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  High-Affinity Target Binding Engineered via Fusion of a Single-Domain Antibody Fragment with a Ligand-Tailored SH3 Domain

Järviluoma, A., Strandin, T., Lülf, S., Bouchet, J., Mäkelä, A. R., Geyer, M., et al. (2012). High-Affinity Target Binding Engineered via Fusion of a Single-Domain Antibody Fragment with a Ligand-Tailored SH3 Domain. PLoS ONE, 7(7): 1, pp. e40331. Retrieved from http://dx.doi.org/10.1371/journal.pone.0040331.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0013-FEC7-7 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0013-FEC8-5
Genre: Journal Article

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 Creators:
Järviluoma, Annika, Author
Strandin, Tomas, Author
Lülf, Sebastian1, Author
Bouchet, Jérôme, Author
Mäkelä, Anna R., Author
Geyer, Matthias2, Author           
Benichou, Serge, Author
Saksela, Kalle, Author
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              

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Free keywords: HIV-1 NEF; ESCHERICHIA-COLI; VARIABLE DOMAINS; ANTIGEN-BINDING; PROTEIN; THERAPEUTICS; FAMILY; MULTIVALENT; STABILITY; EVOLUTION
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Language(s): eng - English
 Dates: 2012-07-05
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 611794
URI: http://dx.doi.org/10.1371/journal.pone.0040331
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Title: PLoS ONE
Source Genre: Journal
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Pages: - Volume / Issue: 7 (7) Sequence Number: 1 Start / End Page: e40331 Identifier: -