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

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

Covering: 1992 up to 2023 Since their discovery, lasso peptides went from peculiarities to
be recognized as a major family of ribosomally synthesized and post-translationally modified …

Abstract Ion Mobility Spectrometry (IMS) is a widely used technique for the post-ionization
separation and structural characterization of biomolecules. Trapped IMS (TIMS) is a …

Lanthipeptides belong to the family of ribosomally synthesized and post-translationally
modified peptides (RiPPs). The (methyl) lanthionine cross-links characteristic to …

A technique combining ion mobility spectrometry‐mass spectrometry (IMS‐MS) and
supercharging electrospray ionization (ESI) has been demonstrated to differentiate protein …

Abstract Trapped Ion Mobility Spectrometry (TIMS) is a recently developed form of ion
mobility spectrometry (IMS) which is flexible in its operation and readily hybridized with mass …

Lasso peptides belong to the natural product superfamily of ribosomally synthesized and
post‐translationally modified peptides (RiPPs). They are defined by an N‐terminal …

Native ion mobility-mass spectrometry (IM-MS) is an emerging biophysical approach to
probe the intricate details of protein structure and function. The instrument design enables …

Entangled proteins have attracted significant research interest. Herein, we report the first
rationally designed lasso proteins, or protein [1] rotaxanes, by using a p53dim‐entwined …