Evidence map›Paper›PMID 29254633›Full record

ArticleJournal of biomechanics2018

Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking.

T A Collier, A Nash, H L Birch, N H de Leeuw

Open access · hybridAbstract read
In one paragraph

Article in Journal of biomechanics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Angiogenesis in Lung Regeneration and Aging.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Use of Collagen in Cosmetic Products.Current issues in molecular biology · 2024
    Review
  6. Microstructural fatigue fracture behavior of glycated cortical bone.Medical & biological engineering & computing · 2023
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. 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

4 authors at 4 institutions in 2 countries.

T A CollierInstitute of Natural and Mathematical Sciences, Massey University, Auckland 0632, New Zealand.
A NashDepartment of Physiology, Anatomy and Genetics, University of Oxford, South Parks Road, Oxford OX1 3QX, United Kingdom.
H L BirchInstitute of Orthopaedics and Musculoskeletal Science, UCL, RNOH Stanmore Campus, London, United Kingdom.
N H de LeeuwSchool of Chemistry, Cardiff University, Cardiff CF10 1DF, United Kingdom. Electronic address: DeLeeuwN@cardiff.ac.uk.
Cardiff University · GBMassey University · NZUniversity College London · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K007785
6 · The paper itself

Abstract

Non-enzymatic advanced glycation end product (AGE) cross-linking of collagen molecules has been hypothesised to result in significant changes to the mechanical properties of the connective tissues within the body, potentially resulting in a number of age related diseases. We have investigated the effect of two of these cross-links, glucosepane and DOGDIC, on the tensile and lateral moduli of the collagen molecule through the use of a steered molecular dynamics approach, using previously identified preferential formation sites for intra-molecular cross-links. Our results show that the presence of intra-molecular AGE cross-links increases the tensile and lateral Young's moduli in the low strain domain by between 3.0-8.5% and 2.9-60.3% respectively, with little effect exhibited at higher strains.

Indexed as

ArginineCollagenCollagen Type IConnective TissueCross-Linking ReagentsDipeptidesElasticityGlycation End Products, AdvancedHumansHydrogen BondingImidazolesLysineMolecular Dynamics SimulationPeptidesProtein DomainsTensile StrengthArgininearginyllysineCollagenCollagen Type ICross-Linking ReagentsDipeptidesglucosepaneGlycation End Products, AdvancedImidazolesLysineN(6)-(2-((4-ammonio-5-oxido-5-oxopentyl)amino)-5-(2,3,4-trihydroxybutyl)3,5-dihydro-4H-imidazol-4-ylidene)lysinatePeptidesAgeingCollagenGlycationMolecular biomechanicsMolecular dynamicsProtein cross-linking

Identifiers

PMID29254633
PMCPMC5773075
OpenAlexW2768172722

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.