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ACS Chemical Neuroscience, 2021
Voltage-dependent anion channels (VDACs) of the outer mitochondrial membrane are known conventionally as metabolite flux proteins. However, research findings in the past decade have revealed the multifaceted regulatory roles of VDACs, from governing cellular physiology and mitochondria-mediated apoptosis to directly regulating debilitating cancers and ...
Altmash Khan +2 more
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Voltage-dependent anion channels (VDACs) of the outer mitochondrial membrane are known conventionally as metabolite flux proteins. However, research findings in the past decade have revealed the multifaceted regulatory roles of VDACs, from governing cellular physiology and mitochondria-mediated apoptosis to directly regulating debilitating cancers and ...
Altmash Khan +2 more
openaire +2 more sources
The voltage-dependent anion channel: an essential player in apoptosis
Biochimie, 2002The increase of outer mitochondrial membrane permeability is a central event in apoptotic cell death, since it releases several apoptogenic factors such as cytochrome c into the cytoplasm that activate the downstream destructive processes. The voltage-dependent anion channel (VDAC or mitochondrial porin) plays an essential role in the increase of ...
Yoshihide, Tsujimoto, Shigeomi, Shimizu
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[Voltage-dependent anion channel and hematological malignancies].
Zhongguo shi yan xue ye xue za zhi, 2011Voltage-dependent anion channel(VDAC)is mainly located on the outer mitochondrial membrane. High-resolution atomic force microscopy topography shows an eye-shaped VDAC with 3.8 nm x 2.7 nm pore dimensions. New work suggests pore formation by the assembly of homo-oligomers and supramolecule of VDAC or hetero oligomers composed of VDAC and pro-apoptotic ...
Yan, Sun, Ye, Chen
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Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC)
Journal of Bioenergetics and Biomembranes, 1992Porin 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.
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Voltage-Dependent Anion Channel (VDAC) in Health and Disease
2023Abstract 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
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The voltage dependent anion selective channel family in Drosophila melanogaster.
The Italian journal of biochemistry, 2007VDACs (voltage-dependent anion-selective channels) or mitochondrial PORINS are transmembrane proteins forming pores in the outer membrane. In eukaryotic genomes multiple genes coding for VDAC homologues have been discovered, but the functional meaning of this gene redundancy is unknown. In Drosophila melanogasterthree additional genes homologous to the
GUARINO, FRANCESCA MARIA +8 more
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[Voltage-dependent anion channels (VDAC) on human sperm membrane].
Zhonghua nan ke xue = National journal of andrology, 2007To further study gene expression and characterization of voltage-dependent anion channels (VDACs) on human spermatozoa.VDACs were cloned by PCR from the testis cDNA library. Recombinant human sperm VDACs were produced in E. coli system by molecular cloning technology.
Zeng-jun, Wang +3 more
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Function and Regulation of Mitochondrial Voltage-Dependent Anion Channel
2015The voltage-dependent anion channel (VDAC) is the major protein of the mitochondrial outer membrane (MOM). It is now generally accepted that this channel is responsible for most of the metabolite flux in and out of mitochondria. Small ions, adenine nucleotides such as ATP and ADP, and other water soluble mitochondrial respiratory substrates cross the ...
Tatiana K. Rostovtseva +1 more
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High Performance Anion Exchange Membranes with Confined Sub‐2‐nm Ion Channel
Advanced Functional Materials, 2023Zidong Wei
exaly