ArticleJournal of diabetes investigation2021
Glyoxal-induced formation of advanced glycation end-products in type 1 collagen decreases both its strength and flexibility in vitro.
Article in Journal of diabetes investigation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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.
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Who cites it
6 citing papers in PubMed, 1 synthesis or guideline pooled it, 8 citations in OpenAlex.
- Advanced Glycation End Products and Health: A Systematic Review.Annals of biomedical engineering · 2024Pooled it
- A nomogram with online dynamic calculator for predicting osteoporosis: development and validation based on NHANES.BMC musculoskeletal disorders · 2026Article
- Glycoxidation of the bone matrix modulates mineralization.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2025Article
- Article
- Prenylflavonoids isolated fromFrontiers in chemistry · 2024Article
- Glyoxal-induced formation of advanced glycation end-products in type 1 collagen decreases both its strength and flexibility in vitro.Journal of diabetes investigation · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
The high plasma glucose induced in glucose metabolism disorders leads to the non-enzymatic glucose-dependent modification (glycation) of type 1 collagen, which is an essential component of bone tissue. The glycation of proteins induces the formation of advanced glycation end-products, such as carboxymethyl arginine, which is preferentially generated in glycated collagen. However, the effect of advanced glycation end-product formation on the characteristics of type 1 collagen remains unclear due to the lack of suitable in vitro experimental systems analyzing type 1 collagen. Here, we show that the glycation of type 1 collagen can be analyzed in vitro using a goldfish-scale bone model. Our study using these scales provides evidence that the advanced glycation end-product formation in type 1 collagen induced by glyoxal, the carboxymethyl arginine inducer, facilitates the crosslinking of type 1 collagen, decreasing both its strength and flexibility.
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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.