Researchers combine magnetic nanoparticles and HSP90 inhibitors for a promising new cancer therapy. This approach offers ...

The answer lies in the molecular chaperone heat shock protein 90 (Hsp90), according to a recent report in Current Biology. ...Hsp90 inhibitors could induce a switch from yeast to filamentous ...

Scientists at the Institute of Nano Science and Technology, Mohali, have developed a combination cancer therapy using 17-DMAG ...

The researchers also hypothesize that the treatment activates an immune response through cytokine secretion, further boosting ...

We determined the structure and function of Heat Shock Protein 90 (Hsp90), a molecular chaperone which is critical for the growth and survival of cancer cells. Photo: Jan Chlebik for the ICR We worked ...

The research team investigated the role of HSP90 -- a gene that is upregulated in response to heat stress. By inhibiting ...

The authors found that the expression of the chaperone protein Hsp90, which helps other proteins acquire their functional ...

They do so indirectly, by preventing the chaperone HSP90 from associating with the protein it is assisting (known as its client). In fact, these drugs are specifically HSP90 inhibitors.

From a structural view, chaperones represent a fascinating class of molecular machines that undergo dramatic structural changes, often by utilizing ATP chemical energy (for example, see conformational ...

There is evidence that lower doses may be equally effective, especially in patients with less severe edema. [10] If beneficial, neurological improvement can be expected within 48 h with this ...

On joining the ICR, Dr Clarke’s research focused on the molecular pharmacology of novel inhibitors of signal transduction in cancer, particularly on the discovery and development of HSP90 and PI3 ...

We recently discovered evidence that a signaling pathway involving the protein chaperone Hsp90, nitric oxide (NO), and cGMP negatively regulates the initiation of metamorphosis in sea urchin and ...