Evidence map›Paper›PMID 35717672›Full record

ArticleSmall (Weinheim an der Bergstrasse, Germany)2022

Label-Free Quantification of Molecular Interaction in Live Red Blood Cells by Tracking Nanometer Scale Membrane Fluctuations.

Bo Yao, Yunze Yang, Nanxi Yu, Nongjian Tao, Di Wang, Shaopeng Wang, Fenni Zhang

Open access · greenAbstract read
In one paragraph

Article in Small (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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 at 2 institutions in 2 countries.

Bo YaoDepartment of Chemistry, Zhejiang University, Hangzhou, 310058, P. R. China.ORCID 0000-0002-7908-2672
Yunze YangCenter for Bioelectronics and Biosensors, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA.
Nanxi YuCenter for Bioelectronics and Biosensors, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA.
Nongjian TaoCenter for Bioelectronics and Biosensors, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA.
Di WangCenter for Bioelectronics and Biosensors, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA.
Shaopeng WangCenter for Bioelectronics and Biosensors, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA.ORCID 0000-0002-2680-0503
Fenni ZhangBiosensor National Special Laboratory, Key Laboratory for Biomedical Engineering of Education Ministry, Department of Biomedical Engineering, Zhejiang University, Hangzhou, 310027, P. R. China.
BioElectronics (United States) · USZhejiang Lab · CN

Funding

Measuring small molecule interactions with membrane proteins on single cells via detecting nanometer scale membrane deformationsR01GM124335 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI WANG, SHAOPENG · 2017 to 2020
$1.1M
NIGMS NIH HHS R01 GM124335NIH HHS R01GM124335
6 · The paper itself

Abstract

Molecular interactions in live cells play an important role in both cellular functions and drug discovery. Current methods for measuring binding kinetics involve extracting the membrane protein and labeling, while the in situ quantification of molecular interaction with surface plasmon resonance (SPR) imaging mainly worked with fixed cells due to the micro-motion related noises of live cells. Here, an optical imaging method is presented to measure the molecular interaction with live red blood cells by tracking the nanometer membrane fluctuations. The membrane fluctuation dynamics are measured by tracking the membrane displacement during glycoprotein interaction. The data are analyzed with a thermodynamic model to determine the elastic properties of the cell observing reduced membrane fluctuations under fixatives, indicating cell fixations affect membrane mechanical properties. The binding kinetics of glycoprotein to several lectins are obtained by tracking the membrane fluctuation amplitude changes on single live cells. The binding kinetics and strength of different lectins are quite different, indicating the glycoproteins expression heterogeneity in single cells. It is anticipated that the method will contribute to the understanding of mechanisms of cell interaction and communication, and have potential applications in the mechanical assessment of cancer or other diseases at the single-cell level, and screening of membrane protein targeting drugs.

Indexed as

ErythrocytesSurface Plasmon ResonanceGlycoproteinsKineticsLectinsMembrane ProteinsGlycoproteinsLectinsMembrane Proteinsbinding kineticslectinlive red blood cellsmembrane fluctuationoptical imaging

Identifiers

PMID35717672
PMCPMC9283308
OpenAlexW4283123477

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.