Results 21 to 30 of about 14,744 (224)

Anti-cancer drugs targeting the NADH-binding site of VDAC rewire channel electrophysiology and partially suppress cation selectivity. [PDF]

FEBS J
VA molecules alter VDAC1 gating by increasing anion flow and reducing cation permeability. In cancer cells, which rely on ER‐mitochondria Ca2+ transfer and overexpress VDAC1, this imbalance triggers bioenergetic stress, ROS buildup, and mitochondrial collapse, leading to cell death.
Conti-Nibali S, Battiato G, Cubisino SAM, Arrigoni C, Lolicato M, Reina S, De Pinto V.   +6 more
europepmc   +2 more sources

Regulation of hexokinase binding to VDAC [PDF]

Journal of Bioenergetics and Biomembranes, 2008
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

Involvement of SIRT3 downstream targets ANT1, VDAC, CYPD, and Drp1 in a rat model of hepatic encephalopathy: Therapeutic role of thymoquinone [PDF]

Iranian Journal of Basic Medical Sciences
Objective(s): Hepatic encephalopathy (HE) is a brain disorder linked to hyperammonemia from liver injury. Elevated ammonia levels are known to impair mitochondrial function, the primary energy source for cells.
Somayeh Hajipour, Mohammad Amin Dehghani, Alireza Sarkaki, Masoud Mahdavinia, Seyedeh Parisa Navabi   +4 more
doaj   +1 more source

The Electrostatics of VDAC: Implications for Selectivity and Gating [PDF]

Journal of Molecular Biology, 2010
The voltage-dependent anion channel (VDAC) is the major pathway mediating the transfer of metabolites and ions across the mitochondrial outer membrane. Two hallmarks of the channel in the open state are high metabolite flux and anion selectivity, while the partially closed state blocks metabolites and is cation selective.
Choudhary, Om P., Ujwal, Rachna, Kowallis, William, Coalson, Rob, Abramson, Jeff, Grabe, Michael   +5 more
openaire   +3 more sources

VDAC, The early days

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2012
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

Using VDAC-Tubulin Interaction to Assess VDAC Orientation in the Mitochondrial Membrane [PDF]

Biophysical Journal, 2010
Recently we have found that dimeric αβ-tubulin at nanomolar concentrations induces reversible partial blockage of VDAC channel, reconstituted into a planar lipid membrane (Rostovtseva et al., PNAS 2008). Tubulin induces characteristic, well resolved fast blocking events with the highly voltage-dependent binding parameters. Tubulin interaction with VDAC
Rostovtseva, Tatiana K., Sheldon, Kely, Bezrukov, Sergey M.   +2 more
openaire   +1 more source

VDAC regulates AAC-mediated apoptosis and cytochrome c release in yeast [PDF]

, 2016
Mitochondrial outer membrane permeabilization is a key event in apoptosis processes leading to the release of lethal factors. We have previously shown that absence of the ADP/ATP carrier (AAC) proteins (yeast orthologues of mammalian ANT proteins ...
Côrte-Real, Manuela, Dário Trindade, Maria João Sousa, Sousa, Maria João, Manon, Stephen, Pereira, Clara Isabel Ferreira, Susana R. Chaves, Chaves, Susana Alexandra Rodrigues, Clara Pereira, Stéphen Manon, Manuela Côrte-Real, Trindade, Dario Alexandre Martins   +11 more
core   +1 more source

Concentration dependent ion selectivity in VDAC: a molecular dynamics simulation study. [PDF]

PLoS ONE, 2011
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, Fabrice Homblé, Martine Prévost   +2 more
doaj   +1 more source

Markov chain Monte Carlo based analysis of post-translationally modified VDAC1 gating kinetics

Frontiers in Physiology, 2015
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, Yifan eZhou, Bradley eOtto, Ranjan K. Dash, Wai-Meng eKwok, Daniel eBeard   +5 more
doaj   +1 more source

Phosphorylation of voltage-dependent anion channel by serine/threonine kinases governs its interaction with tubulin. [PDF]

PLoS ONE, 2011
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, Eduardo N Maldonado, John J Lemasters, Tatiana K Rostovtseva, Sergey M Bezrukov   +4 more
doaj   +1 more source