Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Matías, Capella"'
Autor:
Matías Capella, Imke K. Mandemaker, Lucía Martín Caballero, Fabian den Brave, Boris Pfander, Andreas G. Ladurner, Stefan Jentsch, Sigurd Braun
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
rDNA repeats residing in the nucleolus must be released to the nucleoplasm to allow repair by homologous recombination. Here the authors reveal insights into the molecular mechanism proposing that phosphorylation and SUMOylation of the rDNA-tethering
Externí odkaz:
https://doaj.org/article/7c25cbe4fae14af59e6291014ce9f3bc
Publikováno v:
Microbial Cell, Vol 7, Iss 3, Pp 80-92 (2020)
Maintaining the identity of chromatin states requires mechanisms that ensure their structural integrity through the concerted actions of histone modifiers, readers, and erasers. Histone H3K9me and H3K27me are hallmarks of repressed heterochromatin, w
Externí odkaz:
https://doaj.org/article/a1043ddff8704ecbb1f2e12639c1eaed
Autor:
Anna Schmücker, Bingkun Lei, Zdravko J Lorković, Matías Capella, Sigurd Braun, Pierre Bourguet, Olivier Mathieu, Karl Mechtler, Frédéric Berger
Publikováno v:
PLoS Genetics, Vol 17, Iss 6, p e1009601 (2021)
Selection of C-terminal motifs participated in evolution of distinct histone H2A variants. Hybrid types of variants combining motifs from distinct H2A classes are extremely rare. This suggests that the proximity between the motif cases interferes wit
Externí odkaz:
https://doaj.org/article/4bb13fccf7bd4709836d091ade8013c8
Autor:
Sabine Fischer-Burkart, Yoshiyuki Hirano, Yasuha Kinugasa, Matías Capella, Nikolay Dobrev, Tamás Fischer, Ramón R. Barrales, Irmgard Sinning, Sigurd Braun, van Emden T, Lucía Martín Caballero, Yasushi Hiraoka
Publikováno v:
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, 2022, 29 (9), pp.910-921. ⟨10.1038/s41594-022-00831-6⟩
Nature Structural and Molecular Biology, 2022, 29 (9), pp.910-921. ⟨10.1038/s41594-022-00831-6⟩
Transcriptionally silent chromatin often localizes to the nuclear periphery. However, whether the nuclear envelope (NE) is a site for post-transcriptional gene repression is not well understood. Here we demonstrate that Schizosaccharomyces pombe Lem2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::478dd6336fc4a860c14649591543fb92
http://hdl.handle.net/10261/288565
http://hdl.handle.net/10261/288565
Autor:
Matías Capella, Sigurd Braun
Publikováno v:
Developmental Cell. 53:3-5
ESCRT proteins fulfill an important function in membrane remodeling and scission. In this issue of Developmental Cell, Pieper et al. reveal that the ESCRT machinery releases the inner nuclear membrane protein Lem2 from heterochromatin, thus ensuring
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e1073599f0262bab793578970546ee67
https://doi.org/10.1016/j.devcel.2020.03.013
https://doi.org/10.1016/j.devcel.2020.03.013
Autor:
Sigurd Braun, Boris Pfander, Imke K Mandemaker, Andreas G. Ladurner, Matías Capella, Fabian den Brave, Lucía Martín Caballero, Stefan Jentsch
Ribosomal RNA genes (rDNA) are highly unstable and susceptible to rearrangement due to active transcription and their repetitive nature. Compartmentalization of rDNA in the nucleolus suppresses uncontrolled recombination. However, broken repeats must
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b5e90d286ff7a1b3fb64aeac991bdd5
https://doi.org/10.1101/2021.01.05.425376
https://doi.org/10.1101/2021.01.05.425376
Misassembled nuclear pore complexes (NPCs) are removed by sealing off the surrounding nuclear envelope (NE), which is mediated by members of the ESCRT (endosomal sorting complexes required for transport) machinery. Recruitment of ESCRT proteins to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1f82aeb39f303260e08b787777044e7
https://doi.org/10.1101/2020.06.25.171694
https://doi.org/10.1101/2020.06.25.171694
Publikováno v:
Journal of cell science. 133(24)
Misassembled nuclear pore complexes (NPCs) are removed by sealing off the surrounding nuclear envelope (NE), which is conducted by the endosomal sorting complexes required for transport (ESCRT) machinery. Recruitment of ESCRT proteins to the NE is me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::91c16b1969d1eb3bfeb6711b21c9aa73
https://pubmed.ncbi.nlm.nih.gov/33262311
https://pubmed.ncbi.nlm.nih.gov/33262311
Publikováno v:
Microbial Cell
Microbial Cell, Vol 7, Iss 3, Pp 80-92 (2020)
Microbial Cell, Vol 7, Iss 3, Pp 80-92 (2020)
Maintaining the identity of chromatin states requires mechanisms that ensure their structural integrity through the concerted actions of histone modifiers, readers, and erasers. Histone H3K9me and H3K27me are hallmarks of repressed heterochromatin, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbc7598ee651802a0007d67fcef4ae30
Autor:
Frédéric Berger, Sean A. Montgomery, A. Osakabe, Sigurd Braun, Bingkun Lei, Matías Capella, Malgorzata Goiser, Michael Borg, Abubakar Muhammad
Publikováno v:
Current Biology. 31:182-191.e5
Diversification of histone variants is marked by the acquisition of distinct motifs and functional properties through convergent evolution.1-4 H2A variants are distinguished by specific C-terminal motifs and tend to be segregated within defined domai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88d64aec9700b223ec1026760f6def98
https://doi.org/10.1016/j.cub.2020.09.080
https://doi.org/10.1016/j.cub.2020.09.080