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ProteomicsDrugMap: A quantitative pan-cancer analysis of cysteine ligandability
Cysteine-focused chemical proteomic platforms have accelerated the clinical development of covalent inhibitors of a wide-range of targets in cancer. However, how different oncogenic contexts influence cysteine targeting remains unknown. To address this question, we have developed DrugMap, an atlas o...
ORGANISM(S): Homo sapiens (Human) 
2024-04-23 | PXD047840 | Pride
Cysteine ligandability Quantitative proteomics Lc-ms/ms 
UnknownDrugMap: A quantitative pan-cancer analysis of cysteine ligandability.
Not available
S-EPMC11143475 | biostudies-literature
GenomicsDrugMap: A quantitative pan-cancer analysis of cysteine ligandability
DrugMap: A quantitative pan-cancer analysis of cysteine ligandability
PRJNA1079738 | ENA
UnknownProteome-wide ligandability maps of drugs with diverse cysteine-reactive chemotypes.
Not available
S-EPMC12106687 | biostudies-literature
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 
GenomicsDrugMap: A quantitative pan-cancer analysis of cysteine ligandability (ChIP-Seq)
DrugMap: A quantitative pan-cancer analysis of cysteine ligandability (ChIP-Seq)
PRJNA1079741 | ENA
GenomicsDrugMap: A quantitative pan-cancer analysis of cysteine ligandability (RNA-Seq)
DrugMap: A quantitative pan-cancer analysis of cysteine ligandability (RNA-Seq)
PRJNA1079745 | ENA
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
ProteomicsPervasive aggregation and depletion of host and viral proteins in response to cysteine-reactive electrophilic compounds
isoTOP-ABPP performed for a small library of cysteine-reactive compounds to assess cysteine ligandability of viral and host proteins towards these compounds.
ORGANISM(S): Homo sapiens (Human) 
2024-10-24 | PXD046278 | Pride
Isotop-abpp  sars-cov-2  cysteine-reactive compounds  proteostasis  orbitrap eclipse: sp3  faims 
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 
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