a(CHEBI:novobiocin) directlyDecreases act(p(FPLX:HSP90))

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PubMed:21882945

Since this discovery, a number of high-affinity analogs, such as 17-AAG, and alternative synthetic scaffolds, including radicicol and PU-H71, have been reported (Figure 1) [85,88]. These compounds bind in either the N-terminal ATP-binding site (e.g., 17-AAG, radicicol and PU-H71) [89] or C-terminal dimerization domain (e.g., novobiocin and A4) [90,91], and they show great promise as both anticancer compounds and research tools for understanding Hsp90 biology

Related Edges 9

• a(CHEBI:novobiocin) directlyIncreases complex(a(CHEBI:novobiocin), p(INTERPRO:"HSP90, C-terminal domain"))
• a(CHEBI:radicicol) directlyIncreases complex(a(CHEBI:radicicol), p(INTERPRO:"Heat shock protein Hsp90, N-terminal"))
• a(CHEBI:radicicol) directlyDecreases act(p(FPLX:HSP90))
• a(CHEBI:tanespimycin) directlyIncreases complex(a(CHEBI:tanespimycin), p(INTERPRO:"Heat shock protein Hsp90, N-terminal"))
• a(CHEBI:tanespimycin) directlyDecreases act(p(FPLX:HSP90))
• a(PUBCHEM:501026) directlyIncreases complex(a(PUBCHEM:501026), p(INTERPRO:"HSP90, C-terminal domain"))
• a(PUBCHEM:501026) directlyDecreases act(p(FPLX:HSP90))
• a(PUBCHEM:9549213) directlyIncreases complex(a(PUBCHEM:9549213), p(INTERPRO:"Heat shock protein Hsp90, N-terminal"))
• a(PUBCHEM:9549213) directlyDecreases act(p(FPLX:HSP90))

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