Evidence map›Paper›PMID 34608319›Full record

ArticleNature methods2021

Mass photometry enables label-free tracking and mass measurement of single proteins on lipid bilayers.

Eric D B Foley, Manish S Kushwah, Gavin Young, Philipp Kukura

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 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 124 citations in OpenAlex.

  1. Article
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  3. Immunoglobulin binding protein (BiP) forms two types of dimers.Protein science : a publication of the Protein Society · 2026
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  9. Mass Photometry Analysis of Membrane Proteins in Detergent Micelles.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  10. Article
  11. Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  12. 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
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Label-Free Anti-Brownian Trapping of Single Nanoparticles in Solution.The journal of physical chemistry. C, Nanomaterials and interfaces · 2024
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Eric D B Foley *Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0001-7880-578X
Manish S Kushwah *Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Gavin YoungPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK.
Philipp KukuraPhysical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, UK. philipp.kukura@chem.ox.ac.uk.ORCID http://orcid.org/0000-0003-0136-7704
University of Oxford · GB

Funding

Medical Research Council
6 · The paper itself

Abstract

The quantification of membrane-associated biomolecular interactions is crucial to our understanding of various cellular processes. State-of-the-art single-molecule approaches rely largely on the addition of fluorescent labels, which complicates the quantification of the involved stoichiometries and dynamics because of low temporal resolution and the inherent limitations associated with labeling efficiency, photoblinking and photobleaching. Here, we demonstrate dynamic mass photometry, a method for label-free imaging, tracking and mass measurement of individual membrane-associated proteins diffusing on supported lipid bilayers. Application of this method to the membrane remodeling GTPase, dynamin-1, reveals heterogeneous mixtures of dimer-based oligomers, oligomer-dependent mobilities, membrane affinities and (dis)association of individual complexes. These capabilities, together with assay-based advances for studying integral membrane proteins, will enable the elucidation of biomolecular mechanisms in and on lipid bilayers.

Indexed as

DynaminsLipid BilayersPhotometryProteinsDynaminsLipid BilayersProteins

Identifiers

PMID34608319
PMCPMC8490153
OpenAlexW3184163355

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.