The dance of disulfide formation

This publication has 13 references indexed in Scilit:

• Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell
  Cell, 2004
• Oxidative protein folding in eukaryotes
  The Journal of cell biology, 2004
• Inter-Domain Redox Communication in Flavoenzymes of the Quiescin/Sulfhydryl Oxidase Family: Role of a Thioredoxin Domain in Disulfide Bond Formation^,
  Biochemistry, 2003
• Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes
  Archives of Biochemistry and Biophysics, 2002
• Oxidative protein folding in bacteria
  Molecular Microbiology, 2002
• A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p
  Nature Structural & Molecular Biology, 2001
• A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation
  Nature Cell Biology, 2001
• Biochemical Basis of Oxidative Protein Folding in the Endoplasmic Reticulum
  Science, 2000
• Two Pairs of Conserved Cysteines Are Required for the Oxidative Activity of Ero1p in Protein Disulfide Bond Formation in the Endoplasmic Reticulum
  Molecular Biology of the Cell, 2000
• Ero1p Oxidizes Protein Disulfide Isomerase in a Pathway for Disulfide Bond Formation in the Endoplasmic Reticulum
  Published by Elsevier ,1999