ReviewCurrent opinion in structural biology2009
The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins.
Review in Current opinion in structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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.
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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
40 citing papers in PubMed, 85 citations in OpenAlex.
- Computational Insights into PB1-F2 Mediated Modulation of VDAC1: An Allosteric Mechanism in Mitochondrial Dysfunction.ACS omega · 2026Article
- Decoding Cancer through Silencing the Mitochondrial Gatekeeper VDAC1.Biomolecules · 2024Review
- New insights into the structure and dynamics of the TOM complex in mitochondria.Biochemical Society transactions · 2024Review
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer.Journal of the American Chemical Society · 2022Article
- A Deep Dive into VDAC1 Conformational Diversity Using All-Atom Simulations Provides New Insights into the Structural Origin of the Closed States.International journal of molecular sciences · 2022Article
- Structural characterization of the mitochondrial CaiScience · 2021Review
- Structure, gating and interactions of the voltage-dependent anion channel.European biophysics journal : EBJ · 2021Review
- Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions.Frontiers in physiology · 2021Review
- Fake It 'Till You Make It-The Pursuit of Suitable Membrane Mimetics for Membrane Protein Biophysics.International journal of molecular sciences · 2020Review
- VDAC1 at the Intersection of Cell Metabolism, Apoptosis, and Diseases.Biomolecules · 2020Review
- A Practical Perspective on the Roles of Solution NMR Spectroscopy in Drug Discovery.Molecules (Basel, Switzerland) · 2020Review
- Recombinant yeast VDAC2: a comparison of electrophysiological features with the native form.FEBS open bio · 2019Article
- Structural Variability in the RLR-MAVS Pathway and Sensitive Detection of Viral RNAs.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2019Review
- A VDAC1-Derived N-Terminal Peptide Inhibits Mutant SOD1-VDAC1 Interactions and Toxicity in the SOD1 Model of ALS.Frontiers in cellular neuroscience · 2019Article
- Interaction of the cryptic fragment of myelin basic protein with mitochondrial voltage-dependent anion-selective channel-1 affects cell energy metabolism.The Biochemical journal · 2018Article
- Ten Years of High Resolution Structural Research on the Voltage Dependent Anion Channel (VDAC)-Recent Developments and Future Directions.Frontiers in physiology · 2018Review
- VDAC1 at the crossroads of cell metabolism, apoptosis and cell stress.Cell stress · 2017Article
- Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017Review
- Voltage Dependence of Conformational Dynamics and Subconducting States of VDAC-1.Biophysical journal · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The voltage-dependent anion channel (VDAC) is an essential protein in the eukaryotic outer mitochondrial membrane, providing the pore for substrate diffusion. Three high-resolution structures of the isoform 1 of VDAC in detergent micelles and bicelles have recently been published, using solution NMR and X-ray crystallography. They resolve longstanding discussions about the membrane topology of VDAC and provide the first eukaryotic beta-barrel membrane protein structure. The structure contains a surprising feature that had not been observed in an integral membrane protein before: A parallel beta-strand pairing and thus an odd number of strands. The studies also give a structural and functional basis for the voltage gating mechanism of VDAC and its modulation by NADH; however, they do not fully explain these functions yet. With the de novo structure of VDAC-1, as well as those of half a dozen other proteins, the number of integral membrane protein structures solved by solution NMR has doubled in the past two years. Numerous further structural and functional studies on many different membrane proteins show that solution NMR has become an important tool for membrane protein molecular biology.
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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.