Roles of heat shock factor 1 and 2 in response to proteasome inhibition: consequence on p53 stability (Q84292343)

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3 February 2020

title

Roles of heat shock factor 1 and 2 in response to proteasome inhibition: consequence on p53 stability (English)

1 reference

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3 February 2020

author name string

S Lecomte

1

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3 February 2020

F Desmots

2

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3 February 2020

F Le Masson

3

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3 February 2020

P Le Goff

4

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3 February 2020

D Michel

5

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3 February 2020

E S Christians

6

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3 February 2020

Y Le Dréan

7

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publication date

24 May 2010

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3 February 2020

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3 February 2020

volume

29

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3 February 2020

issue

29

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3 February 2020

page(s)

4216-4224

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https://scigraph.springernature.com/pub.10.1038/onc.2010.171

3 February 2020

exact match

0 references

cites work

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Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome

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Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways

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Hsp27 negatively regulates cell death by interacting with cytochrome c.

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Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance

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Sensitivity of tumor cells to proteasome inhibitors is associated with expression levels and composition of proteasome subunits

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Cell-type specific regulation of gene expression by simian virus 40 T antigens

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Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis

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The oncoprotein gankyrin binds to MDM2/HDM2, enhancing ubiquitylation and degradation of p53

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Demyelination, astrogliosis, and accumulation of ubiquitinated proteins, hallmarks of CNS disease in hsf1-deficient mice.

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Heat shock factor 1 deficiency via its downstream target gene alphaB-crystallin (Hspb5) impairs p53 degradation

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Proteasome inhibition leads to the activation of all members of the heat-shock-factor family

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Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates

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Selection of new HSF1 and HSF2 DNA-binding sites reveals difference in trimer cooperativity

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Up-regulation of the clusterin gene after proteotoxic stress: implication of HSF1-HSF2 heterocomplexes.

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Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis.

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Heat shock transcription factor 2 is not essential for embryonic development, fertility, or adult cognitive and psychomotor function in mice

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Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes

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Heat Shock Factor 2 (HSF2) Contributes to Inducible Expression ofhspGenes through Interplay with HSF1

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Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: therapeutic approaches

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Heterotrimerization of heat-shock factors 1 and 2 provides a transcriptional switch in response to distinct stimuli.

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