How tumors generate a cryptic “dark” proteome absent from healthy tissues, and whether it can be reversibly activated, remains unclear. In Ewing sarcoma, all tumors are driven by EWSR1::ETS fusions, m...

Nature Reviews Molecular Cell Biology, Published online: 18 February 2026; doi:10.1038/s41580-026-00947-3Proteins can localize to multiple cellular compartments and some exhibit distinct functions depending on their location. This Review discusses the mechanisms of protein localization, the control of specialized protein functions through subcellular localization, and how mislocalization is involved in cancer, neurodegeneration and autoimmunity.

Proteoforms are the diverse protein molecules produced from a single gene whose primary sequence and composition can be diversified by genetic, transcriptomic, translational and post-translational var...

Proteomic analyses in mouse hearts with genetic deficiencies in nitric oxide/cGMP signalling pathways reveal significant disruptions in metabolic processes, cardiomyocyte contraction, and kinase/phosp...

Background One of the most promising approaches for early and more precise disease prediction and diagnosis is through the inclusion of proteomics data augmented with clinical data. Clinical proteomic...

The human genome encodes potentially thousands of tiny proteins that were previously overlooked. The search is on to find out what they do.

The PRIDE database is the largest public data repository of mass spectrometry-based proteomics data and currently stores more than 40,000 data sets covering a wide range of organisms, experimental techniques, and biological conditions. During the past few years, PRIDE has seen a significant increase in the amount of submitted data-independent acquisition (DIA) proteomics data sets. This provides an excellent opportunity for large-scale data reanalysis and reuse. We have reanalyzed 15 public label-free DIA data sets across various healthy human tissues to provide a state-of-the-art view of the human proteome in baseline conditions (without any perturbations). We computed baseline protein abundances and compared them across various tissues, samples, and data sets. Our second aim was to compare protein abundances obtained here from the results of previous analyses using human baseline data-dependent acquisition (DDA) data sets. We observed a good correlation across some tissues, especially in the liver and colon, but weak correlations were found in others, such as the lung and pancreas. The reanalyzed results including protein abundance values and curated metadata are made available to view and download from the resource Expression Atlas.

Approaches for profiling the spatial proteome in tissues are the basis of atlas-scale projects that are delivering on their promise for understanding biological complexity in health and disease.