361 related articles for article (PubMed ID: 7547904)
1. Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase.
Darby NJ; Creighton TE
Biochemistry; 1995 Sep; 34(37):11725-35. PubMed ID: 7547904
[TBL] [Abstract][Full Text] [Related]
2. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase.
Darby NJ; Creighton TE
Biochemistry; 1995 Dec; 34(51):16770-80. PubMed ID: 8527452
[TBL] [Abstract][Full Text] [Related]
3. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.
Kemmink J; Darby NJ; Dijkstra K; Nilges M; Creighton TE
Curr Biol; 1997 Apr; 7(4):239-45. PubMed ID: 9094311
[TBL] [Abstract][Full Text] [Related]
4. Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase.
Lundström-Ljung J; Birnbach U; Rupp K; Söling HD; Holmgren A
FEBS Lett; 1995 Jan; 357(3):305-8. PubMed ID: 7835433
[TBL] [Abstract][Full Text] [Related]
5. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.
Lundström J; Holmgren A
Biochemistry; 1993 Jul; 32(26):6649-55. PubMed ID: 8329391
[TBL] [Abstract][Full Text] [Related]
6. Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.
Lyles MM; Gilbert HF
J Biol Chem; 1994 Dec; 269(49):30946-52. PubMed ID: 7983029
[TBL] [Abstract][Full Text] [Related]
7. Enzymatic catalysis of disulfide formation.
Noiva R
Protein Expr Purif; 1994 Feb; 5(1):1-13. PubMed ID: 7909462
[TBL] [Abstract][Full Text] [Related]
8. 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.
Jonda S; Huber-Wunderlich M; Glockshuber R; Mössner E
EMBO J; 1999 Jun; 18(12):3271-81. PubMed ID: 10369668
[TBL] [Abstract][Full Text] [Related]
9. Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate.
Hawkins HC; Blackburn EC; Freedman RB
Biochem J; 1991 Apr; 275 ( Pt 2)(Pt 2):349-53. PubMed ID: 2025222
[TBL] [Abstract][Full Text] [Related]
10. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity.
Lundström J; Holmgren A
J Biol Chem; 1990 Jun; 265(16):9114-20. PubMed ID: 2188973
[TBL] [Abstract][Full Text] [Related]
11. A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease.
Lundström J; Krause G; Holmgren A
J Biol Chem; 1992 May; 267(13):9047-52. PubMed ID: 1577742
[TBL] [Abstract][Full Text] [Related]
12. Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.
Kulp MS; Frickel EM; Ellgaard L; Weissman JS
J Biol Chem; 2006 Jan; 281(2):876-84. PubMed ID: 16368681
[TBL] [Abstract][Full Text] [Related]
13. Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.
Kemmink J; Darby NJ; Dijkstra K; Nilges M; Creighton TE
Biochemistry; 1996 Jun; 35(24):7684-91. PubMed ID: 8672469
[TBL] [Abstract][Full Text] [Related]
14. Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum.
Holst B; Tachibana C; Winther JR
J Cell Biol; 1997 Sep; 138(6):1229-38. PubMed ID: 9298979
[TBL] [Abstract][Full Text] [Related]
15. Identifying and characterizing a structural domain of protein disulfide isomerase.
Darby NJ; Kemmink J; Creighton TE
Biochemistry; 1996 Aug; 35(32):10517-28. PubMed ID: 8756708
[TBL] [Abstract][Full Text] [Related]
16. Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase.
Kemmink J; Darby NJ; Dijkstra K; Scheek RM; Creighton TE
Protein Sci; 1995 Dec; 4(12):2587-93. PubMed ID: 8580850
[TBL] [Abstract][Full Text] [Related]
17. DsbA-mediated disulfide bond formation and catalyzed prolyl isomerization in oxidative protein folding.
Frech C; Schmid FX
J Biol Chem; 1995 Mar; 270(10):5367-74. PubMed ID: 7890650
[TBL] [Abstract][Full Text] [Related]
18. A role of PDI in the reductive cleavage of mixed disulfides.
Nakamura S; Matsushima M; Song H; Kikuchi M
J Biochem; 1996 Sep; 120(3):525-30. PubMed ID: 8902616
[TBL] [Abstract][Full Text] [Related]
19. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity.
LaMantia ML; Lennarz WJ
Cell; 1993 Sep; 74(5):899-908. PubMed ID: 8374956
[TBL] [Abstract][Full Text] [Related]
20. The machinery for oxidative protein folding in thermophiles.
Pedone E; Limauro D; Bartolucci S
Antioxid Redox Signal; 2008 Jan; 10(1):157-69. PubMed ID: 17956189
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
