Towards a universal disulphide stabilised single chain Fv format: importance of interchain disulphide bond location and vL-vH orientation-Reference-Cited by-同舟云学术

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Towards a universal disulphide stabilised single chain Fv format: importance of interchain disulphide bond location and vL-vH orientation

Published:2012-05-14 Issue:7 Volume:25 Page:321-329
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering Design and Selection

Author:

Weatherill E. E.,Cain K. L.,Heywood S. P.,Compson J. E.,Heads J. T.,Adams R.,Humphreys D. P.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/25/7/321/4395735/gzs021.pdf

Reference36 articles.

1. Monospecific bivalent scFv-SH: Effects of linker length and location of an engineered cysteine on production, antigen binding activity and free SH accessibility

2. Factors Influencing the Dimer to Monomer Transition of an Antibody Single-Chain Fv Fragment

3. Tumor Regression in Cancer Patients by Very Low Doses of a T Cell–Engaging Antibody

4. Pharmacokinetics and biodistribution of genetically engineered antibodies

5. Single-Chain Antigen-Binding Proteins

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3. Design and engineering of bispecific antibodies: insights and practical considerations;Frontiers in Bioengineering and Biotechnology;2024-01-25

4. Next generation of multispecific antibody engineering;Antibody Therapeutics;2023-12-08

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