Native disulfide bond formation in proteins

Current Opinion in Chemical Biology

Volumn 4, Issue 5, 2000, Pages 533-539

  Woycechowsky, Kenneth J ^a   Raines, Ronald T ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE C; CYCLOHEXANE; DITHIOTHREITOL;

CATALYST; DISULFIDE BOND; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; REVIEW;

EID: 0033781303     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(00)00128-9     Document Type: Review

References (43)

1. Nature's transitory covalent bond
2. Oxidized redox state of glutathione in the endoplasmic reticulum
3. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
4. Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
5. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
6. Protein disulfide isomerase: Cellular enzymology of the CXXC motif
7. Thiol-disulfide exchange of divalent sulfur
8. Electron avenue: Pathways of disulfide bond formation and isomerization
9. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
10. Competition between glutathione and protein thiols for disulphide-bond formation
11. Sulfhydryl oxidase from egg white: A facile catalyst for disulfide formation in proteins and peptides
12. Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum
13. Oxidative protein folding is driven by the electron transport system
14. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
15. A small-molecule catalyst of protein folding in vitro and in vivo
16. Scanning and escape during protein-disulfide isomerase-assisted protein folding
17. The CXXC motif: A rheostat in the active site
18. Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae
19. Glycoproteins form mixed disulfides with oxidoreductases during folding in living cells
20. Specificity in substrate binding by protein folding catalysts: Tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp
21. Disulfide bonds and protein folding
22. Early intermediates in the PDI-assisted folding of ribonuclease A
23. Effect of protein disulfide isomerase on the regeneration of bovine ribonuclease A with dithiothreitol
24. The oxidative folding of hen lysozyme and its catalysis by protein disulfide isomerase
25. The protein disulphide-isomerase family: Unravelling a string of folds
26. The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding misfolded proteins
27. Recognition of protein substrates by protein-disulfide isomerase
28. The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
29. A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
30. The CXXC motif: Crystal structure of an active-site variant of Escherichia coli thioredoxin
31. Crystal structure of the protein disulfide bond isomerase DsbC from Escherichia coli
32. Identifying and characterizing a second structural domain of protein disulfide isomerase
33. An unconventional role for cytoplasmic disulfide bonds in vaccina virus proteins
34. In vitro folding of inclusion body proteins
35. Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase
36. Expression of human tissue-type plasminogen activator in Escherichia coli
37. Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-accumulation
38. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
39. Disulfide bond formation in the Escherichia coli cytoplasm: An in vivo role reversal for the thioredoxins
40. The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm
41. Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm
42. Glutathione excretion in response to heterologous protein secretion in Saccharomyces cerevisiae
43. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum