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Details on Person Under non-stress conditions monomeric HSF1 is sequestered in...
| Class:Id | Summation:5324623 |
|---|---|
| _displayName | Under non-stress conditions monomeric HSF1 is sequestered in... |
| _timestamp | 2014-02-17 17:00:57 |
| created | [InstanceEdit:5324627] Shamovsky, V, 2014-02-17 |
| literatureReference | [LiteratureReference:4793647] Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex |
| text | Under non-stress conditions monomeric HSF1 is sequestered in a HSP90-containing heterocomplex. FKBP4 (immunophilin) is one of the components of HSP90-chaperone machinery which was found to associate with trimeric, but not monomeric form of HSF1 (Guo Y et al. 2001). Multichaperone complex of HSP90:FKBP4:PKGES3 has been shown to associate with HSF1 trimer through its regulatory domain, and this is thought to repress HSF1 transcriptional activity (Guo Y et al. 2001). |
| (summation) | [Reaction:5324617] HSP90:FKBP4:PTGES3 binds HSF1 trimer [Homo sapiens] |
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No pathways have been reviewed or authored by Under non-stress conditions monomeric HSF1 is sequestered in... (5324623)
