179 related articles for article (PubMed ID: 8300576)
1. Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured reduced proteins. Comparison with protein disulfide isomerase.
Rupp K; Birnbach U; Lundström J; Van PN; Söling HD
J Biol Chem; 1994 Jan; 269(4):2501-7. PubMed ID: 8300576
[TBL] [Abstract][Full Text] [Related]
2. Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding.
Kramer B; Ferrari DM; Klappa P; Pöhlmann N; Söling HD
Biochem J; 2001 Jul; 357(Pt 1):83-95. PubMed ID: 11415439
[TBL] [Abstract][Full Text] [Related]
3. 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]
4. Influence of protein disulfide isomerase (PDI) on antibody folding in vitro.
Lilie H; McLaughlin S; Freedman R; Buchner J
J Biol Chem; 1994 May; 269(19):14290-6. PubMed ID: 8188714
[TBL] [Abstract][Full Text] [Related]
5. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A.
Ruoppolo M; Lundström-Ljung J; Talamo F; Pucci P; Marino G
Biochemistry; 1997 Oct; 36(40):12259-67. PubMed ID: 9315864
[TBL] [Abstract][Full Text] [Related]
6. Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization: catalysis by protein disulfide isomerase.
Ruoppolo M; Freedman RB; Pucci P; Marino G
Biochemistry; 1996 Oct; 35(42):13636-46. PubMed ID: 8885843
[TBL] [Abstract][Full Text] [Related]
7. Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase.
Lundström-Ljung J; Holmgren A
J Biol Chem; 1995 Apr; 270(14):7822-8. PubMed ID: 7713872
[TBL] [Abstract][Full Text] [Related]
8. Influence of the oxidoreductase ER57 on the folding of an antibody fab fragment.
Mayer M; Frey S; Koivunen P; Myllyharju J; Buchner J
J Mol Biol; 2004 Aug; 341(4):1077-84. PubMed ID: 15328618
[TBL] [Abstract][Full Text] [Related]
9. Differential cooperative enzymatic activities of protein disulfide isomerase family in protein folding.
Satoh M; Shimada A; Kashiwai A; Saga S; Hosokawa M
Cell Stress Chaperones; 2005; 10(3):211-20. PubMed ID: 16184766
[TBL] [Abstract][Full Text] [Related]
10. Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme.
Puig A; Gilbert HF
J Biol Chem; 1994 Oct; 269(41):25889-96. PubMed ID: 7929293
[TBL] [Abstract][Full Text] [Related]
11. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer.
Lyles MM; Gilbert HF
Biochemistry; 1991 Jan; 30(3):613-9. PubMed ID: 1988050
[TBL] [Abstract][Full Text] [Related]
12. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase.
Lyles MM; Gilbert HF
Biochemistry; 1991 Jan; 30(3):619-25. PubMed ID: 1988051
[TBL] [Abstract][Full Text] [Related]
13. Refolding by disulfide isomerization: the mixed disulfide between ribonuclease T1 and glutathione as a model refolding substrate.
Ruoppolo M; Freedman RB
Biochemistry; 1995 Jul; 34(29):9380-8. PubMed ID: 7626608
[TBL] [Abstract][Full Text] [Related]
14. Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.
Yao Y; Zhou Y; Wang C
EMBO J; 1997 Feb; 16(3):651-8. PubMed ID: 9034346
[TBL] [Abstract][Full Text] [Related]
15. CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activity.
Van PN; Rupp K; Lampen A; Söling HD
Eur J Biochem; 1993 Apr; 213(2):789-95. PubMed ID: 8477750
[TBL] [Abstract][Full Text] [Related]
16. 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]
17. Association of antibody chains at different stages of folding: prolyl isomerization occurs after formation of quaternary structure.
Lilie H; Rudolph R; Buchner J
J Mol Biol; 1995 Apr; 248(1):190-201. PubMed ID: 7731044
[TBL] [Abstract][Full Text] [Related]
18. Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme.
Puig A; Gilbert HF
J Biol Chem; 1994 Mar; 269(10):7764-71. PubMed ID: 7907332
[TBL] [Abstract][Full Text] [Related]
19. Protein disulfide isomerase-catalyzed renaturation of ribonuclease A modified by S-thiolation with glutathione and cysteine.
Ubuka T
Biochem Mol Biol Int; 1996 May; 38(6):1103-10. PubMed ID: 8739031
[TBL] [Abstract][Full Text] [Related]
20. The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase.
Puig A; Lyles MM; Noiva R; Gilbert HF
J Biol Chem; 1994 Jul; 269(29):19128-35. PubMed ID: 7913469
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]