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MetabolomicsAttenuate host susceptibility to respiratory virus invasion by inhibiting interactions between host proteins SLC16A3 and AP1G1

Modulating cell endocytosis activity to reduce host susceptibility to virus represents a promising strategy for antiviral drug development. In this study, we reveal that lactate transporter SLC16A3 as a critical host factor for reducing diverse virus invasion. By performing metabolomics, proteomi...

2025-07-28 | MTBLS12788 | MetaboLights
ProteomicsThe tumor suppressor Fhit in complex with the alarmone Ap3A binds to the ribosome and impedes translation
Upon cellular stress, the concentration of the alarmone diadenosine triphosphate (Ap3A) increases and is thought to trigger downstream adaptive processes. The known Ap3A-hydrolase fragile histidine triad (Fhit) is known to form a complex with Ap3A. The molecular mechanism of Fhit-Ap3A signaling is h...
ORGANISM(S): Homo sapiens (Human) 
2022-12-20 | PXD029645 | Pride
Ap-ms Mass spectrometry Ribosome Xl-ms Fhit Ap3a Translation 
UnknownDiadenosine polyphosphates (Ap3A and Ap4A) behave as alarmones triggering the synthesis of enzymes of the phenylpropanoid pathway in Arabidopsis thaliana.
Not available
S-EPMC3642049 | biostudies-literature
UnknownChemical Proteomics of the Tumor Suppressor Fhit Covalently Bound to the Cofactor Ap3A Elucidates Its Inhibitory Action on Translation.
Not available
S-EPMC9121386 | biostudies-literature
UnknownNPP4 is a procoagulant enzyme on the surface of vascular endothelium.
Not available
S-EPMC4017314 | biostudies-literature
ProteomicsChemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate
The nucleotides diadenosine triphosphate (Ap3A) and diadenosine tetraphosphate (Ap4A) are formed in prokaryotic and eukaryotic cells. Since their concentrations increase significantly upon cellular stress, they are considered to be alarmones triggering stress adaptive processes. However, their cellu...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2022-02-15 | PXD020740 | Pride
Photo-affinity labeling Proteomics Apna 
UnknownControl of 5',5'-dinucleoside triphosphate catabolism by APH1, a Saccharomyces cerevisiae analog of human FHIT.
Not available
S-EPMC107174 | biostudies-literature
UnknownNeutrophils as sources of dinucleotide polyphosphates and metabolism by epithelial ENPP1 to influence barrier function via adenosine signaling.
Not available
S-EPMC6249842 | biostudies-literature
UnknownIn Vitro Response of Polyscias filicifolia (Araliaceae) Shoots to Elicitation with Alarmone-Diadenosine Triphosphate, Methyl Jasmonate, and Salicylic Acid.
Not available
S-EPMC7922777 | biostudies-literature
UnknownChemical proteomic profiling reveals protein interactors of the alarmones diadenosine triphosphate and tetraphosphate.
Not available
S-EPMC8490401 | biostudies-literature
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