Evidence map›Paper›PMID 26875524›Full record

ArticleScientific reports2016

Constructing modular and universal single molecule tension sensor using protein G to study mechano-sensitive receptors.

Xuefeng Wang, Zainab Rahil, Isaac T S Li, Farhan Chowdhury, Deborah E Leckband, Yann R Chemla, Taekjip Ha

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
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  9. Engineering tunable catch bonds with DNA.Nature communications · 2024
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  11. bioRxiv : the preprint server for biology · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
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  19. 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

7 authors.

Xuefeng WangDepartment of Physics, Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Zainab RahilDepartment of Physics, Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Isaac T S LiDepartment of Physics, Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Farhan ChowdhuryInstitute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Deborah E LeckbandDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Yann R ChemlaDepartment of Physics, Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Taekjip HaDepartment of Physics, Center for the Physics of Living Cells, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

Funding

Cadherin Adhesion and MechanosensingR01GM097443 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI LECKBAND, DEBORAH E · 2012 to 2016
$1.3M
Howard Hughes Medical InstituteNIGMS NIH HHS 5R01 GM 097443NIGMS NIH HHS R01 GM097443
6 · The paper itself

Abstract

Recently a variety of molecular force sensors have been developed to study cellular forces acting through single mechano-sensitive receptors. A common strategy adopted is to attach ligand molecules on a surface through engineered molecular tethers which report cell-exerted tension on receptor-ligand bonds. This approach generally requires chemical conjugation of the ligand to the force reporting tether which can be time-consuming and labor-intensive. Moreover, ligand-tether conjugation can severely reduce the activity of protein ligands. To address this problem, we developed a Protein G (ProG)-based force sensor in which force-reporting tethers are conjugated to ProG instead of ligands. A recombinant ligand fused with IgG-Fc is conveniently assembled with the force sensor through ProG:Fc binding, therefore avoiding ligand conjugation and purification processes. Using this approach, we determined that molecular tension on E-cadherin is lower than dsDNA unzipping force (nominal value: 12 pN) during initial cadherin-mediated cell adhesion, followed by an escalation to forces higher than 43 pN (nominal value). This approach is highly modular and potentially universal as we demonstrate using two additional receptor-ligand interactions, P-selectin &PSGL-1 and Notch &DLL1.

Indexed as

AnimalsBiomechanical PhenomenaBiosensing TechniquesCadherinsCell AdhesionCHO CellsCricetulusDNAHumansMechanoreceptorsRecombinant ProteinsCadherinsDNARecombinant Proteins

Identifiers

PMID26875524
PMCPMC4753514

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Registered trials

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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.