The endoplasmic reticulum (ER) represents the entry point into the secretory pathway where
nascent proteins encounter a specialized environment for their folding and maturation …

The site of protein folding and maturation for the majority of proteins that are secreted,
localized to the plasma membrane or targeted to endomembrane compartments is the …

The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for
protein folding, degradation, chaperone function, and the ER stress response. Our …

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 …

Time-resolved direct observations of proteins in action provide essential mechanistic
insights into biological processes. Here, we present mechanisms of action of protein …

The 70-kD heat shock protein (Hsp70) chaperone system is a central hub of the proteostasis
network that helps maintain protein homeostasis in all organisms. The recruitment of Hsp70 …

Extensive mannose trimming of nascent glycoprotein N-glycans signals their targeting to
endoplasmic reticulum-associated degradation (ERAD). ER mannosidase I (ERManI) and …

The endoplasmic reticulum (ER) maintains an oxidative redox environment that is
advantageous for the oxidative folding of nascent polypeptides entering the ER. Reductive …

Oxidative protein folding occurs primarily in the mammalian endoplasmic reticulum, enabled
by a diverse network comprising more than 20 members of the protein disulfide isomerase …

Time-resolved single-molecule observations by high-speed atomic force microscopy (HS-
AFM), have greatly advanced our understanding of how proteins operate to fulfill their …