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
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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
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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
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Neuroactive Steroids: Receptor Interactions and Responses
Frontiers in Neurology, 2017 Neuroactive steroids (NASs) are naturally occurring steroids, which are synthesized centrally as de novo from cholesterol and are classified as pregnane, androstane, and sulfated neurosteroids (NSs).
Kald Beshir Tuem, Tesfay Mehari Atey
doaj +1 more source
Hexokinase II detachment from mitochondria triggers apoptosis through the permeability transition pore independent of voltage-dependent anion channels. [PDF]
PLoS ONE, 2008 Type II hexokinase is overexpressed in most neoplastic cells, and it mainly localizes on the outer mitochondrial membrane. Hexokinase II dissociation from mitochondria triggers apoptosis.
Federica Chiara +9 more
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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
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Protocol: optimised electrophyiological analysis of intact guard cells from arabidopsis [PDF]
, 2012 Genetic resources available for Arabidopsis thaliana make this species particularly attractive as a model for molecular genetic studies of guard cell homeostasis, transport and signalling, but this facility is not matched by accessible tools for ...
Blatt, M.R. +4 more
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Role of physiological ClC-1 Cl- ion channel regulation for the excitability and function of working skeletal muscle. [PDF]
, 2016 Electrical membrane properties of skeletal muscle fibers have been thoroughly studied over the last five to six decades. This has shown that muscle fibers from a wide range of species, including fish, amphibians, reptiles, birds, and mammals, are all ...
Chen, Tsung-Yu +4 more
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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
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Single-channel measurements of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli [PDF]
, 2012 NanC is an Escherichia coli outer membrane protein involved in sialic acid (Neu5Ac, i.e., N-acetylneuraminic acid) uptake. Expression of the NanC gene is induced and controlled by Neu5Ac. The transport mechanism of Neu5Ac is not known.
Eisenberg, Bob +4 more
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