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UnknownSpatiotemporally resolved mapping of extracellular proteomes via in vivo-compatible TyroID.
Not available
S-EPMC11910615 | biostudies-literature
UnknownSpatiotemporal profiling of modification-specific proteome secretion uncovers an itaconation-activated tyrosine kinase.
Not available
S-EPMC12686461 | biostudies-literature
ProteomicsMulti-phase hybrid metabolomics framework identifies clinically applicable plasma signatures for early detection of gastric cancer
Plasma metabolomics offers significant potential for non-invasive biomarker discovery in gastric cancer (GC), yet conventional analytical workflows face challenges in absolute quantification and biological interpretability, hindering clinical translation. We present an innovative multi-phase hybrid ...
ORGANISM(S): Homo Sapiens 
2025-11-24 | PXD071237 |
ProteomicsSpatiotemporally-resolved mapping of extracellular proteomes via in vivo-compatible TyroID
Extracellular proteins play pivotal roles in both intracellular signaling and intercellular communications in health and disease. While recent advancements in proximity labeling (PL) methods, such as peroxidase- and photocatalyst-based approaches, have facilitated the resolution of extracellular pro...
ORGANISM(S): Homo Sapiens Mus Musculus Bos Taurus 
2024-11-21 | PXD054796 |
ProteomicsSilicon-rhodamine-enabled Identification (SeeID) for Near-Infrared Light Controlled Proximity Labeling In Vitro and In Vivo
Advancement in fluorescence imaging techniques enables the study of protein dynamics and localization with unprecedented spatiotemporal resolution. However, current imaging tools are unable to elucidate dynamic protein interactomes underlying imaging observations. In contrast, proteomics tools such ...
ORGANISM(S): Homo Sapiens Mus Musculus 
2025-08-11 | PXD067243 |
ProteomicsDevelopment of Substrate-Directed Activity-Based Probes via Disulfide-Trapping for Site-Specific Interrogation of Nucleosomal Deubiquitination
Activity-based ubiquitin probes (Ub-ABPs) have been instrumental in interrogating deubiquitinases (DUBs), yet conventional Ub-ABPs lack the substrate-specific and site-specific contextual cues required to investigate nucleosomal DUBs, whose activity is tightly regulated by the chromatin environments...
ORGANISM(S): Homo Sapiens 
2025-12-30 | PXD072417 |
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