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ProteomicsA platform for mapping reactive cysteines within the immunopeptidome
The major histocompatibility complex class I (MHC-I) antigen presentation pathways play pivotal roles in orchestrating immune responses. Recent studies have begun to utilize cysteines within the immunopeptidome for therapeutic applications, such as using covalent ligands to create haptenated neoanti...
ORGANISM(S): Homo sapiens (Human) 
2024-10-17 | PXD054678 | Pride
Immunopeptidome Reactive cysteines 
ProteomicsReimagining high-throughput profiling of reactive cysteines for cell-based screening of large electrophile libraries
Current methods for measuring amino-acid side-chain reactivity lack the throughput needed to screen large chemical libraries for interactions across the proteome. Here we redesigned the workflow for activity-based protein profiling of reactive cysteine residues by using a smaller desthiobiotin-based...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-01-26 | PXD022511 | Pride
Reactive cysteines Chemical proteomics 
ProteomicsChemical-proteomics profiling of reactive cysteines near a hydrophobic pocket
This project investigates reactive cysteine residues located near hydrophobic pockets in proteins, features conserved in autopalmitoylated proteins. S-palmitoylation is a post-translational modification that regulates protein localization and function, and has been implicated in neurological, metabo...
ORGANISM(S): Homo sapiens (Human) 
2025-11-20 | PXD070770 | Pride
Autopalmitoylation Hydrophobic pockets Chemical proteomics Reactive cysteines Druggable sites 
UnknownA platform for mapping reactive cysteines within the immunopeptidome.
Not available
S-EPMC11549463 | biostudies-literature
UnknownHyperCys: A Structure- and Sequence-Based Predictor of Hyper-Reactive Druggable Cysteines.
Not available
S-EPMC10054327 | biostudies-literature
ProteomicsSP3-enabled rapid and high coverage chemoproteomic identification of redox-sensitive cysteines
Cysteine residues undergo various oxidative modifications, acting as key sensors of reactive oxygen species (ROS) and reactive nitrogen species (RNS). Given that ROS and RNS have known roles in many pathophysiological processes, numerous proteome-wide strategies to profile cysteine oxidation state h...
ORGANISM(S): Homo sapiens (Human) 
2022-03-02 | PXD029500 | Pride
Chmoproteomics Cysteines Quantitation Mass spectrometry Redox T cells Isotopic 
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 
UnknownExploratory Covalent Docking of Michael-Acceptor Natural Products at Reactive Cysteines in Cancer Tyrosine Kinases.
Not available
S-EPMC12692623 | biostudies-literature
UnknownPredicting Reactive Cysteines with Implicit-Solvent-Based Continuous Constant pH Molecular Dynamics in Amber.
Not available
S-EPMC7772776 | biostudies-literature
ProteomicsPrioritization of antimicrobial targets by CRISPR-based oligo recombineering
Nucleophilic amino acids are important in covalent drug development yet underutilized as antimicrobial targets. Over recent years, several chemoproteomic technologies have been developed to mine chemically-accessible residues via their intrinsic reactivity toward electrophilic probes. However, these...
ORGANISM(S): Toxoplasma gondii RH 
2022-10-24 | PXD035658 | Pride
Toxoplasma gondii Oligo recombineering Proteomics 
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