ArticleProceedings of the National Academy of Sciences of the United States of America2018
Protonation state of glutamate 73 regulates the formation of a specific dimeric association of mVDAC1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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.
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Who cites it
35 citing papers in PubMed, 49 citations in OpenAlex.
- A membrane-disruptive action of VBIT-4 challenges its role as a widely used VDAC1 oligomerization inhibitor.eLife · 2026Article
- Computational Insights into PB1-F2 Mediated Modulation of VDAC1: An Allosteric Mechanism in Mitochondrial Dysfunction.ACS omega · 2026Article
- Elliptical β-barrel deformation underlies gating in VDAC1.Protein science : a publication of the Protein Society · 2026Article
- A pore is a pore is a pore (or a hub?): VDAC oligomerization in mitochondrial connectivity and modulation.Biochemical Society transactions · 2026Review
- From vibrations to function: Spectroscopic detection and quantification of π-π stacking in drug-responsive protein complexes.Science advances · 2026Article
- Structural basis of apoptosis induction by the mitochondrial voltage-dependent anion channel.Nature communications · 2025Article
- Membrane lipid composition modulates the organization of VDAC1, a mitochondrial gatekeeper.Communications biology · 2025Article
- Protein Modeling with DEER Spectroscopy.Annual review of biophysics · 2025Review
- Hexokinase-I directly binds to a charged membrane-buried glutamate of mitochondrial VDAC1 and VDAC2.Communications biology · 2025Article
- Article
- Review
- Improved Highly Mobile Membrane Mimetic Model for Investigating Protein-Cholesterol Interactions.Journal of chemical information and modeling · 2024Article
- Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase.Nature communications · 2023Article
- Chemoselective Caging of Carboxyl Groups for On-Demand Protein Activation with Small Molecules.Angewandte Chemie (International ed. in English) · 2023Article
- E as in Enigma: The Mysterious Role of the Voltage-Dependent Anion Channel Glutamate E73.International journal of molecular sciences · 2022Review
- Comparative evaluation of spin-label modeling methods for protein structural studies.Biophysical journal · 2022Article
- The Role of Voltage-Dependent Anion Channel in Mitochondrial Dysfunction and Human Disease.Cells · 2021Review
- Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II.Communications biology · 2021Article
- Labeling Preferences of Diazirines with Protein Biomolecules.Journal of the American Chemical Society · 2021Article
- VDAC regulation of mitochondrial calcium flux: From channel biophysics to disease.Cell calcium · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
The voltage-dependent anion channel (VDAC) is the most abundant protein in the outer mitochondrial membrane and constitutes the primary pathway for the exchange of ions and metabolites between the cytosol and the mitochondria. There is accumulating evidence supporting VDAC's role in mitochondrial metabolic regulation and apoptosis, where VDAC oligomerization has been implicated with these processes. Herein, we report a specific pH-dependent dimerization of murine VDAC1 (mVDAC1) identified by double electron-electron resonance and native mass spectrometry. Intermolecular distances on four singly spin-labeled mVDAC1 mutants were used to generate a model of the low-pH dimer, establishing the presence of residue E73 at the interface. This dimer arrangement is different from any oligomeric state previously described, and it forms as a steep function of pH with an apparent pK
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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.