Evidence map›Paper›PMID 27070851›Full record

ArticleACS nano2016

Flow-Induced Crystallization of Collagen: A Potentially Critical Mechanism in Early Tissue Formation.

Jeffrey A Paten, Seyed Mohammad Siadat, Monica E Susilo, Ebraheim N Ismail, Jayson L Stoner, Jonathan P Rothstein, Jeffrey W Ruberti

Erratum issuedAbstract read
In one paragraph

Article in ACS nano, 2016. 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 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Collagen Mechanics.Sub-cellular biochemistry · 2026
    Review
  5. Review
  6. Article
  7. Fibroblast integrin α11β1 is a collagen assembly receptor in mechanoregulated fibrillar adhesions.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
  8. Production of Nanofibrillar Patterned Collagen for Tissue Engineering.Journal of visualized experiments : JoVE · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Mechanochemistry of collagen.Acta biomaterialia · 2023
    Review
  13. Article
  14. Biomedical Applications of Collagen.Bioengineering (Basel, Switzerland) · 2023
    Article
  15. Microengineering 3D Collagen Hydrogels with Long-Range Fiber Alignment.Journal of visualized experiments : JoVE · 2022
    Article
  16. Article
  17. Article
  18. Engineering fiber anisotropy within natural collagen hydrogels.American journal of physiology. Cell physiology · 2021
    Review
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Jeffrey A PatenDepartment of Bioengineering, Northeastern University , 360 Huntington Avenue, Boston, Massachusetts 02115, United States.
Seyed Mohammad SiadatDepartment of Bioengineering, Northeastern University , 360 Huntington Avenue, Boston, Massachusetts 02115, United States.
Monica E SusiloDepartment of Bioengineering, Northeastern University , 360 Huntington Avenue, Boston, Massachusetts 02115, United States.
Ebraheim N IsmailDepartment of Bioengineering, Northeastern University , 360 Huntington Avenue, Boston, Massachusetts 02115, United States.
Jayson L StonerDepartment of Bioengineering, Northeastern University , 360 Huntington Avenue, Boston, Massachusetts 02115, United States.
Jonathan P RothsteinDepartment of Mechanical and Industrial Engineering, University of Massachusetts Amherst , 160 Governors Drive, Amherst, Massachusetts 01003, United States.
Jeffrey W RubertiDepartment of Bioengineering, Northeastern University , 360 Huntington Avenue, Boston, Massachusetts 02115, United States.

Funding

Mechanobiology of Matrix Production by Corneal FibroblastsR01EY015500 · NEI · NORTHEASTERN UNIVERSITY · PI RUBERTI, JEFFREY W · 2005 to 2014
$3.8M
NEI NIH HHS R01 EY015500
6 · The paper itself

Abstract

The type I collagen monomer is one of nature's most exquisite and prevalent structural tools. Its 300 nm triple-helical motifs assemble into tough extracellular fibers that transition seamlessly across tissue boundaries and exceed cell dimensions by up to 4 orders of magnitude. In spite of extensive investigation, no existing model satisfactorily explains how such continuous structures are generated and grown precisely where they are needed (aligned in the path of force) by discrete, microscale cells using materials with nanoscale dimensions. We present a simple fiber drawing experiment, which demonstrates that slightly concentrated type I collagen monomers can be "flow-crystallized" to form highly oriented, continuous, hierarchical fibers at cell-achievable strain rates (<1 s(-1)) and physiologically relevant concentrations (∼50 μM). We also show that application of tension following the drawing process maintains the structural integrity of the fibers. While mechanical tension has been shown to be a critical factor driving collagen fibril formation during tissue morphogenesis in developing animals, the precise role of force in the process of building tissue is not well understood. Our data directly couple mechanical tension, specifically the extensional strain rate, to collagen fibril assembly. We further derive a "growth equation" which predicts that application of extensional strains, either globally by developing muscles or locally by fibroblasts, can rapidly drive the fusion of already formed short fibrils to produce long-range, continuous fibers. The results provide a pathway to scalable connective tissue manufacturing and support a mechano-biological model of collagen fibril deposition and growth in vivo.

Indexed as

CrystallizationAnimalsCollagenCollagen Type IExtracellular MatrixStress, MechanicalTissue EngineeringCollagenCollagen Type Icollagendevelopmentextensional strainflow-induced crystallizationself-assembly

Identifiers

PMID27070851
PMCPMC6037489

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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.