ArticleSmall (Weinheim an der Bergstrasse, Germany)2026
Single-Molecule FRET-Tracking of InlB-Activated MET Receptors in Living Cells.
Article in Small (Weinheim an der Bergstrasse, Germany), 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
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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
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Who cites it
2 citing papers in PubMed.
- Receptor homodimerization significantly prolongs the lifetime of ligand-induced cross-linking of CLEC-2 but not GPVI.Blood vessels, thrombosis & hemostasis · 2026Article
- Single-Molecule FRET-Tracking of InlB-Activated MET Receptors in Living Cells.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The activation of transmembrane receptors through the binding of external ligands initiates information transfer across the cell membrane. Understanding these processes requires observations in living cells. Given the heterogeneity and lack of synchronization of such events, single-molecule experiments are required to resolve distinct sub-populations. Here, single-molecule FRET microscopy and single-particle tracking are combined to track the ligand-induced dimerization and activation of the MET receptor tyrosine kinase in the plasma membrane of living cells. First, using fluorophore-labeled variants of the MET ligand internalin B (InlB), the lifetime of a ligand-activated dimeric (MET:InlB)
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Registered trials
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