Abstract Carnosine (β-alanyl-l-histidine) was discovered in 1900 as an abundant non-
protein nitrogen-containing compound of meat. The dipeptide is not only found in skeletal …

Protein carbonylation, one of the most harmful irreversible oxidative protein modifications, is
considered as a major hallmark of oxidative stress‐related disorders. Protein carbonyl …

Excessive oxidative stress leaves a protein carbonylation fingerprint in biological systems.
Carbonylation is an irreversible post-translational modification (PTM) that often leads to the …

Modification of proteins in conditions of oxidative stress can contribute to protein dysfunction
or tissue damage and disease progression. Bifunctional, most often α, β-unsaturated …

Proteins can become oxidatively modified in many different ways, either by direct oxidation
of amino acid side chains and protein backbone or indirectly by conjugation with oxidation …

The dipeptide carnosine has been observed to exert antiaging activity at cellular and whole
animal levels. This review discusses the possible mechanisms by which carnosine may …

The metabolic syndrome is a risk factor that increases the risk for development of renal and
vascular complications. This study addresses the effects of chronic administration of the …

Abstract Carnosine (β-alanyl-L-histidine) and related peptides such as homocarnosine (γ-
amino-butyryl-histidine), balenine β-alanyl-L-3-methylhistidine) and anserine β-alanyl-L-1 …

The detailed examination of enzyme molecules by mass spectrometry and other techniques
continues to identify hundreds of distinct PTMs. Recently, global analyses of enzymes using …

A polymorphism in the carnosine dipeptidase-1 gene (CNDP1), resulting in decreased
plasma carnosinase activity, is associated with a reduced risk for diabetic nephropathy …