Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Alena Svobodová Kovaříková"'
Autor:
Alena Svobodová Kovaříková, Lenka Stixová, Aleš Kovařík, Denisa Komůrková, Soňa Legartová, Paolo Fagherazzi, Eva Bártová
Publikováno v:
Cells, Vol 13, Iss 21, p 1817 (2024)
The affiliation number 1, “Institute of Biophysics of the Czech Academy of Sciences, Královopolská 135, 612 65 Brno, Czech Republic” changed its zip code to 612 00 [...]
Externí odkaz:
https://doaj.org/article/5ce9949b0b104591a1d47c7928b94f8b
Publikováno v:
Epigenetics & Chromatin, Vol 16, Iss 1, Pp 1-17 (2023)
Abstract RNA modifications have been known for many years, but their function has not been fully elucidated yet. For instance, the regulatory role of acetylation on N4-cytidine (ac4C) in RNA can be explored not only in terms of RNA stability and mRNA
Externí odkaz:
https://doaj.org/article/dccaeeca540a4a2c888d0ed8fb9e00cf
Autor:
Soňa Legartová, Alena Svobodová Kovaříková, Jana Běhalová Suchánková, Hana Polášek-Sedláčková, Eva Bártová
Publikováno v:
RNA Biology, Vol 19, Iss 1, Pp 1153-1171 (2022)
RNA methylation, especially 6-methyladenosine (m6A)-modified RNAs, plays a specific role in DNA damage response (DDR). Here, we also observe that RNA modified at 8-methyladenosine (m8A) is recruited to UVA-damaged chromatin immediately after microirr
Externí odkaz:
https://doaj.org/article/57202bccd64143ef8845697dfaf2ada0
Publikováno v:
Life, Vol 11, Iss 7, p 669 (2021)
METTL16 methyltransferase is responsible for the methylation of N6-adenosine (m6A) in several RNAs. In mouse cells, we showed that the nuclear distribution of METTL16 is cell cycle-specific. In the G1/S phases, METTL16 accumulates to the nucleolus, w
Externí odkaz:
https://doaj.org/article/23039bf3561b4c57b5109e6b130020d4
Publikováno v:
Cells, Vol 9, Iss 4, p 999 (2020)
Cellular senescence, induced by genotoxic or replication stress, is accompanied by defects in nuclear morphology and nuclear membrane-heterochromatin disruption. In this work, we analyzed cytological and molecular changes in the linker of nucleoskele
Externí odkaz:
https://doaj.org/article/3948a1101b2b462a860c25817b0625ec
Autor:
Alena Svobodová Kovaříková, Lenka Stixová, Aleš Kovařík, Denisa Komůrková, Soňa Legartová, Paolo Fagherazzi, Eva Bártová
Publikováno v:
Cells, Vol 9, Iss 2, p 360 (2020)
The DNA damage response is mediated by both DNA repair proteins and epigenetic markers. Here, we observe that N6-methyladenosine (m6A), a mark of the epitranscriptome, was common in RNAs accumulated at UV-damaged chromatin; however, inhibitors of RNA
Externí odkaz:
https://doaj.org/article/0f0ff6109b3c4db9b21e76b0ad6363a6
RNA modifications have been known for many years, but their function has not been fully elucidated yet. For instance, the regulatory role of acetylation on N4-cytidine (ac4C) in RNA should be explored not only from the view of regulation of RNA stabi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4934aca38d41bf610d57898518170d01
https://doi.org/10.21203/rs.3.rs-2210212/v1
https://doi.org/10.21203/rs.3.rs-2210212/v1
Publikováno v:
Life
Volume 11
Issue 7
Life, Vol 11, Iss 669, p 669 (2021)
Volume 11
Issue 7
Life, Vol 11, Iss 669, p 669 (2021)
METTL16 methyltransferase is responsible for the methylation of N6-adenosine (m6A) in several RNAs. In mouse cells, we showed that the nuclear distribution of METTL16 is cell cycle-specific. In the G1/S phases, METTL16 accumulates to the nucleolus, w
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 4
International Journal of Molecular Sciences, Vol 22, Iss 1995, p 1995 (2021)
Volume 22
Issue 4
International Journal of Molecular Sciences, Vol 22, Iss 1995, p 1995 (2021)
G-quadruplexes (G4s) are four-stranded helical structures that regulate several nuclear processes, including gene expression and telomere maintenance. We observed that G4s are located in GC-rich (euchromatin) regions and outside the fibrillarin-posit
Publikováno v:
Aging (Albany NY)
Methylation of histones H4 at lysine 20 position (H4K20me), which is functional in DNA repair, represents a binding site for the 53BP1 protein. Here, we show a radiation-induced increase in the level of H4K20me3 while the levels of H4K20me1 and H4K20