Výsledky vyhledávání - "Sofia Francia"

Akademický článek

Post-Translational Modifications Modulate Proteinopathies of TDP-43, FUS and hnRNP-A/B in Amyotrophic Lateral Sclerosis

Autor: Stefania Farina, Francesca Esposito, Martina Battistoni, Giuseppe Biamonti, Sofia Francia

Publikováno v: Frontiers in Molecular Biosciences, Vol 8 (2021)

It has been shown that protein low-sequence complexity domains (LCDs) induce liquid-liquid phase separation (LLPS), which is responsible for the formation of membrane-less organelles including P-granules, stress granules and Cajal bodies. Proteins ha

Externí odkaz: https://doaj.org/article/becdbda7470f4156a4e5169e2a6bbe54

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Akademický článek

A damaged genome’s transcriptional landscape through multilayered expression profiling around in situ-mapped DNA double-strand breaks

Autor: Fabio Iannelli, Alessandro Galbiati, Ilaria Capozzo, Quan Nguyen, Brian Magnuson, Flavia Michelini, Giuseppina D’Alessandro, Matteo Cabrini, Marco Roncador, Sofia Francia, Nicola Crosetto, Mats Ljungman, Piero Carninci, Fabrizio d’Adda di Fagagna

Publikováno v: Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)

DNA double strand breaks (DSBs) are among the most deleterious types of damage and there is strong evidence indicating a relationship between breaks and transcription. Here the authors provide a high-resolution, genome-wide map of induced DSBs and ob

Externí odkaz: https://doaj.org/article/a4cc05be64fb4756ab65972047e8495b

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TGS1 impacts snRNA 3′-end processing, ameliorates survival motor neuron-dependent neurological phenotypes in vivo and prevents neurodegeneration

Publikováno v: Nucleic Acids Research. 50:12400-12424

Trimethylguanosine synthase 1 (TGS1) is a highly conserved enzyme that converts the 5′-monomethylguanosine cap of small nuclear RNAs (snRNAs) to a trimethylguanosine cap. Here, we show that loss of TGS1 in Caenorhabditis elegans, Drosophila melanog

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a2f84921eec82dd4a2497d79c655c61
https://doi.org/10.1093/nar/gkac659

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DROSHA and DICER RNA products control BMI1-dependent transcriptional repression at DNA damage sites

Autor: Sofia Francia, Ilaria Capozzo, Stefania Modafferi, Fabio Iannelli, Ubaldo Gioia, Fabrizio d'Adda di Fagagna

Genome integrity is safeguarded by the DNA damage response (DDR). Transcriptional modulation of genes around DNA double-strand breaks (DSBs) is important for DNA repair. It has been shown that DSBs repress transcription of DSB-bearing genes in an ATM

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2f38d6743eb8b7310007c43b249afef2
https://doi.org/10.21203/rs.3.rs-1214613/v1

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RNase A treatment and reconstitution with DNA damage response RNA in living cells as a tool to study the role of non-coding RNA in the formation of DNA damage response foci

Autor: Flavia Michelini, Francesca Rossiello, Sofia Francia, Fabrizio d'Adda di Fagagna

Publikováno v: Nature Protocols. 14:1489-1508

Non-coding RNA (ncRNA) molecules have been shown to play a variety of cellular roles; however, the contributions of different types of RNA to specific phenomena are often hard to dissect. To study the role of RNA in the assembly of DNA damage respons

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0af19aeb0c59a6c290f8195658c0935
https://doi.org/10.1038/s41596-019-0147-5

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Pharmacological boost of DNA damage response and repair by enhanced biogenesis of DNA damage response RNAs

Autor: Matteo Cabrini, Fabrizio d'Adda di Fagagna, Sofia Francia, Ubaldo Gioia, Silvia Brambillasca, Corey Winston Jones-Weinert, Flavia Michelini

Publikováno v: Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)

A novel class of small non-coding RNAs called DNA damage response RNAs (DDRNAs) generated at DNA double-strand breaks (DSBs) in a DROSHA- and DICER-dependent manner has been shown to regulate the DNA damage response (DDR). Similar molecules were also

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::942f58e4fd8b2ce2c65e8b2ab87512c5
http://link.springer.com/article/10.1038/s41598-019-42892-6

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DROSHA is recruited to DNA damage sites by the MRN complex to promote non-homologous end joining

Autor: Fabrizio d'Adda di Fagagna, Sofia Francia, Antonio Maffia, Lina Cipolla, Simone Sabbioneda, Matteo Cabrini, Fabio Iannelli, Alessandro Galbiati, Marco Roncador

Publikováno v: Journal of Cell Science
article-version (VoR) Version of Record

The DNA damage response (DDR) is the signaling cascade that recognizes DNA double-strand breaks (DSBs) and promotes their resolution via the DNA repair pathways of non-homologous end joining (NHEJ) or homologous recombination (HR). We and others have

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b44717b661cc59422e28ed1b26f09a5
https://www.zora.uzh.ch/id/eprint/207429/

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A Role for Human DNA Polymerase λ in Alternative Lengthening of Telomeres

Publikováno v: International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2021, 22 (5), pp.2365. ⟨10.3390/ijms22052365⟩
International Journal of Molecular Sciences, Vol 22, Iss 2365, p 2365 (2021)
Volume 22
Issue 5

International audience; Telomerase negative cancer cell types use the Alternative Lengthening of Telomeres (ALT) pathway to elongate telomeres ends. Here, we show that silencing human DNA polymerase (Pol λ) in ALT cells represses ALT activity and in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04c5142fb9ab19ec3f96dfa6f03a9527
https://hal.archives-ouvertes.fr/hal-03407923

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DNA Damage Triggers a New Phase in Neurodegeneration

Autor: Ubaldo Gioia, Stefania Farina, Marta Ceccon, Ornella Brandi, Fabrizio d'Adda di Fagagna, Sofia Francia, Fabio Pessina

Publikováno v: Trends in Genetics

Subcellular compartmentalization contributes to the organization of a plethora of molecular events occurring within cells. This can be achieved in membraneless organelles generated through liquid-liquid phase separation (LLPS), a demixing process tha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0284a904510a847121202256d03cc9c4

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TGS1 controls snRNA 3' end processing, prevents neurodegeneration and amelioratesSMN-dependent neurological phenotypes in vivo

Publikováno v: bioRxiv the preprint server for biology (2020). doi:10.1101/2020.10.27.356782
info:cnr-pdr/source/autori:Lu Chen123*, Caitlin M. Roake123*, Paolo Maccallini4, Francesca Bavasso4, Roozbeh Dehghannasiri3, Pamela Santonicola5, Natalia Mendoza-Ferreira6, Livia Scatolini4, Ludovico Rizzuti4, Alessandro Esposito7, Ivan Gallotta7, Sofia Francia89, Stefano Cacchione4, Matthias Hammerschmidt10, Cristiano De Pittà11, Gabriele Sales11, Julia Salzman13, Livio Pellizzoni121314, Brunhilde Wirth615, Elia Di Schiavi57, Maurizio Gatti416, Steven E. Artandi123# and Grazia D. Raffa417#/titolo:TGS1 controls snRNA 3' end processing, prevents neurodegeneration and amelioratesSMN-dependent neurological phenotypes in vivo/doi:10.1101%2F2020.10.27.356782/rivista:bioRxiv the preprint server for biology/anno:2020/pagina_da:/pagina_a:/intervallo_pagine:/volume

Trimethylguanosine synthase 1 (TGS1) is a highly conserved enzyme that converts the 5’ mono-methylguanosine cap of snRNAs to a trimethylguanosine cap. Here, we show that loss of TGS1 in C. elegans, D. melanogaster and D. rerio results in neurologic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f54fc9aa1ec0818fd097fcf7d36a9bf

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