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ATP induces a conformational change of the 90-kDa heat shock protein (hsp90).
Csermely P, Kajtár J, Hollósi M, Jalsovszky G, Holly S, Kahn CR, Gergely P Jr, Söti C, Mihály K, Somogyi J. Csermely P, et al. J Biol Chem. 1993 Jan 25;268(3):1901-7. J Biol Chem. 1993. PMID: 8420964 Free article.
We have recently demonstrated that hsp90 has an ATP-binding site and autophosphorylating activity (Csermely, P., and Kahn, C. R. (1991) J. Biol. Chem. 266, 4943-4950). ...
We have recently demonstrated that hsp90 has an ATP-binding site and autophosphorylating activity (Csermely, P., and Kahn, C. …
Interaction of vanadate oligomers and permolybdate with the 90-kDa heat-shock protein, Hsp90.
Söti C, Radics L, Yahara I, Csermely P. Söti C, et al. Among authors: csermely p. Eur J Biochem. 1998 Aug 1;255(3):611-7. doi: 10.1046/j.1432-1327.1998.2550611.x. Eur J Biochem. 1998. PMID: 9738900 Free article.
Hsp90 x protein complexes can be stabilized by molybdate and by other transition metal oxyanions such as vanadate. Our earlier findings [Csermely, P., Kajtar, J., Hollosi, M., Jalsovszky, G., Holly, S., Kahn, C. R., Gergely, P. Jr, Soti, C., Mihaly, K. & …
Hsp90 x protein complexes can be stabilized by molybdate and by other transition metal oxyanions such as vanadate. Our earlier findings [ …
Molecular chaperones and the aging process.
Sóti C, Csermely P. Sóti C, et al. Among authors: csermely p. Biogerontology. 2000;1(3):225-33. doi: 10.1023/a:1010082129022. Biogerontology. 2000. PMID: 11707899 Review.
210 results