Single‐domain antibody fragments with high conformational stability
By M. Dumoulin, K. Conrath, Annemieke Van Meirhaeghe, F. Meersman, K. Heremans, L. Frenken, S. Muyldermans, L. Wyns, A. Matagne. Protein Science, 2002
633 citations recorded by the source corpus.
Subfields: Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/2265c4f4d2582a49f8b930b6867cb0c7c1b852e1
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
In Radiology, Nuclear Medicine and Imaging
Citations in the corpus
- Exploiting sequence and stability information for directing nanobody stability engineering (2017, background): “While not detectable for some nanobodies [17], aggregation has been observed for molecules of this binder class [9,18].”
- Nanobodies: natural single-domain antibodies. (2013, background): “behavior, resist temperatures above 90◦C (78), and have a chemical stability of 60 kJ/mol−1 (62, 77).”
- Properties, production, and applications of camelid single-domain antibody fragments (2007, background): “VHHs are especially suited for oral immunotherapy because of their resistance against extremes of pH and the capacity to bind to the target at high concentrations of chaotropic agents (Dumoulin et al. 2002, 2003).”