Domain order of a bispecific diabody dramatically enhances its antitumor activity beyond structural format conversion: the case of the hEx3 diabody-Reference-Cited by-同舟云学术

Domain order of a bispecific diabody dramatically enhances its antitumor activity beyond structural format conversion: the case of the hEx3 diabody

Published:2013-03-06 Issue:5 Volume:26 Page:359-367
ISSN:1741-0134
Container-title:Protein Engineering, Design and Selection
language:en
Short-container-title:

Author:

Asano Ryutaro,Kumagai Takashi,Nagai Keisuke,Taki Shintaro,Shimomura Ippei,Arai Kyoko,Ogata Hiromi,Okada Mai,Hayasaka Fumitaka,Sanada Hideaki,Nakanishi Takeshi,Karvonen Teemu,Hayashi Hiroki,Katayose Yu,Unno Michiaki,Kudo Toshio,Umetsu Mitsuo,Kumagai Izumi

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/26/5/359/17494691/gzt009.pdf

Reference35 articles.

1. Humanization of the Bispecific Epidermal Growth Factor Receptor × CD3 Diabody and Its Efficacy as a Potential Clinical Reagent

2. Highly Effective Recombinant Format of a Humanized IgG-like Bispecific Antibody for Cancer Immunotherapy with Retargeting of Lymphocytes to Tumor Cells

3. Diabody-based Recombinant Formats of Humanized IgG-like Bispecific Antibody With Effective Retargeting of Lymphocytes to Tumor Cells

4. Highly Enhanced Cytotoxicity of a Dimeric Bispecific Diabody, the hEx3 Tetrabody

5. Cytotoxic Enhancement of a Bispecific Diabody by Format Conversion to Tandem Single-chain Variable Fragment (taFv)

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