Evidence map›Paper›PMID 23199919›Full record

ArticleBiophysical journal2012

Fibers with integrated mechanochemical switches: minimalistic design principles derived from fibronectin.

Orit Peleg, Thierry Savin, German V Kolmakov, Isaac G Salib, Anna C Balazs, Martin Kröger, Viola Vogel

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Untensed fibronectin fibers: a novel hallmark of microthrombi.Frontiers in cardiovascular medicine · 2025
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  5. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 2 countries.

Orit PelegLaboratory of Applied Mechanobiology, Department of Health Sciences and Technology, ETH Zürich, Zürich, Switzerland.
Thierry Savin
German V Kolmakov
Isaac G Salib
Anna C Balazs
Martin Kröger
Viola Vogel
ETH Zurich · CHUniversity of Pittsburgh · US

Funding

European Research Council 233157
6 · The paper itself

Abstract

Inspired by molecular mechanisms that cells exploit to sense mechanical forces and convert them into biochemical signals, chemists dream of designing mechanochemical switches integrated into materials. Using the adhesion protein fibronectin, whose multiple repeats essentially display distinct molecular recognition motifs, we derived a computational model to explain how minimalistic designs of repeats translate into the mechanical characteristics of their fibrillar assemblies. The hierarchy of repeat-unfolding within fibrils is controlled not only by their relative mechanical stabilities, as found for single molecules, but also by the strength of cryptic interactions between adjacent molecules that become activated by stretching. The force-induced exposure of cryptic sites furthermore regulates the nonlinearity of stress-strain curves, the strain at which such fibers break, and the refolding kinetics and fraction of misfolded repeats. Gaining such computational insights at the mesoscale is important because translating protein-based concepts into novel polymer designs has proven difficult.

Indexed as

Amino Acid MotifsAmino Acid SequenceBiomechanical PhenomenaFibronectinsMicrofibrilsMolecular Dynamics SimulationMolecular Sequence DataPolymersProtein FoldingRepetitive Sequences, Amino AcidFibronectinsPolymers

Identifiers

PMID23199919
PMCPMC3491717
OpenAlexW1998133862

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.