Evidence map›Paper›PMID 22584606›Full record

ArticleBiomechanics and modeling in mechanobiology2013

Highly sensitive single-fibril erosion assay demonstrates mechanochemical switch in native collagen fibrils.

Brendan P Flynn, Graham E Tilburey, Jeffrey W Ruberti

Erratum issuedAbstract read
In one paragraph

Article in Biomechanics and modeling in mechanobiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Collagen Mechanics.Sub-cellular biochemistry · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mechanochemistry of collagen.Acta biomaterialia · 2023
    Review
  10. Article
  11. Tissue mechanics coevolves with fibrillar matrisomes in healthy and fibrotic tissues.Matrix biology : journal of the International Society for Matrix Biology · 2022
    Review
  12. Article
  13. Article
  14. Review
  15. Tension in fibrils suppresses their enzymatic degradation - A molecular mechanism for 'use it or lose it'.Matrix biology : journal of the International Society for Matrix Biology · 2020
    Review
  16. Article
  17. Models of tendon development and injury.BMC biomedical engineering · 2019
    Article
  18. Multiscale model predicts increasing focal adhesion size with decreasing stiffness in fibrous matrices.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Article
  20. Internal strain drives spontaneous periodic buckling in collagen and regulates remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors.

Brendan P FlynnDepartment of Mechanical and Industrial Engineering, Northeastern University, Boston, MA 02115, USA.
Graham E Tilburey
Jeffrey W Ruberti

Funding

Mechanobiology of Matrix Production by Corneal FibroblastsR01EY015500 · NEI · NORTHEASTERN UNIVERSITY · PI RUBERTI, JEFFREY W · 2005 to 2014
$3.8M
NEI NIH HHS R01 EY015500PHS HHS NEI-R01015500
6 · The paper itself

Abstract

It has been established that the enzyme susceptibility of collagen, the predominant load-bearing protein in vertebrates, is altered by applied tension. However, whether tensile force increases or decreases the susceptibility to enzyme is a matter of contention. It is critical to establish a definitive understanding of the direction and magnitude of the force versus catalysis rate (k C ) relationship if we are to properly interpret connective tissue development, growth, remodeling, repair, and degeneration. In this investigation, we examine collagen/enzyme mechanochemistry at the smallest scale structurally relevant to connective tissue: the native collagen fibril. A single-fibril mechanochemical erosion assay with nN force resolution was developed which permits detection of the loss of a few layers of monomer from the fibril surface. Native type I fibrils (bovine) held at three levels of tension were exposed to Clostridium histolyticum collagenase A. Fibrils held at zero-load failed rapidly and consistently (20 min) while fibrils at 1.8 pN/monomer failed more slowly (35-55 min). Strikingly, fibrils at 23.9 pN/monomer did not exhibit detectable degradation. The extracted force versus k C data were combined with previous single-molecule results to produce a "master curve" which suggests that collagen degradation is governed by an extremely sensitive mechanochemical switch.

Indexed as

AnimalsBiochemistryBiomechanical PhenomenaCattleClostridiumCollagenasesFibrillar CollagensCollagenasesFibrillar Collagens

Identifiers

PMID22584606
PMCPMC3773243

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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.