Articles: 190, H-index: 62 (Google Scholar); 55 (Scopus); Citations: 16000 (Google Scholar): 12000 (Scopus) (* indicates corresponding author; most relevant articles from the last five years are shown).
RNA structure / phase separation
Sanchez de Groot N., Armaos A., Graña-Montes R., ... Vabulas R.M., Tartaglia G.G.* RNA structure drives interaction with proteins, Nature Communications (2019), https://doi.org/10.1038/s41467-019-10923-5. This study investigates the relationship between RNA structure and protein interactions, revealing that highly structured RNAs interact with more proteins, impacting gene regulation and the formation of phase-separated ribonucleoprotein assemblies.
Cerase A., Armaos A., Neumayer C., ... Guttman M, Tartaglia G.G.* Phase separation drives X-chromosome inactivation: a hypothesis, Nature Structural & Molecular Biology (2019), https://doi.org/10.1038/s41594-019-0223-0. This article proposes a hypothesis that the long non-coding RNA Xist induces X-chromosome inactivation through phase separation, supported by evidence showing similarities between Xist assemblies and other phase-separated condensates, suggesting a critical role of RNA-protein interactions in this process.
Luige J., Armaos A., Tartaglia G.G.*, Ørom U.A.V*. Predicting nuclear G-quadruplex RNA-binding proteins with roles in transcription and phase separation, Nature Communications (2024), https://doi.org/10.1038/s41467-024-46731-9. This study identifies and predicts proteins that bind to G-quadruplex RNA in the nucleus, exploring their roles in transcription and phase separation, providing insights into RNA-protein interactions and their implications in gene regulation and cellular processes.
RNA design / phase transitions / aggregation
Zacco E., Kantelberg O., Milanetti E., ... Pastore A., Tartaglia G.G. Probing TDP-43 condensation using an in silico designed aptamer, Nature Communications (2022), https://doi.org/10.1038/s41467-022-30944-x. This article demonstrates the use of an in silico designed aptamer to probe the condensation of TDP-43, providing insights into its aggregation process and potential therapeutic applications.
Rupert J., Monti M., Zacco E., ... Tartaglia G.G.* RNA sequestration driven by amyloid formation: the alpha synuclein case, Nucleic Acids Research (2023), https://doi.org/10.1093/nar/gkad857. This study explores how amyloid formation, particularly by alpha-synuclein, leads to RNA sequestration, providing insights into the interaction between amyloids and nucleic acids and their implications in neurodegenerative diseases.
Luige J., Conrad T., Armaos A., Louloupi A., Vincent A., Meierhofer D., Gajhede M., Tartaglia G.G. (corresponding author), Ørom U.A.V. Design and characterization of G-quadruplex RNA aptamers reveal RNA-binding by KDM5 lysine demethylases, Computational and Structural Biotechnology Journal (2025), https://doi.org/10.1016/j.csbj.2025.06.027 This work characterizes RNA aptamers that adopt G-quadruplex structures and uses them to reveal previously unrecognized RNA-binding activity in the KDM5 family of histone lysine demethylases. Through computational predictions and experimental validation, the authors show that KDM5A and KDM5B preferentially interact with G-quadruplex RNAs, mediated by their ARID and adjacent protein domains, and that RNA binding contributes to the formation of KDM5-containing complexes, expanding the understanding of how RNA structural motifs can influence chromatin regulation and epigenetic function.
RNA structure / phase separation
Sanchez de Groot N., Armaos A., Graña-Montes R., ... Vabulas R.M., Tartaglia G.G.* RNA structure drives interaction with proteins, Nature Communications (2019), https://doi.org/10.1038/s41467-019-10923-5. This study investigates the relationship between RNA structure and protein interactions, revealing that highly structured RNAs interact with more proteins, impacting gene regulation and the formation of phase-separated ribonucleoprotein assemblies.
Cerase A., Armaos A., Neumayer C., ... Guttman M, Tartaglia G.G.* Phase separation drives X-chromosome inactivation: a hypothesis, Nature Structural & Molecular Biology (2019), https://doi.org/10.1038/s41594-019-0223-0. This article proposes a hypothesis that the long non-coding RNA Xist induces X-chromosome inactivation through phase separation, supported by evidence showing similarities between Xist assemblies and other phase-separated condensates, suggesting a critical role of RNA-protein interactions in this process.
Luige J., Armaos A., Tartaglia G.G.*, Ørom U.A.V*. Predicting nuclear G-quadruplex RNA-binding proteins with roles in transcription and phase separation, Nature Communications (2024), https://doi.org/10.1038/s41467-024-46731-9. This study identifies and predicts proteins that bind to G-quadruplex RNA in the nucleus, exploring their roles in transcription and phase separation, providing insights into RNA-protein interactions and their implications in gene regulation and cellular processes.
RNA design / phase transitions / aggregation
Zacco E., Kantelberg O., Milanetti E., ... Pastore A., Tartaglia G.G. Probing TDP-43 condensation using an in silico designed aptamer, Nature Communications (2022), https://doi.org/10.1038/s41467-022-30944-x. This article demonstrates the use of an in silico designed aptamer to probe the condensation of TDP-43, providing insights into its aggregation process and potential therapeutic applications.
Rupert J., Monti M., Zacco E., ... Tartaglia G.G.* RNA sequestration driven by amyloid formation: the alpha synuclein case, Nucleic Acids Research (2023), https://doi.org/10.1093/nar/gkad857. This study explores how amyloid formation, particularly by alpha-synuclein, leads to RNA sequestration, providing insights into the interaction between amyloids and nucleic acids and their implications in neurodegenerative diseases.
Luige J., Conrad T., Armaos A., Louloupi A., Vincent A., Meierhofer D., Gajhede M., Tartaglia G.G. (corresponding author), Ørom U.A.V. Design and characterization of G-quadruplex RNA aptamers reveal RNA-binding by KDM5 lysine demethylases, Computational and Structural Biotechnology Journal (2025), https://doi.org/10.1016/j.csbj.2025.06.027 This work characterizes RNA aptamers that adopt G-quadruplex structures and uses them to reveal previously unrecognized RNA-binding activity in the KDM5 family of histone lysine demethylases. Through computational predictions and experimental validation, the authors show that KDM5A and KDM5B preferentially interact with G-quadruplex RNAs, mediated by their ARID and adjacent protein domains, and that RNA binding contributes to the formation of KDM5-containing complexes, expanding the understanding of how RNA structural motifs can influence chromatin regulation and epigenetic function.
