PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35420390-4 2022 In cells lacking Mlp1, the Hsp90 inhibitor radicicol was found to inhibit the Slt2-mediated catalytic activation of Rlm1, but not the noncatalytic activation of Swi4/Swi6. monorden 43-52 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 27-32 24970820-4 2014 Little synergy was found between the effects of rapamycin and the Hsp90 inhibitor radicicol on yeast growth. monorden 82-91 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 66-71 30612081-3 2019 We have isolated radicicol, an Hsp90 inhibitor, from a fungus occurring in the crevices of marble rocks of Central India. monorden 17-26 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 31-36 20661961-1 2010 A series of resorcylic acid macrolactones, analogues of the natural product radicicol has been prepared by chemical synthesis, and evaluated as inhibitors of heat shock protein 90 (Hsp90), an emerging attractive target for novel cancer therapeutic agents. monorden 76-85 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 158-179 20961859-1 2010 Resorcylic acid lactones are fungal polyketides that display diverse biological activities, with the potent Hsp90 inhibitor radicicol being an important representative member. monorden 124-133 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 108-113 24435512-0 2014 Synthesis of macrolactam analogues of radicicol and their binding to heat shock protein Hsp90. monorden 38-47 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 88-93 20661961-1 2010 A series of resorcylic acid macrolactones, analogues of the natural product radicicol has been prepared by chemical synthesis, and evaluated as inhibitors of heat shock protein 90 (Hsp90), an emerging attractive target for novel cancer therapeutic agents. monorden 76-85 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 181-186 20661961-4 2010 Co-crystallization of one of the new macrolactones with the N-terminal domain of yeast Hsp90 confirms that it binds in a similar way to the natural product radicicol and to our previous synthetic analogues, but that the introduction of the additional hydroxymethyl substituent appears to result in an unexpected change in conformation of the macrocyclic ring. monorden 156-165 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 87-92 20138026-8 2010 We have used this strain to demonstrate that significant levels of resistance to the Hsp90 inhibitors radicicol and 17-allylamino-demethoxygeldanamycin (17-AAG) are generated as a result of the same single point mutation within the native Hsp90 of yeast (A107N), the human Hsp90alpha (A121N) and the human Hsp90beta (A116N). monorden 102-111 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 85-90 20479121-4 2010 Hsp104"s tetratricopeptide repeat (TPR) interaction motif was dispensable for curing; however, cells expressing Sti1 defective in Hsp70 or Hsp90 interaction cured less efficiently, and the Hsp90 inhibitor radicicol abolished curing, implying that Sti1 acts in curing through Hsp70 and Hsp90 interactions. monorden 205-214 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 189-194 20479121-4 2010 Hsp104"s tetratricopeptide repeat (TPR) interaction motif was dispensable for curing; however, cells expressing Sti1 defective in Hsp70 or Hsp90 interaction cured less efficiently, and the Hsp90 inhibitor radicicol abolished curing, implying that Sti1 acts in curing through Hsp70 and Hsp90 interactions. monorden 205-214 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 189-194 20519952-2 2010 It is possible to selectively inhibit Hsp90 using natural products such as geldanamycin (GA) or radicicol (RD), which have served as prototypes for development of synthetic Hsp90 inhibitors. monorden 96-105 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 38-43 20519952-2 2010 It is possible to selectively inhibit Hsp90 using natural products such as geldanamycin (GA) or radicicol (RD), which have served as prototypes for development of synthetic Hsp90 inhibitors. monorden 96-105 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 173-178 20138026-8 2010 We have used this strain to demonstrate that significant levels of resistance to the Hsp90 inhibitors radicicol and 17-allylamino-demethoxygeldanamycin (17-AAG) are generated as a result of the same single point mutation within the native Hsp90 of yeast (A107N), the human Hsp90alpha (A121N) and the human Hsp90beta (A116N). monorden 102-111 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 239-244 19236053-2 2009 Highly selective Hsp90 inhibitors, including the natural antibiotics geldanamycin (GdA) and radicicol (RAD), inactivate this essential molecular chaperone by occupying its nucleotide binding site. monorden 92-101 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 17-22 19962400-4 2010 Radicicol, a direct inhibitor of heat shock protein 90 (Hsp90) and an indirect inhibitor of steroid hormone receptor signaling, was used to determine the functional utility of this yeast reporter system. monorden 0-9 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 33-54 19962400-4 2010 Radicicol, a direct inhibitor of heat shock protein 90 (Hsp90) and an indirect inhibitor of steroid hormone receptor signaling, was used to determine the functional utility of this yeast reporter system. monorden 0-9 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 56-61 19482409-0 2009 The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts. monorden 28-37 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 4-9 19482409-1 2009 We determine the binding mode of a macrocyclic radicicol-like oxime to yeast HSP90 by combining computer simulations and experimental measurements. monorden 47-56 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 77-82 19482409-6 2009 We find that the most likely binding mode of the oxime to yeast HSP90 is very similar to the known structure of the radicicol-HSP90 complex. monorden 116-125 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 64-69 19482409-6 2009 We find that the most likely binding mode of the oxime to yeast HSP90 is very similar to the known structure of the radicicol-HSP90 complex. monorden 116-125 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 126-131 17332351-6 2007 X-ray crystallographic structures of the NH(2)-terminal domain of yeast Hsp90 complexed with CCT018159 or its analogues showed binding properties similar to radicicol. monorden 157-166 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 72-77 15051534-4 2004 Inhibitors of HSP90 ATPase activity including the benzoquinone ansamycins, geldanamycin and 17-allylamino-17-demethoxygeldanamycin, and radicicol have been described. monorden 136-145 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 14-19 15051534-8 2004 The known HSP90 inhibitors geldanamycin and radicicol gave IC(50) values of 4.8 and 0.9 microM respectively, which compare with values found using the conventional coupled-enzyme assay. monorden 44-53 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 10-15 14622256-2 2003 The antibiotics geldanamycin and radicicol act as highly selective inhibitors of in vivo Hsp90 function through their ability to bind within the ADP/ATP binding pocket of the chaperone. monorden 33-42 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 89-94 18808717-8 2008 Treatment of the yeast with the specific HSP90 inhibitors geldanamycin and radicicol inhibited growth at 2 and 10 microM, respectively. monorden 75-84 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 41-46 17681020-7 2007 Remarkably, whereas expression of Hsp90beta as the sole Hsp90 of yeast rendered cells highly sensitive to the Hsp90 inhibitor radicicol, comparable expression of Hsp90alpha did not. monorden 126-135 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 34-39 17681020-7 2007 Remarkably, whereas expression of Hsp90beta as the sole Hsp90 of yeast rendered cells highly sensitive to the Hsp90 inhibitor radicicol, comparable expression of Hsp90alpha did not. monorden 126-135 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 56-61 16806077-3 2006 The use of this system for the identification and characterization of HIF-1 effectors was first validated by showing that two chemical Hsp90 inhibitors, geldanamycin and radicicol, impaired the activity of HIF-1 in yeast. monorden 170-179 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 135-140 16499313-0 2006 Search for Hsp90 inhibitors with potential anticancer activity: isolation and SAR studies of radicicol and monocillin I from two plant-associated fungi of the Sonoran desert. monorden 93-102 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 11-16 16499313-2 2006 Bioassay-guided fractionation of extracts active in these assays derived from Chaetomium chiversii and Paraphaeosphaeria quadriseptata furnished the Hsp90 inhibitors radicicol (1) and monocillin I (2), respectively. monorden 166-175 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 149-154 16499313-4 2006 Radicicol and monocillin I were also evaluated in a solid-phase competition assay for their ability to bind Hsp90 and to deplete cellular levels of two known Hsp90 client proteins with relevance to breast cancer, estrogen receptor (ER), and the type 1 insulin-like growth factor receptor (IGF-1R). monorden 0-9 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 108-113 16499313-4 2006 Radicicol and monocillin I were also evaluated in a solid-phase competition assay for their ability to bind Hsp90 and to deplete cellular levels of two known Hsp90 client proteins with relevance to breast cancer, estrogen receptor (ER), and the type 1 insulin-like growth factor receptor (IGF-1R). monorden 0-9 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 158-163 16499313-6 2006 Isolation of radicicol and monocillin I in this study provides evidence that we have developed an effective strategy for discovering natural product-based Hsp90 inhibitors with potential anticancer activity. monorden 13-22 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 155-160 12130680-4 2002 The antifungal antibiotic radicicol (Monorden) has been shown to bind to the Bergerat fold of HSP90 and to inhibit its ATPase activity. monorden 26-35 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 94-99 12130680-5 2002 The structural similarity between the Bergerat fold of HSP90 and bacterial two-component histidine kinases prompted our inquiry into whether radicicol could be a potential inhibitor of histidine kinase-like proteins. monorden 141-150 Hsp90 family chaperone HSP82 Saccharomyces cerevisiae S288C 55-60