J
Joel A. Dain
Researcher at University of Rhode Island
Publications - 69
Citations - 1461
Joel A. Dain is an academic researcher from University of Rhode Island. The author has contributed to research in topics: Glycation & Human serum albumin. The author has an hindex of 22, co-authored 69 publications receiving 1301 citations. Previous affiliations of Joel A. Dain include Cornell University.
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Evaluation of Polyphenol Anthocyanin-Enriched Extracts of Blackberry, Black Raspberry, Blueberry, Cranberry, Red Raspberry, and Strawberry for Free Radical Scavenging, Reactive Carbonyl Species Trapping, Anti-Glycation, Anti-β-Amyloid Aggregation, and Microglial Neuroprotective Effects.
Hang Ma,Shelby L. Johnson,Weixi Liu,Nicholas A. DaSilva,Susan Meschwitz,Joel A. Dain,Navindra P. Seeram +6 more
TL;DR: The berry ACEs showed superior free radical scavenging, reactive carbonyl species trapping, and anti-glycation effects compared to their respective ACFs, and warrant further in vivo studies to evaluate their potential neuroprotective effects against AD.
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Pomegranate phenolics inhibit formation of advanced glycation endproducts by scavenging reactive carbonyl species
TL;DR: It is suggested that pomegranate may offer an attractive dietary strategy for the prevention and treatment of AGE-related diseases such as type-2 diabetes and Alzheimer's disease.
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The occurrence of histamine and tyramine in rumen ingesta of experimentally over-fed sheep.
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The enzymic synthesis of ganglioside: IV. UDP-N-acetylgalactosamine:(N-acetylneuraminyl)-galactosylglucosyl ceramide N-acetylgalactosaminyl-transferase in rat brain☆
Joseph L. Dicesare,Joel A. Dain +1 more
TL;DR: The enzyme showed highest activity in brain tissue and the specific activity of the enzyme decreased with increasing age of the rats.
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Glucitol-core containing gallotannins inhibit the formation of advanced glycation end-products mediated by their antioxidant potential
TL;DR: The inhibitory effects of five GCGs (containing 1-4 galloyls) on the formation of advanced glycation end-products (AGEs) were evaluated and revealed that the GCGs were able to protect the secondary structure of BSA protein from glycation.