ReviewCurrent opinion in structural biology2017
Protein unfolding under isometric tension-what force can integrins generate, and can it unfold FNIII domains?
Review in Current opinion in structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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.
Who cites it
8 citing papers in PubMed.
- Fibronectin matrix assembly at a glance.Journal of cell science · 2025Review
- Shaping Oncogenic Microenvironments: Contribution of Fibronectin.Frontiers in cell and developmental biology · 2024Review
- Review
- Substrate Resistance to Traction Forces Controls Fibroblast Polarization.Biophysical journal · 2020Article
- Direct observation of a coil-to-helix contraction triggered by vinculin binding to talin.Science advances · 2020Article
- Molecular Tension Sensors: Moving Beyond Force.Current opinion in biomedical engineering · 2019Article
- Article
- Heparin-fibronectin interactions in the development of extracellular matrix insolubility.Matrix biology : journal of the International Society for Matrix Biology · 2018Article
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
Extracellular matrix fibrils of fibronectin (FN) are highly elastic, and are typically stretched three to four times their relaxed length. The mechanism of stretching has been controversial, in particular whether it involves tension-induced unfolding of FNIII domains. Recent studies have found that ∼5pN is the threshold isometric force for unfolding various protein domains. FNIII domains should therefore not be unfolded until the tension approaches 5pN. Integrins have been reported to generate forces ranging from 1 to >50pN, but I argue that studies reporting 1-2pN are the most convincing. This is not enough to unfold FNIII domains. Even if domains were unfolded, 2pN would only extend the worm-like-chain to about twice the length of the folded domain. Overall I conclude that stretching FN matrix fibrils involves primarily the compact to extended conformational change of FN dimers, with minimal contribution from unfolding FNIII domains.
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Registered trials
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.