Modulation of the voltage-dependent anion channel (VDAC) by glutamate.

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

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Short-Term Effects of Nose-Only Cigarette Smoke Exposure on Glutathione Redox Homeostasis, Cytochrome P450 1A1/2 and Respiratory Enzyme Activities in Mice Tissues

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Synapsin I (protein I), a nerve terminal-specific phosphoprotein. III. Its association with synaptic vesicles studied in a highly purified synaptic vesicle preparation.

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Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins

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VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function

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Selectivity Changes in Site-Directed Mutants of the VDAC Ion Channel: Structural Implications

1990 • 269 citations

Regulation of Metabolite Flux through Voltage-Gating of VDAC Channels

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ATP Flux Is Controlled by a Voltage-gated Channel from the Mitochondrial Outer Membrane

1996 • 235 citations

NADH regulates the gating of VDAC, the mitochondrial outer membrane channel.

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The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion

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Toward the molecular structure of the mitochondrial channel, VDAC

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ATP Transport Through a Single Mitochondrial Channel, VDAC, Studied by Current Fluctuation Analysis

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The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin

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Cloning and in situ localization of a brain-derived porin that constitutes a large-conductance anion channel in astrocytic plasma membranes.

1994 • 139 citations

Beta-NADH decreases the permeability of the mitochondrial outer membrane to ADP by a factor of 6.

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VDAC/porin is present in sarcoplasmic reticulum from skeletal muscle

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Porin Is Present in the Plasma Membrane Where It Is Concentrated in Caveolae and Caveolae-related Domains

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Minireview: on the structure and gating mechanism of the mitochondrial channel, VDAC.

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A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues

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Ultrasteep voltage dependence in a membrane channel.

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Studies on Human Porin. VI. Production and Characterization of Eight Monoclonal Mouse Antibodies against the Human VDAC “Porin 31HL” and Their Application for Histotopological Studies in Human Skeletal Muscle

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Permeability properties of the porin of spinach leaf peroxisomes

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Chapter 4 Anion Channels in the Mitochondrial Outer Membrane

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The outer mitochondrial membrane channel, VDAC, is modulated by a protein localized in the intermembrane space

1993 • 58 citations

[16] Preparation and properties of brain mitochondria

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Conformational change in the mitochondrial channel, VDAC, detected by electron cryo-microscopy

1993 • 44 citations

Channel Active Mammalian Porin, Purified from Crude Membrane Fractions of Human B Lymphocytes and Bovine Skeletal Muscle, Reversibly Binds Adenosine Triphosphate (ATP)

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The Voltage-Gating Process of the Voltage-Dependent Anion Channel Is Sensitive to Ion Flow

1998 • 42 citations

Voltage-dependent anion channel proteins in synaptosomes of the torpedo electric organ: immunolocalization, purification, and characterization.

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Large conductance channel in plasma membranes of astrocytic cells is functionally related to mitochondrial VDAC-channels

1998 • 26 citations

Dicyclohexylcarbodiimide interaction with the voltage‐dependent anion channel from sarcoplasmic reticulum

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Diameter of the mammalian porin channel in open and "closed" states: direct measurement at the single channel level in planar lipid bilayer.

1996 • 16 citations

Studies on Human Porin XVI: Polyamines Reduce the Voltage Dependence of Human VDAC in Planar Lipid Bilayers—Spermine and Spermidine Inducing Asymmetric Voltage Gating on the Channel

1998 • 12 citations

Studies on Human Porin XVIII: The Multicompartment Effector Ruthenium Red Reduces the Voltage Dependence of Human VDAC in Planar Lipid Bilayers

1998 • 9 citations