ArticleNucleic acids research2026
The kinase inhibitor palbociclib binds to HIV TAR RNA with very low nanomolar affinity and exquisite specificity.
Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 1 paper.
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
1 citing paper in PubMed.
- Three-dimensional structure of the palbociclib-HIV TAR complex.Nucleic acids research · 2026Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors.
Funding
Abstract
We report that the kinase inhibitor Palbociclib is a very low nanomolar ligand for the HIV-1 TAR, a paradigmatic 'difficult-to-drug' RNA. Binding is exquisitely specific, since simple chemical modifications of the small molecule, single nucleotide substitutions, or base pair inversions abolish high affinity binding, and is independent from kinase inhibition. Palbociclib also inhibits recruitment of the super elongation complex (SEC) at low nM concentration, the long-standing aim of Tat-TAR targeting efforts. Thus, we demonstrate that low nM affinity, specificity, and potent biochemical activity against 'undruggable' RNAs can be readily found within the chemical space of drugs. The structural basis for binding and biochemical activity is demonstrated in the accompanying manuscript.
Indexed as
Identifiers
What Socratic 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 Socratic graph.