ArticleThe Journal of biological chemistry2018
Glycation of type I collagen selectively targets the same helical domain lysine sites as lysyl oxidase-mediated cross-linking.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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.
Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- Sites of non-enzymatic crosslinks pentosidine and glucosepane in collagen I of human cortical bone.Bone · 2026Article
- Serum Advanced Glycation End Products as Drivers of Poor Tendon Outcomes in Diabetes? An Emerging Hypothesis and Narrative Review.Endocrinology, diabetes & metabolism · 2026Review
- Bilateral anterior lens luxation with secondary glaucoma strongly associated with self-application of a percussion massage gun to closed eyelids: a case report.BMC ophthalmology · 2026Article
- Comprehensive profiling of the competitive interplay among carbamylation, glycation, and enzymatic cross-links in human bone.JBMR plus · 2026Article
- Advanced glycation end-product adducts alter the bone collagen network and human cortical bone fracture resistance.JBMR plus · 2026Article
- Menaquinone-7 Supplementation Increases Multiple Advanced Glycation End-Products and Oxidation Markers in Zucker Diabetic Fatty Rats.Nutrients · 2025Article
- Review
- Article
- Glycosylation Modulates the Structure and Functions of Collagen: A Review.Molecules (Basel, Switzerland) · 2024Review
- Article
- Glycation in the cardiomyocyte.Vitamins and hormones · 2024Review
- Exploring the Interplay between Polyphenols and Lysyl Oxidase Enzymes for Maintaining Extracellular Matrix Homeostasis.International journal of molecular sciences · 2023Review
- Collagen breaks at weak sacrificial bonds taming its mechanoradicals.Nature communications · 2023Article
- Temporal application of lysyl oxidase during hierarchical collagen fiber formation differentially effects tissue mechanics.Acta biomaterialia · 2023Article
- Article
- Collagen cross-link profiles and mineral are different between the mandible and femur with site specific response to perturbed collagen.Bone reports · 2022Article
- Review
- Ligament Alteration in Diabetes Mellitus.Journal of clinical medicine · 2022Review
- Regulators of collagen crosslinking in developing and adult tendons.European cells & materials · 2022Review
- Novel regulatory roles of small leucine-rich proteoglycans in remodeling of the uterine cervix in pregnancy.Matrix biology : journal of the International Society for Matrix Biology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Nonenzymatic glycation of collagen has long been associated with the progressive secondary complications of diabetes. How exactly such random glycations result in impaired tissues is still poorly understood. Because of the slow turnover rate of most fibrillar collagens, they are more susceptible to accumulate time-dependent glycations and subsequent advanced glycation end-products. The latter are believed to include cross-links that stiffen host tissues. However, diabetic animal models have also displayed weakened tendons with reduced stiffness. Strikingly, not a single experimentally identified specific molecular site of glycation in a collagen has been reported. Here, using targeted MS, we have identified partial fructosyl-hydroxylysine glycations at each of the helical domain cross-linking sites of type I collagen that are elevated in tissues from a diabetic mouse model. Glycation was not found at any other collagen lysine residues. Type I collagen in mouse tendons is cross-linked intermolecularly by acid-labile aldimine bonds formed by the addition of telopeptide lysine aldehydes to hydroxylysine residues at positions α1(I)Lys
Indexed as
Identifiers
What Socratic holds
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 Socratic graph.