"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 )."
"The differential aggregation properties of p53 isoforms in EC cells may open up new avenues in the development of therapeutic strategies that preferentially target specific p53 isoforms to prevent p53 amyloid aggregate formation."
"Recent studies have suggested that amyloid formation of tumor suppressor p53 can lead to loss of its physiological function, resulting in accelerated cancer progression."
"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."
"Using amyloid seed of p53 fragment (P8, p53(250-257)), we show that p53 amyloid formation in cells not only leads to its functional inactivation but also transforms it into an oncoprotein."
"We discuss previous as well as recent findings regarding the amyloid formation of p53 in vitro and in vivo."
"There is evidence that the three functional domains of p53 could form amyloid-like aggregates [ xref , xref – xref ], which leads us to speculate that p53 amyloid formation might participate in the malignant process [ xref , xref ]."
"Ghosh and his colleagues, recently showed that p53 amyloid formation leads to its functional inactivation but also transforms p53 in to an oncoprotein  ."
"Recent studies have suggested that amyloid formation of p53 could lead to its loss of physiological function as a tumor suppressor."
"In the current study, we provide several evidences for the presence of p53 amyloid formation (in human and animal cancer tissues); along with its isolation from human cancer tissues and the biophysical characterization of these tissue-derived fibrils."
"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 ] ."
"The present study suggests that p53 amyloid formation could be one of the possible cause of p53 loss of function and therefore, inhibiting p53 amyloidogenesis could restore p53 tumor suppressor functions."
"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 c[MISSING/INVALID API KEY: limited to 200 char for Elsevier]"
"In vivo, p53 forms predominantly amorphous aggregates [ xref , xref ], but under certain conditions, p53 can also form amyloid fibrils [ xref ]."
"Our study reveals p53 amyloid formation and demonstrates its dual role in the pathogenesis of cancer by producing a loss of protein function and a gain of toxic function, extensively described in several amyloidogenic diseases."
"It has been shown that the tetramerization domain of the p53 protein is capable of forming amyloid fibrils."
"The mutant p53 amyloid form can confer a dominant phenotype on the remaining wild-type p53 form of protein and sequester native p53 in an inactive conformation [ xref ]."