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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 (189) 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.
VDAC1 is a direct target of miR (show MLXIP Proteins)-320a in non-small cell lung cancer (NSCLC) cells, and miR (show MLXIP Proteins)-320a inhibits VDAC1 expression in NSCLC cells
The results of this study shown VDAC1, the Potential Target of miR (show MLXIP Proteins)-320a, is Upregulated in Response to HIV-1 Tat (show TAT Proteins).
the present study indicated that VDAC1 may interact with HPV16 E7 to promote the malignant progression of HPV-related cervical cancer
Porin expression was lower in patients with heart failure with preserved ejection fraction compared to controls.
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.
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.
microcirculatory ischemia/reperfusion injury can be attributed to Mff (show MFF Proteins)-dependent mitochondrial fission via voltage-dependent anion channel 1/hexokinase 2 (show HK2 Proteins)-mediated mitochondrial permeability transition pore opening and mitochondrial reactive oxygen species/cardiolipin involved cyt-c (show CYCS Proteins) release.
This study demonstrated that Vdac1 was significantly downregulated in amnesic mice and showed interaction with other proteins in interaction network.
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.
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