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ProteomicsHYPE mediated AMPylation profiling in human lysates
We describe here the first example of global chemoproteomic screening and substrate validation for HYPE mediated AMPylation in mammalian cell lysate. Through quantitative mass spectrometry-based proteomics coupled with novel chemoproteomic tools providing MS/MS evidence of AMP modification we identi...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080782 | MassIVE
ProteomicsIdentification of myristoylated proteins in Human cell lines (HEK293, HeLa, MCF7)
Multi-functional capture reagents reported here enable robust identification of metabolically-tagged myristoylated proteomes with unprecedented confidence resulting from the combination of chemical probe-based enrichment, and release and direct detection of lipid-modified peptides by MS. Whilst capt...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080690 | MassIVE
ProteomicsHYPE mediated AMPylation profiling in human lysates
We describe here the first example of global chemoproteomic screening and substrate validation for HYPE mediated AMPylation in mammalian cell lysate. Through quantitative mass spectrometry-based proteomics coupled with novel chemoproteomic tools providing MS/MS evidence of AMP modification we identi...
ORGANISM(S): Homo sapiens (Human) 
2015-12-02 | PXD002601 | Pride
Hype Chemical proteomics Ampylation Fic 
ProteomicsQuantitative Chemical Proteomic Profiling of Ubiquitin Specific Proteases in Intact Cancer Cells
Deubiquitinating enzymes play an important role in a plethora of therapeutically relevant processes, and are emerging as pioneering drug targets. Herein, we present a novel Ubiquitin Specific Protease (USP) inhibitor, alongside an alkyne-tagged activity-based probe analogue. Activity-based proteome ...
ORGANISM(S): Homo sapiens (Human) 
2016-12-14 | PXD004875 | Pride
Abpp Chemical proteomics Lc-msms Ubiquitin 
ProteomicsQuantitative lipoproteomics in Clostridium difficile reveals a role for lipoproteins in sporulation
Bacterial lipoproteins are surface exposed, anchored to the membrane by S diacylglyceryl modification of the N-terminal cysteine thiol. They play important roles in many essential cellular processes including, in bacterial pathogens, at the host-pathogen interface. Clostridium difficile is a Gram-po...
ORGANISM(S): Peptoclostridium difficile (strain R20291) (Clostridium difficile) Peptoclostridium difficile (strain 630) (Clostridium difficile) 
2022-03-02 | PXD002426 | Pride
R20291 Ynmyr Lipoproteome Clostridium difficile 630 Peptoclostridium difficile 
ProteomicsValidation and invalidation of chemical probes for the human N-myristoyltransferases.
On-target, cell-active chemical probes are of fundamental importance in both chemical and cell biology, whereas the application of poorly-characterised probes often leads to invalid conclusions. Human N-myristoyltransferase (NMT) has attracted increasing interest as a target in cancer and infectious...
ORGANISM(S): Homo sapiens (Human) 
2019-11-14 | PXD012722 | Pride
N-myristoylation Imp-366 (ddd85646) Metabolic tagging Tris-dba palladium Myristic acid alkyne ynmyr Chemical proteomics Imp-1088 D-nmappd (b13) 2-hydroxymyristic acid 
ProteomicsIdentification of protein-protein interactions in live cells using photoactivatable myristate probe X10
19 TST-tagged myristoylated proteins (baits) were transfected into cells and labeled with photoactivatable clickable myristate probe X10. mCitrine-TST was used as a negative control. X10-labeled proteins were photocrosslinked in live cells to their interacting partners with the aim of identifying ne...
ORGANISM(S): Homo sapiens (Human) 
2023-02-04 | PXD027394 | Pride
Myristoylation  photocrosslinking  protein-protein interaction 
ProteomicsHYPE mediated AMPylation site profiling with YnATP in human lysates
We describe here the first example of global chemoproteomic screening for HYPE mediated AMPylation sites of human proteins. Catalytically active mutant HYPE E234G was applied in combination with an alkynylated ATP and an alkynyl-biotinylated side ID reagent for capture of chemoenzymatically tagged ...
ORGANISM(S): Homo sapiens (Human) 
2015-12-02 | PXD003053 | Pride
Human Protein ampylation Chemoproteomics 
ProteomicsProfiling N-myristoyltransferase activity and inhibition in breast cancer cells (MD-MB-231) using Sortase-A labelling
We report a novel application for Sortase A (SrtA), labeling N-terminal Gly proteins across the proteome at endogenous levels. We combined SrtA labeling of whole-cell lysates with a potent and selective NMT inhibitor, delivering a method capable of quantifying changes in cellular NMT activity in mul...
ORGANISM(S): Homo sapiens (Human) 
2018-10-25 | PXD010634 | Pride
Sortase a  srta  n-myristoylation  nmt 
ProteomicsN-Myristoyltransferase inhibition in HeLa
N-Myristoyltransferase (NMT) covalently attaches a C14-fatty acid to the N-terminal glycine of proteins and has been proposed as a therapeutic target in cancer. We used quantitative proteomics to map protein expression changes for more than 2700 proteins in response to treatment with an NMT inhibito...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080783 | MassIVE
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