ArticleFrontiers in molecular biosciences2022
Substrate Protein Interactions and Methylglyoxal Modifications Reduce the Aggregation Propensity of Human Alpha-A-Crystallin G98R Mutant.
Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
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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
2 citing papers in PubMed, 2 citations in OpenAlex.
- Methylglyoxal-Induced Modification of Hen Egg White Lysozyme: Detection of Advanced Glycation End Products by High Resolution Mass Spectrometry.The protein journal · 2025Article
- SIRT1 inhibits apoptosis of human lens epithelial cells through suppressing endoplasmic reticulum stressInternational journal of ophthalmology · 2024Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The G98R mutation in αA-crystallin is associated with presenile cataract development in humans. Previous studies have indicated that mutant proteins altered structure, decreased stability, increased oligomeric size, loss of chaperone-like activity, and susceptibility to proteolysis could be contributing factors to cataract formation. To evaluate the effect of substrate protein interactions with the mutant protein on cataract formation, we have performed chaperone assays with alcohol dehydrogenase (ADH), citrate synthase (CS), and βB
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Registered trials
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