Evidence map›Paper›PMID 28945706›Full record

ArticleNature methods2017

Multiplexing molecular tension sensors reveals piconewton force gradient across talin-1.

Pia Ringer, Andreas Weißl, Anna-Lena Cost, Andrea Freikamp, Benedikt Sabass, Alexander Mehlich, Marc Tramier, Matthias Rief, Carsten Grashoff

Abstract read
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Article in Nature methods, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing 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

95 citing papers in PubMed.

  1. Article
  2. Mechanical regulation of cell memory.Nature structural & molecular biology · 2026
    Review
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  6. Article
  7. Review
  8. Review
  9. Article
  10. Force-dependent structural dynamics of the giant nesprin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

35 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

9 authors.

Pia RingerGroup of Molecular Mechanotransduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Andreas WeißlPhysics Department E22, Technical University of Munich, Garching, Germany.
Anna-Lena CostGroup of Molecular Mechanotransduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Andrea FreikampGroup of Molecular Mechanotransduction, Max Planck Institute of Biochemistry, Martinsried, Germany.
Benedikt SabassICS-2/IAS-2, Forschungszentrum Jülich, Jülich, Germany.
Alexander MehlichPhysics Department E22, Technical University of Munich, Garching, Germany.
Marc TramierCNRS, UMR 6290, Rennes, France.
Matthias RiefPhysics Department E22, Technical University of Munich, Garching, Germany.
Carsten GrashoffGroup of Molecular Mechanotransduction, Max Planck Institute of Biochemistry, Martinsried, Germany.ORCID http://orcid.org/0000-0003-0118-9231

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Förster resonance energy transfer (FRET)-based tension sensor modules (TSMs) are available for investigating how distinct proteins bear mechanical forces in cells. Yet, forces in the single piconewton (pN) regime remain difficult to resolve, and tools for multiplexed tension sensing are lacking. Here, we report the generation and calibration of a genetically encoded, FRET-based biosensor called FL-TSM, which is characterized by a near-digital force response and increased sensitivity at 3-5 pN. In addition, we present a method allowing the simultaneous evaluation of coexpressed tension sensor constructs using two-color fluorescence lifetime microscopy. Finally, we introduce a procedure to calculate the fraction of mechanically engaged molecules within cells. Application of these techniques to new talin biosensors reveals an intramolecular tension gradient across talin-1 that is established upon integrin-mediated cell adhesion. The tension gradient is actomyosin- and vinculin-dependent and sensitive to the rigidity of the extracellular environment.

Indexed as

CalibrationFluorescence Resonance Energy TransferFocal AdhesionsMicroscopy, FluorescenceMyosinsTalinMyosinsTalinTLN1 protein, human

Identifiers

PMID28945706

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.