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Issue 16, 2015
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C-terminal heat shock protein 90 modulators produce desirable oncogenic properties

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Abstract

The cellular protection mechanism, the heat shock response, is only activated by classical heat shock 90 inhibitors (Hsp90) that “target” the N-terminus of the protein, but not by those that modulate the C-terminus. Significant differences in cytotoxicity (nanomolar) for classical inhibitors versus their ability to modulate Hsp90 (low micromolar) are discussed. In contrast, molecules that modulate Hsp90's C-terminus show similar IC50 values for cytotoxicity and Hsp90 inhibition. A comparison between the two types of Hsp90 inhibitors suggests that classical inhibitors may be modulating an alternative biological target that stresses the cell rather directly inhibiting Hsp90, whereas C-terminal modulators are most likely acting by directly inhibiting Hsp90.

Graphical abstract: C-terminal heat shock protein 90 modulators produce desirable oncogenic properties

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Publication details

The article was received on 09 Jan 2015, accepted on 13 Feb 2015 and first published on 13 Feb 2015


Article type: Perspective
DOI: 10.1039/C5OB00044K
Author version available: Download Author version (PDF)
Citation: Org. Biomol. Chem., 2015,13, 4627-4631
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    C-terminal heat shock protein 90 modulators produce desirable oncogenic properties

    Y. Wang and S. R. McAlpine, Org. Biomol. Chem., 2015, 13, 4627
    DOI: 10.1039/C5OB00044K

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