Results 21 to 30 of about 71,736 (190)
Flexibility of the N-Terminal mVDAC1 Segment Controls the Channel’s Gating Behavior [PDF]
, 2012 Since the solution of the molecular structures of members of the voltage dependent anion channels (VDACs), the N-terminal α-helix has been the main focus of attention, since its strategic location, in combination with its putative conformational ...
Anastasia Salisowski +8 more
core +6 more sources
Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions
Frontiers in Physiology, 2021 Mitochondrial porins, also known as voltage-dependent anion selective channels (VDACs), are pore-forming molecules of the outer mitochondrial membranes, involved in the regulation of metabolic flux between cytosol and mitochondria.
Maria Carmela Di Rosa +7 more
doaj +1 more source
Tumor Biology, 2020 The exchange of metabolites between mitochondria and cytosol occurs through pores formed by voltage-dependent anion channel proteins. Voltage-dependent anion channels appear to be master regulators of mitochondrial bioenergetics and the intracellular ...
Paweł Jóźwiak +8 more
doaj +1 more source
A Lipid Bilayer Formed on a Hydrogel Bead for Single Ion Channel Recordings
Micromachines, 2020 Ion channel proteins play important roles in various cell functions, making them attractive drug targets. Artificial lipid bilayer recording is a technique used to measure the ion transport activities of channel proteins with high sensitivity and ...
Minako Hirano +6 more
doaj +1 more source
A 3D model of the voltage‐dependent anion channel (VDAC) [PDF]
FEBS Letters, 2002 Eukaryotic porins are a group of membrane proteins whose best known role is to form an aqueous pore channel in the mitochondrial outer membrane. As opposed to the bacterial porins (a large family of protein whose 3D structure has been determined by X‐ray diffraction), the structure of eukaryotic porins (also termed VDACs, voltage‐dependent anion ...
Casadio, Rita +3 more
openaire +4 more sources
Voltage-Dependent Anion Channel-1, a Possible Ligand of Plasminogen Kringle 5. [PDF]
PLoS ONE, 2016 Kringle 5, the fifth fragment of plasminogen, is known to be important for inhibiting the proliferation and migration of vascular endothelial cell (VEC), while not having any effects on normal endothelial cells.
Yin-Ku Liang, Liu-Jiao Bian
doaj +1 more source
Nucleotide Interactions of the Human Voltage-dependent Anion Channel [PDF]
Journal of Biological Chemistry, 2014 The voltage-dependent anion channel (VDAC) mediates and gates the flux of metabolites and ions across the outer mitochondrial membrane and is a key player in cellular metabolism and apoptosis. Here we characterized the binding of nucleotides to human VDAC1 (hVDAC1) on a single-residue level using NMR spectroscopy and site-directed mutagenesis.
Saskia Villinger +6 more
openaire +4 more sources
Hydrogen sulphide regulates inward-rectifying K+ channels in conjunction with stomatal closure [PDF]
, 2015 Hydrogen sulphide (H2S) is the third biological gasotransmitter and, in animals, affects many physiological processes by modulating ion channels. H2S has been reported to protect plants from oxidative stress in diverse physiological responses. H2S closes
Blatt, Mike R. +3 more
core +2 more sources
VDAC: Voltage Dependant Anion Channel
The FASEB Journal, 2011 VDAC (Voltage Dependent Anion Channel) is a channel protein located on the outer mitochondrial membrane. It regulates mitochondria functions and cell respiration through the exchange of molecules between the cytoplasm and the organelle, such as ADP, ATP, anions, cations, and other small, hydrophilic molecules.
Patrick Jordan +18 more
openaire +1 more source
Subcellular Localization of Human Voltage-dependent Anion Channel Isoforms [PDF]
Journal of Biological Chemistry, 1995 The voltage-dependent anion channel of the outer mitochondrial membrane, VDAC (also known as mitochondrial porin), is a small abundant protein which forms a voltage-gated pore when incorporated into planar lipid bilayers. This protein forms the primary pathway for movement of major metabolites through the outer membrane.
W H, Yu, W, Wolfgang, M, Forte
openaire +2 more sources