The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Selection and identification of single domain antibody fragments from camel heavy‐chain antibodies
Open accessAbstract
Functional heavy‐chain γ‐immunoglobulins lacking light chains occur naturally in Camelidae. We now show the feasibility of immunising a dromedary, cloning the repertoire of the variable domains of its heavy‐chain antibodies and panning, leading to the successful identification of minimum sized antigen binders. The recombinant binders are expressed well in E. coli, extremely stable, highly soluble, and react specifically and with high affinity to the antigens. This approach can be viewed as a general route to obtain small binders with favourable characteristics and valuable perspectives as modular building blocks to manufacture multispecific or multifunctional chimaeric proteins.
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Citations
Cites
Naturally occurring antibodies devoid of light chains
Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hammers, C., Songa, E. B., Bendahman, N., & Hammers, R. (1993) · Nature · doi:10.1038/363446a0 · Cited by 3,241
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Cited by
Nanobodies: natural single-domain antibodies
Muyldermans, S. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-063011-092449 · Cited by 2,304
Self-citationProperties, production, and applications of camelid single-domain antibody fragments
Harmsen, M. M., & De Haard, H. J. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1142-2 · Cited by 809
“Methods to isolate antigen-specific VHHs from immune ( Arbabi-Ghahroudi et al. 1997; Van der Linden et al. 2000a), nonimmune (Tanha et al. 2002; Yau et al. 2003; Verheesen et al. 2006), or semisynthetic (Goldman et al. 2006) libraries using phage, yeast, or ribosome display are now well established.”
BackgroundTargeting and tracing antigens in live cells with fluorescent nanobodies
Rothbauer, U., Zolghadr, K., Tillib, S., Nowak, D., Schermelleh, L., Gahl, A., Backmann, N., Conrath, K., Muyldermans, S., Cardoso, M. C., et al. (2006) · Nature Methods · doi:10.1038/nmeth953 · Cited by 710
Self-citationvan der Linden, R. H. J., Frenken, L. G. J., de Geus, B., Harmsen, M. M., Ruuls, R. C., Stok, W., de Ron, L., Wilson, S., Davis, P., & Verrips, C. T. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00030-8 · Cited by 471
Els Conrath, K., Lauwereys, M., Wyns, L., & Muyldermans, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007734200 · Cited by 300
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Metadata
- Authors
- Arbabi Ghahroudi, M., Desmyter, A., Wyns, L., Hamers, R., & Muyldermans, S.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1997-09-15
- Volume
- 414
- Issue
- 3
- Pages
- 521-526
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2020368956
- Cited by
- 768
- References
- 1
- FWCI
- 9.45
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Arbabi Ghahroudi, M., Desmyter, A., Wyns, L., Hamers, R., & Muyldermans, S. (1997). Selection and identification of single domain antibody fragments from camel heavy‐chain antibodies. FEBS Letters. https://doi.org/10.1016/s0014-5793(97)01062-4
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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