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 …

Mass spectrometry-based biomolecular analyses have become permanent fixtures of
academic, industrial, and clinical research settings. The rise in utilization of mass …

N-Glycoproteomics, the system-wide study of glycans asparagine-linked to protein carriers,
holds a unique and still largely untapped potential to provide deep insights into the …

Glycosylation, and especially O-linked glycosylation, remains a critical blind spot in the
understanding of post-translational modifications. Due to their nature as proteins defined by …

The proteome, or collection of proteoforms expressed in a biological system, is dynamic and
heterogeneous. As our appreciation for the complexity of the proteome has evolved, so have …

Capillary zone electrophoresis-tandem mass spectrometry (CZE-MS/MS) has emerged as
an essential technique for top-down proteomics (TDP), providing superior separation …

Recent advancements in mass spectrometry (MS) have revolutionized quantitative
proteomics, with multiplex isotope labeling emerging as a key strategy for enhancing …

Mapping the ligandability or potential druggability of all proteins in the human proteome is a
central goal of mass spectrometry-based covalent chemoproteomics. Achieving this …

Understanding the thermal stability of the plant proteome in the context of the native cellular
environment would aid the design of crops with high thermal tolerance, but only limited such …

High-field asymmetric waveform ion mobility spectrometry (FAIMS) separates glycopeptides
in the gas phase prior to mass spectrometry (MS) analysis, thus offering the potential to …