Sergey A. Akimov

Dr. Sergey A. Akimov

Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 31/4 Leninskiy Prospekt, 119071 Moscow, Russia
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Research Focus & Metrics

Academic Career Length

23Years (2004-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 December 2008 in Cell
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Journal Article
Closed access
PBPavel V. Bashkirov
Pavel V. Bashkirov
Sergey A. AkimovSergey A. Akimov
Sergey A. Akimov
AEAlexey I. Evseev
Alexey I. Evseev
SSSandra L. Schmid
Sandra L. Schmid
JZJoshua Zimmerberg
Joshua Zimmerberg
VFVadim A. Frolov
Vadim A. Frolov

1 February 2005 in Biophysical Journal
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Journal Article
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PKPeter I. Kuzmin
Peter I. Kuzmin
Sergey A. AkimovSergey A. Akimov
Sergey A. Akimov
YCYuri A. Chizmadzhev
Yuri A. Chizmadzhev
JZJoshua Zimmerberg
Joshua Zimmerberg
FCFredric S. Cohen
Fredric S. Cohen

6 March 2015 in Science Advances
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Journal Article
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Andreas HornerAndreas Horner
Andreas Horner
FZFlorian Zocher
Florian Zocher
JPJohannes Preiner
Johannes Preiner
NONicole Ollinger
Nicole Ollinger
CSChristine Siligan
Christine Siligan
Peter PohlPeter Pohl
Peter Pohl
Channel geometry governs the unitary osmotic water channel permeability, pf, according to classical hydrodynamics. Yet, pf varies by several orders of magnitude for membrane channels with a constriction zone that is one water molecule in width and four to eight molecules in length. We show that both the pf of those channels and the diffusion coefficient of the single-file waters within them are determined by the number NH of residues in the channel wall that may form a hydrogen bond with the single-file waters. The logarithmic dependence of water diffusivity on NH is in line with the multiplicity of binding options at higher NH densities. We obtained high-precision pf values by (i) having measured the abundance of the reconstituted aquaporins in the vesicular membrane via fluorescence correlation spectroscopy and via high-speed atomic force microscopy, and (ii) having acquired the vesicular water efflux from scattered light intensities via our new adaptation of the Rayleigh-Gans-Debye equation.

22 March 2013 in Science
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Journal Article
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ASAnna V. Shnyrova
Anna V. Shnyrova
PBPavel V. Bashkirov
Pavel V. Bashkirov
Sergey A. AkimovSergey A. Akimov
Sergey A. Akimov
TPThomas J. Pucadyil
Thomas J. Pucadyil
JZJoshua Zimmerberg
Joshua Zimmerberg
VFVadim A. Frolov
Vadim A. Frolov
Making the Cut: Dynamin is the prototypical member of a large family of structurally related guanosine triphosphatases involved in membrane fission and fusion. A variety of models have been suggested to explain how dynamin works. Shnyrova et al. (p. 1433 ; see the Perspective by Holz ) reconstituted dynamin-mediated membrane scission on lipid nanotubes and suggest a molecular model for dynamin activity that takes into consideration all known aspects of dynamin function.

22 September 2017 in Scientific Reports
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Journal Article
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Sergey A. AkimovSergey A. Akimov
Sergey A. Akimov
PVPavel E. Volynsky
Pavel E. Volynsky
TGTimur Galimzyanov
Timur Galimzyanov
PKPeter I. Kuzmin
Peter I. Kuzmin
KPKonstantin Vladimirovich Pavlov
Konstantin Vladimirovich Pavlov
Oleg BatishchevOleg Batishchev
Oleg Batishchev
Lipid membranes serve as effective barriers allowing cells to maintain internal composition differing from that of extracellular medium. Membrane permeation, both natural and artificial, can take place via appearance of transversal pores. The rearrangements of lipids leading to pore formation in the intact membrane are not yet understood in details. We applied continuum elasticity theory to obtain continuous trajectory of pore formation and closure, and analyzed molecular dynamics trajectories of pre-formed pore reseal. We hypothesized that a transversal pore is preceded by a hydrophobic defect: intermediate structure spanning through the membrane, the side walls of which are partially aligned by lipid tails. This prediction was confirmed by our molecular dynamics simulations. Conversion of the hydrophobic defect into the hydrophilic pore required surmounting some energy barrier. A metastable state was found for the hydrophilic pore at the radius of a few nanometers. The dependence of the energy on radius was approximately quadratic for hydrophobic defect and small hydrophilic pore, while for large radii it depended on the radius linearly. The pore energy related to its perimeter, line tension, thus depends of the pore radius. Calculated values of the line tension for large pores were in quantitative agreement with available experimental data.

18 January 2007 in Physical Review E
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Journal Article
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Sergey A. AkimovSergey A. Akimov
Sergey A. Akimov
PKPeter I. Kuzmin
Peter I. Kuzmin
JZJoshua Zimmerberg
Joshua Zimmerberg
FCFredric S. Cohen
Fredric S. Cohen
The effect of an external applied lateral tension on the line tension between two domains of different thickness in a lipid bilayer membrane is calculated. The thick domain is treated as a liquid-ordered phase in order to model a raft in a biological membrane; the thin domain is considered a liquid-disordered phase to model the surrounding region. In our model, the monolayers elastically distort at the boundary to create a smooth rather than steplike boundary to avoid exposure of the hydrophobic interior of the thick raft to water. The energy of this distortion is described by the fundamental deformations of splay and tilt. This energy per unit length of boundary yields the line tension of the raft. Applying lateral tension alters the fundamental deformations such that line tension increases. This increase in line tension is larger when the spontaneous curvature of a raft is greater than that of the surround; if the spontaneous curvature of the raft is less than that of the surround, the increase of the line tension due to application of the lateral tension is more modest.