IndraLab
Statements
sparser
"It is thought that p53 residues 252–258 within the p53DBD are highly aggregation prone and a recent study has shown that targeting this region with the small residue 252–258-derived peptide ReACp53 can prevent aggregation and amyloid formation of p53 in vivo [ xref ], [ xref ] ."
sparser
"The time-course of ThT fluorescence observed for the atheronal-A ( KA ) and atheronal-B ( ALD )-initiated His 6 -p53 amyloid formation, a rapid rise in ThT fluorescence to a plateau phase with no lag-phase, is indicative of a ‘seeded’ or so-called down-hill polymerization that is thermodynamically favoured from the outset ( xref ), and is in-line with what we have observed previously for the atheronal-initiated polymerization of amyloid-β and α-synuclein ( xref , xref )."
sparser
"Here we show that a cell-penetrating peptide, ReACp53, designed to inhibit p53 amyloid formation, rescues p53 function in cancer cell lines and in organoids derived from high-grade serous ovarian carcinomas (HGSOC), an aggressive cancer characterized by ubiquitous p53 mutations."