The investigation of macromolecular biomolecules with ion mobility mass spectrometry (IM-
MS) techniques has provided substantial insights into the field of structural biology over the …

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

Imaging of proteoforms in human tissues is hindered by low molecular specificity and limited
proteome coverage. Here, we introduce proteoform imaging mass spectrometry (PiMS) …

Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is one of the
most widely used techniques in proteomics to achieve structural identification and …

Imaging mass spectrometry has become a mature molecular map** technology that is
used for molecular discovery in many medical and biological systems. While powerful by …

Mass spectrometry imaging (MSI) combines molecular and spatial information in a valuable
tool for a wide range of applications. Matrix‐assisted laser desorption/ionization (MALDI) is …

Small molecules with molecular weights less than 1500 Da represented by natural
metabolites such as amino acids, nucleotides, carbohydrates, lipids, flavonoids, alkaloids …

Simultaneous spatial localization and structural characterization of molecules in complex
biological samples currently represents an analytical challenge for mass spectrometry …

Imaging mass spectrometry (IMS) technologies are capable of map** a wide array of
biomolecules in diverse cellular and tissue environments. IMS has emerged as an essential …

Field asymmetric ion mobility spectrometry (FAIMS), when used in proteomics studies,
provides superior selectivity and enables more proteins to be identified by providing …