Evidence map›Paper›PMID 35922374›Full record

ArticleAngewandte Chemie (International ed. in English)2022

In Situ Analysis of Membrane-Protein Binding Kinetics and Cell-Surface Adhesion Using Plasmonic Scattering Microscopy.

Pengfei Zhang, Xinyu Zhou, Jiapei Jiang, Jayeeta Kolay, Rui Wang, Guangzhong Ma, Zijian Wan, Shaopeng Wang

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
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  6. Quantitative, Label-Free Mapping of Cell Force Dynamics.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. [Progress in the analysis of hemolysis and coagulation models for interventional micro-axial flow blood pumps].Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi · 2024
    Review
  13. Review
  14. Review
  15. Article
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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

8 authors.

Pengfei ZhangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ 85287, USA.ORCID 0000-0002-3595-0490
Xinyu ZhouBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ 85287, USA.
Jiapei JiangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ 85287, USA.
Jayeeta KolayBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ 85287, USA.
Rui WangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ 85287, USA.
Guangzhong MaBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ 85287, USA.
Zijian WanBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ 85287, USA.
Shaopeng WangBiodesign Center for Bioelectronics and Biosensors, Arizona State University, Tempe, AZ 85287, USA.ORCID 0000-0002-2680-0503

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

Surface plasmon resonance microscopy (SPRM) is an excellent platform for in situ studying cell-substrate interactions. However, SPRM suffers from poor spatial resolution and small field of view. Herein, we demonstrate plasmonic scattering microscopy (PSM) by adding a dry objective on a popular prism-coupled surface plasmon resonance (SPR) system. PSM not only retains SPRM's high sensitivity and real-time analysis capability, but also provides ≈7 times higher spatial resolution and ≈70 times larger field of view than the typical SPRM, thus providing more details about membrane protein response to ligand binding on over 100 cells simultaneously. In addition, PSM allows quantifying the target movements in the axial direction with a high spatial resolution, thus allowing mapping adhesion spring constants for quantitatively describing the mechanical properties of the cell-substrate contacts. This work may offer a powerful and cost-effective strategy for upgrading current SPR products.

Indexed as

Membrane ProteinsMicroscopyKineticsLigandsProtein BindingSurface Plasmon ResonanceLigandsMembrane ProteinsBiosensorsCell AdhesionDrug DiscoveryMembrane ProteinsSurface Plasmon Resonance

Identifiers

PMID35922374
PMCPMC9561081

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.