Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Thomas Markus Leissing"'
Autor:
Clara Lemos, Luise Schulze, Joerg Weiske, Hanna Meyer, Nico Braeuer, Naomi Barak, Uwe Eberspächer, Nicolas Werbeck, Carlo Stresemann, Martin Lange, Ralf Lesche, Nina Zablowsky, Katrin Juenemann, Atanas Kamburov, Laura Martina Luh, Thomas Markus Leissing, Jeremie Mortier, Michael Steckel, Holger Steuber, Knut Eis, Ashley Eheim, Patrick Steigemann
Publikováno v:
iScience, Vol 23, Iss 9, Pp 101517- (2020)
Summary: Structural mutants of p53 induce global p53 protein destabilization and misfolding, followed by p53 protein aggregation. First evidence indicates that p53 can be part of protein condensates and that p53 aggregation potentially transitions th
Externí odkaz:
https://doaj.org/article/a212af021eff409c84704cd1ec1f0308
Publikováno v:
Drug discovery today. Technologies. 37
Small molecule induced protein degradation has created tremendous excitement in drug discovery within recent years. Not being confined to target inhibition and being able to remove disease-causing protein targets via engagement and subsequent ubiquit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::25891ebfa4b2fa21b0bd52b0f9907890
https://pubmed.ncbi.nlm.nih.gov/34895657
https://pubmed.ncbi.nlm.nih.gov/34895657
Autor:
Naomi Barak, Atanas Kamburov, Nina Zablowsky, Laura M. Luh, Hanna Meyer, Uwe Eberspächer, Martin Lange, Jérémie Mortier, Clara Lemos, Nico Braeuer, Thomas Markus Leissing, Patrick Steigemann, Joerg Weiske, Ralf Lesche, Michael Steckel, Holger Steuber, Carlo Stresemann, Nicolas Werbeck, Ashley Eheim, Luise Schulze, Katrin Juenemann, Knut Eis
Publikováno v:
iScience, Vol 23, Iss 9, Pp 101517-(2020)
iScience
iScience
Summary Structural mutants of p53 induce global p53 protein destabilization and misfolding, followed by p53 protein aggregation. First evidence indicates that p53 can be part of protein condensates and that p53 aggregation potentially transitions thr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eccfc45a184f7faf9f0cb161ae90385f
https://pubmed.ncbi.nlm.nih.gov/32927263
https://pubmed.ncbi.nlm.nih.gov/32927263