ArticleiScience2021
Influence of nanobody binding on fluorescence emission, mobility, and organization of GFP-tagged proteins.
Article in iScience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Clustering hinders APP α-secretase processing in the plasma membrane.Biophysical journal · 2026Article
- Quantifying biomolecular organisation in membranes with brightness-transit statistics.Nature communications · 2024Article
- Biophysical characterization of synthetic adhesins for predicting and tuning engineered living material properties.Matter · 2024Article
- Microscopic clusters feature the composition of biochemical tetraspanin-assemblies and constitute building-blocks of tetraspanin enriched domains.Scientific reports · 2024Article
- Extreme thermal stability of the antiGFP nanobody - GFP complex.BMC research notes · 2023Article
- Diffusion and interaction dynamics of the cytosolic peroxisomal import receptor PEX5.Biophysical reports · 2022Article
- The transmembrane domain of the amyloid precursor protein is required for antiamyloidogenic processing by α-secretase ADAM10.The Journal of biological chemistry · 2022Article
- The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE-SNARE interactions.eLife · 2021Article
- Light-guided intrabodies for on-demandChemical science · 2021Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
Abstract
Advanced fluorescence microscopy studies require specific and monovalent molecular labeling with bright and photostable fluorophores. This necessity led to the widespread use of fluorescently labeled nanobodies against commonly employed fluorescent proteins (FPs). However, very little is known how these nanobodies influence their target molecules. Here, we tested commercially available nanobodies and observed clear changes of the fluorescence properties, mobility and organization of green fluorescent protein (GFP) tagged proteins after labeling with the anti-GFP nanobody. Intriguingly, we did not observe any co-diffusion of fluorescently labeled nanobodies with the GFP-labeled proteins. Our results suggest significant binding of the nanobodies to a non-emissive, likely oligomerized, form of the FPs, promoting disassembly into monomeric form after binding. Our findings have significant implications on the application of nanobodies and GFP labeling for studying dynamic and quantitative protein organization in the plasma membrane of living cells using advanced imaging techniques.
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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.