186 related articles for article (PubMed ID: 15163408)
1. Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell.
Gross E; Kastner DB; Kaiser CA; Fass D
Cell; 2004 May; 117(5):601-10. PubMed ID: 15163408
[TBL] [Abstract][Full Text] [Related]
2. Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum.
Frand AR; Kaiser CA
Mol Biol Cell; 2000 Sep; 11(9):2833-43. PubMed ID: 10982384
[TBL] [Abstract][Full Text] [Related]
3. Disulfide relays between and within proteins: the Ero1p structure.
Hiniker A; Bardwell JC
Trends Biochem Sci; 2004 Oct; 29(10):516-9. PubMed ID: 15450603
[TBL] [Abstract][Full Text] [Related]
4. Disulfide transfer between two conserved cysteine pairs imparts selectivity to protein oxidation by Ero1.
Sevier CS; Kaiser CA
Mol Biol Cell; 2006 May; 17(5):2256-66. PubMed ID: 16495342
[TBL] [Abstract][Full Text] [Related]
5. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p.
Gross E; Sevier CS; Heldman N; Vitu E; Bentzur M; Kaiser CA; Thorpe C; Fass D
Proc Natl Acad Sci U S A; 2006 Jan; 103(2):299-304. PubMed ID: 16407158
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum.
Pollard MG; Travers KJ; Weissman JS
Mol Cell; 1998 Jan; 1(2):171-82. PubMed ID: 9659914
[TBL] [Abstract][Full Text] [Related]
8. Steps in reductive activation of the disulfide-generating enzyme Ero1p.
Heldman N; Vonshak O; Sevier CS; Vitu E; Mehlman T; Fass D
Protein Sci; 2010 Oct; 19(10):1863-76. PubMed ID: 20669236
[TBL] [Abstract][Full Text] [Related]
9. 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]
10. Balanced Ero1 activation and inactivation establishes ER redox homeostasis.
Kim S; Sideris DP; Sevier CS; Kaiser CA
J Cell Biol; 2012 Mar; 196(6):713-25. PubMed ID: 22412017
[TBL] [Abstract][Full Text] [Related]
11. 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]
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. Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1.
Sevier CS; Qu H; Heldman N; Gross E; Fass D; Kaiser CA
Cell; 2007 Apr; 129(2):333-44. PubMed ID: 17448992
[TBL] [Abstract][Full Text] [Related]
14. Biochemical basis of oxidative protein folding in the endoplasmic reticulum.
Tu BP; Ho-Schleyer SC; Travers KJ; Weissman JS
Science; 2000 Nov; 290(5496):1571-4. PubMed ID: 11090354
[TBL] [Abstract][Full Text] [Related]
15. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.
Sevier CS; Cuozzo JW; Vala A; Aslund F; Kaiser CA
Nat Cell Biol; 2001 Oct; 3(10):874-82. PubMed ID: 11584268
[TBL] [Abstract][Full Text] [Related]
16. Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family.
Gerber J; Mühlenhoff U; Hofhaus G; Lill R; Lisowsky T
J Biol Chem; 2001 Jun; 276(26):23486-91. PubMed ID: 11313344
[TBL] [Abstract][Full Text] [Related]
17. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum.
Frand AR; Kaiser CA
Mol Cell; 1998 Jan; 1(2):161-70. PubMed ID: 9659913
[TBL] [Abstract][Full Text] [Related]
18. The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum.
Tu BP; Weissman JS
Mol Cell; 2002 Nov; 10(5):983-94. PubMed ID: 12453408
[TBL] [Abstract][Full Text] [Related]
19. The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function.
Pagani M; Pilati S; Bertoli G; Valsasina B; Sitia R
FEBS Lett; 2001 Nov; 508(1):117-20. PubMed ID: 11707280
[TBL] [Abstract][Full Text] [Related]
20. Identification of small molecular inhibitors for Ero1p by structure-based virtual screening.
Chu Y; Chen X; Yang Y; Tang Y
Bioorg Med Chem Lett; 2011 Feb; 21(4):1118-21. PubMed ID: 21269829
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]