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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 
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 
UnknownSmall-Molecule FICD Inhibitors Suppress Endogenous and Pathologic FICD-Mediated Protein AMPylation.
Not available
S-EPMC12007993 | biostudies-literature
UnknownSmall molecule FICD inhibitors suppress endogenous and pathologic FICD-mediated protein AMPylation.
Not available
S-EPMC11275912 | biostudies-literature
UnknownCatalytic deAMPylation in AMPylation-inhibitory/assistant forms of FICD protein.
Not available
S-EPMC9905249 | biostudies-literature
UnknownFICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP.
Not available
S-EPMC5221731 | biostudies-literature
UnknownFicD sensitizes cellular response to glucose fluctuations in mouse embryonic fibroblasts.
Not available
S-EPMC11420183 | biostudies-literature
UnknownFICD activity and AMPylation remodelling modulate human neurogenesis.
Not available
S-EPMC6981130 | biostudies-literature
UnknownProduction of an Active, Human Membrane Protein in Saccharomyces cerevisiae: Full-Length FICD.
Not available
S-EPMC8910494 | biostudies-literature
UnknownStructures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD.
Not available
S-EPMC8373988 | biostudies-literature
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