Peptide Binding by Catalytic Domains of the Protein Disulfide Isomerase-Related Protein ERp46
Andreas Funkner(Max Planck Research Unit for Enzymology of Protein Folding), David M. Ferrari(Universitätsmedizin Göttingen), Hauke Lilie(Martin Luther University Halle-Wittenberg), Johnny Zerweck(JPT Peptide Technologies (Germany)), Natalya Gyrych(Max Planck Research Unit for Enzymology of Protein Folding), Gunter Fischer(Leibniz Institute for High Performance Microelectronics), Mike Schutkowski(Martin Luther University Halle-Wittenberg), Milton T. Stubbs(University Hospital in Halle), C. Parthier(Martin Luther University Halle-Wittenberg)
Cited by 25
Related Papers
The protein disulphide-isomerase family: unravelling a string of folds
|Biochemical Journal|1999|500
The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease
|EMBO Molecular Medicine|2009|230
The protein disulphide-isomerase family: unravelling a string of folds
|Biochemical Journal|1999|140
ERp28, a human endoplasmic‐reticulum‐lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin‐box motif
|European Journal of Biochemistry|1998|85
Reduction of protein disulfide bonds in an oxidizing environment
|FEBS Letters|1997|80