A pore is a pore is a pore (or a hub?): VDAC oligomerization in mitochondrial connectivity and modulation. [PDF]
De Pinto V +3 more
europepmc +1 more source
Anti-cancer drugs targeting the NADH-binding site of VDAC rewire channel electrophysiology and partially suppress cation selectivity. [PDF]
Conti-Nibali S +6 more
europepmc +1 more source
Three mammalian VDAC isoforms distinctly regulate mitochondrial function and proteome to maintain cell metabolism. [PDF]
Rajendran M +11 more
europepmc +1 more source
Small-Molecule Targeting of VDAC Disrupts Mitochondrial Bioenergetics and Suppresses Melanoma Cell Survival and Migration. [PDF]
Ye ZW +7 more
europepmc +1 more source
Revealing Molecular Coupling between Anion Selectivity and Structural Transitions in Voltage-Dependent Anion Channel (VDAC) [PDF]
Van Ngo +3 more
openaire +1 more source
Targeting ST18-mediated pathomechanism in pemphigus vulgaris through voltage-dependent anion channel inhibition. [PDF]
Assaf S +13 more
europepmc +1 more source
The voltage-dependent anion channel (VDAC) binds tissue-type plasminogen activator and promotes activation of plasminogen on the cell surface. [PDF]
Gonzalez-Gronow M +3 more
europepmc +1 more source
Mitochondrial voltage-dependent anion-selective channel (VDAC): a global player in cells.
Mitochondria are primary ATP producing organelles and are involved in many cellular signalling pathways. Mitochondrial porin, which forms voltage-dependent anion-selective channels (VDAC) in the mitochondrial outer membrane (MOM), can be folded into a 19 β-stranded barrel.
openaire +1 more source
The N-terminal α helix domain of the mitochondrial VDAC protein Por2 is dispensable for promoting the nuclear localization of yeast AMPK. [PDF]
Brown K +3 more
europepmc +1 more source

