Pages that link to "Q39956199"
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The following pages link to Xenopus small heat shock proteins, Hsp30C and Hsp30D, maintain heat- and chemically denatured luciferase in a folding-competent state (Q39956199):
Displaying 8 items.
- The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro (Q24300223) (← links)
- The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10 (Q24563241) (← links)
- Withaferin A induces proteasome inhibition, endoplasmic reticulum stress, the heat shock response and acquisition of thermotolerance (Q34316709) (← links)
- Differences in the chaperone-like activities of the four main small heat shock proteins of Drosophila melanogaster (Q34446489) (← links)
- Proteasome inhibition induces hsp30 and hsp70 gene expression as well as the acquisition of thermotolerance in Xenopus laevis A6 cells (Q39786119) (← links)
- The microtubule-associated protein, NUD-1, exhibits chaperone activity in vitro (Q43140307) (← links)
- Mutation or deletion of the C-terminal tail affects the function and structure of Xenopus laevis small heat shock protein, hsp30. (Q44132288) (← links)
- Phosphorylation-dependent structural alterations in the small hsp30 chaperone are associated with cellular recovery. (Q44442854) (← links)