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Benjamin S. Szwergold
Researcher at Dartmouth College
Publications - 60
Citations - 2867
Benjamin S. Szwergold is an academic researcher from Dartmouth College. The author has contributed to research in topics: Glycation & Fructose. The author has an hindex of 27, co-authored 60 publications receiving 2733 citations. Previous affiliations of Benjamin S. Szwergold include Dartmouth–Hitchcock Medical Center & Fox Chase Cancer Center.
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Journal ArticleDOI
Metformin reduces systemic methylglyoxal levels in type 2 diabetes.
TL;DR: MG is elevated in diabetes and relates to glycemic control, and metformin treatment may protect against diabetic complications by mechanisms independent of its antihyperglycemic effect.
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Identification of fructose 3-phosphate in the lens of diabetic rats.
TL;DR: The increase in the concentration of fructose 3-phosphate in the lens of diabetic rats suggests that it and its hydrolysis product, 3-deoxyglucosone, may be responsible in part for the development of some diabetic complications in the Lens.
Journal ArticleDOI
Susceptibility to diabetic nephropathy is related to dicarbonyl and oxidative stress.
Paul J. Beisswenger,Keith S. Drummond,Robert G. Nelson,Scott K. Howell,Benjamin S. Szwergold,Michael Mauer +5 more
TL;DR: In this article, the relationship of methylglyoxal, 3-deoxyglucosone (3DG), and oxidative stress levels to diabetic nephropathy risk was examined in three populations with diabetes.
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α-Dicarbonyls Increase in the Postprandial Period and Reflect the Degree of Hyperglycemia
Paul J. Beisswenger,Scott K. Howell,Rita M. O’Dell,Mary E. Wood,Allison D. Touchette,Benjamin S. Szwergold +5 more
TL;DR: The higher postprandial levels of MG and 3-DG observed with greater PPGE may provide a partial explanation for the adverse effects of glycemic lability and support the value of agents that reduce glucose excursions.
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Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo.
TL;DR: The purification and characterization of a mammalian fructosamine-3-kinase (FN3K) is described, which phosphorylation destabilizes the FL adduct and leads to its spontaneous decomposition, thereby reversing the nonenzymatic glycation process at an early stage.