Concentration dependent ion selectivity in VDAC: a molecular dynamics simulation study. [PDF]
The voltage-dependent anion channel (VDAC) forms the major pore in the outer mitochondrial membrane. Its high conducting open state features a moderate anion selectivity.
Eva-Maria Krammer +2 more
doaj +1 more source
TSPO: kaleidoscopic 18-kDa amid biochemical pharmacology, control and targeting of mitochondria [PDF]
The 18-kDa translocator protein (TSPO) localizes in the outer mitochondrial membrane (OMM) of cells and is readily up-regulated under various pathological conditions such as cancer, inflammation, mechanical lesions and neurological diseases. Able to bind
Aghazadeh +189 more
core +1 more source
Markov chain Monte Carlo based analysis of post-translationally modified VDAC1 gating kinetics
The voltage-dependent anion channel (VDAC) is the main conduit for permeation of solutes (including nucleotides and metabolites) of up to 5 kDa across the mitochondrial outer membrane (MOM). Recent studies suggest that VDAC activity is regulated via post-
Shivendra eTewari +5 more
doaj +1 more source
Targeting the Multiple Physiologic Roles of VDAC With Steroids and Hydrophobic Drugs
There is accumulating evidence that endogenous steroids and non-polar drugs are involved in the regulation of mitochondrial physiology. Many of these hydrophobic compounds interact with the Voltage Dependent Anion Channel (VDAC).
Tatiana K. Rostovtseva +3 more
doaj +1 more source
Phosphorylation of voltage-dependent anion channel by serine/threonine kinases governs its interaction with tubulin. [PDF]
Tubulin was recently found to be a uniquely potent regulator of the voltage-dependent anion channel (VDAC), the most abundant channel of the mitochondrial outer membrane, which constitutes a major pathway for ATP/ADP and other metabolites across this ...
Kely L Sheldon +4 more
doaj +1 more source
Photoaffinity labeling with cholesterol analogues precisely maps a cholesterol-binding site in voltage-dependent anion channel-1 [PDF]
Voltage-dependent anion channel-1 (VDAC1) is a highly regulated β-barrel membrane protein that mediates transport of ions and metabolites between the mitochondria and cytosol of the cell.
Abramson, Jeff +10 more
core +3 more sources
Mitochondria critically regulate a range of cellular processes including bioenergetics, cellular metabolism, apoptosis, and cellular Ca2+ signaling. The voltage-dependent anion channel (VDAC) functions as a passageway for the exchange of ions, including ...
Hirohito Shimizu +11 more
doaj +1 more source
VDAC is now universally accepted as the channel in the mitochondrial outer membrane responsible for metabolite flux in and out of mitochondria. Its discovery occurred over two independent lines of investigation in the 1970s and 80s. This retrospective article describes the history of VDAC's discovery and how these lines merged in a collaboration by the
Colombini, Marco, Mannella, Carmen A.
openaire +2 more sources
Regulation of hexokinase binding to VDAC [PDF]
Hexokinase isoforms I and II bind to mitochondrial outer membranes in large part by interacting with the outer membrane voltage-dependent anion channel (VDAC). This interaction results in a shift in the susceptibility of mitochondria to pro-apoptotic signals that are mediated through Bcl2-family proteins. The upregulation of hexokinase II expression in
John G, Pastorino, Jan B, Hoek
openaire +2 more sources
Voltage-dependent anion channels mediated apoptosis in refractory epilepsy
The purpose of this study was to investigate the role of voltage-dependent anion channel (VDAC) in mitochondria-mediated apoptosis of neurons in refractory epilepsy. Western blot analyses were carried out to detect the changes in cytochrome C, caspase 9,
Zhao Yan +4 more
doaj +1 more source

