Erastin Disrupts Mitochondrial Permeability Transition Pore (mPTP) and Induces Apoptotic Death of Colorectal Cancer Cells. [PDF]
PLoS ONE, 2016 We here evaluated the potential anti-colorectal cancer activity by erastin, a voltage-dependent anion channel (VDAC)-binding compound. Our in vitro studies showed that erastin exerted potent cytotoxic effects against multiple human colorectal cancer cell
Haizhong Huo +5 more
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Cell-free electrophysiology of human VDACs incorporated into nanodiscs: An improved method
Biophysical Reports, 2021 Voltage-dependent anion-selective channel (VDAC) is one of the main proteins of the outer mitochondrial membrane of all eukaryotes, where it forms aqueous, voltage-sensitive, and ion-selective channels.
Stefano Conti Nibali +5 more
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Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase
Nature Communications, 2023 Mitochondria are double-membrane-bounded organelles that depend critically on phospholipids supplied by the endoplasmic reticulum. These lipids must cross the outer membrane to support mitochondrial function, but how they do this is unclear.
Helene Jahn +6 more
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The proapoptotic protein BNIP3 interacts with VDAC to induce mitochondrial release of endonuclease G. [PDF]
PLoS ONE, 2014 BNIP3 is a proapoptotic protein that induces cell death through a mitochondria-mediated pathway. We reported previously that mitochondrial localization of BNIP3 and translocation of EndoG from mitochondria to the nucleus are critical steps of the BNIP3 ...
Xiaosha Zhang, Xiuwu Bian, Jiming Kong
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Modulation of the mitochondrial voltage dependent anion channel (VDAC) by curcumin
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2015 Voltage dependent anion channel (VDAC) of mitochondria plays a crucial role in apoptosis. Human VDAC-1, reconstituted in planar lipid bilayer showed reduced conductance when treated with curcumin. Curcumin interacts with residues in the α helical N-terminus of VDAC and in the channel wall, as revealed by molecular docking, followed by mutational ...
TEWARI, D +6 more
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Frontiers in Oncology, 2017 The voltage-dependent anion channel (VDAC) is well known as the pathway for passive diffusion of anionic hydrophilic mitochondrial metabolites across the outer membrane, but a more complex functionality of the three isoforms of VDAC has emerged, as ...
John J. Lemasters, John J. Lemasters
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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 +5 more
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Tubulin βII and βIII Isoforms as the Regulators of VDAC Channel Permeability in Health and Disease
Cells, 2019 In recent decades, there have been several models describing the relationships between the cytoskeleton and the bioenergetic function of the cell. The main player in these models is the voltage-dependent anion channel (VDAC), located in the mitochondrial
Marju Puurand +6 more
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Precocene II, a Trichothecene Production Inhibitor, Binds to Voltage-Dependent Anion Channel and Increases the Superoxide Level in Mitochondria of Fusarium graminearum. [PDF]
PLoS ONE, 2015 Precocene II, a constituent of essential oils, shows antijuvenile hormone activity in insects and inhibits trichothecene production in fungi. We investigated the molecular mechanism by which precocene II inhibits trichothecene production in Fusarium ...
Tomohiro Furukawa +5 more
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Voltage Dependent Anion Channels (VDAC) and Regulation of Mitochondrial Metabolism [PDF]
Biophysical Journal, 2015 Voltage dependent anion channels (VDAC) are responsible for permeability of mitochondrial outer membranes to hydrophilic metabolites like ATP, ADP and respiratory substrates. Although previously assumed to remain open, VDAC closure is emerging as an important mechanism for regulation of global mitochondrial function. Acetaldehyde formation from hepatic
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