Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Jelmer Eerland"'
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
Abstract The nucleosome surface contains an area with negative electrostatic potential known as the acidic patch, which functions as a binding platform for various proteins to regulate chromatin biology. The dense clustering of acidic residues may im
Externí odkaz:
https://doaj.org/article/544c1de6121f412da6043bec52db0a82
Autor:
Velten Horn, Michael Uckelmann, Heyi Zhang, Jelmer Eerland, Ivette Aarsman, Ulric B. le Paige, Chen Davidovich, Titia K. Sixma, Hugo van Ingen
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Ubiquitination of histone H2A can occur on distinct lysine residues, but how each site is recognised by the specific E3 ligase remains poorly understood. Here the authors demonstrate that the E3 ligase RNF168 binds the acidic patch on the nucleosome
Externí odkaz:
https://doaj.org/article/3e125f2b63794fa29d89db5f5520deba
Autor:
Ivette Aarsman, Velten Horn, Chen Davidovich, Titia K. Sixma, Heyi Zhang, Hugo van Ingen, Michael Uckelmann, Jelmer Eerland, Ulric B. le Paige
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Nature Communications, 10(1). Nature Publishing Group
Nature Communications
Nature Communications, 10(1). Nature Publishing Group
Nature Communications
Ubiquitination of chromatin by modification of histone H2A is a critical step in both regulation of DNA repair and regulation of cell fate. These very different outcomes depend on the selective modification of distinct lysine residues in H2A, each by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bcbdcaa97ab2dce3401f8bd749a50bd
https://hdl.handle.net/1874/387663
https://hdl.handle.net/1874/387663