ArticleJournal of fluorescence2014
Effect of non-enzymatic glycation on cystatin: a spectroscopic study.
Article in Journal of fluorescence, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed, 21 citations in OpenAlex.
- Label-Free Evaluation of Advanced Glycation End Products by a Comprehensive Biophysical Analysis.Analytical chemistry · 2026Article
- Antiglycation potential of metal ions and polyphenolic extract of chickpea on thiol-protease inhibitor: A management for diabetic complications.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024Article
- Advanced glycation end products induce neural tube defects through elevating oxidative stress in mice.Neural regeneration research · 2018Article
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The study shows the effect of nonenzymatic glycation on conformation and inhibitory activity of chick pea cystatin (CPC). CPC was incubated with different reducing sugars, pentose (D-Ribose), hexoses (D-Glucose, D-Fructose) at 37 °C for 5 weeks. To evaluate the modification of CPC by these different sugars during the glycation process the extent of the Maillard reaction, conformational, structural and functional changes were investigated. The behaviour of glycated CPC was monitored by the techniques of UV and fluorescence spectroscopies. Specific fluorescence was employed to characterise the glycation and AGEs. The anti-papain activity of glycated CPC was found to be significantly lower as compared to its non-glycated form. Glycation with ribose led to maximum loss in inhibitory activity. It was found that the incubation of CPC with all the mentioned sugars led to a parallel increase in tryptophan fluorescence as well as in Maillard and other AGEs specific fluorescence values and hyperchromicity in the UV-region. Among the sugars studied comparatively ribose was found to be the most active in inducing structural and conformational alterations in the protein suggesting its high reactivity with protein amino groups.
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What OpenQuestion 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 OpenQuestion graph.