Intrinsic aggregation propensity of the p63 and p73 TI domains correlates with p53R175H interaction and suggests further significance of aggregation events in the p53 family
Sebastian Kehrloesser(Goethe University Frankfurt), Volker Dötsch(Goethe University Frankfurt)
Cited by 58
Related Papers
Conformational Switches Modulate Protein Interactions in Peptide Antibiotic Synthetases
|Science|2006|154
Structural basis for the selectivity of the external thioesterase of the surfactin synthetase
|Nature|2008|131
Ubiquitination in the ERAD Process
|International Journal of Molecular Sciences|2020|81
Disease-related p63 DBD mutations impair DNA binding by distinct mechanisms and varying degree
|Cell Death and Disease|2023|15
Cotranslational assembly of membrane protein/nanoparticles in cell-free systems
|Biochimica et Biophysica Acta (BBA) - Biomembranes|2022|11