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Csaba Söti

Showing results (1-10 of 7) with videos related to

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Neurochemistry International|September 6, 2002
Chaperones and aging: role in neurodegeneration and in other civilizational diseasesCsaba Söti, Péter Csermely
The Journal of Biological Chemistry|December 26, 2001
A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocketCsaba Söti, Attila Rácz, Péter Csermely
Experimental Gerontology|December 10, 2002
Chaperone function and chaperone overload in the aged. A preliminary analysisGábor Nardai, Péter Csermely, Csaba Söti
Advances in Experimental Medicine and Biology|January 9, 2007
Chaperones as parts of cellular networksPeter Csermely, Csaba Söti, Gregory L Blatch
Biofactors (Oxford, England)|August 5, 2003
Molecular chaperones, stress proteins and redox homeostasisEszter Papp, Gábor Nardai, Csaba Söti, et al.
Biochimica Et Biophysica Acta|February 19, 2008
Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 bindingSheril Daniel, Graeme Bradley, Victoria M Longshaw, et al.
The FEBS Journal|August 8, 2007
Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicolStefan H Millson, Andrew W Truman, Attila Rácz, et al.
Pageof 1

Showing results (1-10 of 7) with videos related to

Sort By:
Pageof 1
Neurochemistry International|September 6, 2002
Chaperones and aging: role in neurodegeneration and in other civilizational diseasesCsaba Söti, Péter Csermely
The Journal of Biological Chemistry|December 26, 2001
A Nucleotide-dependent molecular switch controls ATP binding at the C-terminal domain of Hsp90. N-terminal nucleotide binding unmasks a C-terminal binding pocketCsaba Söti, Attila Rácz, Péter Csermely
Experimental Gerontology|December 10, 2002
Chaperone function and chaperone overload in the aged. A preliminary analysisGábor Nardai, Péter Csermely, Csaba Söti
Advances in Experimental Medicine and Biology|January 9, 2007
Chaperones as parts of cellular networksPeter Csermely, Csaba Söti, Gregory L Blatch
Biofactors (Oxford, England)|August 5, 2003
Molecular chaperones, stress proteins and redox homeostasisEszter Papp, Gábor Nardai, Csaba Söti, et al.
Biochimica Et Biophysica Acta|February 19, 2008
Nuclear translocation of the phosphoprotein Hop (Hsp70/Hsp90 organizing protein) occurs under heat shock, and its proposed nuclear localization signal is involved in Hsp90 bindingSheril Daniel, Graeme Bradley, Victoria M Longshaw, et al.
The FEBS Journal|August 8, 2007
Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicolStefan H Millson, Andrew W Truman, Attila Rácz, et al.
Pageof 1