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Thorsten P. Degenhardt

Researcher at University of South Carolina

Publications -  18
Citations -  1753

Thorsten P. Degenhardt is an academic researcher from University of South Carolina. The author has contributed to research in topics: Glycation & Pentosidine. The author has an hindex of 11, co-authored 16 publications receiving 1680 citations. Previous affiliations of Thorsten P. Degenhardt include Heidelberg University & University of Minnesota.

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N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins.

TL;DR: Levels of CML and CEL are proposed to provide an index of glyoxal and methylglyoxal concentrations in tissues, alterations in glutathione homoeostasis and dicarbonyl metabolism in disease, and sources of advanced glycation end-products in tissue proteins in aging and disease.
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Role of the Maillard Reaction in Aging of Tissue Proteins ADVANCED GLYCATION END PRODUCT-DEPENDENT INCREASE IN IMIDAZOLIUM CROSS-LINKS IN HUMAN LENS PROTEINS

TL;DR: The presence of GOLD and MOLD in tissue proteins implicates methylglyoxal and glyoxal, either free or protein-bound, as important precursors of protein cross-links formed during Maillard reactions in vivo during aging and in disease.
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Technical note. The serum concentration of the advanced glycation end-product N epsilon-(carboxymethyl)lysine is increased in uremia.

TL;DR: It is demonstrated that an antibody used in a previous study, reporting increased levels of AGEs in patients with diabetes or on continuous ambulatory peritoneal dialysis and hemodialysis, recognizes CML as its major epitope, suggesting that ELISA assays for CML should be useful for the clinical measurement of A GEs in serum proteins.
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Carboxymethylethanolamine, a biomarker of phospholipid modification during the maillard reaction in vivo.

TL;DR: CME inhibited detection of advanced glycation end product (AGE)-modified protein in a competitive enzyme-linked immunosorbent assay using an anti-AGE antibody previously shown to recognize CML, suggesting that carboxymethyl-PE may be a component of AGE lipids detected in AGE low density lipoprotein.