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ProteomicsUnbiased identification of the liposome protein corona using photoaffinity based chemoproteomics
Determination of protein adsorption to the surface of a nanoparticle determined by photoaffinity based chemoproteomics.
ORGANISM(S): Homo sapiens (Human) 
2020-04-02 | PXD016229 | Pride
Chemoproteomics photoaffinity labelling human serum protein corona 
GenomicsComprehensive landscape of active deubiquitinating enzymes profiled by advanced chemoproteomics
Comprehensive landscape of active deubiquitinating enzymes profiled by advanced chemoproteomics
PRJNA556874 | ENA
ProteomicsEnantioselective OTUD7B fragment discovery through chemoproteomics screening and high-throughput optimisation
Deubiquitinating enzymes (DUBs) are key regulators of cellular homeostasis, and their dysregulation is associated with several human diseases. The ovarian tumour protease (OTU) family of DUBs are biochemically well-characterised and of therapeutic interest, yet only a few tool compounds exist to stu...
ORGANISM(S): Homo sapiens (Human) 
2025-01-13 | PXD057851 | Pride
Dubs Dia Iodoacetamide-desthiobiotin (ia-dtb) Chemoproteomics Cysteine reactivity profiling Abpp 
ProteomicsEnantioselective OTUD7B fragment discovery through chemoproteomics screening and high-throughput optimisation
Here we present a chemoproteomics fragment screening platform for identifying novel DUB-specific hit matter, that combines activity-based protein profiling with high-throughput chemistry direct-to-biology optimisation to enable rapid elaboration of initial fragment hits against OTU DUBs. Applying th...
ORGANISM(S): Homo sapiens (Human) 
2025-01-13 | PXD054883 | Pride
Chemoproteomics Covalent fragments Data-independent acquisition Activity-based protein profiling Deubiquitinating enzymes 
ProteomicsRobust proteome profiling of cysteine-reactive fragments using label-free chemoproteomics - 80 compound screen (HEK293T and Jurkat)
In this manuscript we describe our work on the development of a label-free chemoproteomics screening platform for cysteine reactive covalent fragments on a 96 well plate format. Within this workflow, we profile cysteine reactive fragments by competition with the hyper-reactive iodoacetamide desthiob...
ORGANISM(S): Homo sapiens (Human) 
2024-11-18 | PXD054127 | Pride
Chemoproteomics Data independant acquisition Label-free qauntification 
ProteomicsChemoproteomics enables identification of coatomer subunit zeta-1 targeted by a small molecule for enterovirus A71 inhibition
Chemoproteomics identitied coatomer subunit zeta-1 as the anti-EV71 target of a marinopyrrole A derivate
ORGANISM(S): Homo Sapiens 
PXD052206 |
ProteomicsDifferential Chemoproteomics Reveals MARK2/3 as Cell Migration-Relevant Targets of the ALK Inhibitor Brigatinib
Metastasis poses a major challenge in cancer management, including EML4-ALK-rearranged non-small cell lung cancer (NSCLC). As cell migration is a critical step during metastasis, we assessed the anti-migratory activities of several clinical ALK inhibitors in NSCLC cells and observed differential ant...
ORGANISM(S): Homo sapiens (Human) 
2024-04-05 | PXD036716 | Pride
Anaplastic lymphoma kinase Lung cancer Brigatinib Chemical proteomics Alk 
UnknownCysDB: a human cysteine database based on experimental quantitative chemoproteomics.
Not available
S-EPMC10510411 | biostudies-literature
UnknownEnantioselective OTUD7B fragment discovery through chemoproteomics screening and high-throughput optimisation.
Not available
S-EPMC11732987 | biostudies-literature
ProteomicsActivity-based profiling of Shigella virulence factor OspF in human cells
Phosphothreonine lyases are a small family of bacterial virulence factors secreted into host cells during infection by certain Gram-negative pathogens. This family of enzymes is known for its unique mechanism of silencing host immune signaling via the irreversible β-elimination of phosphothreonine (...
ORGANISM(S): Homo sapiens (Human) 
2026-02-27 | PXD073985 | Pride
Ospf Dehydrobutyrine Chemoproteomics Phosphothreonine lyase Shigella Bacterial infection Human 
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