ArticleiScience2026
Insights into human TLR9 structural dynamics and recognition of pathogen-associated CpG DNA using molecular dynamics simulation.
Article in iScience, 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
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human toll-like receptor 9 (TLR9) is a key pattern-recognition receptor that detects unmethylated CpG motifs in pathogen single-stranded (ss) DNA. Although structural information for non-human TLR9 ectodomains exists, the conformational dynamics of human TLR9 remain poorly understood. Here, we modeled the TLR9 ectodomain and performed all-atom simulations of apo TLR9, CpG-bound TLR9, and CpG-immunomodulator (IM) co-bound TLR9. We show that the apo ectodomain formed a stable pre-assembled homodimer and CpG ssDNA was observed to bind with a 2:2 stoichiometry, bridging both monomers and inducing localized rearrangements within the leucine-rich repeat region. CpG ssDNA binding enhanced Z-loop flexibility by ∼2 folds in the TLR9_CpG and TLR9_CpG_IM complexes. Furthermore, CpG ssDNA and IM engagement reorganized inter-monomer contacts and revealed previously unrecognized functional residues like H612, H641, T642, and K690, that supports cooperative ligand stabilization. Together, these simulations identify candidate structural transitions and putative allosteric nodes in human TLR9 for future experimental studies.
Indexed as
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.