During oxidative protein folding, efficient catalysis of disulfide rearrangements by protein-disulfide isomerase is found to involve an escape mechanism that prevents the enzyme from becoming trapped in covalent complexes with substrates that fail to rearrange in a timely fashion. Protein-disulfide isomerase mutants with only a single active-site cysteine catalyze slow disulfide rearrangements ...

Cell entry of Simian Virus 40 (SV40) involves caveolar/lipid raft-mediated endocytosis, vesicular transport to the endoplasmic reticulum (ER), translocation into the cytosol, and import into the nucleus. We analyzed the effects of ER-associated processes and factors on infection and on isolated viruses and found that SV40 makes use of the thiol-disulfide oxidoreductases, ERp57 and PDI, as well ...

A novel synthetic N-(9-fluorenyl methoxy carbonyl)-L-Cysteine (Fmoc-Cys(SH)-OH) receptor was prepared by co-polymerizing (9-fluorenyl methoxy carbonyl)-S-(1-propene-2-thiol)-L-Cysteine (FmocCys(SCH2CHCH2)-OH) and a non-imprinted polymer prepared from 1-propene-1-thiol photo-chemically 15 h at room temperature and additional 3 h thermally at 80 ̊C. Subsequently, disulfides were reduced with lithi...

Introduction of disulfide bonds into proteins entering the secretory pathway is catalyzed by Ero1p, which generates disulfide bonds de novo, and Pdi1p, which transfers disulfides to substrate proteins. A sufficiently oxidizing environment must be maintained in the endoplasmic reticulum (ER) to allow for disulfide formation, but a pool of reduced thiols is needed for isomerization of incorrectly...