geldanamycin has been researched along with monorden* in 3 studies
3 other study(ies) available for geldanamycin and monorden
| Article | Year |
|---|---|
Study of marine natural products including resorcyclic acid lactones from Humicola fuscoatra that reactivate latent HIV-1 expression in an in vitro model of central memory CD4+ T cells.
An extract of Humicola fuscoatra (UCSC strain no. 108111A) was shown to reactivate latent HIV-1 expression in an in vitro model of central memory CD4+ T cells. We report the bioassay-guided isolation and structure determination of several resorcyclic acid lactones, including four known compounds, radicicol (1, aka. monorden) and pochonins B (2), C (3), and N (4), and three new analogues, radicicols B-D (5-7). Compounds 1-3 and 5 showed moderate activities in the memory T cell model of HIV-1 latency. Radicicol (1) displayed lower potency in reactivating latent HIV-1 (EC50 = 9.1 μM) relative to the HDAC inhibitors apicidin (EC50 = 0.3 μM), romidepsin (EC50 = 0.003 μM), and SAHA (EC50 = 0.6 μM); however, it achieved equivalent maximum efficacy relative to the positive control compounds (98% of SAHA and romidepsin). Topics: Ascomycota; Biological Products; CD4-Positive T-Lymphocytes; Histone Deacetylase Inhibitors; HIV Infections; HIV-1; Humans; Lactones; Macrolides; Marine Biology; Models, Biological; Molecular Structure; Virus Latency | 2014 |
Design, synthesis, and biological activity of bicyclic radester analogues as Hsp90 inhibitors.
Bicyclic radester analogues have been synthesized and evaluated for Hsp90 inhibitory activity. These analogues induce concentration-dependent degradation of Hsp90-dependent client proteins with the six-membered bicyclic analogues manifesting increased activity versus the five-membered counterparts. Topics: Antineoplastic Agents; Benzene Derivatives; Benzoquinones; Bridged Bicyclo Compounds; Cell Line, Tumor; Cell Proliferation; Drug Design; HSP90 Heat-Shock Proteins; Humans; Lactams, Macrocyclic; Macrolides; Protein Conformation | 2009 |
Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.
The cellular activity of several regulatory and signal transduction proteins, which depend on the Hsp90 molecular chaperone for folding, is markedly decreased by geldanamycin and by radicicol (monorden). We now show that these unrelated compounds both bind to the N-terminal ATP/ADP-binding domain of Hsp90, with radicicol displaying nanomolar affinity, and both inhibit the inherent ATPase activity of Hsp90 which is essential for its function in vivo. Crystal structure determinations of Hsp90 N-terminal domain complexes with geldanamycin and radicicol identify key aspects of their nucleotide mimicry and suggest a rational basis for the design of novel antichaperone drugs. Topics: Adenosine Diphosphate; Adenosine Triphosphatases; Antibiotics, Antineoplastic; Benzoquinones; Calorimetry; Crystallography, X-Ray; HSP90 Heat-Shock Proteins; Lactams, Macrocyclic; Lactones; Macrolides; Models, Molecular; Molecular Mimicry; Quinones; Structure-Activity Relationship | 1999 |