Stressed-Out Endoplasmic Reticulum Inflames the Mitochondria.
Philadelphia, United States. In Immunity, Oct 2015
(2015) show that during Brucella abortus infection, an endoplasmic reticulum stress sensor, IRE1α, initiates NLRP3- and caspase-2-mediated mitochondrial damage that potentiates NLRP3 inflammasome assembly.
Poly(ADP-ribose) in the bone: from oxidative stress signal to structural element.
Debrecen, Hungary. In Free Radic Biol Med, May 2015
In the past decades numerous studies demonstrating production of reactive oxygen or nitrogen intermediates, effects of different antioxidants, and involvement of prototypical redox control mechanisms (Nrf2-Keap1, Steap4, FoxO, PAMM, caspase-2) have proven the central role of redox regulation in the bone.
Caspase-2: the reinvented enzyme.
Stockholm, Sweden. In Oncogene, May 2015
On the basis of evidences that caspase-2 gene targeting in several generated mouse models accelerates tumor formation, this enzyme was recently implicated in tumor suppression.
Caspase-2 as a tumour suppressor.
Adelaide, Australia. In Cell Death Differ, 2013
Ever since its discovery 20 years ago, caspase-2 has been enigmatic and its function somewhat controversial.
[Caspase-2: what do we know today?].
In Mol Biol (mosk), 2013
This review is focused on various mechanisms of signal transduction through caspase-2 which believed to be one of the most enigmatical protease involved in apoptosis.
Meeting the (N-terminal) end with acetylation.
Durham, United States. In Cell, 2011
In this issue, Yi et al. (2011) introduce a mechanism by which Bcl-xL lowers the threshold for apoptosis by suppressing acetyl-CoA production, which, in turn, suppresses the N-alpha-acetylation important for activation of the proapoptotic protease caspase-2.