a(CHEBI:geldanamycin)

Entity

Name

geldanamycin

Namespace

chebi

Namespace Version

20180906

Namespace URL

https://raw.githubusercontent.com/pharmacome/terminology/b46b65c3da259b6e86026514dfececab7c22a11b/external/chebi-names.belns

One strategy is to directly activate HSF1, thereby increasing the expression of multiple molecular chaperones simultaneously. This approach has been traditionally achieved by inhibition of HSP90 with compounds that bind the N-terminal ATP-binding pocket, such as radicicol, geldanamycin, or 17-AAG (64, 132–134). PubMed:25784053

Among compounds that inhibit HSP90, geldanamycin promoted elimination of both hyper- phosphorylated tau and oligomeric α-synuclein in cell lines 219,220 . PubMed:30116051

Among compounds that inhibit HSP90, geldanamycin promoted elimination of both hyper- phosphorylated tau and oligomeric α-synuclein in cell lines 219,220 . PubMed:30116051

Among compounds that inhibit HSP90, geldanamycin promoted elimination of both hyper- phosphorylated tau and oligomeric α-synuclein in cell lines 219,220 . PubMed:30116051

In CHO cells overexpressing P301L mutant tau, treatment with the Hsp90 inhibitor geldanamycin led to a more pronounced proteasome-mediated reduction in tau phosphorylated at proline-directed S/T sites compared to total tau (67). PubMed:24027553

For example, the Hsp90 inhibitor geldanamycin mimics ADP binding, but also inhibits recruitment of p23, which is a necessary step in client maturation [145]. PubMed:21882945

For example, the Hsp90 inhibitor geldanamycin mimics ADP binding, but also inhibits recruitment of p23, which is a necessary step in client maturation [145]. PubMed:21882945

Work on Hsp90 inhibitors benefited from the early discovery of the natural product, geldanamycin, which competes with ATP and induces destabilization of Hsp90-bound proteins [87] PubMed:21882945

For exam- ple, small molecules (e.g., geldanamycin) that activate heat shock factor 1, the main transcrip- tional regulator of the cytosolic stress response, increase the effective concentration of cytosolic chaperones and suppress the aggregation of various disease proteins (8, 38, 228–230). PubMed:23746257