Evidence map›Paper›PMID 34608318›Full record

ArticleNature methods2021

Mass-sensitive particle tracking to elucidate the membrane-associated MinDE reaction cycle.

Tamara Heermann, Frederik Steiert, Beatrice Ramm, Nikolas Hundt, Petra Schwille

Open access · hybridAbstract read
In one paragraph

Article in Nature methods, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.7field-weighted citation impact, top 4% of its field
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

33 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Cardiolipin membranes drive Myosin VI activation, oligomerization, and processive cargo transport.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Label-Free Anti-Brownian Trapping of Single Nanoparticles in Solution.The journal of physical chemistry. C, Nanomaterials and interfaces · 2024
    Article
  8. Review
  9. Review
  10. Oligomerization-driven avidity correlates with SARS-CoV-2 cellular binding and inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Roadmap on Label-Free Super-Resolution Imaging.Laser & photonics reviews · 2023
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 2 countries.

Tamara Heermann *Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Planegg, Germany.ORCID http://orcid.org/0000-0003-1607-0727
Frederik Steiert *Department of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Planegg, Germany.ORCID http://orcid.org/0000-0001-5871-8064
Beatrice RammDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Planegg, Germany.ORCID http://orcid.org/0000-0002-7402-1942
Nikolas Hundt *Department of Cellular Physiology, Biomedical Center (BMC), Ludwig-Maximilians-Universität München, Planegg, Germany. nikolas.hundt@med.uni-muenchen.de.ORCID http://orcid.org/0000-0001-8217-671X
Petra SchwilleDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Planegg, Germany. schwille@biochem.mpg.de.ORCID http://orcid.org/0000-0002-6106-4847
Max Planck Institute of Biochemistry · DELudwig-Maximilians-Universität München · DEMax Planck Institute of Biophysics · DEPrinceton University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In spite of their great importance in biology, methods providing access to spontaneous molecular interactions with and on biological membranes have been sparse. The recent advent of mass photometry to quantify mass distributions of unlabeled biomolecules landing on surfaces raised hopes that this approach could be transferred to membranes. Here, by introducing a new interferometric scattering (iSCAT) image processing and analysis strategy adapted to diffusing particles, we enable mass-sensitive particle tracking (MSPT) of single unlabeled biomolecules on a supported lipid bilayer. We applied this approach to the highly nonlinear reaction cycles underlying MinDE protein self-organization. MSPT allowed us to determine the stoichiometry and turnover of individual membrane-bound MinD/MinDE protein complexes and to quantify their size-dependent diffusion. This study demonstrates the potential of MSPT to enhance our quantitative understanding of membrane-associated biological systems.

Indexed as

Biophysical PhenomenaAdenosine TriphosphatasesCell Cycle ProteinsCell MembraneEscherichia coliEscherichia coli ProteinsLipid BilayersAdenosine TriphosphatasesCell Cycle ProteinsEscherichia coli ProteinsLipid BilayersMinD protein, E coliMinE protein, E coli

Identifiers

PMID34608318
PMCPMC8490154
OpenAlexW3203100140

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.