Evidence map›Paper›PMID 32591769›Full record

ArticleNature protocols2020

Reconstitution and real-time quantification of membrane remodeling by single proteins and protein complexes.

Pavel V Bashkirov, Peter I Kuzmin, Ksenia Chekashkina, Pedro Arrasate, Javier Vera Lillo, Anna V Shnyrova, Vadim A Frolov

Abstract read
In one paragraph

Article in Nature protocols, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

  1. Article
  2. SARS-CoV-2 FP1 Destabilizes Lipid Membranes and Facilitates Pore Formation.International journal of molecular sciences · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Membrane activity of viral proteins.Biophysical reviews · 2023
    Article
  7. Article
  8. Review
  9. Review
  10. Nonlinear material and ionic transport through membrane nanotubes.Biochimica et biophysica acta. Biomembranes · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Pavel V BashkirovFederal Research and Clinical Centre of Physical-Chemical Medicine, Moscow, Russia. pavel.bashkirov@niifhm.ru.ORCID http://orcid.org/0000-0003-2250-9759
Peter I KuzminA. N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, Moscow, Russia.
Ksenia ChekashkinaFederal Research and Clinical Centre of Physical-Chemical Medicine, Moscow, Russia.
Pedro ArrasateBiofisika Institute (CSIC, UPV/EHU), University of the Basque Country, Leioa, Spain.
Javier Vera LilloBiofisika Institute (CSIC, UPV/EHU), University of the Basque Country, Leioa, Spain.
Anna V ShnyrovaBiofisika Institute (CSIC, UPV/EHU), University of the Basque Country, Leioa, Spain.
Vadim A FrolovBiofisika Institute (CSIC, UPV/EHU), University of the Basque Country, Leioa, Spain. vadim.frolov@ehu.eus.ORCID http://orcid.org/0000-0002-0653-5669

Funding

Functional nanoscopy of membrane deformations and fission by dynamin superfamily membersR01GM121725 · NIGMS · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI FROLOV, VADIM A, NOY, ALEKSANDR · 2017 to 2021
$2.3M
NIGMS NIH HHS R01 GM121725
6 · The paper itself

Abstract

Cellular membrane processes, from signal transduction to membrane fusion and fission, depend on acute membrane deformations produced by small and short-lived protein complexes working in conditions far from equilibrium. Real-time monitoring and quantitative assessment of such deformations are challenging; hence, mechanistic analyses of the protein action are commonly based on ensemble averaging, which masks important mechanistic details of the action. In this protocol, we describe how to reconstruct and quantify membrane remodeling by individual proteins and small protein complexes in vitro, using an ultra-short (80- to 400-nm) lipid nanotube (usNT) template. We use the luminal conductance of the usNT as the real-time reporter of the protein interaction(s) with the usNT. We explain how to make and calibrate the usNT template to achieve subnanometer precision in the geometrical assessment of the molecular footprints on the nanotube membrane. We next demonstrate how membrane deformations driven by purified proteins implicated in cellular membrane remodeling can be analyzed at a single-molecule level. The preparation of one usNT takes ~1 h, and the shortest procedure yielding the basic geometrical parameters of a small protein complex takes 10 h.

Indexed as

Cell MembraneLipid BilayersMembrane ProteinsNanotechnologyNanotubesLipid BilayersMembrane Proteins

Identifiers

PMID32591769
PMCPMC10839814

What OpenQuestion holds

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Registered trials

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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.