Results 131 to 140 of about 8,482 (180)

Mitochondrial Calcium Signaling in Hepatocyte Health and Disease. [PDF]

open access: yesCold Spring Harb Perspect Biol
Eberhardt DR, Chaudhuri D.
europepmc   +1 more source

Glycerol Kinase 2 as a Metabolic Sentinel for Human Sperm Motility and Male Fertility. [PDF]

open access: yesBiomolecules
Oliveira JS   +4 more
europepmc   +1 more source

Quinidine partially blocks mitochondrial voltage-dependent anion channel (VDAC)

European Biophysics Journal, 2020
Quinidine is an antiarrhythmic drug commonly used for the treatment of cardiac ailments. It affects oxidative phosphorylation, calcium uptake, and ion channels of mitochondria. We have investigated the interaction of Quinidine and mitochondrial voltage-dependent anion channel (VDAC).
Chetan Malik, Subhendu Ghosh
openaire   +2 more sources

Voltage-Dependent Anion Channel (VDAC) in Health and Disease

2023
Abstract The voltage-dependent anion channel (VDAC) is recognized as the key metabolite pathway of water-soluble metabolites, small ions, and polypeptides across the outer mitochondrial membrane. The significance of this relatively simple β-barrel channel arises from its crucial position at the interface between the mitochondria and ...
Megha Rajendran   +2 more
openaire   +1 more source

Modulation of the Voltage-Dependent Anion Channel (VDAC) by Glutamate1

Journal of Bioenergetics and Biomembranes, 2000
The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is a large channel permeable to anions, cations, ATP, and other metabolites. VDAC was purified from sheep brain synaptosomes or rat liver mitochondria using a reactive red-agarose column, in addition to the hydroxyapatitate column.
Dan Gincel   +2 more
openaire   +2 more sources

Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC)

Journal of Bioenergetics and Biomembranes, 1992
Porin or voltage-dependent anion-selective channel (VDAC) is the main protein responsible for the high permeability of the outer mitochondrial membrane. The mitochondrial porin is mainly composed of sided beta-strands, in analogy with bacterial porin, whose structure has been resolved at 1.8 A resolution.
DE PINTO, Vito Nicola, PALMIERI F.
openaire   +3 more sources

Localisation and function of voltage-dependent anion channels (VDAC) in bovine spermatozoa

Pflügers Archiv - European Journal of Physiology, 2007
Sperm motility, regulation of cell volume, sperm capacitation, acrosome reaction and tight binding of spermatozoa to the zona pellucida are crucial events in the process of fertilisation. Voltage-dependent anion channels (VDAC) are highly conserved pore-forming proteins implicated in apoptosis, metabolite transport between mitochondria and cytosol ...
Xenia, Triphan   +6 more
openaire   +2 more sources

Structural Analysis of Murine Voltage Dependent Anion Channel (VDAC) 1

The FASEB Journal, 2006
VDAC is a mammalian integral protein expressed in the outer mitochondrial membrane. It has a bi‐functional role in mitochondrial biology: under physiological conditions, it transports nucleotides and small molecules across the outer membrane and
Rachna Ujwal   +6 more
openaire   +1 more source

Expression and localization of voltage-dependent anion channels (VDAC) in human spermatozoa

Biochemical and Biophysical Research Communications, 2009
Voltage-dependent anion channels (VDAC), also known as mitochondrial porins, are a group of proteins first identified in the mitochondrial outer membrane that are able to form hydrophilic pore structures. VDAC allow the passage of the metabolites across the mitochondrial outer membrane, and are involved in metabolite transport and signal transduction ...
Bianjiang, Liu   +3 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy