Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies.
By E. D. De Genst, K. Silence, K. Decanniere, K. Conrath, R. Loris, J. Kinne, S. Muyldermans, L. Wyns. Proceedings of the National Academy of Sciences of the United States of America, 2006
659 citations recorded by the source corpus.
Subfields: Ecology, Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/69776afcd7d723ae7efb5bbc27fde00baef39108
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Citations in the corpus
- Properties, production, and applications of camelid single-domain antibody fragments (2007, background): “Occasionally, VHHs with affinity constants (KD) as low as 100 pM are isolated (Saerens et al. 2004; De Genst et al. 2006; Harmsen et al. 2006), which equals the affinity ceiling proposed for natural antibodies (Sundberg and Mariuzza 2002).”
- Nanobodies: natural single-domain antibodies. (2013, background): “To provide a sufficiently large antigeninteracting surface of 600–800 Å2 (30), the loops are longer in a VHH than in a VH of a conventional antibody.”
- Antigen recognition by γδ T cells (2007, background): “HCAbs use a single variable domain that features an extended CDR3 loop (66) that is capable of binding into clefts (67), such as the active sites of enzymes (68).”