The endoplasmic reticulum (ER) is the major folding compartment for secreted and
membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for …

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 …

Protein disulfide isomerases (PDIs) are enzymes that mediate oxidative protein folding in the
endoplasmic reticulum. Understanding of PDIs has historically been hampered by lack of …

Protein disulfide–isomerase (PDI) was the first protein-folding catalyst to be characterized,
half a century ago. It plays critical roles in a variety of physiological events by displaying …

The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the
study of oxidative protein folding. Oxidative protein folding refers to the composite process …

Although tyrosine phosphorylation of extracellular proteins has been reported to occur
extensively in vivo, no secreted protein tyrosine kinase has been identified. As a result …

Double electron–electron resonance (DEER) distance measurements of a protein complex
tagged with two Gd3+ chelates developed for rigid positioning of the metal ion are shown to …

Site-specific attachment of paramagnetic lanthanide ions to a protein generates
pseudocontact shifts (PCS) in the nuclear magnetic resonance (NMR) spectra of the protein …

This is a methodological guide to the use of deep neural networks in the processing of
pulsed dipolar spectroscopy (PDS) data encountered in structural biology, organic …

Lanthanoids are gaining popularity as paramagnetic centers for high resolution nuclear
magnetic resonance (NMR) spectroscopy. They provide valuable angular and long-distance …