341 related articles for article (PubMed ID: 9094311)
1. 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]
2. The structure in solution of the b domain of protein disulfide isomerase.
Kemmink J; Dijkstra K; Mariani M; Scheek RM; Penka E; Nilges M; Darby NJ
J Biomol NMR; 1999 Apr; 13(4):357-68. PubMed ID: 10383197
[TBL] [Abstract][Full Text] [Related]
3. Redox-dependent domain rearrangement of protein disulfide isomerase from a thermophilic fungus.
Nakasako M; Maeno A; Kurimoto E; Harada T; Yamaguchi Y; Oka T; Takayama Y; Iwata A; Kato K
Biochemistry; 2010 Aug; 49(32):6953-62. PubMed ID: 20695532
[TBL] [Abstract][Full Text] [Related]
4. 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]
5. Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface.
Serve O; Kamiya Y; Maeno A; Nakano M; Murakami C; Sasakawa H; Yamaguchi Y; Harada T; Kurimoto E; Yagi-Utsumi M; Iguchi T; Inaba K; Kikuchi J; Asami O; Kajino T; Oka T; Nakasako M; Kato K
J Mol Biol; 2010 Feb; 396(2):361-74. PubMed ID: 19944705
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. Generating an unfoldase from thioredoxin-like domains.
Forster ML; Mahn JJ; Tsai B
J Biol Chem; 2009 May; 284(19):13045-56. PubMed ID: 19289469
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. 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]
10. 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]
11. 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]
12. Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A.
Ruoppolo M; Orrù S; Talamo F; Ljung J; Pirneskoski A; Kivirikko KI; Marino G; Koivunen P
Protein Sci; 2003 May; 12(5):939-52. PubMed ID: 12717017
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif.
Ferrari DM; Nguyen Van P; Kratzin HD; Söling HD
Eur J Biochem; 1998 Aug; 255(3):570-9. PubMed ID: 9738895
[TBL] [Abstract][Full Text] [Related]
15. 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]
16. Zinc-dependent dimerization of the folding catalyst, protein disulfide isomerase.
Solovyov A; Gilbert HF
Protein Sci; 2004 Jul; 13(7):1902-7. PubMed ID: 15169950
[TBL] [Abstract][Full Text] [Related]
17. 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]
18. Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.
Pirneskoski A; Ruddock LW; Klappa P; Freedman RB; Kivirikko KI; Koivunen P
J Biol Chem; 2001 Apr; 276(14):11287-93. PubMed ID: 11134056
[TBL] [Abstract][Full Text] [Related]
19. Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase.
Pirneskoski A; Klappa P; Lobell M; Williamson RA; Byrne L; Alanen HI; Salo KE; Kivirikko KI; Freedman RB; Ruddock LW
J Biol Chem; 2004 Mar; 279(11):10374-81. PubMed ID: 14684740
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]
