ReviewJournal of bioenergetics and biomembranes2008
Mini review on the structure and supramolecular assembly of VDAC.
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 18 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
18 citing papers in PubMed, 33 citations in OpenAlex.
- A single-vesicle fluorescence microscopy platform to quantify phospholipid scrambling.Nature structural & molecular biology · 2026Article
- A single vesicle fluorescence microscopy platform to quantify phospholipid scrambling.bioRxiv : the preprint server for biology · 2025Article
- Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase.Nature communications · 2023Article
- Counter-Intuitive Features of Particle Dynamics in Nanopores.International journal of molecular sciences · 2023Review
- VDAC1 Knockout Affects Mitochondrial Oxygen Consumption Triggering a Rearrangement of ETC by Impacting on Complex I Activity.International journal of molecular sciences · 2023Article
- Article
- Alpha-Synuclein and Mitochondrial Dysfunction in Parkinson's Disease: The Emerging Role of VDAC.Biomolecules · 2021Review
- Collective Dynamics of Ion Channels on Bilayer Lipid Membranes.ACS omega · 2021Article
- Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions.Frontiers in physiology · 2021Review
- Ischemic postconditioning confers cerebroprotection by stabilizing VDACs after brain ischemia.Cell death & disease · 2018Article
- Stochastic Gating as a Novel Mechanism for Channel Selectivity.Biophysical journal · 2018Article
- Putative roles of mitochondrial Voltage-Dependent Anion Channel, Bcl-2 family proteins and c-Jun N-terminal Kinases in ischemic stroke associated apoptosis.Biochimie open · 2017Review
- GSK3β and VDAC Involvement in ER Stress and Apoptosis Modulation during Orthotopic Liver Transplantation.International journal of molecular sciences · 2017Article
- Mitochondrial ion channels/transporters as sensors and regulators of cellular redox signaling.Antioxidants & redox signaling · 2014Review
- Trapping by clusters of channels, receptors, and transporters: quantitative description.Biophysical journal · 2014Review
- Methyl jasmonate: putative mechanisms of action on cancer cells cycle, metabolism, and apoptosis.International journal of cell biology · 2014Review
- Proteomic analysis reveals late exercise effects on cardiac remodeling following myocardial infarction.Journal of proteomics · 2010Article
- Mitochondrial Ca2+ channels: Great unknowns with important functions.FEBS letters · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Voltage Dependent Anion Channel (VDAC) is the most abundant protein in the outer membrane of mitochondria. This strategic localization puts it at the heart of a great number of phenomena. Its recent implication in apoptosis is an example of the major importance of this protein and has created a surge of interest in VDAC. There is no atomic-resolution structure allowing a better understanding of the function of VDAC, so alternative techniques to X-ray diffraction have been used to study VDAC. Here we discuss structural models from folding predictions and review data acquired by Atomic Force Microscopy (AFM) imaging that allowed to observe VDAC's structure and supramolecular organization in the mitochondrial outer membrane.
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.