Ontology highlight
ABSTRACT:
SUBMITTER: Gibert B
PROVIDER: S-EPMC3251601 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Gibert Benjamin B Eckel Bénédicte B Fasquelle Lydie L Moulin Maryline M Bouhallier Frantz F Gonin Vincent V Mellier Gregory G Simon Stéphanie S Kretz-Remy Carole C Arrigo André-Patrick AP Diaz-Latoud Chantal C
PloS one 20120104 1
Hsp27 belongs to the heat shock protein family and displays chaperone properties in stress conditions by holding unfolded polypeptides, hence avoiding their inclination to aggregate. Hsp27 is often referenced as an anti-cancer therapeutic target, but apart from its well-described ability to interfere with different stresses and apoptotic processes, its role in non-stressed conditions is still not well defined. In the present study we report that three polypeptides (histone deacetylase HDAC6, tra ...[more]