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 …

Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure
their performance of normal biological functions. Moreover, biological molecular assembly …

Proper folding is essential for the biological functions of all proteins. The folding process is
intrinsically error-prone, and the misfolding of a polypeptide chain can cause the formation …

Autocatalytic and oscillatory networks of organic reactions are important for designing life-
inspired materials and for better understanding the emergence of life on Earth; however, the …

Thioredoxin domain-containing protein 5 (TXNDC5) is a member of the protein disulfide
isomerase (PDI) family. It can promote the formation and rearrangement of disulfide bonds …

Complicated and sophisticated protein homeostasis (proteostasis) networks in the
endoplasmic reticulum (ER), comprising disulfide catalysts, molecular chaperones, and their …

Proteins form native structures through folding processes, many of which proceed through
intramolecular hydrophobic effect, hydrogen bond and disulfide-bond formation. In vivo …

We report the first example of a synthetic thiol-based compound that promotes oxidative
protein folding upon 1-equivalent loading to the disulfide bonds in the client protein to afford …

Folding is a key process to form functional conformations of proteins. Folding via on-pathway
intermediates leads to the formation of native structures, while folding through off-pathways …

Biological macromolecules must fold into native structures to gain functional activities. In
living cells, proteins called molecular chaperones mediate productive folding by preventing …