Disulfide bonds (SS) are post-translational modifications important for the proper folding and
stabilization of many cellular proteins with therapeutic uses, including antibodies and other …

Cysteine oxidation states of extracellular proteins participate in functional regulation and in
disease pathophysiology. In the most common inherited dementia, cerebral autosomal …

Disulfide bonds are a class of important post-translational modifications that play important
roles in modulating the structures and functions of proteins. Therefore, the mapping of …

Excessive hydrogen peroxide causes oxidative stress in cells. The oxidation of two tyrosine
residues in proteins can generate o, o′-dityrosine, a putative biomarker for protein …

Motivation Cross-linking technique coupled with mass spectrometry (MS) is widely used in
the analysis of protein structures and protein-protein interactions. In order to identify cross …

Abstract Bone morphogenetic protein 1 (BMP-1) is an essential metalloproteinase to trigger
extracellular matrix assembly and organogenesis. Previous structural studies on the …

Despite huge efforts to map the human proteome using mass spectrometry the overall
sequence coverage achieved to date is still below 50%. Reasons for missing areas of the …

A disulfide bond is an important protein post-translational modification and plays a key role
in regulating protein oxidation status, protein structure, and stability. Analysis of a disulfide …

Mapping highly complicated disulfide linkages and free thiols via liquid chromatography–
tandem mass spectrometry (LC–MS2) is challenging because of the difficulties in optimizing …

Quorum sensing regulates the biofilm formation and expression of virulence factors in Vibrio
cholerae, an obligate human pathogen that continues to imperil human health. Cytoplasmic …