TP53 and cancer: Indeed, despite the cellular mechanisms of protein folding control, through dominant negative (DN) mutation in TP53 gene under abnormal conditions, mutant misfolded p53 proteins can be produced and aggregate with each other and with wild-type (wt) p53 that ultimately can lead to ER stress and form pathological prion-like aggregations (e.g., amyloid fibrils) with gain of function (GOF) phenotype and without tumor-suppressor activity that can act as cancer stimulators [11,[13], [14], [15], [16], [17]].