Mass spectrometry has potential as a tool for ecological studies and bioprospecting of natural products from marine cyanobacteria and algae.

A community-based international effort generates standardized HLA allele-specific peptide assay libraries and enables the analysis of the human immunopeptidome by SWATH mass spectrometry.

By performing ¹⁵N pulse-labeling of mice, the turnover of hundreds of proteins in eye tissues was measured by mass spectrometry that revealed long-lived metabolic enzymes in the lens.

Mass spectrometry exposes a post-transcriptionally regulated reduction in protein diversity in hematopoietic stem cells, including a lack of detectable Dnmt3a protein levels despite mRNA levels comparable to progenitors.

Protein mass spectrometry can be used to uncover developmental trajectories in small single cells of differentiating tissues.

An enrichable cross-linker with optional isotope labeling quadruples the number of cross-linked peptides identified from high-complexity samples, enhancing proteome-wide analysis of protein-protein interactions and protein conformational changes by mass spectrometry.

Phosphatidylglycerol binding at multiple sites stabilizes the open state relative to the desensitized state of a pentameric ligand-gated ion channel.

Comprehensive structural and compositional characterization of the in vivo 30S ribosomal assembly landscape reveals parallel pathways for 3′-domain formation and a previously unknown role for the assembly factor RimP.

Molecular details of how the iron–sulfur cluster cofactor of a bacterial global iron regulatory protein simultaneously senses iron and O₂ are revealed by mass spectrometry and spectroscopy.

Activation and autophosphorylation of CaMKII releases the regulatory segment, which can then bind to and destabilize the hub assembly by trapping large fluctuations in the hub architecture.