Evidence map›Paper›PMID 30218106›Full record

ArticleScientific reports2018

Proline provides site-specific flexibility for in vivo collagen.

Wing Ying Chow, Chris J Forman, Dominique Bihan, Anna M Puszkarska, Rakesh Rajan, David G Reid, David A Slatter, Lucy J Colwell, David J Wales, Richard W Farndale and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 80 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Chemistry of materials : a publication of the American Chemical Society · 2025
    Article
  7. Article
  8. Review
  9. Review
  10. Proton Conduction in Gly-X (X = Ser, Ser-Gly-Ser) and GS50.Bioengineering (Basel, Switzerland) · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Collagen fibril formationMaterials today. Bio · 2022
    Review
  15. Review
  16. Review
  17. Review
  18. Collagen- and hyaluronic acid-based hydrogels and their biomedical applications.Materials science & engineering. R, Reports : a review journal · 2021
    Article
  19. Article
  20. Article
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

11 authors at 4 institutions in 4 countries.

Wing Ying ChowDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0003-0719-5958
Chris J FormanDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Dominique BihanDepartment of Biochemistry, University of Cambridge, Downing Site, Cambridge, CB2 1QW, UK.
Anna M PuszkarskaDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Rakesh RajanDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
David G ReidDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
David A SlatterInstitute of Infection and Immunity, School of Medicine, Cardiff University, Cardiff, CF14 4XN, UK.
Lucy J ColwellDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
David J WalesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Richard W FarndaleDepartment of Biochemistry, University of Cambridge, Downing Site, Cambridge, CB2 1QW, UK.ORCID 0000-0001-6130-8808
Melinda J DuerDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK. mjd13@cam.ac.uk.
University of Cambridge · GBCardiff University · GBNorthwestern University · USUniversity of Calgary · CA

Funding

Biotechnology and Biological Sciences Research Council BB/G021392/1Wellcome Trust
6 · The paper itself

Abstract

Fibrillar collagens have mechanical and biological roles, providing tissues with both tensile strength and cell binding sites which allow molecular interactions with cell-surface receptors such as integrins. A key question is: how do collagens allow tissue flexibility whilst maintaining well-defined ligand binding sites? Here we show that proline residues in collagen glycine-proline-hydroxyproline (Gly-Pro-Hyp) triplets provide local conformational flexibility, which in turn confers well-defined, low energy molecular compression-extension and bending, by employing two-dimensional

Indexed as

Amino AcidsAmino Acid SequenceAnimalsCollagenFemaleFibrillar CollagensGlycineHydroxyprolineMagnetic Resonance SpectroscopyMiceMice, Inbred C57BLOsteoblastsPeptidesProlineProtein ConformationSheepAmino AcidsCollagenFibrillar CollagensGlycineHydroxyprolinePeptidesProline

Identifiers

PMID30218106
PMCPMC6138679
OpenAlexW2889610509

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.