Identification of Internal Ribosomal Entry Site inside Open Reading Frame of 14-3-3β Gene

Prion diseases are characterized by neurodegeneration and protein aggregation,which are caused by the accumulation of a misfolded and protease-resistant form of the cellular prion protein.Several studies suggest that the accumulation of a misfolded alternate cellular protein disturbs quality control mechanisms,leading to endoplasmic reticulum(ER)stress involved in prion diseases[1-3].Prion infection activates the splicing of the unfolded protein response transcription factor XBP-1.Misfolded mutant PrP associated with inherited.