Protein glycosylation involves the co-translational or post-translational addition of glycans to
proteins and is a crucial protein modification in health and disease. The aim of …

Background. Cholinesterases are a group of serine hydrolases that split the neurotransmitter
acetylcholine (ACh) and terminate its action. Of the two types, butyrylcholinesterase and …

Chromatographic stationary phases based on porous graphitic carbon were invented 30
years ago, while columns have been commercially available for 20 years. This special …

Almost all therapeutic proteins are glycosylated, with the carbohydrate component playing a
long-established, substantial role in the safety and pharmacokinetic properties of this …

The comprehensive analysis of protein glycosylation is a major requirement for
understanding glycoprotein function in biological systems, and is a prerequisite for …

Protein glycosylation is one of the most common post-translational modifications that are
essential for cell function across all domains of life. Changes in glycosylation are considered …

Mass spectrometry (MS) is used to quantify the relative distribution of glycans attached to
particular protein glycosylation sites (micro‐heterogeneity) and evaluate the molar site …

Structural analysis of complex mixtures of oligosaccharides using tandem mass
spectrometry is regularly complicated by the presence of a multitude of structural isomers …

In eukaryotes, class I α-mannosidases are involved in early N-glycan processing reactions
and in N-glycan–dependent quality control in the endoplasmic reticulum (ER). To investigate …

The burden of neonicotinoid insecticides (neonics) in humans has attracted widespread
attention in recent years due to the potential adverse effects. Nonetheless, information on …