ArticleAngewandte Chemie (International ed. in English)2025
Developing HaloTag and SNAP-Tag Chemical Inducers of Dimerization to Probe Receptor Oligomerization and Downstream Signaling.
Article in Angewandte Chemie (International ed. in English), 2025. 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
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
3 citing papers in PubMed.
- Chemical biology approaches to study and target circadian clocks and their components.FEBS letters · 2026Review
- Developing HaloTag and SNAP-Tag Chemical Inducers of Dimerization to Probe Receptor Oligomerization and Downstream Signaling.Angewandte Chemie (International ed. in English) · 2025Article
- Decoding cardiac metabolic reprogramming through single-cell multi-omics: from mechanisms to therapeutic applications.Frontiers in cell and developmental biology · 2025Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
Abstract
Controlling protein-protein interactions is critical for dissecting signaling pathways, especially those initiated by ligand-receptor interactions, which alter receptor oligomerization and drive downstream signaling cascades. Traditional methods for driving protein-protein complexes use antibodies that face limitations in terms of stoichiometry, geometric rigidity, and antibody specificity. Chemical inducers of dimerization (CIDs) for fusion proteins such as HaloTag (Halo) and SNAP-Tags (SNAP) offer precise and covalent control of protein proximities, overcoming limitations of antibody-dependent methods. In this study, we expand the toolkit of Halo and SNAP CIDs with (1) benzylguanine (BG) and HaloTag ligand (HTL) crosslinkers featuring varying polyethylene glycol linker lengths and update this kit with (2) a FRET-based dimerizing sensor to induce and verify protein proximity. Here we establish our CIDs on extracellularly Halo- and SNAP-tagged TGFβ, BMP, neurotrophic factor, and metabotropic glutamate receptors, thereby elucidating the signaling potential of ligand-independent dimerization in a heteromeric fashion.
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.