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Review

Inhibitors of HSP90 and other chaperones for the treatment of cancer

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Pages 837-847 | Published online: 25 Feb 2005

Bibliography

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  • ••Overview and introduction to a series ofrecent articles, published within a special issue, that provide an up to date insight into the biology of HSP90 and the therapeutic potential of inhibitors of this molecular chaperone.
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  • •Commentary on [ll].
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  • ••A paper that has generated considerableinterest by providing an explanation for the therapeutic selectivity of the Hsp90 inhibitor 17AAG. The results show that the super-chaperone complexes that predominate in cancer but not normal cells exhibit markedly increased sensitivity to the drug compared to the uncomplexed chaperone.
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  • ••This paper illustrates the therapeuticpotential of HSP90 inhibitors in chronic myeloid leukaemia patients resistant to the Bcr-Abl inhibitor imatinib.
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  • ••Timely review of the development of17AAG.
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  • ••This paper and [43] provide a crystallographic explanation for the SAR of purine scaffold HSP90 inhibitors (see also [39]).
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  • ••This paper and [41] provide a crystallographic explanation for the SAR of purine scaffold Hsp90 inhibitors (see also [39]).
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  • ••First paper describing high-throughputscreening to identify HSP90 inhibitors, including CCT018159.
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  • ••Identification of the novel co-chaperoneAhal as a potent activator of the ATPase activity of HSP90.
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  • ••Ground breaking paper demonstrating thatHSP90 has the ability to buffer the effects of mutations, which are then expressed when HSP90 is inhibited. This has implications for developmental evolution and potentially for therapy.

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