ArticleNature structural & molecular biology2014
Structure-guided simulations illuminate the mechanism of ATP transport through VDAC1.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed, 102 citations in OpenAlex.
- Elliptical β-barrel deformation underlies gating in VDAC1.Protein science : a publication of the Protein Society · 2026Article
- Phosphorothioate backbone modification of oligodeoxynucleotides induces TLR9-independent lung epithelial antimicrobial responses.American journal of respiratory cell and molecular biology · 2026Article
- Membrane protein structure and dynamics probed by MicroED.Biochemical Society transactions · 2026Review
- Ferritin iron uptake and oxidation are dynamically modulated by nucleotide phosphate architecture via electrostatic gating.International journal of biological macromolecules · 2026Article
- Mitochondrial membrane junction-mediated ATP channeling drives activity-dependent glucose metabolism.bioRxiv : the preprint server for biology · 2025Article
- Molecular permeation through large pore channels: computational approaches and insights.The Journal of physiology · 2025Review
- Oligomer-based functions of mitochondrial porin.Nature communications · 2025Article
- Hexokinase-I directly binds to a charged membrane-buried glutamate of mitochondrial VDAC1 and VDAC2.Communications biology · 2025Article
- Modulation of mitochondrial voltage dependent anion channel: studies on bilayer electrophysiology.Frontiers in physiology · 2025Review
- Multi-target neuroprotection by dl-PHPB in APP/PS1 mice: a proteomic analysis.Frontiers in pharmacology · 2025Article
- Article
- Article
- Screw sense and screw sensibility: communicating information by conformational switching in helical oligomers.Chemical Society reviews · 2023Review
- Post-translational modifications and protein quality control of mitochondrial channels and transporters.Frontiers in cell and developmental biology · 2023Review
- Mitochondrial Permeability Transition in Stem Cells, Development, and Disease.Advances in experimental medicine and biology · 2023Review
- The Single Residue K12 Governs the Exceptional Voltage Sensitivity of Mitochondrial Voltage-Dependent Anion Channel Gating.Journal of the American Chemical Society · 2022Article
- Mechanisms of membrane protein crystallization in 'bicelles'.Scientific reports · 2022Article
- Computational investigations on target-site searching and recognition mechanisms by thymine DNA glycosylase during DNA repair process.Acta biochimica et biophysica Sinica · 2022Review
- Targeting calcium-mediated inter-organellar crosstalk in cardiac diseases.Expert opinion on therapeutic targets · 2022Article
- Review
5 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The voltage-dependent anion channel (VDAC) mediates the flow of metabolites and ions across the outer mitochondrial membrane of all eukaryotic cells. The open channel passes millions of ATP molecules per second, whereas the closed state exhibits no detectable ATP flux. High-resolution structures of VDAC1 revealed a 19-stranded β-barrel with an α-helix partially occupying the central pore. To understand ATP permeation through VDAC, we solved the crystal structure of mouse VDAC1 (mVDAC1) in the presence of ATP, revealing a low-affinity binding site. Guided by these coordinates, we initiated hundreds of molecular dynamics simulations to construct a Markov state model of ATP permeation. These simulations indicate that ATP flows through VDAC through multiple pathways, in agreement with our structural data and experimentally determined physiological rates.
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.