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VDAC2 encodes a member of the voltage-dependent anion channel pore-forming family of proteins that are considered the main pathway for metabolite diffusion across the mitochondrial outer membrane. Additionally we are shipping VDAC2 Antibodies (70) and many more products for this protein.
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The works available on VDAC cysteines support the notion that VDAC1, VDAC2, and VDAC3 proteins are paralogs with a similar pore-function and slightly different, but important, ancillary biological functions. (Review)
The evolutionary demand for the NTE (show PNPLA6 Proteins) in the presence of cysteines clearly emerges from our biochemical and functional studies, providing insight into factors that functionally demarcate hVDAC-2 from the other VDACs.
Motifs of VDAC2 required for mitochondrial Bak (show BAK1 Proteins) import and tBid-induced apoptosis.
Results show that in thyroid tumours and cell lines, VDAC2 is upregulated and BAK1 (show BAK1 Proteins) downregulated. Also, transient knockdown of VDAC2 promoted upregulation of the BAK1 (show BAK1 Proteins) expression, and increased susceptibility to sorafenib treatment.
These data suggest that an interaction between Mcl-1 (show MCL1 Proteins) and VDAC promotes lung cancer cell migration by a mechanism that involves Ca(2 (show CA2 Proteins)+)-dependent reactive oxygen species production.
RACK1 (show GNB2L1 Proteins) plays an antiapoptotic role during IBDV infection via interaction with VDAC2 and VP5.
GSK-3beta translocates from the cytosol to mitochondria in a kinase activity- and VDAC2-dependent manner in which an N-terminal domain of GSK-3beta may function as a mitochondrial targeting sequence
Cysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial beta-barrel anion channel VDAC-2.
minor conformational variations in local residues are sufficient to define the membrane protein dynamics in hVDAC-2.
The reconstitution of functional VDAC-2 in lauryldimethylamine-oxide (LDAO) detergent micelles and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) lipid bilayer nanodiscs, is reported.
an important MYBL2 (show MYBL2 Proteins)-VDAC2-BECN1 (show BECN1 Proteins)-BCL2L1 (show BCL2L1 Proteins) pathway linking autophagy suppression in the developing ovary, is reported.
Bax (show BAX Proteins) localizes to the mitochondrial outer membrane via alternate mechanisms, either constitutively via an interaction with VDAC2 or after activation via interaction with Bcl-2 (show BCL2 Proteins) family proteins.
Bcl-xL (show BCL2L1 Proteins) interacts functionally with VDAC1 (show VDAC1 Proteins) and -3 but not VDAC2.
VDAC2 acts as a crucial component in mitochondrial apoptosis by allowing the mitochondrial recruitment of BAK (show BAK1 Proteins), thereby controlling tBID-induced OMM permeabilization and cell death.
VDAC2 regulates the activity of BAK (show BAK1 Proteins) and provides a connection between mitochondrial physiology and the core apoptotic pathway
Vdacs are dispensable for both MPT and Bcl-2 (show BCL2 Proteins) family member-driven cell death.
Genetic depletion of Vdac2 in the thymus resulted in excessive cell death & hypersensitivity to diverse death stimuli including engagement of the T cell receptor. The VDAC2-BAK (show BAK1 Proteins) axis governs the homeostasis of thymocytes.
ENO1 (show ENO1 Proteins), VDAC2, and UQCRC2 (show UQCRC2 Proteins) were significantly correlated with individual fertility in bulls.
Results describe the expression of voltage-dependent anion channel isoforms in rat, bovine, and chicken brain mitochondria, and suggest that the nature of hexokinase binding site is not determined by the expression of a single VDAC isoform.
VDAC2 and VDAC3 might have an alternative structural organization and different functions in outer dense fibers (show ODF1 Proteins) than in mitochondria
Confirm the localisation of VDAC2 in the acrosomal region of bovine spermatozoa using immunoelectron microscopy.
The present study is the first work to report the purification and characterization of VDAC2 from a mammalian tissue.
These findings demonstrate a critical modulatory role for VDAC2-dependent mitochondrial Ca(2 (show CA2 Proteins)+) uptake in the regulation of cardiac rhythmicity.
Data indicate the structure of voltage-dependent anion channel 2 zfVDAC2 at 2.8 A resolution, revealing a crystallographic dimer.
Data confirm the synthesis of VDAC1 (show VDAC1 Proteins) and 2 subtypes in GV (germinal vesicle) and MII (meiosis II) stage porcine oocytes as well as their protein expression.
AtVDAC2 has a main function in mitochondria
VDAC2 and VDAC4 are important for leaf development, the mitochondrial membrane potential, and pollen development.
This gene encodes a member of the voltage-dependent anion channel pore-forming family of proteins that are considered the main pathway for metabolite diffusion across the mitochondrial outer membrane. The encoded protein is also thought to be involved in the mitochondrial apoptotic pathway via regulation of BCL2-antagonist/killer 1 protein activity. Pseudogenes have been identified on chromosomes 1, 2, 12 and 21, and alternative splicing results in multiple transcript variants.
outer mitochondrial membrane protein porin 2
, voltage-dependent anion-selective channel protein 2
, voltage-dependent anion-selective channel protein 6
, voltage-dependent anion channel 2
, outer mitochondrial membrane protein porin