First-pass extracted concept

kinase-substrate phosphomotif analysis

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We performed kinase-substrate phosphomotif analysis based on prior studies and employed computational tools to identify putative phosphosites in NiV proteins and corresponding host kinases.

Evidence 1Source 1DOI PubMedprovenance

Supporting Sources

Source 1primary paper2025MEDDOI PubMed

1 evidence snippet 4 linked claims Claim 1 Claim 2 Claim 3

Linked Claims

Claim 1computational predictionsupports2025Source 1DOI PubMed

LRRK2, HASPIN, MAST2, and EEF2K were predicted to phosphorylate experimentally validated sites on Nipah virus N, P, and W proteins.

Claim 2computational predictionsupports2025Source 1DOI PubMed

Motif-based kinase-substrate analysis identified 51 human kinases predicted to target 1180 phosphorylation sites across nine Nipah virus proteins.

Claim 3mechanistic inferencesupports2025Source 1DOI PubMed

The findings indicate that EEF2K phosphorylates key Nipah virus proteins at conserved phosphosites across variants.

Claim 4therapeutic hypothesissupports2025Source 1DOI PubMed

Known inhibitors of prioritized host kinases were identified as compounds that could potentially be repurposed as antiviral agents against Nipah virus infection.