ReviewFEBS open bio2026
Molecular determinants of signal transduction in tropomyosin receptor kinases.
Review in FEBS open bio, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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
2 citing papers in PubMed.
- Neurotrophin System as a Complex Set of Potential Biomarkers in Psychiatric Disorders and Therapy-Overview of Recent Advances.International journal of molecular sciences · 2026Review
- Highlights of the FEBS3+ meeting Exploring molecular frontiers.FEBS open bio · 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
1 author.
Funding
Abstract
Tropomyosin receptor kinase (Trk) receptors are essential regulators of neuronal development, survival, and plasticity through their interactions with neurotrophins. This review examines the structural and molecular mechanisms connecting ligand binding to the diverse signaling outcomes of Trk receptors. We analyze how neurotrophin binding and allosteric interactions trigger conformational changes that activate distinct signaling pathways. Our discussion explores how allosteric modulation-binding of ligands to sites distinct from the primary receptor site-and ligand bias-where different neurotrophins binding the same receptor preferentially activate certain downstream pathways-may together shape receptor function, focusing on structural and conformational mechanisms. Despite recent advances, important structural details remain unresolved. Further insights into Trk receptor structure and dynamics could significantly enhance therapeutic development by enabling the design of drugs that selectively target-specific signaling pathways.
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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.