Protein aggregation is arguably the most common and troubling manifestation of protein
instability, encountered in almost all stages of protein drug development. Protein …

Disulfide bond formation is probably involved in the biogenesis of approximately one third of
human proteins. A central player in this essential process is protein disulfide isomerase or …

We have studied the effects of polysaccharide and protein crowding agents on the refolding
of oxidized and reduced hen lysozyme in order to test the prediction that association …

The enzymes of the protein disulfide isomerase (PDI) family are thiol–disulfide
oxidoreductases of the endoplasmic reticulum (ER). They contain a CXXC active-site …

Recent breakthroughs in highly accurate protein structure prediction using deep neural
networks have made considerable progress in solving the structure prediction component of …

Background: Exposure of biomacromolecules to ionising radiation results in damage that is
initiated by free radicals and progresses through a variety of mechanisms. A widely used …

We have studied the effects of macromolecular crowding on protein folding kinetics by
studying the oxidative refolding of hen lysozyme in the absence and presence of high …

Aggregation of α-synuclein is thought to play a major role in the pathogenesis of Parkinson's
disease (PD), which is characterized by the presence of intracytoplasmic Lewy bodies (LB) …

In mammalian cells, nearly one-third of proteins are inserted into the endoplasmic reticulum
(ER), where they undergo oxidative folding and chaperoning assisted by approximately 20 …

Pichia pastoris has been recognized as an important platform for the production of various
heterologous proteins in recent years. The strong promoter AOX1, induced by methanol …