Crystal Structure and Functional Analysis of the Protein Disulfide Isomerase-Related Protein ERp29
Naomi Barak(Max Planck Research Unit for Enzymology of Protein Folding), David M. Ferrari(Universitätsmedizin Göttingen), Piotr Neumann(Martin Luther University Halle-Wittenberg), Gunter Fischer(Leibniz Institute for High Performance Microelectronics), Heike Reichardt(Max Planck Research Unit for Enzymology of Protein Folding), Miroslav Malešević(Martin Luther University Halle-Wittenberg), Milton T. Stubbs(University Hospital in Halle), Kai Naumann(Leibniz Institute of Plant Biochemistry), Mike Schutkowski(Martin Luther University Halle-Wittenberg), Madhumati Sevvana(University of Göttingen)
Cited by 67
Related Papers
The protein disulphide-isomerase family: unravelling a string of folds
|Biochemical Journal|1999|500
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