Ontology highlight
ABSTRACT:
SUBMITTER: Tomasello MF
PROVIDER: S-EPMC3855671 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Tomasello Marianna F MF Guarino Francesca F Reina Simona S Messina Angela A De Pinto Vito V
PloS one 20131206 12
Voltage-Dependent Anion selective Channel maintains the permeability of the outer mitochondrial membrane and is relevant in bioenergetic metabolism and apoptosis. The structure of the protein was shown to be a β-barrel formed by 19 strands. The topology or sideness of the pore has been predicted with various approaches but a general consensus was never reached. This is an important issue since VDAC is considered receptor of Hexokinase and Bcl-2. We fused at VDAC1 C-terminus two tags separated by ...[more]