Sergey M. Bezrukov

Also affiliated with Eunice Kennedy Shriver National Institute of Child Health and Human Development

EngineeringBiochemistry, Genetics and Molecular BiologyPhysics and Astronomy

Pilot corpus only

This score is computed over theSindex pilot corpus and does not cover the full scientific literature. Scores are relative to papers we have ingested — papers, authors, and institutions outside the pilot are not represented. Methodology.

Top 100%percentile

0Author DataRank

Indexed papers

0in pilot corpus

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Papers

Driven by 36 papers. Top paper: “A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology”.

A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology

The Journal of General Physiology(2020)10.1085/jgp.201912501

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58 citations

Lucie Bergdoll, Óscar Teijido, Nabill Munshi, Daniel Jacobs, Adam J. Kuszak +8 more

Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations

ACS Nano(2020)10.1021/acsnano.0c07672

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15 citations

Tatiana K. Rostovtseva, Daniel Jacobs, Philip A. Gurnev, Sergey M. Bezrukov, David P. Hoogerheide

Targeting the Multiple Physiologic Roles of VDAC With Steroids and Hydrophobic Drugs

Frontiers in Physiology(2020)10.3389/fphys.2020.00446

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31 citations

María Queralt-Martín, William M. Rosencrans, Sergey M. Bezrukov, Tatiana K. Rostovtseva

Effect of a post-translational modification mimic on protein translocation through a nanopore

Nanoscale(2020)10.1039/d0nr01577f

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27 citations

Philip A. Gurnev, Tatiana K. Rostovtseva, Sergey M. Bezrukov, David P. Hoogerheide

Peculiarities of the Mean Transition Path Time Dependence on the Barrier Height in Entropy Potentials

The Journal of Physical Chemistry B(2020)10.1021/acs.jpcb.9b09595

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8 citations

Leonardo Dagdug, Sergey M. Bezrukov, Alexander M. Berezhkovskii

α-Synuclein emerges as a potent regulator of VDAC-facilitated calcium transport

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.11.15.383729

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2 citations

Vicente M. Aguilella, Tatiana K. Rostovtseva, Sergey M. Bezrukov, William M. Rosencrans

Correction to: Molecular mechanism of olesoxime-mediated neuroprotection through targeting α-synuclein interaction with mitochondrial VDAC

Cellular and Molecular Life Sciences(2020)10.1007/s00018-019-03417-6

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1 citations

Philip A. Gurnev, Alexandra Beilina, María Queralt-Martín, William M. Rosencrans, Mark Cookson +3 more

Membrane Transport | Mitochondrial Outer Membrane and the VDAC Channel

Elsevier eBooks(2020)10.1016/b978-0-12-809633-8.21371-x

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0 citations

Sergey M. Bezrukov, Tatiana K. Rostovtseva

VDAC regulation of mitochondrial calcium flux: From channel biophysics to disease

Cell Calcium(2021)10.1016/j.ceca.2021.102356

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138 citations

Megha Rajendran, Sergey M. Bezrukov, Tatiana K. Rostovtseva, William M. Rosencrans

α-Synuclein emerges as a potent regulator of VDAC-facilitated calcium transport

Cell Calcium(2021)10.1016/j.ceca.2021.102355

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59 citations

Vicente M. Aguilella, Tatiana K. Rostovtseva, Sergey M. Bezrukov, William M. Rosencrans

Regulation of Mitochondrial Respiration by VDAC Is Enhanced by Membrane-Bound Inhibitors with Disordered Polyanionic C-Terminal Domains

International Journal of Molecular Sciences(2021)10.3390/ijms22147358

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36 citations

Sergey M. Bezrukov, David P. Hoogerheide, Tatiana K. Rostovtseva

Voltage‐activated complexation of α‐synuclein with three diverse β‐barrel channels: VDAC, MspA, and α‐hemolysin

PROTEOMICS(2021)10.1002/pmic.202100060

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14 citations

Philip A. Gurnev, Tatiana K. Rostovtseva, Sergey M. Bezrukov, David P. Hoogerheide

Evaluating diffusion resistance of a constriction in a membrane channel by the method of boundary homogenization

Physical review. E(2021)10.1103/physreve.103.012408

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10 citations

Leonardo Dagdug, Alexander M. Berezhkovskii, Ian MacGillivray, Sergey M. Bezrukov, Alexei T. Skvortsov

Exploring lipid-dependent conformations of membrane-bound α-synuclein with the VDAC nanopore

Biochimica et Biophysica Acta (BBA) - Biomembranes(2021)10.1016/j.bbamem.2021.183643

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19 citations

Tatiana K. Rostovtseva, Sergey M. Bezrukov, David P. Hoogerheide

Capturing single molecules by nanopores: measured times and thermodynamics

Physical Chemistry Chemical Physics(2021)10.1039/d0cp04747c

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6 citations

Sergey M. Bezrukov, Alexander M. Berezhkovskii

Effective diffusivity of a Brownian particle in a two-dimensional periodic channel of abruptly alternating width

Physical review. E(2021)10.1103/physreve.103.062106

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6 citations

Alexander M. Berezhkovskii, V. Yu. Zitserman, Sergey M. Bezrukov, Leonardo Dagdug

Trapping of particles diffusing in two dimensions by a hidden binding site

Physical review. E(2021)10.1103/physreve.103.012135

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5 citations

Alexander M. Berezhkovskii, V. Yu. Zitserman, Sergey M. Bezrukov, Leonardo Dagdug

MspA Porin as a Local Nanopore Probe for Membrane-bound Proteins

bioRxiv (Cold Spring Harbor Laboratory)(2021)10.1101/2021.10.15.464579

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1 citations

Philip A. Gurnev, Jens H. Gundlach, Andrew H. Laszlo, Tatiana K. Rostovtseva, Sergey M. Bezrukov +1 more

Blocker Effect on Diffusion Resistance of a Membrane Channel: Dependence on the Blocker Geometry

The Journal of Physical Chemistry B(2022)10.1021/acs.jpcb.2c00715

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9 citations

Alexei T. Skvortsov, Alexander M. Berezhkovskii, Sergey M. Bezrukov, Leonardo Dagdug

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(2022)10.1007/s00018-022-04389-w

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22 citations

María Queralt-Martín, Philip A. Gurnev, William M. Rosencrans, Amandine Rovini, Daniel Jacobs +5 more

The Single Residue K12 Governs the Exceptional Voltage Sensitivity of Mitochondrial Voltage-Dependent Anion Channel Gating

Journal of the American Chemical Society(2022)10.1021/jacs.2c03316

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19 citations

María Queralt-Martín, Farha Khan, Lucie Bergdoll, Jeff Abramson, Sergey M. Bezrukov +4 more

Intrinsic diffusion resistance of a membrane channel, mean first-passage times between its ends, and equilibrium unidirectional fluxes

The Journal of Chemical Physics(2022)10.1063/5.0082482

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6 citations

Sergey M. Bezrukov, Alexander M. Berezhkovskii

Trapping of single diffusing particles by a circular disk on a reflecting flat surface. Absorbing hemisphere approximation

Physical Chemistry Chemical Physics(2022)10.1039/d2cp04357b

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1 citations

Alexander M. Berezhkovskii, Sergey M. Bezrukov, Leonardo Dagdug

Restricting α-Synuclein Transport into Mitochondria by Inhibition of α-Synuclein-VDAC Complexation as a Potential Therapeutic Target for Parkinson’s Disease Treatment

bioRxiv (Cold Spring Harbor Laboratory)(2022)10.1101/2022.04.07.487541

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0 citations

María Queralt-Martín, Philip A. Gurnev, William M. Rosencrans, Amandine Rovini, Daniel Jacobs +5 more

Blocker effect on diffusion resistance of a membrane channel. Dependence on the blocker geometry

arXiv (Cornell University)(2022)10.48550/arxiv.2207.08812

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0 citations

Alexei T. Skvortsov, Alexander M. Berezhkovskii, Sergey M. Bezrukov, Leonardo Dagdug

Permeability and diffusion resistance of porous membranes: Analytical theory and its numerical test

The Journal of Chemical Physics(2023)10.1063/5.0138036

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8 citations

Leonardo Dagdug, Emily F. Hilder, Alexander M. Berezhkovskii, Sergey M. Bezrukov, Alexei T. Skvortsov

Counter-Intuitive Features of Particle Dynamics in Nanopores

International Journal of Molecular Sciences(2023)10.3390/ijms242115923

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4 citations

Sergey M. Bezrukov, Alexander M. Berezhkovskii

Beta-Barrel Channel Response to High Electric Fields: Functional Gating or Reversible Denaturation?

International Journal of Molecular Sciences(2023)10.3390/ijms242316655

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6 citations

Sergey M. Bezrukov, Ekaterina M. Nestorovich

Dimeric Tubulin Modifies Mechanical Properties of Lipid Bilayer, as Probed Using Gramicidin A Channel

International Journal of Molecular Sciences(2024)10.3390/ijms25042204

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4 citations

Michael Weinrich, Daniel Jacobs, William M. Rosencrans, Sergey M. Bezrukov, Tatiana K. Rostovtseva

Conformational plasticity of mitochondrial VDAC2 controls the kinetics of its interaction with cytosolic proteins

bioRxiv (Cold Spring Harbor Laboratory)(2024)10.1101/2024.11.08.622687

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0 citations

Harisankar Khuntia, Motahareh Ghahari Larimi, Radhakrishnan Mahalakshmi, Tsyr‐Yan Yu, Sergey M. Bezrukov +2 more

Antimicrobial peptide class that forms discrete β-barrel stable pores anchored by transmembrane helices

Nature Communications(2025)10.1038/s41467-025-62604-1

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10 citations

Dylan J. Burgin, Ama N Antwi, Amer E. Villaruz, Madeline R. Galac, Gordon Y. C. Cheung +9 more

Three mammalian VDAC isoforms distinctly regulate mitochondrial function and proteome to maintain cell metabolism

Journal of Biological Chemistry(2025)10.1016/j.jbc.2025.111009

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4 citations

William M. Rosencrans, Nina Bautista, Wendy Fitzgerald, Diana Huynh, Bethel G. Beyene +7 more

Trapping of particles diffusing in a cavity by hidden binding sites analyzed with the Reimann–Schmid–Hanggi steady-state approach

Physical Chemistry Chemical Physics(2025)10.1039/d5cp03400k

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2 citations

Leonardo Dagdug, Sergey M. Bezrukov, Alexander M. Berezhkovskii

Particle dynamics in biconical cavities: First-passage, direct-transit, and looping time distributions

The Journal of Chemical Physics(2025)10.1063/5.0274941

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2 citations

Leonardo Dagdug, Sergey M. Bezrukov, Alexander M. Berezhkovskii

A Membrane-Disruptive Action of VBIT-4 Challenges Its Role as a Widely Used VDAC Oligomerization Inhibitor

eLife(2025)10.1101/2025.06.30.661942

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2 citations

Luis Borges-Araujo, Megha Rajendran, Elodie Lafargue, Deborah Byrne, Nicolas Buzhinsky +12 more

Unlocking the Distinct Roles of the Three Mammalian VDAC Isoforms in Mitochondrial Respiration and Cancer Cell Metabolism

bioRxiv (Cold Spring Harbor Laboratory)(2025)10.1101/2025.02.20.639106

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0 citations

William M. Rosencrans, Wendy Fitzgerald, Diana Huynh, Bethel G. Beyene, Baiyi Quan +6 more