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VDAC1 encodes a voltage-dependent anion channel protein that is a major component of the outer mitochondrial membrane. Additionally we are shipping VDAC1 Antibodies (190) and VDAC1 Kits (20) and many more products for this protein.
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Abnormal ovules in the process of female gametogenesis were observed. Both mitochondrial transmembrane potential and ATP synthesis rate were obviously reduced in the mitochondria isolated from atvdac1 plants.
Data indicate that both voltage-dependent anion channel 1 (AtVDAC1) and calcium sensor CBL1 regulate cold stress responses during seed germination and plant development.
AtVDAC1 has a main function in mitochondria
VDAC1 is not only necessary for normal growth but also important for disease resistance through regulation of hydrogen peroxide generation.
Studied voltage-dependent anion channel 1 (VDAC1) structure and oligomerization using an Escherichia coli cell-free protein synthesis system and bicelle crystallization.
In this study, molecular dynamics simulations and single-channel experiments of VDAC-1 show agreement for the current-voltage relationships of an "open" channel and they also show several subconducting transient states that are more cation selective in the simulations. We observed voltage-dependent asymmetric distortions of the VDAC-1 barrel and the displacement of particular charged amino acids.
VDAC1 was accumulated in the desmin (show DES Proteins) highly stained area of muscle fibers of desminopathy patients.
work raises the interesting possibility that cholesterol-mediated regulation of VDAC1 may be facilitated through a specific binding site at the functionally important Glu (show DCTN1 Proteins)(73) residue.
this study describes novel drug candidates with a defined mechanism of action that involves inhibition of VDAC1 oligomerization, apoptosis, and mitochondrial dysfunction. The compounds VBIT-3 and VBIT-4 offer a therapeutic strategy for treating different diseases associated with enhanced apoptosis and point to VDAC1 as a promising target for therapeutic intervention.
Results from the simulations show that HK2 (show HK2 Proteins) binding restricts the movement of the VDAC1 N-terminal helix. As a result, VDAC1 is kept in the open state most of the time and probably allows a constant supply of ATP to HK2 (show HK2 Proteins) for glycolysis.
The findings of this study suggest that inhibition of intracellular Ca(2 (show CA2 Proteins)+/-) overload could protect cells from damage and that VDAC1 plays a considerable role in Cr(VI)-induced liver injury.
Our study suggested that miR-7 (show LILRB1 Proteins) suppressed the expression of VDAC1 in hepatocellular carcinoma
Results shows that beta-barrel of human VDAC1 embedded into a membrane is highly flexible and that Ca2+, a key regulator of metabolism and apoptosis, strongly decreases its plasticity suggesting that physiological VDAC function depends on the molecular plasticity of its channel.
High VDAC1 expression is associated with cervical cancer.
Data confirm the synthesis of VDAC1 and 2 subtypes in GV (germinal vesicle) and MII (meiosis II) stage porcine oocytes as well as their protein expression.
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.
Suggest that VDAC1 participates in volume regulatory processes in spermatozoa.
In cornu ammonis 1 region astrocytes, increasing miR (show MLXIP Proteins)-29a decreased VDAC1 and improved cell survival, while knockdown of VDAC1 improved survival.
VDAC1-interacting anion transport inhibitors inhibited apoptosis via direct interaction with VDAC1 to inhibit its oligomerization and subsequent Cyto c release and apoptosis.
Reducing VDAC1 expression induces a non-apoptotic role for pro-apoptotic proteins in glioblastoma multiforme cancer cell differentiation.
TSPO (show TSPO Proteins) as a novel element in the regulation of mitochondrial quality control by autophagy, and demonstrate the importance for cell homeostasis of its expression ratio with voltage-dependent anion channel 1
ATP flows through VDAC through multiple pathways, in agreement with our structural data and experimentally determined physiological rates.
Reduced VDAC1 expression protects against Alzheimer's disease and synaptic deficiencies.
Data suggest presence of unstructured C-terminal tubulin (show TUBB Proteins) tail in VDAC pore decreases conductance and switches selectivity from anionic to cationic rendering ATP transport virtually impossible; involves stable salt bridge (K336-tubulin (show TUBB Proteins)/D186-Vdac1).
MAVS (show MAVS Proteins) binds to voltage-dependent anion channel 1 (VDAC1) and induces apoptosis by caspase-3 (show CASP3 Proteins) activation, which is independent of its role in innate immunity.
we found that Bcl-wav controls intracellular Ca(2+) trafficking by acting on the mitochondrial voltage-dependent anion channel, and possibly on MCU, with direct consequences on actin microfilament dynamics and blastomere migration guidance.
This gene encodes a voltage-dependent anion channel protein that is a major component of the outer mitochondrial membrane. The encoded protein facilitates the exchange of metabolites and ions across the outer mitochondrial membrane and may regulate mitochondrial functions. This protein also forms channels in the plasma membrane and may be involved in transmembrane electron transport. Alternate splicing results in multiple transcript variants. Multiple pseudogenes of this gene are found on chromosomes 1, 2 3, 6, 9, 12, X and Y.
voltage-dependent anion channel 1
, outer mitochondrial membrane protein porin 1
, plasmalemmal porin
, porin 31HL
, porin 31HM
, voltage-dependent anion-selective channel protein 1
, brain-derived voltage-dependent anion channel 1
, voltage-dependent anion-selective channel protein 5