The reaction of reducing carbohydrates with amino compounds described in 1912 by Louis‐
Camille Maillard is responsible for the aroma, taste, and appearance of thermally processed …

Methylglyoxal (MG) is a potent protein glycating agent. Glycation is directed to guanidino
groups of arginine residues forming mainly hydroimidazolone N δ-(5-hydro-5-methyl-4 …

Glycation of proteins, nucleotides and basic phospholipids by glyoxal and methylglyoxal-
physiological substrates of glyoxalase 1-iso potentially damaging to the proteome, genome …

The discovery of the enzymatic formation of lactic acid from methylglyoxal dates back to
1913 and was believed to be associated with one enzyme termed ketonaldehydemutase or …

Proteins are continuously affected by various intrinsic and extrinsic factors. Damaged
proteins influence several intracellular pathways and result in different disorders and …

Glycation is a major cause of spontaneous damage to proteins in physiological systems.
This is exacerbated in diabetes as a consequence of the increase in glucose and other …

Protein glycation is initiated by a nucleophilic addition reaction between the free amino
group from a protein, lipid or nucleic acid and the carbonyl group of a reducing sugar. This …

The traditionally perceived function of nutrition includes supplying the consumer with the
appropriate quantity and quality of substrates. As nutritional substrates, proteins are prone to …

The long‐term complications of diabetes have major consequences for individual subjects
and growing healthcare delivery and cost implications for society. Evidence for the benefits …

Ever since the discovery of the Maillard reaction in 1912 and the discovery of the interaction
between advanced glycation end-products and cellular receptors, impressive progress has …