266 related articles for article (PubMed ID: 26286954)
1. The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry.
Schmidt C; Beilsten-Edmands V; Robinson CV
Oncotarget; 2015 Jul; 6(21):18276-81. PubMed ID: 26286954
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90.
Morgner N; Schmidt C; Beilsten-Edmands V; Ebong IO; Patel NA; Clerico EM; Kirschke E; Daturpalli S; Jackson SE; Agard D; Robinson CV
Cell Rep; 2015 May; 11(5):759-69. PubMed ID: 25921532
[TBL] [Abstract][Full Text] [Related]
4. S100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complex.
Okada M; Hatakeyama T; Itoh H; Tokuta N; Tokumitsu H; Kobayashi R
J Biol Chem; 2004 Feb; 279(6):4221-33. PubMed ID: 14638689
[TBL] [Abstract][Full Text] [Related]
5. Coordinated Conformational Processing of the Tumor Suppressor Protein p53 by the Hsp70 and Hsp90 Chaperone Machineries.
Dahiya V; Agam G; Lawatscheck J; Rutz DA; Lamb DC; Buchner J
Mol Cell; 2019 May; 74(4):816-830.e7. PubMed ID: 31027879
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex.
Hernández MP; Sullivan WP; Toft DO
J Biol Chem; 2002 Oct; 277(41):38294-304. PubMed ID: 12161444
[TBL] [Abstract][Full Text] [Related]
8. Importance of the C-terminal domain of Harc for binding to Hsp70 and Hop as well as its response to heat shock.
Cartledge K; Elsegood C; Roiniotis J; Hamilton JA; Scholz GM
Biochemistry; 2007 Dec; 46(51):15144-52. PubMed ID: 18052042
[TBL] [Abstract][Full Text] [Related]
9. The Hsp70-Hsp90 Chaperone Cascade in Protein Folding.
Morán Luengo T; Mayer MP; Rüdiger SGD
Trends Cell Biol; 2019 Feb; 29(2):164-177. PubMed ID: 30502916
[TBL] [Abstract][Full Text] [Related]
10. Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway.
Cintron NS; Toft D
J Biol Chem; 2006 Sep; 281(36):26235-44. PubMed ID: 16854979
[TBL] [Abstract][Full Text] [Related]
11. Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes.
Ebong IO; Morgner N; Zhou M; Saraiva MA; Daturpalli S; Jackson SE; Robinson CV
Proc Natl Acad Sci U S A; 2011 Nov; 108(44):17939-44. PubMed ID: 22011577
[TBL] [Abstract][Full Text] [Related]
12. Hsp90 can accommodate the simultaneous binding of the FKBP52 and HOP proteins.
Hildenbrand ZL; Molugu SK; Herrera N; Ramirez C; Xiao C; Bernal RA
Oncotarget; 2011; 2(1-2):43-58. PubMed ID: 21378414
[TBL] [Abstract][Full Text] [Related]
13. Alterations of the Hsp70/Hsp90 chaperone and the HOP/CHIP co-chaperone system in cancer.
Ruckova E; Muller P; Nenutil R; Vojtesek B
Cell Mol Biol Lett; 2012 Sep; 17(3):446-58. PubMed ID: 22669480
[TBL] [Abstract][Full Text] [Related]
14. Exploring Mechanisms of Allosteric Regulation and Communication Switching in the Multiprotein Regulatory Complexes of the Hsp90 Chaperone with Cochaperones and Client Proteins: Atomistic Insights from Integrative Biophysical Modeling and Network Analysis of Conformational Landscapes.
Verkhivker GM
J Mol Biol; 2022 Sep; 434(17):167506. PubMed ID: 35202628
[TBL] [Abstract][Full Text] [Related]
15. Multiple domains of the co-chaperone Hop are important for Hsp70 binding.
Carrigan PE; Nelson GM; Roberts PJ; Stoffer J; Riggs DL; Smith DF
J Biol Chem; 2004 Apr; 279(16):16185-93. PubMed ID: 14960564
[TBL] [Abstract][Full Text] [Related]
16. The switch from client holding to folding in the Hsp70/Hsp90 chaperone machineries is regulated by a direct interplay between co-chaperones.
Dahiya V; Rutz DA; Moessmer P; Mühlhofer M; Lawatscheck J; Rief M; Buchner J
Mol Cell; 2022 Apr; 82(8):1543-1556.e6. PubMed ID: 35176233
[TBL] [Abstract][Full Text] [Related]
17. Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro.
Rauch JN; Gestwicki JE
J Biol Chem; 2014 Jan; 289(3):1402-14. PubMed ID: 24318877
[TBL] [Abstract][Full Text] [Related]
18. In silico identification of carboxylate clamp type tetratricopeptide repeat proteins in Arabidopsis and rice as putative co-chaperones of Hsp90/Hsp70.
Prasad BD; Goel S; Krishna P
PLoS One; 2010 Sep; 5(9):e12761. PubMed ID: 20856808
[TBL] [Abstract][Full Text] [Related]
19. High affinity binding between Hsp70 and the C-terminal domain of the measles virus nucleoprotein requires an Hsp40 co-chaperone.
Couturier M; Buccellato M; Costanzo S; Bourhis JM; Shu Y; Nicaise M; Desmadril M; Flaudrops C; Longhi S; Oglesbee M
J Mol Recognit; 2010; 23(3):301-15. PubMed ID: 19718689
[TBL] [Abstract][Full Text] [Related]
20. Functions of the Hsp90-Binding FKBP Immunophilins.
Ortiz NR; Guy N; Garcia YA; Sivils JC; Galigniana MD; Cox MB
Subcell Biochem; 2023; 101():41-80. PubMed ID: 36520303
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
