Evidence map›Paper›PMID 30024378›Full record

ArticleeLife2018

Tunable molecular tension sensors reveal extension-based control of vinculin loading.

Andrew S LaCroix, Andrew D Lynch, Matthew E Berginski, Brenton D Hoffman

Abstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

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  16. Article
  17. Principles and regulation of mechanosensing.Journal of cell science · 2024
    Review
  18. bioRxiv : the preprint server for biology · 2024
    Article
  19. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Andrew S LaCroixDepartment of Biomedical Engineering, Duke University, Durham, United States.ORCID 0000-0003-0117-4785
Andrew D LynchDepartment of Biomedical Engineering, Duke University, Durham, United States.
Matthew E BerginskiDepartment of Biomedical Engineering, Duke University, Durham, United States.
Brenton D HoffmanDepartment of Biomedical Engineering, Duke University, Durham, United States.ORCID 0000-0003-2296-1331

Funding

Visualizing and Elucidating the Role of Force on Type IV Collagen in DevelopmentR21HD084290 · NICHD · DUKE UNIVERSITY · PI SHERWOOD, DAVID R · 2016 to 2017
$412k
The Role of Ezrin in Membrane and Actin InteractionsF32GM119294 · NIGMS · DUKE UNIVERSITY · PI BERGINSKI, MATTHEW EDWARD · 2016 to 2016
$56k
NICHD NIH HHS R21 HD084290NIGMS NIH HHS F32 GM119294NIH HHS 1R21-HD084290-01NIH HHS F32-GM-119294
6 · The paper itself

Abstract

Molecular tension sensors have contributed to a growing understanding of mechanobiology. However, the limited dynamic range and inability to specify the mechanical sensitivity of these sensors has hindered their widespread use in diverse contexts. Here, we systematically examine the components of tension sensors that can be altered to improve their functionality. Guided by the development of a first principles model describing the mechanical behavior of these sensors, we create a collection of sensors that exhibit predictable sensitivities and significantly improved performance

Indexed as

Biosensing TechniquesAmidesAmino Acid SequenceAnimalsBiomechanical PhenomenaBiophysical PhenomenaCalibrationFluorescence Resonance Energy TransferFocal AdhesionsHEK293 CellsHumansLuminescent ProteinsMiceModels, BiologicalPeptidesPyridinesAmidesLuminescent ProteinsPeptidesPyridinesTalinVinculinY 27632cell biologyfocal adhesionFRETmechanobiologymolecular biophysicsnonestructural biologytension sensorvinculin

Identifiers

PMID30024378
PMCPMC6053308

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.