Non-phosphorylatable mutants of Ser184 lead to incomplete activation of Bax.

The S184 residue of Bax is the target of several protein kinases regulating cell fate, including AKT. It is well-established that, , the substitution of S184 by a non-phosphorylatable residue stimulates both the mitochondrial localization of Bax, cytochrome c release, and apoptosis. However, in experiments, substituted mutants did not exhibit any increase in their binding capacity to isolated mitochondria or liposomes.

A Critical Role for DLK and LZK in Axonal Repair in the Mammalian Spinal Cord.

The limited ability for axonal repair after spinal cord injury underlies long-term functional impairment. Dual leucine-zipper kinase [DLK; MAP kinase kinase kinase 12; MAP3K12] is an evolutionarily conserved MAP3K implicated in neuronal injury signaling from to mammals. However, whether DLK or its close homolog leucine zipper kinase (LZK; MAP3K13) regulates axonal repair in the mammalian spinal cord remains unknown.

The epidemiological status of African swine fever in domestic swine herds in the Tavush Province region, Armenia.

KEEN The factors associated with the spread and persistence of African swine fever (ASF) in the Caucasus region remain to be fully identified. It is assumed that large naive populations of domestic free-ranging and wild pigs are critical to disease transmission and maintenance. Nonetheless, 11 years since its epidemic introduction into the region in 2007, ASF virus (ASFV) is still circulating, suggesting that an endemic cycle has been established based on contact between free-ranging domestic pigs and wild pigs, and that native Ornithodoros ticks probably serve as reservoirs for the virus.

The substitution of Proline 168 favors Bax oligomerization and stimulates its interaction with LUVs and mitochondria.

Bax is a major player in the apoptotic process, being at the core of the mitochondria permeabilization events. In spite of the major recent advances in the knowledge of Bax organization within the membrane, the precise behavior of the C-terminal helix α9 remains elusive, since it was absent from the resolved structure of active Bax. The Proline 168 (P168) residue, located in the short loop between α8 and α9, has been the target of site-directed mutagenesis experiments, with conflicting results.