1896 related articles for article (PubMed ID: 15497503)
1. 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]
2. Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants.
Chen S; Sullivan WP; Toft DO; Smith DF
Cell Stress Chaperones; 1998 Jun; 3(2):118-29. PubMed ID: 9672247
[TBL] [Abstract][Full Text] [Related]
3. Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity.
Odunuga OO; Hornby JA; Bies C; Zimmermann R; Pugh DJ; Blatch GL
J Biol Chem; 2003 Feb; 278(9):6896-904. PubMed ID: 12482845
[TBL] [Abstract][Full Text] [Related]
4. Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.
Assimon VA; Southworth DR; Gestwicki JE
Biochemistry; 2015 Dec; 54(48):7120-31. PubMed ID: 26565746
[TBL] [Abstract][Full Text] [Related]
5. The common tetratricopeptide repeat acceptor site for steroid receptor-associated immunophilins and hop is located in the dimerization domain of Hsp90.
Carrello A; Ingley E; Minchin RF; Tsai S; Ratajczak T
J Biol Chem; 1999 Jan; 274(5):2682-9. PubMed ID: 9915798
[TBL] [Abstract][Full Text] [Related]
6. Heat shock cognate protein 70 chaperone-binding site in the co-chaperone murine stress-inducible protein 1 maps to within three consecutive tetratricopeptide repeat motifs.
Van Der Spuy J; Kana BD; Dirr HW; Blatch GL
Biochem J; 2000 Feb; 345 Pt 3(Pt 3):645-51. PubMed ID: 10642524
[TBL] [Abstract][Full Text] [Related]
7. C-terminal sequences outside the tetratricopeptide repeat domain of FKBP51 and FKBP52 cause differential binding to Hsp90.
Cheung-Flynn J; Roberts PJ; Riggs DL; Smith DF
J Biol Chem; 2003 May; 278(19):17388-94. PubMed ID: 12611898
[TBL] [Abstract][Full Text] [Related]
8. Cyclophilin 40 (CyP-40), mapping of its hsp90 binding domain and evidence that FKBP52 competes with CyP-40 for hsp90 binding.
Ratajczak T; Carrello A
J Biol Chem; 1996 Feb; 271(6):2961-5. PubMed ID: 8621687
[TBL] [Abstract][Full Text] [Related]
9. A structure-based mutational analysis of cyclophilin 40 identifies key residues in the core tetratricopeptide repeat domain that mediate binding to Hsp90.
Ward BK; Allan RK; Mok D; Temple SE; Taylor P; Dornan J; Mark PJ; Shaw DJ; Kumar P; Walkinshaw MD; Ratajczak T
J Biol Chem; 2002 Oct; 277(43):40799-809. PubMed ID: 12145316
[TBL] [Abstract][Full Text] [Related]
10. S100 proteins regulate the interaction of Hsp90 with Cyclophilin 40 and FKBP52 through their tetratricopeptide repeats.
Shimamoto S; Kubota Y; Tokumitsu H; Kobayashi R
FEBS Lett; 2010 Mar; 584(6):1119-25. PubMed ID: 20188096
[TBL] [Abstract][Full Text] [Related]
11. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.
Scheufler C; Brinker A; Bourenkov G; Pegoraro S; Moroder L; Bartunik H; Hartl FU; Moarefi I
Cell; 2000 Apr; 101(2):199-210. PubMed ID: 10786835
[TBL] [Abstract][Full Text] [Related]
12. Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes.
Brinker A; Scheufler C; Von Der Mulbe F; Fleckenstein B; Herrmann C; Jung G; Moarefi I; Hartl FU
J Biol Chem; 2002 May; 277(22):19265-75. PubMed ID: 11877417
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.
Ballinger CA; Connell P; Wu Y; Hu Z; Thompson LJ; Yin LY; Patterson C
Mol Cell Biol; 1999 Jun; 19(6):4535-45. PubMed ID: 10330192
[TBL] [Abstract][Full Text] [Related]
15. The carboxy-terminal domain of Hsc70 provides binding sites for a distinct set of chaperone cofactors.
Demand J; Lüders J; Höhfeld J
Mol Cell Biol; 1998 Apr; 18(4):2023-8. PubMed ID: 9528774
[TBL] [Abstract][Full Text] [Related]
16. Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants.
Owens-Grillo JK; Stancato LF; Hoffmann K; Pratt WB; Krishna P
Biochemistry; 1996 Dec; 35(48):15249-55. PubMed ID: 8952474
[TBL] [Abstract][Full Text] [Related]
17. Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock.
Mark PJ; Ward BK; Kumar P; Lahooti H; Minchin RF; Ratajczak T
Cell Stress Chaperones; 2001 Jan; 6(1):59-70. PubMed ID: 11525244
[TBL] [Abstract][Full Text] [Related]
18. Characterization of a plant homolog of hop, a cochaperone of hsp90.
Zhang Z; Quick MK; Kanelakis KC; Gijzen M; Krishna P
Plant Physiol; 2003 Feb; 131(2):525-35. PubMed ID: 12586877
[TBL] [Abstract][Full Text] [Related]
19. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery.
Pratt WB; Toft DO
Exp Biol Med (Maywood); 2003 Feb; 228(2):111-33. PubMed ID: 12563018
[TBL] [Abstract][Full Text] [Related]
20. Overlapping sites of tetratricopeptide repeat protein binding and chaperone activity in heat shock protein 90.
Ramsey AJ; Russell LC; Whitt SR; Chinkers M
J Biol Chem; 2000 Jun; 275(23):17857-62. PubMed ID: 10751404
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
