ArticleNature communications2026
Dynamic control of IDP interaction network via diverse binding pathways.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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
3 citing papers in PubMed.
- Review
- Advancements in single-molecule fluorescence spectroscopy for probing conformations, dynamics, and interactions in disordered protein regions.Current opinion in structural biology · 2026Review
- Dynamic control of IDP interaction network via diverse binding pathways.Nature communications · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Binding promiscuity is a central feature of interactions involving intrinsically disordered proteins (IDPs). IDPs can interact even simultaneously with multiple binding partners, but quantitative characterization of these multi-component interactions is challenging. Here, we characterize the binding pathways of the transactivation domain (TAD) of p53 with two binding partners (Taz2 and Mdm2) using three-color single-molecule Förster resonance energy transfer (FRET) spectroscopy. We show that the interactions of these three proteins occur via two pathways. The first pathway is competitive in that binding of one partner occurs after the other partner completely dissociates. The second is an allosteric pathway via the formation of a ternary complex. High time-resolution FRET using photon-by-photon analysis shows that these heterogeneous three-component interaction pathways are closely related with diverse transition paths of two-component TAD-Taz2 binding. Kinetic analysis shows that the allosteric pathway allows faster exchange of the binding partners with opposite functions. Our work demonstrates how a heterogeneous allosteric binding network can enable a faster response to changes in the external environment.
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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.