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Pinto R, Hansen L, Hintze J, Almeida R, Larsen S, Coskun M, Davidsen J; Mitchelmore C, David L, Troelsen J, Bennett EP. Precise integration of inducible transcriptional elements (PrIITE) enables absolute control of gene expression. Nucleic Acids Research, 2017 45(13):e123.

Pinto R, Barros R, Pereira-Castro I, Mesquita P, da Costa LT, Bennett EP, Almeida R, David L. CDX2 homeoprotein is involved in the regulation of ST6GalNAc-I gene in intestinal metaplasia. Lab Invest, 2015 95(7):718-27.

Ricardo S, Marcos-Silva L, Pereira D, Pinto R, Almeida R, Söderberg O, Mandel U, Clausen H, Félix A, Lunet N, David L. Detection of glyco-mucin profiles improves specificity of MUC16 and MUC1 biomarkers in ovarian serous tumours. Mol Oncol, 2015 9(2):503-12.

Sousa SF, Coimbra JTS, Carvalho DP, Pinto R, Guimarães R, Teixeira V, Fernandes PA, Ramos MJ. Molecular dynamics analysis of a series of 22 potential farnesyltransferase substrates containing a CAAX-motif. J Mol Model, 2013. 19(2):673-88

Pinto R, Carvalho AS, Conze T, Magalhães A, Picco G, Burchell JM, Taylor-Papadimitriou J, Reis CA, Almeida R, Mandel U, Clausen H, Söderberg O, David L. Identification of new cancer biomarkers based on aberrant mucin glycoforms by in situ Proximity Ligation. J Cell Mol Med, 2012. 16(7):1474-84.

de Oliveira JT, de Matos AJ, Santos AL, Pinto R, Gomes J, Hespanhol V, Chammas R, Aki M, Bernardes ES, Reis CA, Rutteman GR, Gärtner F. Sialylation regulates galectin-3/ligand interplay during mammary tumour progression: a case of targeted uncloaking. Int J Dev Biol, 2011. 55(7-9): 823-34.

• Pinto, Rita; Hauge, Tobias; Jeanmougin, Marine; Pharo, Heidi Dietrichson; Kresse, Stine Henrichson & Honne, Hilde [Show all 13 contributors for this article] (2022). Targeted genetic and epigenetic profiling of esophageal adenocarcinomas and non-dysplastic Barrett’s esophagus. Clinical Epigenetics. ISSN 1868-7075. 14(77), p. 1–11. doi: 10.1186/s13148-022-01287-7. Full text in Research Archive
• Malecki, Jedrzej Mieczyslaw; O'Donohue, Marie-Francoise; Kim, Yeji; Jakobsson, Magnus; Gessa, Luca & Pinto, Rita [Show all 14 contributors for this article] (2021). Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function. Nucleic Acids Research (NAR). ISSN 0305-1048. 49(6), p. 3185–3203. doi: 10.1093/nar/gkab088. Full text in Research Archive
• Davydova, Erna; Shimazu, Tadahiro; Schuhmacher, Maren Kirstin; Jakobsson, Magnus E.; Willemen, Hanneke L.D.M. & Liu, Tongri [Show all 28 contributors for this article] (2021). The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes. Nature Communications. ISSN 2041-1723. 12, p. 1–14. doi: 10.1038/s41467-020-20670-7. Full text in Research Archive
• da Costa Florim Ribeiro Lopes, Nair Susana; Bergsland, Christian Holst; Bruun, Jarle; Bjørnslett, Merete Pauline; Vieira, André Filipe & Mesquita, Patrícia [Show all 14 contributors for this article] (2020). A panel of intestinal differentiation markers (CDX2, GPA33, and LI-cadherin) identifies gastric cancer patients with favourable prognosis. Gastric Cancer. ISSN 1436-3291. 23(5), p. 811–823. doi: 10.1007/s10120-020-01064-6.
• Flatin, Bjørnar Tovson Bae; Vedeld, Hege Marie; Pinto, Rita; Langerud, Jonas; Lind, Guro Elisabeth & Lothe, Ragnhild A [Show all 8 contributors for this article] (2020). Multiregional assessment of CIMP in primary colorectal cancers: Phenotype concordance but marker variability. International Journal of Cancer. ISSN 0020-7136. p. 1–6. doi: 10.1002/ijc.33425. Full text in Research Archive
• Pinto, Rita; Vågbø, Cathrine Broberg; Jakobsson, Magnus; Yeji, Kim; Baltissen, Marijke P & O'Donohue, Marie-Francoise [Show all 16 contributors for this article] (2019). The human methyltransferase ZCCHC4 catalyses N6-methyladenosine modification of 28S ribosomal RNA. Nucleic Acids Research (NAR). ISSN 0305-1048. 48(2), p. 830–846. doi: 10.1093/nar/gkz1147. Full text in Research Archive
• Malecki, Jedrzej Mieczyslaw; Willemen, Hanneke L.D.M.; Pinto, Rita; Ho, Angela Yeuan Yen; Moen, Anders & Eijkelkamp, Niels [Show all 7 contributors for this article] (2019). Human FAM173A is a mitochondrial lysine-specific methyltransferase that targets adenine nucleotide translocase and affects mitochondrial respiration . Journal of Biological Chemistry. ISSN 0021-9258. 294(31), p. 11654–11664. doi: 10.1074/jbc.RA119.009045.
• Malecki, Jedrzej Mieczyslaw; Willemen, Hanneke L.D.M.; Pinto, Rita; Ho, Angela Yeuan Yen; Moen, Anders & Kjønstad, Ingrid Fadum [Show all 10 contributors for this article] (2018). Lysine methylation by the mitochondrial methyltransferase FAM173B optimizes the function of mitochondrial ATP synthase. Journal of Biological Chemistry. ISSN 0021-9258. 294(4), p. 1128–1141. doi: 10.1074/jbc.RA118.005473. Show summary

  Lysine methylation is an important post-translational modification that is also present on mitochondrial proteins, but the mitochondrial lysine-specific methyltransferases (KMTs) responsible for modification are in most cases unknown. Here, we set out to determine the function of human family with sequence similarity 173 member B (FAM173B), a mitochondrial methyltransferase (MTase) reported to promote chronic pain. Using bioinformatics analyses and biochemical assays, we found that FAM173B contains an atypical, noncleavable mitochondrial targeting sequence responsible for its localization to mitochondria. Interestingly, CRISPR/Cas9-mediated KO of FAM173B in mammalian cells abrogated trimethylation of Lys-43 in ATP synthase c-subunit (ATPSc), a modification previously reported as ubiquitous among metazoans. ATPSc methylation was restored by complementing the KO cells with enzymatically active human FAM173B or with a putative FAM173B orthologue from the nematode Caenorhabditis elegans. Interestingly, lack of Lys-43 methylation caused aberrant incorporation of ATPSc into the ATP synthase complex and resulted in decreased ATP-generating ability of the complex, as well as decreased mitochondrial respiration. In summary, we have identified FAM173B as the long-sought KMT responsible for methylation of ATPSc, a key protein in cellular ATP production, and have demonstrated functional significance of ATPSc methylation. We suggest renaming FAM173B to ATPSc-KMT (gene name ATPSCKMT).

• Jakobsson, Magnus; Malecki, Jedrzej Mieczyslaw; Halabelian, Levon; Nilges, Benedikt S.; Pinto, Rita & Kudithipudi, Srikanth [Show all 14 contributors for this article] (2018). The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates. Nature Communications. ISSN 2041-1723. 9:3411, p. 1–15. doi: 10.1038/s41467-018-05646-y. Full text in Research Archive
• Pinto, Rita; Hansen, Lars; Hintze, John; Almeida, Raquel; Larsen, Sylvester & Coskun, Mehmet [Show all 11 contributors for this article] (2017). Precise integration of inducible transcriptional elements (PrIITE) enables absolute control of gene expression. Nucleic Acids Research (NAR). ISSN 0305-1048. 45:e123(13), p. 1–15. doi: 10.1093/nar/gkx371.

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