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2. Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors. Gaiser AM, Kretzschmar A, Richter K. J Biol Chem; 2010 Dec 24; 285(52):40921-32. PubMed ID: 20880838 [Abstract] [Full Text] [Related]
6. A primate specific extra domain in the molecular chaperone Hsp90. Tripathi V, Obermann WM. PLoS One; 2013 Dec 24; 8(8):e71856. PubMed ID: 23951259 [Abstract] [Full Text] [Related]
19. Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37. Roiniotis J, Masendycz P, Ho S, Scholz GM. Biochemistry; 2005 May 03; 44(17):6662-9. PubMed ID: 15850399 [Abstract] [Full Text] [Related]
20. The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation. Mercier R, Wolmarans A, Schubert J, Neuweiler H, Johnson JL, LaPointe P. Nat Commun; 2019 Mar 20; 10(1):1273. PubMed ID: 30894538 [Abstract] [Full Text] [Related] Page: [Next] [New Search]