157 related articles for article (PubMed ID: 18845159)
1. Yeast Mpd1p reveals the structural diversity of the protein disulfide isomerase family.
Vitu E; Gross E; Greenblatt HM; Sevier CS; Kaiser CA; Fass D
J Mol Biol; 2008 Dec; 384(3):631-40. PubMed ID: 18845159
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.
Kimura T; Hosoda Y; Sato Y; Kitamura Y; Ikeda T; Horibe T; Kikuchi M
J Biol Chem; 2005 Sep; 280(36):31438-41. PubMed ID: 16002399
[TBL] [Abstract][Full Text] [Related]
4. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.
Xiao R; Wilkinson B; Solovyov A; Winther JR; Holmgren A; Lundström-Ljung J; Gilbert HF
J Biol Chem; 2004 Nov; 279(48):49780-6. PubMed ID: 15377672
[TBL] [Abstract][Full Text] [Related]
5. The Eps1p protein disulfide isomerase conserves classic thioredoxin superfamily amino acid motifs but not their functional geometries.
Biran S; Gat Y; Fass D
PLoS One; 2014; 9(12):e113431. PubMed ID: 25437863
[TBL] [Abstract][Full Text] [Related]
6. Structural insight into the dimerization of human protein disulfide isomerase.
Bastos-Aristizabal S; Kozlov G; Gehring K
Protein Sci; 2014 May; 23(5):618-26. PubMed ID: 24549644
[TBL] [Abstract][Full Text] [Related]
7. PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.
van Lith M; Hartigan N; Hatch J; Benham AM
J Biol Chem; 2005 Jan; 280(2):1376-83. PubMed ID: 15475357
[TBL] [Abstract][Full Text] [Related]
8. Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.
Kojima R; Okumura M; Masui S; Kanemura S; Inoue M; Saiki M; Yamaguchi H; Hikima T; Suzuki M; Akiyama S; Inaba K
Structure; 2014 Mar; 22(3):431-43. PubMed ID: 24462249
[TBL] [Abstract][Full Text] [Related]
9. Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1.
Niu Y; Zhang L; Yu J; Wang CC; Wang L
J Biol Chem; 2016 Apr; 291(15):8283-94. PubMed ID: 26846856
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.
Hudson DA; Gannon SA; Thorpe C
Free Radic Biol Med; 2015 Mar; 80():171-82. PubMed ID: 25091901
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum.
Vitu E; Kim S; Sevier CS; Lutzky O; Heldman N; Bentzur M; Unger T; Yona M; Kaiser CA; Fass D
J Biol Chem; 2010 Jun; 285(24):18155-65. PubMed ID: 20348090
[TBL] [Abstract][Full Text] [Related]
14. A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain.
Wilkinson B; Xiao R; Gilbert HF
J Biol Chem; 2005 Mar; 280(12):11483-7. PubMed ID: 15649885
[TBL] [Abstract][Full Text] [Related]
15. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum.
Frand AR; Kaiser CA
Mol Cell; 1999 Oct; 4(4):469-77. PubMed ID: 10549279
[TBL] [Abstract][Full Text] [Related]
16. Enzymatic catalysis of disulfide formation.
Noiva R
Protein Expr Purif; 1994 Feb; 5(1):1-13. PubMed ID: 7909462
[TBL] [Abstract][Full Text] [Related]
17. ERp29, an unusual redox-inactive member of the thioredoxin family.
Mkrtchian S; Sandalova T
Antioxid Redox Signal; 2006; 8(3-4):325-37. PubMed ID: 16677078
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. 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]
20. Protein disulfide isomerase: the structure of oxidative folding.
Gruber CW; Cemazar M; Heras B; Martin JL; Craik DJ
Trends Biochem Sci; 2006 Aug; 31(8):455-64. PubMed ID: 16815710
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
