Corrigendum to "OncoProExp: An interactive shiny web application for comprehensive cancer proteomics and phosphoproteomics analysis" [Comput. Struct. Biotechnol. J. 27 (2025) 3993-4006]. [PDF]
Rahmani ES +6 more
europepmc +1 more source
Deciphering Cancer Therapy-Induced Cardiotoxicity in the Era of Spatial and Multi-Omics from Systemic Mechanisms to <i>In Situ</i> Microenvironments. [PDF]
Gou C +6 more
europepmc +1 more source
The role and mechanisms of AMPK in neurovascular unit injury in Parkinson's disease. [PDF]
Liu B +5 more
europepmc +1 more source
Strategies for multimodal spatiotemporal profiling of phosphorylation in cilia biology. [PDF]
Turn RE +3 more
europepmc +1 more source
Sabinineoside B alleviates metabolic dysfunction-associated steatotic liver disease by targeting PPAR α. [PDF]
Feng Y +8 more
europepmc +1 more source
Subcellular phosphoproteomics [PDF]
AbstractProtein phosphorylation represents one of the most extensively studied post‐translational modifications, primarily due to the emergence of sensitive methods enabling the detection of this modification both in vitro and in vivo. The availability of enrichment methods combined with sensitive mass spectrometry instrumentation has played a crucial ...
Trost, Matthias +3 more
openaire +4 more sources
Phosphoproteomics: Methods and Challenges [PDF]
Protein phosphorylation is a widespread post-translational modification that regulates many biological processes. This covalent modification alters the biochemical properties of proteins and can act as an activity switch or as a docking site for protein-protein interactions.
Kang, Taewook +3 more
openaire +3 more sources
Plant phosphoproteomics: An update [PDF]
Abstract Phosphoproteomics involves identification of phosphoproteins, precise mapping, and quantification of phosphorylation sites, and eventually, revealing their biological function. In plants, several systematic phosphoproteomic analyses have recently been performed to optimize in vitro
Kersten, B. +6 more
openaire +4 more sources

