Evidence map›Paper›PMID 27410733›Full record

ArticleBiophysical journal2016

Nanomechanics of Type I Collagen.

Sameer Varma, Joseph P R O Orgel, Jay D Schieber

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.0field-weighted citation impact, top 10% 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

49 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
  2. Observational
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Mechanosignaling in Osteoporosis: When Cells Feel the Force.International journal of molecular sciences · 2025
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Tendon mechanobiology in the context of tendon biofabrication.Frontiers in bioengineering and biotechnology · 2025
    Review
  14. The Multifaced Role of Collagen in Cancer Development and Progression.International journal of molecular sciences · 2024
    Review
  15. Extracellular derivatives for bone metabolism.Journal of advanced research · 2024
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Research Progress on Bioactive Factors against Skin Aging.International journal of molecular sciences · 2024
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Sameer VarmaDepartment of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, Florida. Electronic address: svarma@usf.edu.
Joseph P R O OrgelCenter for Molecular Study of Condensed Soft Matter, Illinois Institute of Technology, Chicago, Illinois; Department of Biology, Illinois Institute of Technology, Chicago, Illinois; Department of Physics, Illinois Institute of Technology, Chicago, Illinois.
Jay D SchieberCenter for Molecular Study of Condensed Soft Matter, Illinois Institute of Technology, Chicago, Illinois; Department of Physics, Illinois Institute of Technology, Chicago, Illinois; Department of Chemical and Biological Engineering, Illinois Institute of Technology, Chicago, Illinois. Electronic address: schieber@iit.edu.
Illinois Institute of Technology · USUniversity of South Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type I collagen is the predominant collagen in mature tendons and ligaments, where it gives them their load-bearing mechanical properties. Fibrils of type I collagen are formed by the packing of polypeptide triple helices. Higher-order structures like fibril bundles and fibers are assembled from fibrils in the presence of other collagenous molecules and noncollagenous molecules. Curiously, however, experiments show that fibrils/fibril bundles are less resistant to axial stress compared to their constituent triple helices-the Young's moduli of fibrils/fibril bundles are an order-of-magnitude smaller than the Young's moduli of triple helices. Given the sensitivity of the Young's moduli of triple helices to solvation environment, a plausible explanation is that the packing of triple helices into fibrils perhaps reduces the Young's modulus of an individual triple helix, which results in fibrils having smaller Young's moduli. We find, however, from molecular dynamics and accelerated conformational sampling simulations that the Young's modulus of the buried core of the fibril is of the same order as that of a triple helix in aqueous phase. These simulations, therefore, suggest that the lower Young's moduli of fibrils/fibril bundles cannot be attributed to the specific packing of triple helices in the fibril core. It is not the fibril core that yields initially to axial stress. Rather, it must be the portion of the fibril exposed to the solvent and/or the fibril-fibril interface that bears the initial strain. Overall, this work provides estimates of Young's moduli and persistence lengths at two levels of collagen's structural assembly, which are necessary to quantitatively investigate the response of various biological factors on collagen mechanics, including congenital mutations, posttranslational modifications and ligand binding, and also engineer new collagen-based materials.

Indexed as

Mechanical PhenomenaNanotechnologyBiomechanical PhenomenaCollagen Type IElastic ModulusMolecular Dynamics SimulationProtein Structure, SecondaryCollagen Type I

Identifiers

PMID27410733
PMCPMC4945622
OpenAlexW2466192351

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.