Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae

Lifeact: a versatile marker to visualize F-actin

Riedl, J., Crevenna, A. H., Kessenbrock, K., Yu, J. H., Neukirchen, D., Bista, M., Bradke, F., Jenne, D., Holak, T. A., Werb, Z., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1220 · Cited by 2,189 · see citing works

A simple and efficient method for direct gene deletion inSaccharomyces cerevisiae

Baudin‐Baillieu, A., Ozier-Kalogéropoulos, O., DENOUEL, A., Lacroute, F., & Cullin, C. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.14.3329 · Cited by 1,268 · see citing works

The BioGRID interaction database: 2013 update

Chatr‐aryamontri, A., Breitkreutz, B., Heinicke, S., Boucher, L., Winter, A. G., Stark, C., Nixon, J., Ramage, L., Kolas, N. K., O’Donnell, L., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1158 · Cited by 1,010 · see citing works

Trna: Structure, Biosynthesis, and Function

Söll, D. G., & RajBhandary, U. L. (1995) · Cited by 901 · see citing works

The BioGRID Interaction Database: 2011 update

Stark, C., Breitkreutz, B., Chatr‐aryamontri, A., Boucher, L., Oughtred, R., Livstone, M. S., Nixon, J., Auken, K. M. V., Wang, X., Shi, X., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq1116 · Cited by 853 · see citing works

tRNAdb 2009: compilation of tRNA sequences and tRNA genes

Jühling, F., Mörl, M., Hartmann, R. K., Sprinzl, M., Stadler, P. F., & Pütz, J. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn772 · Cited by 848 · see citing works

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 · see citing works

tRNA biology charges to the frontPreprint

Phizicky, E. M., & Hopper, A. K. (2010) · Genes & Development · doi:10.1101/gad.1956510 · Cited by 764 · see citing works

SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold.

Martin, J. L., & Mcmillan, F. M. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00391-3 · Cited by 581 · see citing works

tRNA’s Wobble Decoding of the Genome: 40 Years of Modification

Agris, P. F., Vendeix, F. A. P., & Graham, W. D. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.046 · Cited by 543 · see citing works

MODOMICS: a database of RNA modification pathways

Dunin-Horkawicz, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gkj084 · Cited by 511 · see citing works

Selective stabilization of mammalian microRNAs by 3′ adenylation mediated by the cytoplasmic poly(A) polymerase GLD-2Preprint

Katoh, T., Sakaguchi, Y., Miyauchi, K., Suzuki, T., Kashiwabara, S., Baba, T., & Suzuki, T. (2009) · Genes & Development · doi:10.1101/gad.1761509 · Cited by 438 · see citing works

CYGD: the Comprehensive Yeast Genome Database

Güldener, U. (2004) · Nucleic Acids Research · doi:10.1093/nar/gki053 · Cited by 333 · see citing works

Transcription and processing of intervening sequences in yeast tRNA genes

Knapp, G., Beckmann, J. S., Johnson, P. F., Fuhrman, S. A., & Abelson, J. N. (1978) · Cell · doi:10.1016/0092-8674(78)90109-5 · Cited by 317 · see citing works

Ribosomal frameshifting in the yeast retrotransposon Ty: tRNAs induce slippage on a 7 nucleotide minimal site

Belcourt, M. F., & Farabaugh, P. J. (1990) · Cell · doi:10.1016/0092-8674(90)90371-k · Cited by 292 · see citing works

Natural history of S-adenosylmethionine-binding proteins

Kozbial, P., & Mushegian, A. (2005) · BMC Structural Biology · doi:10.1186/1472-6807-5-19 · Cited by 287 · see citing works

Biosynthesis and Function of Modified Nucleosides

Björk, G. R. (2014) · ASM Press eBooks · doi:10.1128/9781555818333.ch11 · Cited by 243 · see citing works

Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions

Noma, A., Sakaguchi, Y., & Suzuki, T. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn1023 · Cited by 229 · see citing works

Biosynthesis of wybutosine, a hyper‐modified nucleoside in eukaryotic phenylalanine tRNA

Noma, A., Kirino, Y., Ikeuchi, Y., & Suzuki, T. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601105 · Cited by 218 · see citing works

An RNA-Modifying Enzyme that Governs Both the Codon and Amino Acid Specificities of Isoleucine tRNA

Soma, A., Ikeuchi, Y., Kanemasa, S., Kobayashi, K., Ogasawara, N., Ote, T., Kato, J., Watanabe, K., Sekine, Y., & Suzuki, T. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00346-0 · Cited by 211 · see citing works

The RNA modification database

Crain, P. F., & McCloskey, J. A. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.1.126 · Cited by 200 · see citing works

Actin cable dynamics in budding yeast

Yang, H., & Pon, L. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.022462899 · Cited by 198 · see citing works

The methylated nucleotide sequences in HeLa cell ribosomal RNA and its precursors

Maden, B. E. H., & Salim, M. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90299-x · Cited by 173 · see citing works

Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea

Ikeuchi, Y., 木村聡, Numata, T., Nakamura, D., Yokogawa, T., Ogata, T., Wada, T., Suzuki, T., & Suzuki, T. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.323 · Cited by 141 · see citing works

Mass Spectrometric Identification and Characterization of RNA‐Modifying Enzymes

Suzuki, T., Ikeuchi, Y., Noma, A., Suzuki, T., & Sakaguchi, Y. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)25009-8 · Cited by 128 · see citing works

A rare tRNA-Arg(CCU) that regulates Ty1 element ribosomal frameshifting is essential for Ty1 retrotransposition in Saccharomyces cerevisiae.

Kawakami, K., Pande, S., Faiola, B., Moore, D., Boeke, J. D., Farabaugh, P. J., Strathern, J. N., Nakamura, Y., & Garfinkel, D. J. (1993) · Genetics · doi:10.1093/genetics/135.2.309 · Cited by 126 · see citing works

Isolation and characterization of a novel actin filament-binding protein from Saccharomyces cerevisiae

Asakura, T., Sasaki, T., Nagano, F., Satoh, A., Obaishi, H., Nishioka, H., Imamura, H., Hotta, K., Tanaka, K., Nakanishi, H., et al. (1998) · Oncogene · doi:10.1038/sj.onc.1201487 · Cited by 118 · see citing works

Methylated bases of ribosomal ribonucleic acid from HeLa cells

Iwanami, Y., & Brown, G. M. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90553-5 · Cited by 114 · see citing works

Wobble modification differences and subcellular localization of tRNAs in Leishmania tarentolae: implication for tRNA sorting mechanism

Kaneko, T., Suzuki, T., Kapushoc, S. T., Rubio, M. A., Ghazvini, J., Watanabe, K., Simpson, L., & Suzuki, T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg066 · Cited by 113 · see citing works

Specific residues at every third position of siRNA shape its efficient RNAi activity

Katoh, T., & Suzuki, T. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkl1120 · Cited by 107 · see citing works

Biosynthesis and function of tRNA wobble modifications

Suzuki, T. (2005) · Topics in current genetics · doi:10.1007/b106361 · Cited by 99 · see citing works

tRNA residues that have coevolved with their anticodon to ensure uniform and accurate codon recognition

Olejniczak, M., & Uhlenbeck, O. C. (2006) · Biochimie · doi:10.1016/j.biochi.2006.06.005 · Cited by 98 · see citing works

Yeast retrotransposons and tRNAs

Voytas, D. F., & Boeke, J. D. (1993) · Trends in Genetics · doi:10.1016/0168-9525(93)90105-q · Cited by 95 · see citing works

Catalytic Mechanism of Glycine N-Methyltransferase,

Takata, Y., Huang, Y., Komoto, J., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M., & Takusagawa, F. (2003) · Biochemistry · doi:10.1021/bi034245a · Cited by 90 · see citing works

Automated parallel isolation of multiple species of non-coding RNAs by the reciprocal circulating chromatography method

Miyauchi, K., Ohara, T., & Suzuki, T. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkl1129 · Cited by 90 · see citing works

Modified Nucleosides in Translation

Curran, J. F. (2014) · ASM Press eBooks · doi:10.1128/9781555818296.ch27 · Cited by 88 · see citing works

Regulation of tRNA Bidirectional Nuclear-Cytoplasmic Trafficking inSaccharomyces cerevisiae

Murthi, A., Shaheen, H., Huang, H., Preston, M. A., Lai, T., Phizicky, E. M., & Hopper, A. K. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-07-0551 · Cited by 88 · see citing works

The ribosome in focus: new structures bring new insights

Korostelev, A. A., & Noller, H. F. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.08.002 · Cited by 86 · see citing works

Computational identification of putative programmed translational frameshift sites

Shah, A. A., Giddings, M. C., Parvaz, J. B., Gesteland, R. F., Atkins, J. F., & Ivanov, I. P. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.8.1046 · Cited by 80 · see citing works

Only one of two closely related yeast suppressor tRNA genes contains an intervening sequence

Olson, M. V., Page, G. S., Sentenac, A., Piper, P. W., Worthington, M., Weiss, R. B., & Hall, B. D. (1981) · Nature · doi:10.1038/291464a0 · Cited by 78 · see citing works

Chemical-genetic profile analysis of five inhibitory compounds in yeast

Alamgir, M. S., Erukova, V., Jessulat, M., Azizi, A., & Golshani, A. (2010) · BMC Chemical Biology · doi:10.1186/1472-6769-10-6 · Cited by 72 · see citing works

The nucleotide in position 32 of the tRNA anticodon loop determines ability of anticodon UCC to discriminate among glycine codons.

Lustig, F., Borén, T., Claesson, C., Simonsson, C., Barciszewska, M., & Lagerkvist, U. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3343 · Cited by 68 · see citing works

Isolation of 3-methyluridine and 3-methylcytidine from soluble ribonucleic acid

Hall, R. H. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90105-0 · Cited by 50 · see citing works

Bases in the anticodon loop of tRNAAlaGGC prevent misreading

Murakami, H., Ohta, A., & Suga, H. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1580 · Cited by 41 · see citing works

The Ribosomal Grip of the Peptidyl-tRNA is Critical for Reading Frame Maintenance

Näsvall, J., Nilsson, K. L., & Björk, G. R. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.10.069 · Cited by 33 · see citing works

Evolution of +1 Programmed Frameshifting Signals and Frameshift-Regulating tRNAs in the Order Saccharomycetales

Farabaugh, P. J., Kramer, E. B., Vallabhaneni, H., & Raman, A. (2006) · Journal of Molecular Evolution · doi:10.1007/s00239-005-0311-0 · Cited by 33 · see citing works

Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC

Sunita, S. C., Purta, E., Durawa, M., Tkaczuk, K. L., Jayaraman, S., Bujnicki, J. M., & Sivaraman, J. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm411 · Cited by 32 · see citing works

Structure primaire des tRNAThrla et b de levure de bière

Weissenbach, J., Kiraly, I., & Dirheimer, G. (1977) · Biochimie · doi:10.1016/s0300-9084(77)80314-3 · Cited by 23 · see citing works

Identification and characterization of CRT10 as a novel regulator of Saccharomyces cerevisiae ribonucleotide reductase genes

Fu, Y. V. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl100 · Cited by 20 · see citing works

Human Mitochondrial tRNAs: Biogenesis, Function, Structural Aspects, and Diseases

Suzuki, T., Nagao, A., & Suzuki, T. (2011) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132531 · Cited by 554 · see citing works

Biosynthesis and Function of Posttranscriptional Modifications of Transfer RNAs

Yacoubi, B. E., Bailly, M. A., & de Crécy‐Lagard, V. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110711-155641 · Cited by 546 · see citing works

Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use

Atkins, J. F., Loughran, G., Bhatt, P. R., Firth, A. E., & Baranov, P. V. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw530 · Cited by 320 · see citing works

A complete landscape of post-transcriptional modifications in mammalian mitochondrial tRNAs

Suzuki, T., & Suzuki, T. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku390 · Cited by 305 · see citing works

Cell Polarization and Cytokinesis in Budding Yeast

Bi, E., & Park, H.-O. (2012) · Genetics · doi:10.1534/genetics.111.132886 · Cited by 303 · see citing works

Complete chemical structures of human mitochondrial tRNAs

Suzuki, T., Yashiro, Y., Kikuchi, I., Ishigami, Y., Saito, H., Matsuzawa, I., Okada, S., Mito, M., Iwasaki, S., Ma, D., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18068-6 · Cited by 281 · see citing works

RNA methylation and cancer treatment

Yang, B., Wang, J., Tan, Y., Yuan, R., Chen, Z., & Zou, C. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105937 · Cited by 239 · see citing works

Actin and Endocytosis in Budding Yeast

Goode, B. L., Eskin, J. A., & Wendland, B. (2015) · Genetics · doi:10.1534/genetics.112.145540 · Cited by 221 · see citing works

Naturally occurring modified ribonucleosides

McCown, P. J., Ruszkowska, A., Kunkler, C. N., Breger, K., Hulewicz, J. P., Wang, M. C., Springer, N. A., & Brown, J. A. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1595 · Cited by 210 · see citing works

Three distinct 3-methylcytidine (m3C) methyltransferases modify tRNA and mRNA in mice and humans

Xu, L., Liu, X., Sheng, N., Oo, K. S., Liang, J., Chionh, Y. H., Xu, J., Ye, F., Gao, Y., Dedon, P. C., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.798298 · Cited by 208 · see citing works

Transfer RNA Post-Transcriptional Processing, Turnover, and Subcellular Dynamics in the YeastSaccharomyces cerevisiae

Hopper, A. K. (2013) · Genetics · doi:10.1534/genetics.112.147470 · Cited by 189 · see citing works

Methylated nucleosides in tRNA and tRNA methyltransferases

Hori, H. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00144 · Cited by 188 · see citing works

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

Dever, T. E., Kinzy, T. G., & Pavitt, G. D. (2016) · Genetics · doi:10.1534/genetics.115.186221 · Cited by 143 · see citing works

Epitranscriptomic Code and Its Alterations in Human Disease

Kadumuri, R. V., & Janga, S. C. (2018) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.07.010 · Cited by 140 · see citing works

Human transfer RNA modopathies: diseases caused by aberrations in transfer RNA modifications

Chujo, T., & Tomizawa, K. (2021) · FEBS Journal · doi:10.1111/febs.15736 · Cited by 121 · see citing works

The life and times of a tRNA

Phizicky, E. M., & Hopper, A. K. (2023) · RNA · doi:10.1261/rna.079620.123 · Cited by 122 · see citing works

A rationale for tRNA modification circuits in the anticodon loop

Han, L., & Phizicky, E. M. (2018) · RNA · doi:10.1261/rna.067736.118 · Cited by 113 · see citing works

METTL6 is a tRNA m 3 C methyltransferase that regulates pluripotency and tumor cell growth

Ignatova, V. V., Kaiser, S., Ho, J., Bing, X., Stolz, P., Tan, Y. X., Lee, C. L., Gay, F. P. H., Lastres, P. R., Gerlini, R., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz4551 · Cited by 100 · see citing works

Transfer RNA Methytransferases and Their Corresponding Modifications in Budding Yeast and Humans: Activities, Predications, and Potential Roles in Human Health

Towns, W. L., & Begley, T. J. (2011) · DNA and Cell Biology · doi:10.1089/dna.2011.1437 · Cited by 98 · see citing works

Highly Predictive Reprogramming of tRNA Modifications Is Linked to Selective Expression of Codon-Biased Genes

Chan, C. T. Y., Deng, W., Li, F., DeMott, M. S., Babu, I. R., Begley, T. J., & Dedon, P. C. (2015) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5b00004 · Cited by 91 · see citing works

Nucleotide resolution profiling of m3C RNA modification by HAC-seq

Cui, J., Liu, Q., Sendinc, E., Shi, Y., & Gregory, R. I. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1186 · Cited by 86 · see citing works

Evolving specificity of tRNA 3-methyl-cytidine-32 (m3C32) modification: a subset of tRNAsSer requires N6-isopentenylation of A37

Arimbasseri, G. A., Iben, J., Wei, F., Rijal, K., Tomizawa, K., Hafner, M., & Maraia, R. J. (2016) · RNA · doi:10.1261/rna.056259.116 · Cited by 80 · see citing works

DALRD3 encodes a protein mutated in epileptic encephalopathy that targets arginine tRNAs for 3-methylcytosine modification

Lentini, J. M., Alsaif, H. S., Faqeih, E., Alkuraya, F. S., & Fu, D. (2020) · Nature Communications · doi:10.1038/s41467-020-16321-6 · Cited by 72 · see citing works

Diversity in mechanism and function of tRNA methyltransferases

Swinehart, W. E., & Jackman, J. E. (2015) · RNA Biology · doi:10.1080/15476286.2015.1008358 · Cited by 68 · see citing works

Biogenesis and growth phase-dependent alteration of 5-methoxycarbonylmethoxyuridine in tRNA anticodons

Sakai, Y., Miyauchi, K., 木村聡, & Suzuki, T. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1470 · Cited by 67 · see citing works

S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates

Han, L., Marcus, E., D’Silva, S., & Phizicky, E. M. (2016) · RNA · doi:10.1261/rna.059667.116 · Cited by 67 · see citing works

Biosynthesis of Albomycin δ2 Provides a Template for Assembling Siderophore and Aminoacyl-tRNA Synthetase Inhibitor Conjugates

Zeng, Y., Kulkarni, A. S., Yang, Z., Patil, P. B., Zhou, W., Chi, X., Lanen, S. G. V., & Chen, S. (2012) · ACS Chemical Biology · doi:10.1021/cb300173x · Cited by 66 · see citing works

Mutually exclusive substrate selection strategy by human m3C RNA transferases METTL2A and METTL6

Mao, X.-L., Li, Z.-H., Huang, M.-H., Wang, J., Zhou, J.-B., Li, Q., Xu, H. Y., Wang, X., & Zhou, X.-L. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab603 · Cited by 62 · see citing works

Discovery of the β-barrel–type RNA methyltransferase responsible forN6-methylation ofN6-threonylcarbamoyladenosine in tRNAs

木村聡, Miyauchi, K., Ikeuchi, Y., Thiaville, P. C., de Crécy‐Lagard, V., & Suzuki, T. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku618 · Cited by 62 · see citing works

Identification of tRNA nucleoside modification genes critical for stress response and development in rice and Arabidopsis

Wang, Y., Pang, C., Li, X., Hu, Z., Lv, Z., Zheng, B., & Chen, P. (2017) · BMC Plant Biology · doi:10.1186/s12870-017-1206-0 · Cited by 62 · see citing works

Dual pathways of tRNA hydroxylation ensure efficient translation by expanding decoding capability

Sakai, Y., 木村聡, & Suzuki, T. (2019) · Nature Communications · doi:10.1038/s41467-019-10750-8 · Cited by 62 · see citing works

The RNA methyltransferase METTL8 installs m3C32 in mitochondrial tRNAsThr/Ser(UCN) to optimise tRNA structure and mitochondrial translation

Kleiber, N., Lemus-Diaz, N., Stiller, C., Heinrichs, M., Mai, M. M.-Q., Hackert, P., Richter‐Dennerlein, R., Höbartner, C., Bohnsack, K. E., & Bohnsack, M. T. (2022) · Nature Communications · doi:10.1038/s41467-021-27905-1 · Cited by 60 · see citing works

Lack of 2'-O-methylation in the tRNA anticodon loop of two phylogenetically distant yeast species activates the general amino acid control pathway

Han, L., Guy, M. P., Kon, Y., & Phizicky, E. M. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007288 · Cited by 53 · see citing works

Aberrant RNA methylation triggers recruitment of an alkylation repair complex

Tsao, N., Brickner, J. R., Rodell, R., Ganguly, A., Wood, M., Oyeniran, C., Ahmad, T., Sun, H., Bacolla, A., Zhang, L., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.024 · Cited by 46 · see citing works

Roles and dynamics of 3-methylcytidine in cellular RNAs

Bohnsack, K. E., Kleiber, N., Lemus-Diaz, N., & Bohnsack, M. T. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.03.004 · Cited by 44 · see citing works

Molecular basis for human mitochondrial tRNA m3C modification by alternatively spliced METTL8

Huang, M.-H., Peng, G.-X., Mao, X.-L., Wang, J., Zhou, J.-B., Zhang, J., Chen, M., Wang, E., & Zhou, X.-L. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac184 · Cited by 44 · see citing works

Biogenesis and iron-dependency of ribosomal RNA hydroxylation

木村聡, Sakai, Y., Ishiguro, K., & Suzuki, T. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx969 · Cited by 42 · see citing works

Cotranslational transport of ABP140 mRNA to the distal pole of S. cerevisiae

Kilchert, C., & Spang, A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.247 · Cited by 40 · see citing works

Factors That Shape Eukaryotic tRNAomes: Processing, Modification and Anticodon–Codon Use

Maraia, R. J., & Arimbasseri, G. A. (2017) · Biomolecules · doi:10.3390/biom7010026 · Cited by 39 · see citing works

Methyltransferase METTL8 is required for 3-methylcytosine modification in human mitochondrial tRNAs

Lentini, J. M., Bargabos, R., Chen, C., & Fu, D. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101788 · Cited by 35 · see citing works

Modifications of the human tRNA anticodon loop and their associations with genetic diseases

Zhou, J.-B., Wang, E., & Zhou, X.-L. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03948-x · Cited by 34 · see citing works

Base Pairing and Functional Insights into N 3 -Methylcytidine (m 3 C) in RNA

Mao, S., Haruehanroengra, P., Ranganathan, S. V., Shen, F., Begley, T. J., & Sheng, J. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00735 · Cited by 31 · see citing works

Novel dual methylation of cytidines in the RNA of mammals

Cheng, M.-Y., You, X., Ding, J.-H., Dai, Y., Chen, M., Yuan, B., & Feng, Y. (2021) · Chemical Science · doi:10.1039/d1sc01972d · Cited by 28 · see citing works

The covalent nucleotide modifications within plant mRNAs: What we know, how we find them, and what should be done in the future

Prall, W., Ganguly, D. R., & Gregory, B. D. (2023) · The Plant Cell · doi:10.1093/plcell/koad044 · Cited by 28 · see citing works

The impact of tRNA modifications on translation in cancer: identifying novel therapeutic avenues

Añazco-Guenkova, A. M., Miguel‐López, B., Monteagudo-García, Ó., García-Vílchez, R., & Blanco, S. (2024) · NAR Cancer · doi:10.1093/narcan/zcae012 · Cited by 27 · see citing works

Variations in transfer and ribosomal RNA epitranscriptomic status can adapt eukaryote translation to changing physiological and environmental conditions

Dannfald, A., Favory, J.-J., & Deragon, J. (2021) · RNA Biology · doi:10.1080/15476286.2021.1931756 · Cited by 27 · see citing works

m3C32 tRNA modification controls serine codon-biased mRNA translation, cell cycle, and DNA-damage response

Cui, J., Sendinc, E., Liu, Q., Kim, S., Fang, J. Y., & Gregory, R. I. (2024) · Nature Communications · doi:10.1038/s41467-024-50161-y · Cited by 26 · see citing works

Multi-Substrate Specificity and the Evolutionary Basis for Interdependence in tRNA Editing and Methylation Enzymes

Dixit, S., Henderson, J. C., & Alfonzo, J. D. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00104 · Cited by 25 · see citing works

Mitochondrial RNA m3C methyltransferase METTL8 relies on an isoform-specific N-terminal extension and modifies multiple heterogenous tRNAs

Huang, M.-H., Wang, J., Zhang, J., Mao, X.-L., Peng, G.-X., Lin, X., Lv, D., Yuan, C., Lin, H., Wang, E., et al. (2023) · 中国科学通报：英文版 · doi:10.1016/j.scib.2023.08.002 · Cited by 21 · see citing works

Structural basis of tRNA recognition by the m3C RNA methyltransferase METTL6 in complex with SerRS seryl-tRNA synthetase

Throll, P., Dolce, L. G., Rico-Lastres, P., Arnold, K., Tengo, L., Basu, S., Kaiser, S., Schneider, R., & Kowalinski, E. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01341-3 · Cited by 19 · see citing works

How Natural Enzymes and Synthetic Ribozymes Generate Methylated Nucleotides in RNA

Höbartner, C., Bohnsack, K. E., & Bohnsack, M. T. (2024) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-030222-112310 · Cited by 16 · see citing works

A new modification for mammalian messenger RNA

Liu, F., & He, C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.h117.798298 · Cited by 14 · see citing works

Disclosing the functional changes of two genetic alterations in a patient with Chronic Progressive External Ophthalmoplegia: Report of the novel mtDNA m.7486G>A variant

Bacalhau, M., Simões, M., Rocha, M. C., Hardy, S. A., Vincent, A. E., Durães, J., Macário, C., Santos, M. J., Rebelo, O., Lopes, C., et al. (2017) · Neuromuscular Disorders · doi:10.1016/j.nmd.2017.11.006 · Cited by 13 · see citing works

Identification of factors that promote biogenesis of tRNACGASer

Xu, F., Zhou, Y., Byström, A. S., & Johansson, M. (2018) · RNA Biology · doi:10.1080/15476286.2018.1526539 · Cited by 11 · see citing works

A tRNA methyltransferase paralog is important for ribosome stability and cell division in Trypanosoma brucei

Fleming, I. M. C., Paris, Z., Gaston, K. W., Balakrishnan, R., Fredrick, K. L., Rubio, M. A. T., & Alfonzo, J. D. (2016) · Scientific Reports · doi:10.1038/srep21438 · Cited by 10 · see citing works

Binding synergy as an essential step for tRNA editing and modification enzyme codependence in Trypanosoma brucei

McKenney, K. M., Rubio, M. A. T., & Alfonzo, J. D. (2017) · RNA · doi:10.1261/rna.062893.117 · Cited by 10 · see citing works

The potential of RNA methylation in the treatment of cardiovascular diseases

Wang, K., Wang, Y., Li, Y., Fang, B., Li, B., Cheng, W., Wang, K., & Yang, S. (2024) · iScience · doi:10.1016/j.isci.2024.110524 · Cited by 9 · see citing works

METTLing in the right place: METTL8 is a mitochondrial tRNA-specific methyltransferase

Kowalinski, E., & Alfonzo, J. D. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.11.009 · Cited by 9 · see citing works

Improved tools for live imaging of F-actin structures in yeast

Wirshing, A. C. E., & Goode, B. L. (2024) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-05-0212-t · Cited by 7 · see citing works

Mechanisms by which PE21, an extract from the white willow Salix alba, delays chronological aging in budding yeast

Medkour, Y., Mohammad, K., Arlia‐Ciommo, A., Svistkova, V., Dakik, P., Mitrofanova, D., Rodriguez, M. E. L., Junio, J. A. B., Taifour, T., Escudero, P., et al. (2019) · Oncotarget · doi:10.18632/oncotarget.27209 · Cited by 6 · see citing works

Synthesis and Purification of N3‐Methylcytidine (m3C) Modified RNA Oligonucleotides

Mathivanan, J., Du, J., Mao, S., Zheng, Y. Y., & Sheng, J. (2021) · Current Protocols · doi:10.1002/cpz1.307 · Cited by 4 · see citing works

METTL2B m3C RNA transferase: oncogenic role in ovarian cancer progression via regulation of the mTOR/AKT pathway and its link to the tumor immune microenvironment

Meng, Y., Meng, Y., Zheng, H., Huo, J., Li, P., Shan, Y., & He, J. (2024) · BMC Cancer · doi:10.1186/s12885-024-13225-2 · Cited by 1 · see citing works

Analysis of CK2-dependent regulation of Myo5-induced actin polymerization during the endocytic uptake in S.cerevisiae

Golbano, F., & Isabel, M. (2012) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

Picking the high hanging fruit : automated ways to annotate awkward genes

hÉigeartaigh, S. Ó. (2012) · Arrow@dit (Dublin Institute of Technology)

A semi-quantitative pull-down assay to study tRNA substrate specificity of modification enzymes

Han, L., Marcus, E., & Phizicky, E. M. (2021) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2021.06.010

Is Language a Mechanical Signal? Cytoskeletal Responses to Speech in YeastPreprint

Shirzadian, M., Gollob, E., Reiter, C., Rauter, U., Paschinger, M., Caballero, C., Rinnerthaler, M., & Spiess, K. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.08.663738

Structural and Functional Characterization of the APOBEC1 Editosome and of tRNA Modification by METTL6

Throll, P. (2022) · doi:10.70675/2d1a7d1az4f72z4ff9zb0acz8a714c33fda8

Etude des mécanismes de formation et des fonctions physiologiques des Actin Bodies chez Saccharomyces cerevisiae

Mauboules, D. (2023) · doi:10.70675/ce716e6fzcb79z4965z9beez42e660e585ec

A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop

D'Silva, S., Haider, S. J., & Phizicky, E. M. (2011) · RNA · doi:10.1261/rna.2652611 · Cited by 83 · see citing works

S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates

Han, L., Marcus, E., D’Silva, S., & Phizicky, E. M. (2016) · RNA · doi:10.1261/rna.059667.116 · Cited by 67 · see citing works

Evolving specificity of tRNA 3-methyl-cytidine-32 (m3C32) modification: a subset of tRNAsSer requires N6-isopentenylation of A37

Arimbasseri, G. A., Iben, J., Wei, F., Rijal, K., Tomizawa, K., Hafner, M., & Maraia, R. J. (2016) · RNA · doi:10.1261/rna.056259.116 · Cited by 80 · see citing works

Three distinct 3-methylcytidine (m3C) methyltransferases modify tRNA and mRNA in mice and humans

Xu, L., Liu, X., Sheng, N., Oo, K. S., Liang, J., Chionh, Y. H., Xu, J., Ye, F., Gao, Y., Dedon, P. C., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.798298 · Cited by 208 · see citing works

Isolation of 3-methyluridine and 3-methylcytidine from soluble ribonucleic acid

Hall, R. H. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90105-0 · Cited by 50 · see citing works