Deyasini Chakraborty
@deyasinic.bsky.social
Postdoc at the Novartis BR, Switzerland
PhD, Thomä lab at the Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Interested in chromatin biology.
PhD, Thomä lab at the Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Interested in chromatin biology.
Big shoutout to the FMI Structural Biology platform - Simone Cavadini, Lukas Kater and Georg Kempf, and the amazing scientific environment provided by the FMI Basel @fmiscience.bsky.social
August 4, 2025 at 4:44 PM
Big shoutout to the FMI Structural Biology platform - Simone Cavadini, Lukas Kater and Georg Kempf, and the amazing scientific environment provided by the FMI Basel @fmiscience.bsky.social
Special thanks to co-author Colby @csandate.bsky.social for joining the p53 team and to all the contributing authors and the members of the Thomä lab @labthoma.bsky.social. Grateful to Nico for supporting this project and the fruitful collaboration with the Schübeler lab @schubelerlab.bsky.social
August 4, 2025 at 4:42 PM
Special thanks to co-author Colby @csandate.bsky.social for joining the p53 team and to all the contributing authors and the members of the Thomä lab @labthoma.bsky.social. Grateful to Nico for supporting this project and the fruitful collaboration with the Schübeler lab @schubelerlab.bsky.social
2. We reported the first cryo-EM structure of cofactor-TF (USP7-p53) complex on nucleosome.
3. Additionally, we resolved high-resolution cryo-EM structures of E6AP-E6-p53 ternary complex showing multiple oligomeric states.
4. We further showed that USP7 remains functional in a chromatinised context.
3. Additionally, we resolved high-resolution cryo-EM structures of E6AP-E6-p53 ternary complex showing multiple oligomeric states.
4. We further showed that USP7 remains functional in a chromatinised context.
August 4, 2025 at 4:36 PM
2. We reported the first cryo-EM structure of cofactor-TF (USP7-p53) complex on nucleosome.
3. Additionally, we resolved high-resolution cryo-EM structures of E6AP-E6-p53 ternary complex showing multiple oligomeric states.
4. We further showed that USP7 remains functional in a chromatinised context.
3. Additionally, we resolved high-resolution cryo-EM structures of E6AP-E6-p53 ternary complex showing multiple oligomeric states.
4. We further showed that USP7 remains functional in a chromatinised context.
In this study, we discovered that nucleosomes play a decisive role in determining the interacting partners of p53.
1. DUB USP7 forms a nucleosome-bound complex with p53 while human papilloma virus protein, E6 in complex with E3-ubiquitin ligase E6AP cannot do so.
1. DUB USP7 forms a nucleosome-bound complex with p53 while human papilloma virus protein, E6 in complex with E3-ubiquitin ligase E6AP cannot do so.
August 4, 2025 at 4:33 PM
In this study, we discovered that nucleosomes play a decisive role in determining the interacting partners of p53.
1. DUB USP7 forms a nucleosome-bound complex with p53 while human papilloma virus protein, E6 in complex with E3-ubiquitin ligase E6AP cannot do so.
1. DUB USP7 forms a nucleosome-bound complex with p53 while human papilloma virus protein, E6 in complex with E3-ubiquitin ligase E6AP cannot do so.