معرفی
Dr Philip Robinson is a Research Fellow in the Institute of Molecular, Cell and Systems Biology at the University of Glasgow. His work focuses on protein folding mechanisms, particularly in the endoplasmic reticulum (ER), with an emphasis on disulfide bond formation, redox regulation, and structural determinants of folding kinetics.
- Current Affiliation: University of Glasgow, Institute of Molecular, Cell and Systems Biology
His research explores the interplay between oxidative folding in the ER and cytosolic redox pathways, including thioredoxin reductase systems. He investigates how secondary structure influences the timing of disulfide bond formation and the roles of ER-resident enzymes like ERp57 and ERdj5 in protein quality control.
Recent publications highlight his contributions to understanding disulfide isomerase activity (2023), the temporal hierarchy of folding and bond formation (2020-2017), and the post-translational insertion of membrane proteins (2013, 2012). Collaborative work with Neil Bulleid and others underscores his focus on ER stress and redox biology.
Key collaborators include Marie Pringle, Xiaofei Cao, and Neil Bulleid. His work has implications for neurodegenerative diseases and protein misfolding disorders.
