ArticleBiophysical chemistry2016
Intra-molecular lysine-arginine derived advanced glycation end-product cross-linking in Type I collagen: A molecular dynamics simulation study.
Article in Biophysical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Iontophoretic Delivery of Hyaluronic Acid Nanogel-Loaded Fermented Rice Extract Mitigates Skin Glycation.International journal of nanomedicine · 2025Article
- An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition.Biophysical reviews · 2024Review
- The Regulation of Collagen Processing by miRNAs in Disease and Possible Implications for Bone Turnover.International journal of molecular sciences · 2021Review
- Mechanistic Insights into the Structural Stability of Collagen-Containing Biomaterials Such as Bones and Cartilage.The journal of physical chemistry. B · 2021Article
- Lysine-arginine advanced glycation end-product cross-links and the effect on collagen structure: A molecular dynamics study.Proteins · 2021Article
- Allosteric Communications between Domains Modulate the Activity of Matrix Metalloprotease-1.Biophysical journal · 2020Article
- Matrix regeneration proteins in the hypoxia-triggered exosomes of shoulder tenocytes and adipose-derived mesenchymal stem cells.Molecular and cellular biochemistry · 2020Article
- Advancements in composition and structural characterization of bone to inform mechanical outcomes and modelling.Current opinion in biomedical engineering · 2019Article
- Protein Interaction with Charged Macromolecules: From Model Polymers to Unfolded Proteins and Post-Translational Modifications.International journal of molecular sciences · 2019Review
- Glycation of type I collagen selectively targets the same helical domain lysine sites as lysyl oxidase-mediated cross-linking.The Journal of biological chemistry · 2018Article
- Effect on the mechanical properties of type I collagen of intra-molecular lysine-arginine derived advanced glycation end-product cross-linking.Journal of biomechanics · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Covalently cross-linked advanced glycation end products (AGE) are among the major post-translational modifications to proteins as a result of non-enzymatic glycation. The formation of AGEs has been shown to have adverse effects on the properties of the collagenous tissue; they are even linked to a number of age related disorders. Little is known about the sites at which these AGEs form or why certain sites within the collagen are energetically more favourable than others. In this study we have used a proven fully atomistic molecular dynamics approach to identify six sites where the formation of the intra-molecular 3-deoxyglucosone-derived imidazolium cross-link (DOGDIC) is energetically favourable. We have also conducted a comparison of these positions with those of the more abundant glucosepane cross-link, to determine any site preference. We show that when we consider both lysine and arginine AGEs, they exhibit a prevalence to form within the gap region of the collagen fibril.
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Registered trials
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.