380 related articles for article (PubMed ID: 11298772)
1. Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding.
Minami M; Nakamura M; Emori Y; Minami Y
Eur J Biochem; 2001 Apr; 268(8):2520-4. PubMed ID: 11298772
[TBL] [Abstract][Full Text] [Related]
2. A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding.
Minami Y; Kawasaki H; Minami M; Tanahashi N; Tanaka K; Yahara I
J Biol Chem; 2000 Mar; 275(12):9055-61. PubMed ID: 10722756
[TBL] [Abstract][Full Text] [Related]
3. Hsc70/Hsp40 chaperone system mediates the Hsp90-dependent refolding of firefly luciferase.
Minami Y; Minami M
Genes Cells; 1999 Dec; 4(12):721-9. PubMed ID: 10620017
[TBL] [Abstract][Full Text] [Related]
4. In vitro evidence that hsp90 contains two independent chaperone sites.
Young JC; Schneider C; Hartl FU
FEBS Lett; 1997 Nov; 418(1-2):139-43. PubMed ID: 9414113
[TBL] [Abstract][Full Text] [Related]
5. Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells.
Kampinga HH; Kanon B; Salomons FA; Kabakov AE; Patterson C
Mol Cell Biol; 2003 Jul; 23(14):4948-58. PubMed ID: 12832480
[TBL] [Abstract][Full Text] [Related]
6. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding.
Freeman BC; Morimoto RI
EMBO J; 1996 Jun; 15(12):2969-79. PubMed ID: 8670798
[TBL] [Abstract][Full Text] [Related]
7. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein.
Murata S; Minami Y; Minami M; Chiba T; Tanaka K
EMBO Rep; 2001 Dec; 2(12):1133-8. PubMed ID: 11743028
[TBL] [Abstract][Full Text] [Related]
8. Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.
Carrello A; Allan RK; Morgan SL; Owen BA; Mok D; Ward BK; Minchin RF; Toft DO; Ratajczak T
Cell Stress Chaperones; 2004; 9(2):167-81. PubMed ID: 15497503
[TBL] [Abstract][Full Text] [Related]
9. Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53.
King FW; Wawrzynow A; Höhfeld J; Zylicz M
EMBO J; 2001 Nov; 20(22):6297-305. PubMed ID: 11707401
[TBL] [Abstract][Full Text] [Related]
10. Proteins interacting with the molecular chaperone hsp70/hsc70: physical associations and effects on refolding activity.
Gebauer M; Zeiner M; Gehring U
FEBS Lett; 1997 Nov; 417(1):109-13. PubMed ID: 9395086
[TBL] [Abstract][Full Text] [Related]
11. Effect of geldanamycin on the kinetics of chaperone-mediated renaturation of firefly luciferase in rabbit reticulocyte lysate.
Thulasiraman V; Matts RL
Biochemistry; 1996 Oct; 35(41):13443-50. PubMed ID: 8873613
[TBL] [Abstract][Full Text] [Related]
12. Efficient Hsp90-independent in vitro activation by Hsc70 and Hsp40 of duck hepatitis B virus reverse transcriptase, an assumed Hsp90 client protein.
Beck J; Nassal M
J Biol Chem; 2003 Sep; 278(38):36128-38. PubMed ID: 12851401
[TBL] [Abstract][Full Text] [Related]
13. Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
Brychzy A; Rein T; Winklhofer KF; Hartl FU; Young JC; Obermann WM
EMBO J; 2003 Jul; 22(14):3613-23. PubMed ID: 12853476
[TBL] [Abstract][Full Text] [Related]
14. Cofactor-induced modulation of the functional specificity of the molecular chaperone Hsc70.
Lüders J; Demand J; Schönfelder S; Frien M; Zimmermann R; Höhfeld J
Biol Chem; 1998 Oct; 379(10):1217-26. PubMed ID: 9820582
[TBL] [Abstract][Full Text] [Related]
15. Specific association of a set of molecular chaperones including HSP90 and Cdc37 with MOK, a member of the mitogen-activated protein kinase superfamily.
Miyata Y; Ikawa Y; Shibuya M; Nishida E
J Biol Chem; 2001 Jun; 276(24):21841-8. PubMed ID: 11278794
[TBL] [Abstract][Full Text] [Related]
16. Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.
Yun BG; Huang W; Leach N; Hartson SD; Matts RL
Biochemistry; 2004 Jun; 43(25):8217-29. PubMed ID: 15209518
[TBL] [Abstract][Full Text] [Related]
17. Differential effects of the hsp70-binding protein BAG-1 on glucocorticoid receptor folding by the hsp90-based chaperone machinery.
Kanelakis KC; Morishima Y; Dittmar KD; Galigniana MD; Takayama S; Reed JC; Pratt WB
J Biol Chem; 1999 Nov; 274(48):34134-40. PubMed ID: 10567384
[TBL] [Abstract][Full Text] [Related]
18. Hop modulates Hsp70/Hsp90 interactions in protein folding.
Johnson BD; Schumacher RJ; Ross ED; Toft DO
J Biol Chem; 1998 Feb; 273(6):3679-86. PubMed ID: 9452498
[TBL] [Abstract][Full Text] [Related]
19. Modulation of the chaperone activities of Hsc70/Hsp40 by Hsp105alpha and Hsp105beta.
Yamagishi N; Nishihori H; Ishihara K; Ohtsuka K; Hatayama T
Biochem Biophys Res Commun; 2000 Jun; 272(3):850-5. PubMed ID: 10860841
[TBL] [Abstract][Full Text] [Related]
20. Cooperative action of Hsp70, Hsp90, and DnaJ proteins in protein renaturation.
Schumacher RJ; Hansen WJ; Freeman BC; Alnemri E; Litwack G; Toft DO
Biochemistry; 1996 Nov; 35(47):14889-98. PubMed ID: 8942653
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
