André-Patrick Arrigo

TL;DR: Hsp27 binds to cytochrome c released from the mitochondria to the cytosol and prevents cy tochrome-c-mediated interaction of Apaf-1 with procaspase-9, which interferes specifically with the mitochondrial pathway of caspases-dependent cell death.

TL;DR: It is demonstrated that large oligomers of sHsps are necessary for chaperone action and resistance against oxidative stress whereas phosphorylation down-regulates these activities by dissociation of s Hsps complexes to tetramers.

TL;DR: It is shown that constitutive expression of human heat shock protein (hsp)27 in murine L929 cells blocks Fas/APO-1-mediated cell death and that the expression of small stress proteins from different species, such as human hsp 27, Drosophila Dhsp27, or human αB-crystallin, confers resistance to apoptotic cell death induced by staurosporine, a protein kinase C inhibitor.

TL;DR: The results suggest that the protective activity shared by human hsp27, Drosophila hsp 27 and human alphaB‐crystallin against TNFalpha‐mediated cell death and probably other types of oxidative stress results from their conserved ability to raise the intracellular concentration of glutathione.

TL;DR: This review is focused on the recent knowledge concerning some eukaryotic transcription factors, whose activation and DNA binding is controlled by the thiol redox status of the cell.