ReviewJournal of bioenergetics and biomembranes2008
Structure of the voltage dependent anion channel: state of the art.
Review in Journal of bioenergetics and biomembranes, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 70 citations in OpenAlex.
- Identification and validation of oxidative stress-related genes for the diagnosis of sepsis-induced acute lung injury.PloS one · 2025Article
- Voltage-Dependent Anion Channels in Male Reproductive Cells: Players in Healthy Fertility?Biomolecules · 2024Review
- Homocysteine-Thiolactone Modulates Gating of Mitochondrial Voltage-Dependent Anion Channel (VDAC) and Protects It from Induced Oxidative Stress.The Journal of membrane biology · 2022Article
- VDAC Genes Expression and Regulation in Mammals.Frontiers in physiology · 2021Review
- Quinidine partially blocks mitochondrial voltage-dependent anion channel (VDAC).European biophysics journal : EBJ · 2020Article
- The Structural Basis for Low Conductance in the Membrane Protein VDAC upon β-NADH Binding and Voltage Gating.Structure (London, England : 1993) · 2020Article
- Hypoxic-induced truncation of voltage-dependent anion channel 1 is mediated by both asparagine endopeptidase and calpain 1 activities.Oncotarget · 2018Article
- Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics.Frontiers in oncology · 2017Review
- Voltage Dependence of Conformational Dynamics and Subconducting States of VDAC-1.Biophysical journal · 2016Article
- Current state of theoretical and experimental studies of the voltage-dependent anion channel (VDAC).Biochimica et biophysica acta · 2016Review
- N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry.The Journal of biological chemistry · 2015Article
- Magic angle spinning nuclear magnetic resonance characterization of voltage-dependent anion channel gating in two-dimensional lipid crystalline bilayers.Biochemistry · 2015Article
- Comparative proteome analysis of brown adipose tissue in obese C57BL/6J mice using iTRAQ-coupled 2D LC-MS/MS.PloS one · 2015Article
- Acidification asymmetrically affects voltage-dependent anion channel implicating the involvement of salt bridges.The Journal of biological chemistry · 2014Article
- Article
- Cysteine residues impact the stability and micelle interaction dynamics of the human mitochondrial β-barrel anion channel hVDAC-2.PloS one · 2014Article
- The voltage-dependent anion selective channel 1 (VDAC1) topography in the mitochondrial outer membrane as detected in intact cell.PloS one · 2013Article
- β-Barrel mobility underlies closure of the voltage-dependent anion channel.Structure (London, England : 1993) · 2012Article
- The role of VDAC in cell death: friend or foe?Biochimica et biophysica acta · 2012Review
- Saccharomyces cerevisiae porin pore forms complexes with mitochondrial outer membrane proteins Om14p and Om45p.The Journal of biological chemistry · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The eukaryotic porin or Voltage Dependent Anion-selective Channels (VDAC) is the protein forming the aqueous pore channel in the mitochondrial outer membrane. It can modulate the energy-dependent metabolism of the cell forming a diffusion barrier to ions, adenine-nucleotides and other metabolites and it is probably involved in the regulation of apoptotic-relevant events. For these reasons, VDAC co-responsibility in unphysiological events leading to important pathologies such as onset or sustainment of cancer has been envisaged very early. The knowledge of the VDAC atomic structure is thus a relevant step in the design of modern drugs acting upon the mitochondrial function and its related apoptotic balance. This goal, despite many efforts, has not been gained until now. Several predictive or descriptive techniques have been employed to obtain models or representations of the pore-structure. The results obtained are reported in this review. The emerging picture arising from these many results is coherent and sufficiently informative. From these efforts it appears that VDAC is functionally monomeric but can cluster in tight but regular groups; it is asymmetric with larger exposed domains on the cytosolic side of the outer mitochondrial membrane; the diameter of the pore is between 2.5-3.0 nm and it is apparently free from obstructions (in the open state); the channel wall is mainly formed by typical amphipathic beta-strands; mobile components (the N-terminal ?) can have functional relevance to the pore regulation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.