ArticleNanoscale2017
Mechanism of α-synuclein translocation through a VDAC nanopore revealed by energy landscape modeling of escape time distributions.
Article in Nanoscale, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 52 citations in OpenAlex.
- Mitochondrial Voltage-Dependent Anion Channel: From a Passive Pore to a Cellular Hub Through Protein Complexation.International journal of molecular sciences · 2026Review
- Logarithmic Binding and Stretched-Exponential Kinetics in Peripheral Protein Interactions with Lipid Membrane Surfaces.The journal of physical chemistry letters · 2026Article
- Global and local effects in lipid-mediated interactions between peripheral and integral membrane proteins.Frontiers in molecular biosciences · 2025Review
- Restricting α-synuclein transport into mitochondria by inhibition of α-synuclein-VDAC complexation as a potential therapeutic target for Parkinson's disease treatment.Cellular and molecular life sciences : CMLS · 2022Article
- The Potential Role of Voltage-Dependent Anion Channel in the Treatment of Parkinson's Disease.Oxidative medicine and cellular longevity · 2022Review
- Multiple rereads of single proteins at single-amino acid resolution using nanopores.Science (New York, N.Y.) · 2021Article
- Nanopore sensing: A physical-chemical approach.Biochimica et biophysica acta. Biomembranes · 2021Review
- Exploring lipid-dependent conformations of membrane-bound α-synuclein with the VDAC nanopore.Biochimica et biophysica acta. Biomembranes · 2021Article
- Regulation of Mitochondrial Respiration by VDAC Is Enhanced by Membrane-Bound Inhibitors with Disordered Polyanionic C-Terminal Domains.International journal of molecular sciences · 2021Review
- Neurons and Glia Interplay in α-Synucleinopathies.International journal of molecular sciences · 2021Review
- Article
- Laser-based temperature control to study the roles of entropy and enthalpy in polymer-nanopore interactions.Science advances · 2021Article
- VDAC regulation of mitochondrial calcium flux: From channel biophysics to disease.Cell calcium · 2021Review
- VDAC-A Primal Perspective.International journal of molecular sciences · 2021Review
- Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations.ACS nano · 2021Article
- Capturing single molecules by nanopores: measured times and thermodynamics.Physical chemistry chemical physics : PCCP · 2021Article
- A Calcium Guard in the Outer Membrane: Is VDAC a Regulated Gatekeeper of Mitochondrial Calcium Uptake?International journal of molecular sciences · 2021Review
- High-Resolution Respirometry Reveals MPPInternational journal of molecular sciences · 2020Article
- Molecular mechanism of olesoxime-mediated neuroprotection through targeting α-synuclein interaction with mitochondrial VDAC.Cellular and molecular life sciences : CMLS · 2020Article
- Effect of a post-translational modification mimic on protein translocation through a nanopore.Nanoscale · 2020Article
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 3 institutions in 1 country.
Funding
Abstract
We probe the energy landscape governing the passage of α-synuclein, a natural "diblock copolymer"-like polypeptide, through a nanoscale pore. α-Synuclein is an intrinsically disordered neuronal protein associated with Parkinson's pathology. The motion of this electrically heterogeneous polymer in the β-barrel voltage-dependent anion channel (VDAC) of the mitochondrial outer membrane strongly depends on the properties of both the charged and uncharged regions of the α-synuclein polymer. We model this motion in two ways. First, a simple Markov model accounts for the transitions of the channel between the states of different occupancy by α-synuclein. Second, the detailed energy landscape of this motion can be accounted for using a drift-diffusion framework that incorporates the α-synuclein binding energy and the free energy cost of its confinement in the VDAC pore. The models directly predict the probability of α-synuclein translocation across the mitochondrial outer membrane, with immediate implications for the physiological role of α-synuclein in regulation of mitochondrial bioenergetics. Time-resolved measurements of the electrical properties of VDAC occupied by α-synuclein reveal distinct effects of the motion of the junction separating the differently charged regions of the polymer.
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.