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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
ProteomicsDiadenosine tetraphosphate as a cosubstrate for AMPylation mediated by FICD
Diadenosine polyphosphates (ApnAs) are noncanonical nucleotides that are ubiquitous across all forms of life. Due to their strong accumulation upon cellular stress, they are considered alarmones to signal homeostatic imbalance. Nonetheless, their cellular role is poorly understood. In this work, we ...
ORGANISM(S): Homo sapiens (Human) 
2023-01-27 | PXD036450 | Pride
Diadenosine tetraphosphate Ampylation Ficd Post-translational modification Proteomics 
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 
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 
ProteomicsFICD activity and AMPylation remodelling modulate human neurogenesis
The AMPylation is novel protein post-translation modification. In consist of attachment of the adenosine monophosphate onto the serine, threonine or tyrosine amino acid residues of the protein. This process is catalysed by bacterial effectors or in human by protein FICD (also called HYPE) which cont...
ORGANISM(S): Homo sapiens (Human) 
2019-12-04 | PXD015062 | Pride
Chemical-proteomics Cerebral organoids. Phosphoramidate prodrugs Ficd Ampylation Neuronal development 
ProteomicsAMPylation profiling during neuronal differentiation reveals extensive variation on lysosomal proteins
Protein AMPylation is a prevalent posttranslational modification with an emerging role in neurodevelopment and neurodegeneration. Although in metazoans the two highly conserved protein AMP-transferases together with diverse group of AMPylated proteins have been identified using chemical proteomics a...
ORGANISM(S): Homo sapiens (Human) 
2021-12-01 | PXD023873 | Pride
Lysosome Ampylation 
ProteomicsPronucleotide probe for in vivo imaging of protein AMPylation.
Protein AMPylation is a prevalent posttranslational modification in human cells involved in the regulation of unfolded protein response and neural development. Here we present a novel pro-N6azA probe suitable for in vivo imaging and chemical proteomics profilling of AMPylated proteins. The pro-N6azA...
ORGANISM(S): Homo sapiens (Human) 
2019-12-10 | PXD016011 | Pride
Chemical proteomics Ampylation 
ProteomicsRab1b-AMPylation by Legionella DrrA is allosterically activated by Rab1
Legionella pneumophila infect eukaryotic cells by forming a replicative organelle – the Legionella containing vacuole. During this process, the bacterial protein DrrA/SidM is secreted and manipulates the activity and posttranslational modification (PTM) states of the vesicular trafficking regulator ...
ORGANISM(S): Legionella pneumophila Homo sapiens (Human) 
2021-01-04 | PXD019043 | Pride
Crosslink Legionella Rab Drra 
ProteomicsThe DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3
Intracellular bacterial pathogens such as Coxiella burnetii evade their host's immune response by secreting effector proteins that bind and modify host proteins, thereby reshaping cell signaling pathways that help establish a replication-friendly niche. Previous research has identified Filamentation...
ORGANISM(S): Homo sapiens (Human) Coxiella burnetii cb109 
2024-01-26 | PXD040330 | Pride
Ampylation Histone h3 Fic enzyme Dna-binding Coxiella burnetii 
ProteomicsAMPylation Regulates 5'-3' Exonuclease PLD3 processing
The 5’-3’ exonuclease phospholipase D3 (PLD3) is a type II transmembrane protein undergoing sequential post-translational modifications (PTM) by N-glycosylation, AMPylation and proteolytic cleavage. The substrates of PLD3 5’-3’ exonuclease activity are single-stranded DNAs and RNAs, which act as lig...
ORGANISM(S): Homo sapiens (Human) 
2025-09-11 | PXD057707 | Pride
Pld3 Ampylation Chemical proteomics Protein post-translational modifications 
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