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ProteomicsVoltage-Dependent Anion-Selective Channels and Other Mitochondrial Membrane Proteins Form Diverse Complexes in Beetroots Subjected to Flood-Induced Programmed Cell Death
In plants, programmed cell death (PCD) is involved in both the development and in the response to biotic and abiotic aggressions. In early stages of PCD, mitochondrial membranes are made permeable by the formation of permeability transition pores, whose protein composition is debated. Since flooding...
ORGANISM(S): Beta vulgaris subsp. vulgaris 
2021-10-28 | PXD027781 | Pride
Mitochondrial membrane protein complexes Flooding stress Voltage-dependent anion-selective channels (vdac) Beta vulgaris Programmed cell death (pcd) 
ProteomicsA High Resolution Mass Spectrometry Study Reveals the Potential of Disulfide Formation in Human Mitochondrial Voltage-Dependent Anion Selective Channel Isoforms (hVDACs)
The voltage-dependent anion-selective channels (VDACs), also known as eukaryotic porins, are pore-forming proteins which allow the passage of ions and small molecules across the outer mitochondrial membrane (OMM). They are involved in complex interactions regulating organelle and cellular metabolism...
ORGANISM(S): Homo sapiens (Human) 
2020-03-09 | PXD017482 | Pride
Cysteine over-oxidation  mitochondria  orbitrap fusion tribrid  hydroxyapatite  mitochondrial intermembrane space  outer mitochondrial membrane  post-translational modification 
UnknownVoltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions.
Not available
S-EPMC8171188 | biostudies-literature
ProteomicsStructural characterization of intra- and intermolecular disulfide bonds in Voltage-Dependent Anion Channel 3 (VDAC3) protein from Rattus norvegicus by high-resolution mass spectrometry
Voltage-Dependent Anion Channels, the most abundant proteins of the mitochondrial outer membrane, are responsible for exchange of ions and metabolites between cytosol and mitochondria. They participate in the control of glycolytic metabolism through interaction with numerous enzymes and play a key r...
ORGANISM(S): Rattus norvegicus (Rat) 
2025-09-08 | PXD064110 | Pride
High-resolution mass spectrometry  intra- and intermolecular disulfide bonds  rattus voltage-dependent anion selective channel isoform 3 (rvdac3)  cysteine redox state  structural characterization 
ProteomicsProteomic shifts reflecting oxidative stress and reduced capacity for protein synthesis, and alterations to mitochondrial membranes in Neurospora crassa lacking VDAC
Proteomic analysis of N. crassa was performed to explore the role of VDAC (voltage dependent anion-selective channels) in the regulation of cellular processes. Differential label free quantitation was applied to both wild-type and VDAC-knockout versions, involving both cytosolic and mitochondrial i...
ORGANISM(S): Neurospora Crassa (ncbitaxon:5141) 
2021-12-14 | MSV000088567 | MassIVE
ProteomicsPINK1-TOM-TIM23 complex SDA XL-MS
3xFLAG-tagged human wild-type PINK1 was expressed and immunoprecipitated with anti-FLAG beads. Chemical cross-linking MS (XL-MS) analysis using SDA and UV exposure was performed followed by in solution trypsin digestion and MS analysis.
ORGANISM(S): Homo Sapiens (human) 
2025-05-29 | PXD058526 | JPOST Repository
UnknownVoltage-Dependent Anion-Selective Channels and Other Mitochondrial Membrane Proteins Form Diverse Complexes in Beetroots Subjected to Flood-Induced Programmed Cell Death.
Not available
S-EPMC8457146 | biostudies-literature
UnknownCharged residues distribution modulates selectivity of the open state of human isoforms of the voltage dependent anion-selective channel.
Not available
S-EPMC4146382 | biostudies-literature
UnknownA High Resolution Mass Spectrometry Study Reveals the Potential of Disulfide Formation in Human Mitochondrial Voltage-Dependent Anion Selective Channel Isoforms (hVDACs).
Not available
S-EPMC7073118 | biostudies-literature
UnknownThe physiological properties of a novel family of VDAC-like proteins from Drosophila melanogaster.
Not available
S-EPMC1303779 | biostudies-literature
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