Evidence map›Paper›PMID 32958922›Full record

ArticleNature methods2020

Plasmonic scattering imaging of single proteins and binding kinetics.

Pengfei Zhang, Guangzhong Ma, Wei Dong, Zijian Wan, Shaopeng Wang, Nongjian Tao

Abstract read
In one paragraph

Article in Nature methods, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing 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

74 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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  7. Article
  8. The Fantastic Single-Molecule Techniques.Chemical & biomedical imaging · 2026
    Review
  9. IR-AMES uncovers structure and composition of Alzheimer's tau oligomers.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Quantum relaxometry for detecting biomolecular interactions with single NV centers.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Quantitative, Label-Free Mapping of Cell Force Dynamics.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  19. Label-Free Single-Molecule Immunoassay.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  20. Article

14 more citing papers are in PubMed but not listed here.

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

6 authors.

Pengfei ZhangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ, USA.ORCID http://orcid.org/0000-0002-3595-0490
Guangzhong MaBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ, USA.ORCID http://orcid.org/0000-0002-1197-659X
Wei DongBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ, USA.
Zijian WanBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ, USA.
Shaopeng WangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ, USA. Shaopeng.Wang@asu.edu.ORCID http://orcid.org/0000-0002-2680-0503
Nongjian TaoBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ, USA.

Funding

Quantitative label-free imaging of membrane protein interaction kinetics on cellsR01GM107165 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI WANG, SHAOPENG · 2014 to 2021
$2.2M
NIGMS NIH HHS R01 GM107165
6 · The paper itself

Abstract

Measuring the binding kinetics of single proteins represents one of the most important and challenging tasks in protein analysis. Here we show that this is possible using a surface plasmon resonance (SPR) scattering technique. SPR is a popular label-free detection technology because of its extraordinary sensitivity, but it has never been used for imaging single proteins. We overcome this limitation by imaging scattering of surface plasmonic waves by proteins. This allows us to image single proteins, measure their sizes and identify them based on their specific binding to antibodies. We further show that it is possible to quantify protein binding kinetics by counting the binding of individual molecules, providing a digital method to measure binding kinetics and analyze heterogeneity of protein behavior. We anticipate that this imaging method will become an important tool for single protein analysis, especially for low volume samples, such as single cells.

Indexed as

Single Molecule ImagingHumansImmunoglobulin AImmunoglobulin MKineticsProtein BindingProtein Interaction MappingProteinsSurface Plasmon ResonanceImmunoglobulin AImmunoglobulin MProteins

Identifiers

PMID32958922
PMCPMC7541716

What OpenQuestion holds

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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.