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Cell Death and Differentiation|March 22, 2022
Structural diversity of p63 and p73 isoformsChristian Osterburg, Volker DötschCancers|February 12, 2021
Isoform-Specific Roles of Mutant p63 in Human DiseasesChristian Osterburg, Susanne Osterburg, Huiqing Zhou, et al.Cell Death Discovery|December 18, 2024
Cardiocutaneous syndrome is caused by aggregation of iASPP mutantsRebecca Lotz, Christian Osterburg, Birgit Schäfer, et al.Cell Death and Differentiation|July 23, 2016
Intrinsic aggregation propensity of the p63 and p73 TI domains correlates with p53R175H interaction and suggests further significance of aggregation events in the p53 familySebastian Kehrloesser, Christian Osterburg, Marcel Tuppi, et al.Cell Death & Disease|September 19, 2019
TA*p63 and GTAp63 achieve tighter transcriptional regulation in quality control by converting an inhibitory element into an additional transactivation domainSusanne Pitzius, Christian Osterburg, Jakob Gebel, et al.Journal of Cell Science|August 11, 2017
Control mechanisms in germ cells mediated by p53 family proteinsJakob Gebel, Marcel Tuppi, Katharina Krauskopf, et al.The Journal of General Virology|September 26, 2023
ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infectionArtem Smirnov, Andrea Magri, Rebecca Lotz, et al.Cell Death and Differentiation|June 18, 2022
Designed Ankyrin Repeat Proteins as a tool box for analyzing p63Alexander Strubel, Philipp Münick, Apirat Chaikuad, et al.Cell Death & Disease|April 18, 2023
Disease-related p63 DBD mutations impair DNA binding by distinct mechanisms and varying degreeChristian Osterburg, Marco Ferniani, Dario Antonini, et al.Elife|September 10, 2025
p53 isoforms have a high aggregation propensity, interact with chaperones and lack binding to p53 interaction partnersAnamari Brdar, Christian Osterburg, Philipp Münick, et al.Pageof 2