Aggregation-resistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions-Reference-Cited by-同舟云学术

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Aggregation-resistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions

Published:2012-07-27 Issue:10 Volume:25 Page:591-602
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering Design and Selection

Author:

Perchiacca J. M.,Ladiwala A. R. A.,Bhattacharya M.,Tessier P. M.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/25/10/591/4444684/gzs042.pdf

Reference42 articles.

1. Aggregation-resistant VHs selected by in vitro evolution tend to have disulfide-bonded loops and acidic isoelectric points

2. Comprehensive Analysis of the Factors Contributing to the Stability and Solubility of Autonomous Human VH Domains

3. Structural repertoire of the human VH segments

4. AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides

5. Antigen Binding and Solubility Effects upon the Veneering of a Camel VHH in Framework-2 to Mimic a VH

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