142 related articles for article (PubMed ID: 8798629)
1. Purification and biochemical properties of Saccharomyces cerevisiae's Mge1p, the mitochondrial cochaperone of Ssc1p.
Deloche O; Georgopoulos C
J Biol Chem; 1996 Sep; 271(39):23960-6. PubMed ID: 8798629
[TBL] [Abstract][Full Text] [Related]
2. Structure-function analyses of the Ssc1p, Mdj1p, and Mge1p Saccharomyces cerevisiae mitochondrial proteins in Escherichia coli.
Deloche O; Kelley WL; Georgopoulos C
J Bacteriol; 1997 Oct; 179(19):6066-75. PubMed ID: 9324254
[TBL] [Abstract][Full Text] [Related]
3. Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system.
Kubo Y; Tsunehiro T; Nishikawa S; Nakai M; Ikeda E; Toh-e A; Morishima N; Shibata T; Endo T
J Mol Biol; 1999 Feb; 286(2):447-64. PubMed ID: 9973563
[TBL] [Abstract][Full Text] [Related]
4. Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding.
Krzewska J; Langer T; Liberek K
FEBS Lett; 2001 Jan; 489(1):92-6. PubMed ID: 11231020
[TBL] [Abstract][Full Text] [Related]
5. Purification and biochemical properties of Saccharomyces cerevisiae Mdj1p, the mitochondrial DnaJ homologue.
Deloche O; Liberek K; Zylicz M; Georgopoulos C
J Biol Chem; 1997 Nov; 272(45):28539-44. PubMed ID: 9353316
[TBL] [Abstract][Full Text] [Related]
6. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins.
Laloraya S; Dekker PJ; Voos W; Craig EA; Pfanner N
Mol Cell Biol; 1995 Dec; 15(12):7098-105. PubMed ID: 8524277
[TBL] [Abstract][Full Text] [Related]
7. A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation.
Laloraya S; Gambill BD; Craig EA
Proc Natl Acad Sci U S A; 1994 Jul; 91(14):6481-5. PubMed ID: 8022808
[TBL] [Abstract][Full Text] [Related]
8. The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1.
Schmidt S; Strub A; Röttgers K; Zufall N; Voos W
J Mol Biol; 2001 Oct; 313(1):13-26. PubMed ID: 11601843
[TBL] [Abstract][Full Text] [Related]
9. Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation.
Prip-Buus C; Westerman B; Schmitt M; Langer T; Neupert W; Schwarz E
FEBS Lett; 1996 Feb; 380(1-2):142-6. PubMed ID: 8603724
[TBL] [Abstract][Full Text] [Related]
10. Complementation studies of the DnaK-DnaJ-GrpE chaperone machineries from Vibrio harveyi and Escherichia coli, both in vivo and in vitro.
Zmijewski MA; Kwiatkowska JM; Lipińska B
Arch Microbiol; 2004 Dec; 182(6):436-49. PubMed ID: 15448982
[TBL] [Abstract][Full Text] [Related]
11. The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria.
Westermann B; Prip-Buus C; Neupert W; Schwarz E
EMBO J; 1995 Jul; 14(14):3452-60. PubMed ID: 7628446
[TBL] [Abstract][Full Text] [Related]
12. Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae.
Miao B; Davis JE; Craig EA
J Mol Biol; 1997 Feb; 265(5):541-52. PubMed ID: 9048947
[TBL] [Abstract][Full Text] [Related]
13. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE.
Groemping Y; Klostermeier D; Herrmann C; Veit T; Seidel R; Reinstein J
J Mol Biol; 2001 Feb; 305(5):1173-83. PubMed ID: 11162122
[TBL] [Abstract][Full Text] [Related]
14. The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.
Silberg JJ; Hoff KG; Vickery LE
J Bacteriol; 1998 Dec; 180(24):6617-24. PubMed ID: 9852006
[TBL] [Abstract][Full Text] [Related]
15. Interaction between the nucleotide exchange factor Mge1 and the mitochondrial Hsp70 Ssc1.
Sakuragi S; Liu Q; Craig E
J Biol Chem; 1999 Apr; 274(16):11275-82. PubMed ID: 10196216
[TBL] [Abstract][Full Text] [Related]
16. Yge1p, a eukaryotic Grp-E homolog, is localized in the mitochondrial matrix and interacts with mitochondrial Hsp70.
Nakai M; Kato Y; Ikeda E; Toh-e A; Endo T
Biochem Biophys Res Commun; 1994 Apr; 200(1):435-42. PubMed ID: 8166717
[TBL] [Abstract][Full Text] [Related]
17. Recognizability of heterologous co-chaperones with Streptococcus intermedius DnaK and Escherichia coli DnaK.
Tomoyasu T; Tsuruno K; Tanatsugu R; Miyazaki A; Kondo H; Tabata A; Whiley RA; Sonomoto K; Nagamune H
Microbiol Immunol; 2018 Nov; 62(11):681-693. PubMed ID: 30239035
[TBL] [Abstract][Full Text] [Related]
18. Thermal adaptation of the yeast mitochondrial Hsp70 system is regulated by the reversible unfolding of its nucleotide exchange factor.
Moro F; Muga A
J Mol Biol; 2006 May; 358(5):1367-77. PubMed ID: 16600294
[TBL] [Abstract][Full Text] [Related]
19. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli.
Zolkiewski M
J Biol Chem; 1999 Oct; 274(40):28083-6. PubMed ID: 10497158
[TBL] [Abstract][Full Text] [Related]
20. Two-step purification of mitochondrial Hsp70, Ssc1p, using Mge1(His)(6) immobilized on Ni-agarose.
Weiss C; Niv A; Azem A
Protein Expr Purif; 2002 Mar; 24(2):268-73. PubMed ID: 11858722
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]