Disruption of disulfide bond formation sensitizes resistant Gram-negative bacteria expressing β-lactamases and mobile colistin resistance enzymes to currently available antibiotics.

The major protein disulfide isomerase family member, PDIA1, is essential in beta cells of mice fed a high-fat diet to maintain glucose homeostasis, proinsulin maturation and organelle integrity.

The import of proteins into the intermembrane space of mitochondria is driven by binding to the trans-site receptor Mia40 and not by the oxidation of cysteine residues.

Compressive force spectroscopy of single molecules reveals that intra-protein forces underlie the long-distance coordination of structural changes within a cytotoxin during pore formation.

Ligand binding, force and chemistry combine to control the function of a cell surface receptor.

The C-terminus of A_2A receptor drives oligomer formation via an intricate network of disulfide bonds, hydrogen bonds, electrostatic interactions, and hydrophobic interactions, all of which are enhanced by depletion interactions.

The mechanism identified here that mediates olanzapine-induced b-cell dysfunction should be considered, along with weight gain, in mitigating adverse side effects when patients with schizophrenia are prescribed olanzapine.

The mechanism triggering HBV membrane fusion involves ERp57, a cellular protein disulfide isomerase, and ultimately leads to the exposition of a fusion peptide that was identified in the pre-S1 determinant.

Signal-peptide cleavage of HIV-1 envelope glycoprotein is delayed because of alpha-helical structure covering the cleavage site, effecting early cleavage alters the folding pathway and resulting in localized misfolding and reduced viral fitness.

Disulfide-bridged fibroblast growth factor 2 (FGF2) dimerization at the inner plasma membrane leaflet produces the building block for higher FGF2 oligomers that drive FGF2 membrane translocation into the extracellular space.