ArticleComputational and structural biotechnology journal2026
SARS-CoV-2 NSP8-Derived Peptide Effectively Suppresses the Activity of Helicase NSP13.
Article in Computational and structural biotechnology journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nonstructural protein 13 (NSP13) is a multifunctional helicase that plays a central role in viral RNA replication and suppression of host innate immunity. Beyond its essential function within the replication-transcription complex (RTC), NSP13 antagonizes type I interferon (IFN-I) signaling through interaction with the host kinase TBK1, making its protein-protein interactions attractive antiviral targets. In this study, we investigated whether fragments derived from the viral cofactor NSP8 can competitively interfere with NSP13 interactions. Using molecular dynamics simulations, interaction mapping, and neural network-based binding free energy prediction, we characterized NSP13 interfaces with (a) full-length NSP8 in 2 RTC binding modes, (b) N- and C-terminal NSP8 fragments, and (c) TBK1. Structural analyses revealed that the N-terminal fragment of NSP8 (NSP8-N, residues 1 to 87) binds NSP13 with high affinity and occupies residues critical for both TBK1 association and canonical NSP8-NSP13 interactions, including Met
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.