Targeting and tracing antigens in live cells with fluorescent nanobodies
By U. Rothbauer, Kourosh Zolghadr, Sergei Tillib, Danny Nowak, Lothar Schermelleh, A. Gahl, Natalija Backmann, K. Conrath, S. Muyldermans, M. Cardoso and 1 more. Nature Methods, 2006
712 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/66d5da205c94ddf9722607c1518f9dd8909cd164
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In Immunology
In Molecular Biology
- S. Muyldermans
- D. Baty
- M. H. V. Van Regenmortel
- Etienne Weiss
- Lothar Schermelleh
- Rainer Heintzmann
- H. Leonhardt
- P. Chames
In Radiology, Nuclear Medicine and Imaging
Citations in the corpus
- A Versatile Nanotrap for Biochemical and Functional Studies with Fluorescent Fusion Proteins*S (2008, methodology): “To generate a nanotrap for fast and efficient purification of GFP fusion proteins we used a small recombinant 13-kDa GBP comprising the epitope recognition domain of a heavy chain antibody raised in an alpaca (Lama pacos) against GFP (17).”
- A guide to super-resolution fluorescence microscopy (2010, background): “Finally, new types of molecular probes such as extremely small and stable chromobodies that can detect antigens in living cells (Rothbauer et al., 2006) in combination with these super-resolution techniques will further expand the repertoire of modern cell biology.”
- Protein-binding assays in biological liquids using microscale thermophoresis. (2010, background): “We further analysed a recently described interaction between green fluorescent protein (GFP) and a small antibody fragment known as GFP-binding protein (GBP”
- Therapeutic antibodies: successes, limitations and hopes for the future (2009, positive): “…(Manikandan et al., 2007), sdAbs such as human VH and VL and camelid frameworks (Tanaka et al., 2003; Aires da Silva et al., 2004; Paz et al., 2005; Rothbauer et al., 2006; Tanaka et al., 2007) are being increasingly explored as intrabodies. dAbs do not require pairing of two variable domains or…”
- Properties, production, and applications of camelid single-domain antibody fragments (2007, background): “Because of their stability, VHHs are especially suited for intrabody production because this requires expression in the reducing environment of the cytoplasm (Gueorguieva et al. 2006; Rothbauer et al. 2006).”