Pub. Date : 1999 Jan 8
PMID : 9920768
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Proteasome inhibitors MG132 and lactacystin hyperphosphorylate HSF1 and induce hsp70 and hsp27 expression. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock transcription factor 1 | Homo sapiens |
| 2 | Proteasome inhibitors MG132 and lactacystin hyperphosphorylate HSF1 and induce hsp70 and hsp27 expression. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock protein family A (Hsp70) member 4 | Homo sapiens |
| 3 | Proteasome inhibitors MG132 and lactacystin hyperphosphorylate HSF1 and induce hsp70 and hsp27 expression. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock protein family B (small) member 1 | Homo sapiens |
| 4 | Since trimerization of HSF1 is known to precede the acquisition of HSF1-DNA binding activity, it seems that MG132- and lactacystin-induced hyperphosphorylation of HSF1 causes conformational changes of HSF1 molecules at 37 degreesC and subsequently triggers its trimerization. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock transcription factor 1 | Homo sapiens |
| 5 | Since trimerization of HSF1 is known to precede the acquisition of HSF1-DNA binding activity, it seems that MG132- and lactacystin-induced hyperphosphorylation of HSF1 causes conformational changes of HSF1 molecules at 37 degreesC and subsequently triggers its trimerization. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock transcription factor 1 | Homo sapiens |
| 6 | Since trimerization of HSF1 is known to precede the acquisition of HSF1-DNA binding activity, it seems that MG132- and lactacystin-induced hyperphosphorylation of HSF1 causes conformational changes of HSF1 molecules at 37 degreesC and subsequently triggers its trimerization. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock transcription factor 1 | Homo sapiens |
| 7 | Since trimerization of HSF1 is known to precede the acquisition of HSF1-DNA binding activity, it seems that MG132- and lactacystin-induced hyperphosphorylation of HSF1 causes conformational changes of HSF1 molecules at 37 degreesC and subsequently triggers its trimerization. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock transcription factor 1 | Homo sapiens |
| 8 | Inhibition of protein synthesis by cycloheximide abolished the MG132- or lactacystin-induced hyperphosphorylation and DNA-binding activity of HSF1. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock transcription factor 1 | Homo sapiens |
| 9 | These data suggest that the activity of a putative kinase(s) targeting HSF1 is upregulated in the presence of MG132 or lactacystin. | benzyloxycarbonylleucyl-leucyl-leucine aldehyde | heat shock transcription factor 1 | Homo sapiens |