Do peters plus syndrome mutations disrupt a noncanonical ER quality-control mechanism?
While known ER quality-control machinery rely on identifying and tagging unfolded proteins, we find that POFUT2 and B3GLCT mediate a noncanonical ER quality-control mechanism that recognizes folded TSRs and stabilizes them by glycosylation. Our findings provide a molecular basis for the defects observed in PPS and potential targets that contribute to the pathology.
Improved fatigue life in tandem with the absence of porcelain fractures were observed in slow cooled crowns, regardless of framework design. Crowns fast cooled chiefly failed by porcelain cohesive fractures.