cited by 118

Locations of methyl groups in 28 S rRNA of Xenopus laevis and man

Maden, B. E. H. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90139-8 · Cited by 117

The Splicing Factor Prp43p, a DEAH Box ATPase, Functions in Ribosome Biogenesis

Leeds, N. B., Small, E. C., Hiley, S. L., Hughes, T. R., & Staley, J. P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.2.513-522.2006 · Cited by 115

Structural Mechanism of Substrate RNA Recruitment in H/ACA RNA-Guided Pseudouridine Synthase

Duan, J., Li, L., Lu, J., Wang, W., & Ye, K. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.05.005 · Cited by 115

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 115

NML-mediated rRNA base methylation links ribosomal subunit formation to cell proliferation in a p53-dependent manner

Waku, T., Nakajima, Y., Yokoyama, W., Nomura, N., Kako, K., Kobayashi, A., Shimizu, T., & Fukamizu, A. (2016) · Journal of Cell Science · doi:10.1242/jcs.183723 · Cited by 115

Spb1p-Directed Formation of Gm2922 in the Ribosome Catalytic Center Occurs at a Late Processing Stage

Lapeyre, B., & Purushothaman, S. K. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.022 · Cited by 112

snOPY: a small nucleolar RNA orthological gene database

Yoshihama, M., Nakao, A., & Kenmochi, N. (2013) · BMC Research Notes · doi:10.1186/1756-0500-6-426 · Cited by 111

Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120

Bourgeois, G., Ney, M., Gáspár, I., Aigueperse, C., Schaefer, M., Kellner, S. M., Helm, M., & Motorin, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0133321 · Cited by 108

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

Novel Stress-responsive Genes EMG1 and NOP14 Encode Conserved, Interacting Proteins Required for 40S Ribosome Biogenesis

Liu, P. C. C., & Thiele, D. J. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.11.3644 · Cited by 104

Identification of a novel methyltransferase, Bmt2, responsible for the N-1-methyl-adenosine base modification of 25S rRNA in Saccharomyces cerevisiae

Sharma, S., Watzinger, P., Kötter, P., & Entian, K. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt195 · Cited by 103

Loss of ribosomal RNA modification causes developmental defects in zebrafish

Higa‐Nakamine, S., Suzuki, T., Uechi, T., Chakraborty, A., Nakajima, Y., Nakamura, M., Hirano, N., Suzuki, T., & Kenmochi, N. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr700 · Cited by 102

A computational screen for mammalian pseudouridylation guide H/ACA RNAs

SCHATTNER, P., Barberán-Soler, S., & Lowe, T. M. (2005) · RNA · doi:10.1261/rna.2210406 · Cited by 100

The evolution of the ribosome biogenesis pathway from a yeast perspective

Ebersberger, I., Simm, S., Leisegang, M. S., Schmitzberger, P., Mirus, O., von Haeseler, A., Bohnsack, M. T., & Schleiff, E. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1137 · Cited by 99

Structural and functional studies of Bud23–Trm112 reveal 18S rRNA N 7 -G1575 methylation occurs on late 40S precursor ribosomes

Létoquart, J., Huvelle, E., Wacheul, L., Bourgeois, G., Zorbas, C., Graille, M., Heurgué‐Hamard, V., & Lafontaine, D. L. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413089111 · Cited by 98

Clustering of Pseudouridine Residues Around the Peptidyltransferase Center of Yeast Cytoplasmic and Mitochondrial Ribosomes

Bakin, A. V., Lane, B. G., & Ofengand, J. (1994) · Biochemistry · doi:10.1021/bi00249a036 · Cited by 97

Characterization of two novel genes, WBSCR20 and WBSCR22, deleted in Williams-Beuren syndrome

Doll, A., & Grzeschik, K.-H. (2001) · Cytogenetic and Genome Research · doi:10.1159/000057012 · Cited by 94

Methylation of the nucleobases in RNA oligonucleotides mediates duplex–hairpin conversion

Micura, R., Pils, W., Höbartner, C., Grubmayr, K., Ebert, M., & Jaun, B. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.19.3997 · Cited by 94

5'ETS rRNA processing facilitated by four small RNAs: U14, E3, U17, and U3.

Enright, C., Maxwell, E. S., Eliceiri, G. L., & Sollner-Webb, B. (1996) · Europe PMC (PubMed Central) · Cited by 91

The association of late-acting snoRNPs with human pre-ribosomal complexes requires the RNA helicase DDX21

Sloan, K. E., Leisegang, M. S., Doebele, C., Ramίrez, A. S., Simm, S., Safferthal, C., Kretschmer, J., Schorge, T., Markoutsa, S., Haag, S., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1291 · Cited by 89

Snapshots of pre-rRNA structural flexibility reveal eukaryotic 40S assembly dynamics at nucleotide resolution

Hector, R. D., Burlacu, E., Aitken, S., Bihan, T. L., Tuijtel, M. W., Zaplatina, A., Cook, A. G., & Granneman, S. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku815 · Cited by 89

Trm112 Is Required for Bud23-Mediated Methylation of the 18S rRNA at Position G1575

Figaro, S., Wacheul, L., Schillewaert, S., Graille, M., Huvelle, E., Mongeard, R., Zorbas, C., Lafontaine, D. L. J., & Heurgué‐Hamard, V. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06623-11 · Cited by 89

A novel partial modification at C2501 in Escherichia coli 23S ribosomal RNA

Andersen, T. E., Porse, B. T., & Kirpekar, F. (2004) · RNA · doi:10.1261/rna.5259404 · Cited by 88

A systematic RNAi synthetic interaction screen reveals a link between p53 and snoRNP assembly

Krastev, D. B., Slabicki, M. M., Paszkowski‐Rogacz, M., Hubner, N. C., Junqueira, M., Shevchenko, A., Mann, M., Neugebauer, K. M., & Buchholz, F. (2011) · Nature Cell Biology · doi:10.1038/ncb2264 · Cited by 88

A cluster of methylations in the domain IV of 25S rRNA is required for ribosome stability

Gigova, A., Duggimpudi, S., Pollex, T., Schaefer, M., & Koš, M. (2014) · RNA · doi:10.1261/rna.043398.113 · Cited by 86

Ribosome biogenesis factor Tsr3 is the aminocarboxypropyl transferase responsible for 18S rRNA hypermodification in yeast and humans

Meyer, B., Wurm, J. P., Sharma, S., Immer, C., Pogoryelov, D., Kötter, P., Lafontaine, D. L. J., Wöhnert, J., & Entian, K. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw244 · Cited by 82

Emerging roles of RNA modifications in bacteria

Marbaniang, C. N., & Vogel, J. (2016) · Current Opinion in Microbiology · doi:10.1016/j.mib.2016.01.001 · Cited by 80

Box C/D snoRNP catalysed methylation is aided by additional pre‐rRNA base‐pairing

van Nues, R. W., Granneman, S., Kudla, G., Sloan, K. E., Chicken, M., Tollervey, D. W., & Watkins, N. J. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.148 · Cited by 78

Dyskerin depletion increases VEGF mRNA internal ribosome entry site-mediated translation

Rocchi, L., Pacilli, A., Sethi, R., Penzo, M., Schneider, R. J., Treré, D., Brigotti, M., & Montanaro, L. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt587 · Cited by 77

Requirement of rRNA Methylation for 80S Ribosome Assembly on a Cohort of Cellular Internal Ribosome Entry Sites

Basu, A., Das, P., Chaudhuri, S., Bevilacqua, E., Andrews, J., Barik, S., Hatzoglou, M., Komar, A. A., & Mazumder, B. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05804-11 · Cited by 75

An Evolutionary Study of the Methylation of Transfer and Ribosomal Ribonucleic Acid in Prokaryote and Eukaryote Organisms

Klagsbrun, M. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44151-3 · Cited by 74

Nucleocytoplasmic Transport of RNAs and RNA–Protein Complexes

Sloan, K. E., Gleizes, P., & Bohnsack, M. T. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.09.023 · Cited by 74

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 73

The yeast ribosome synthesis factor Emg1 is a novel member of the superfamily of alpha/beta knot fold methyltransferases

Leulliot, N., Bohnsack, M. T., Graille, M., Tollervey, D. W., & TILBEURGH, H. V. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1074 · Cited by 72

A snoRNA that guides the two most conserved pseudouridine modifications within rRNA confers a growth advantage in yeast

Badis, G., Fromont‐Racine, M., & Jacquier, A. (2003) · RNA · doi:10.1261/rna.5240503 · Cited by 71

Transfer RNA contains sites of localized positive charge: carbon NMR studies of [13C]methyl-enriched Escherichia coli and yeast tRNAPhe

Agris, P. F., Sierzputowska‐Gracz, H., & Smith, C. E. (1986) · Biochemistry · doi:10.1021/bi00366a022 · Cited by 70

Partial Methylation at Am100 in 18S rRNA of Baker's Yeast Reveals Ribosome Heterogeneity on the Level of Eukaryotic rRNA Modification

Buchhaupt, M., Sharma, S., Kellner, S. M., Oswald, S., Paetzold, M., Peifer, C., Watzinger, P., Schrader, J., Helm, M., & Entian, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089640 · Cited by 62

The Box H/ACA RNP Assembly Factor Naf1p Contains a Domain Homologous to Gar1p Mediating its Interaction with Cbf5p

Leulliot, N., Godin, K. S., Hoareau‐Aveilla, C., Quevillon‐Chéruel, S., Varani, G., Henry, Y. A. L., & TILBEURGH, H. V. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.06.031 · Cited by 60

RNAsnoop: efficient target prediction for H/ACA snoRNAs

Tafer, H., Kehr, S., Jana Hertel, A., Hofacker, I. L., & Stadler, P. F. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp680 · Cited by 60

PLEXY : efficient target prediction for box C/D snoRNAs

Kehr, S., Canzler, S., Stadler, P. F., & Tafer, H. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq642 · Cited by 60

Nep1p (Emg1p), a novel protein conserved in eukaryotes and archaea, is involved in ribosome biogenesis

Eschrich, D., Buchhaupt, M., Kötter, P., & Entian, K. (2002) · Current Genetics · doi:10.1007/s00294-001-0269-4 · Cited by 58

Burkitt’s lymphoma-associated c-Myc mutations converge on a dramatically altered target gene response and implicate Nol5a/Nop56 in oncogenesis

Cowling, V. H., Turner, S. A., & Cole, M. D. (2013) · Oncogene · doi:10.1038/onc.2013.338 · Cited by 55

A pre-ribosomal RNA interaction network involving snoRNAs and the Rok1 helicase

Martin, R., Hackert, P., Ruprecht, M., Simm, S., Brüning, L., Mirus, O., Sloan, K. E., Kudla, G. R., Schleiff, E., & Bohnsack, M. T. (2014) · RNA · doi:10.1261/rna.044669.114 · Cited by 54

Assembly and nuclear export of pre-ribosomal particles in budding yeast

Gerhardy, S., Menet, A. M., Peña, C., Petkowski, J. J., & Panse, V. G. (2014) · Chromosoma · doi:10.1007/s00412-014-0463-z · Cited by 53

Effects of the Bowen-Conradi syndrome mutation in EMG1 on its nuclear import, stability and nucleolar recruitment

Warda, A. S., Freytag, B., Haag, S., Sloan, K. E., Görlich, D., & Bohnsack, M. T. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw351 · Cited by 53

Identification of novel methyltransferases, Bmt5 and Bmt6, responsible for the m3U methylations of 25S rRNA in Saccharomyces cerevisiae

Sharma, S., Yang, J., Düttmann, S., Watzinger, P., Kötter, P., & Entian, K. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1281 · Cited by 49

Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly

Rothé, B., Back, R., Quinternet, M., Bizarro, J., Robert, M.-C., Blaud, M., Romier, C., Manival, X., Charpentier, B., Bertrand, É., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1091 · Cited by 49

The crystal structure of Nep1 reveals an extended SPOUT-class methyltransferase fold and a pre-organized SAM-binding site

Taylor, A. B., Meyer, B., Leal, B. Z., Kötter, P., Schirf, V. R., Demeler, B., Hart, P. J., Entian, K.-D., & Wöhnert, J. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkm1172 · Cited by 44

Mapping of the 13 pseudouridine residues in Saccharomyces cerevisiae small subunit ribosomal RNA to nucleotide resolution

Bakin, A. V., & Ofengand, J. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.16.3290 · Cited by 42

Genetic evidence for 18S rRNA binding and an Rps19p assembly function of yeast nucleolar protein Nep1p

Buchhaupt, M., Meyer, B., Kötter, P., & Entian, K. (2006) · Molecular Genetics and Genomics · doi:10.1007/s00438-006-0132-x · Cited by 42

Hepatic rRNA Transcription Regulates High-Fat-Diet-Induced Obesity

Oie, S., Matsuzaki, K., Yokoyama, W., Tokunaga, S., Waku, T., Han, S., Iwasaki, N., Mikogai, A., Yasuzawa-Tanaka, K., Kishimoto, H., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.038 · Cited by 39

Box C/D guide RNAs recognize a maximum of 10 nt of substrates

Yang, Z., Lin, J., & Ye, K. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604872113 · Cited by 35

Increased Expression of a Nucleolar Nop5/Sik Family Member in Metastatic Melanoma Cells

Nakamoto, K., Ito, A., Watabe, K., Koma, Y., Asada, H., Yoshikawa, K., Shinomura, Y., Matsuzawa, Y., Nojima, H., & Kitamura, Y. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62523-0 · Cited by 32

Physical and Functional Interaction between the Methyltransferase Bud23 and the Essential DEAH-Box RNA Helicase Ecm16

Sardana, R., Zhu, J., Gill, M. K., & Johnson, A. M. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01656-13 · Cited by 32

Different Mechanisms for Pseudouridine Formation in Yeast 5S and 5.8S rRNAs

Decatur, W. A., & Schnare, M. N. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01574-07 · Cited by 31

Pseudouridine distribution in mammalian 18 S ribosomal RNA. A major cluster in the central region of the molecule

Maden, B. E. H., & Wakeman, J. A. (1988) · Biochemical Journal · doi:10.1042/bj2490459 · Cited by 26

Identification of a new ribose methylation in the 18S rRNA of S. cerevisiae

Yang, J., Sharma, S., Kötter, P., & Entian, K. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv058 · Cited by 21

Unusual C′/D′ motifs enable box C/D snoRNPs to modify multiple sites in the same rRNA target region

van Nues, R. W., & Watkins, N. J. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw842 · Cited by 21

Dynamic RNA Modifications in Gene Expression Regulation

Roundtree, I. A., Evans, M., Pan, T., & He, C. (2017) · Cell · doi:10.1016/j.cell.2017.05.045 · Cited by 3,512

Role of RNA modifications in cancer

Barbieri, I., & Kouzarides, T. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-0253-2 · Cited by 1,350

RNA modifications modulate gene expression during development

Frye, M., Harada, B. T., Behm, M., & He, C. (2018) · Science · doi:10.1126/science.aau1646 · Cited by 1,263

Human METTL16 is a N6‐methyladenosine (m6A) methyltransferase that targets pre‐mRNAs and various non‐coding RNAs

Warda, A. S., Kretschmer, J., Hackert, P., Lenz, C., Urlaub, H., Höbartner, C., Sloan, K. E., & Bohnsack, M. T. (2017) · EMBO Reports · doi:10.15252/embr.201744940 · Cited by 655

Transcriptome-wide Mapping of Internal N7-Methylguanosine Methylome in Mammalian mRNA

Zhang, L., Liu, C., Ma, H., Dai, Q., Sun, H., Luo, G., Zhang, Z. S., Zhang, L., Hu, L., Dong, X., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.036 · Cited by 531

Synthesis, Function, and Heterogeneity of snoRNA-Guided Posttranscriptional Nucleoside Modifications in Eukaryotic Ribosomal RNAs

Henras, A. K., Plisson‐Chastang, C., Humbert, O., Roméo, Y., & Henry, Y. A. L. (2017) · The Enzymes · doi:10.1016/bs.enz.2017.03.007 · Cited by 41

Concerted modification of nucleotides at functional centers of the ribosome revealed by single-molecule RNA modification profiling

Bailey, A. D., Talkish, J., Ding, H., Igel, H., Durán, A., Mantripragada, S., Paten, B., & Ares, M. (2022) · eLife · doi:10.7554/elife.76562 · Cited by 44

Conserved ribosomal RNA modification and their putative roles in ribosome biogenesis and translation

Lapeyre, B. (2004) · Topics in current genetics · doi:10.1007/b105433 · Cited by 21

Ribosomal RNA modifications within the A-site of the large subunit : consequences for ribosome assembly and translation

Yelland, J. N. (2023) · Texas Digital Library (University of Texas) · doi:10.26153/tsw/59300

The ribosome epitranscriptome: inert—or a platform for functional plasticity?

Georgeson, J. M., & Schwartz, S. (2021) · RNA · doi:10.1261/rna.078859.121 · Cited by 21