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[Stress proteins in medicine].
Csermely P, Somogyi J. Csermely P, et al. Orv Hetil. 1992 May 31;133(22):1347-51. Orv Hetil. 1992. PMID: 1608603 Review. Hungarian.
The 90 kDa heat shock protein (hsp90) induces the condensation of the chromatin structure.
Csermely P, Kajtár J, Hollósi M, Oikarinen J, Somogyi J. Csermely P, et al. Biochem Biophys Res Commun. 1994 Aug 15;202(3):1657-63. doi: 10.1006/bbrc.1994.2124. Biochem Biophys Res Commun. 1994. PMID: 8060353
Demonstrating that hsp90 has an ATP binding site and autophosphorylating activity we have observed that histones, especially histone H1, are able to modulate the autophosphorylation of hsp90 [Csermely, P. and Kahn, C.R. (1991) J. Biol. Chem. 266, 4943-4950]. ...
Demonstrating that hsp90 has an ATP binding site and autophosphorylating activity we have observed that histones, especially histone H1, are …
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
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. …
Signalling and transport through the nuclear membrane.
Csermely P, Schnaider T, Szántó I. Csermely P, et al. Biochim Biophys Acta. 1995 Dec 20;1241(3):425-51. doi: 10.1016/0304-4157(95)00015-1. Biochim Biophys Acta. 1995. PMID: 8547304 Review. No abstract available.
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