Oops!
https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | The small heat shock proteins of vertebrates are thought to play a major role in the cellular response to stress, and appear to play a role in a range of other physiological activities. Indeed, in response to many forms of stress, including heat, the expression of heat shock proteins is increased, and coincidentally these cells become more stress-resistant. One of these proteins is Heat Shock Protein (hsp) 27, for which 3 hypotheses currently exist to explain its mechanism of action: (i) it has chaperone-like activity, serving as a site where denatured, unfolding proteins can bind until hsp70-dependent refolding can occur; (ii) it stabilises microfilaments, strengthening the cytoskeleton; and (iii) it enhances levels of the cellular antioxidant glutathione []. It was hypothesised that hsp27 associates with different protein partners in order to effect its various cellular functions. Thus, a yeast two-hybrid screen was performed on a rat Sertoli cell cDNA library, which identified a novel binding protein, termed HSPB1-associated protein 1 or Protein Associated with Small Stress protein 1. | Name | HSPB1-associated protein 1 |
| Short Name | HSPB1-associated_protein_1 | Type | Family |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
