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ProteomicsProfiling nuclear cysteine ligandability and effects on nuclear localization using proximity labeling-coupled chemoproteomics
The nucleus controls cell growth and reproduction by well-orchestrated interactions between nuclear proteins and chromatin. Mutations that result in the dysregulation of these chromatin-associated proteins are known to lead to the onset of numerous diseases. Many of these nuclear proteins have remai...
ORGANISM(S): Homo sapiens (Human) 
2024-01-24 | PXD043732 | Pride
Chromatin association Turboid Nuclear cysteine ligandability Proximity labeling 
ProteomicsA Global Ligandability Map of Tryptoline Butynamide Stereoprobes Identifies Covalent Inhibitors of the Actin Maturation Protease ACTMAP
Covalent chemistry coupled with activity-based protein profiling (ABPP) offers a versatile approach for small-molecule ligand discovery in native biological contexts. The covalent ligandability maps generated by ABPP that target cysteine have frequently leveraged the acrylamide as a reactive group d...
ORGANISM(S): Homo sapiens (Human) 
2026-05-20 | PXD074619 | Pride
ProteomicsMAPK Pathway Inhibition Reshapes Kinase Chemoproteomic Ligandability Reporting on Cellular Activation States
Despite the pivotal role of oncogenic kinases in cancer initiation, progression, and resistance, functional profiling of their conformational states within cells remains challenging. Current methodologies often struggle to capture the dynamic structural features and inhibitor-bound conformations of ...
ORGANISM(S): Homo sapiens (Human) 
2026-05-13 | PXD063040 | Pride
Ia-alkyne Tmt Braf Trametinib Chemoproteomics Mass spectrometry Mek1/2 Vemurafenib Arsq-alkyne Cysteine and lysine ligandability Abpp Click chemistry 
UnknownGlobal profiling of lysine reactivity and ligandability in the human proteome.
Not available
S-EPMC5726523 | biostudies-literature
ProteomicsAssigning functionality to cysteines by base editing of cancer dependency genes
Chemical probes are lacking for most human proteins. Covalent chemistry represents an attractive strategy for expanding the ligandability of the proteome, and chemical proteomics has revealed numerous electrophile-reactive cysteines on diverse proteins. Determining which of these covalent binding ev...
ORGANISM(S): Homo sapiens (Human) 
2023-09-06 | PXD038239 | Pride
Cysteine Base editing Electrophile Cancer dependency Ligandability 
ProteomicsCysteine reactivity profiling identifies host regulators of Mycobacterium tuberculosis replication in human macrophages
Innate immune cells such as monocytes and macrophages provide the earliest defense against infection by intracellular pathogens by initiating signaling pathways and restricting pathogen replication. However, the full complement of proteins that mediate cell-autonomous immunity remains incompletely d...
ORGANISM(S): Homo sapiens (Human) 
2026-03-02 | PXD067709 | Pride
Innate immunity Cysteine Macrophage Mycobacterium tuberculosis Mass spectrometry Chemical proteomics Covalent probes 
ProteomicsAssigning functionality to cysteines by base editing of cancer dependency genes
Chemical probes are lacking for most human proteins. Covalent chemistry represents an attractive strategy for expanding the ligandability of the proteome, and chemical proteomics has revealed numerous electrophile-reactive cysteines on diverse proteins. Determining which of these covalent binding ev...
ORGANISM(S): Homo sapiens (Human) 
2023-09-06 | PXD038232 | Pride
Cysteine Base editing Electrophile Cancer dependency Ligandability 
UnknownFunctionalized Scout Fragments for Site-Specific Covalent Ligand Discovery and Optimization.
Not available
S-EPMC8155467 | biostudies-literature
ProteomicsSulfonyl-Imidazopyridines Decouple Reactivity from Stability for Ligandability Mapping and Covalent Inhibitor Discovery
Covalent probes and therapeutics require a balance between sufficient reactivity toward protein sites and stability for function in biological systems, yet enhancing stability often attenuates electrophilicity, constraining ligand discovery. Here, we show that single-atom N-to-C substitutions of sul...
ORGANISM(S): Mus musculus (Mouse) 
2026-08-21 | PXD079357 | Pride
Chemoproteomics 
ProteomicsAssigning functionality to cysteines by base editing of cancer dependency genes
  Covalent chemistry represents an attractive strategy for expanding the ligandability of the proteome, and chemical proteomics has revealed numerous electrophile-reactive cysteines on diverse human proteins. Determining which of these covalent binding events impact protein function, however, remain...
ORGANISM(S): Homo sapiens (Human) 
2023-09-06 | PXD041314 | Pride
Abpp Cysteine Base editing Covalent probe 
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