The proximity of the N- and C- termini of bovine knob domains enable engineering of target specificity into polypeptide chains-Reference-Cited by-同舟云学术

The proximity of the N- and C- termini of bovine knob domains enable engineering of target specificity into polypeptide chains

Published:2022-05-29 Issue:1 Volume:14 Page:
ISSN:1942-0862
Container-title:mAbs
language:en
Short-container-title:mAbs

Author:

Hawkins Alice¹,Joyce Callum¹²,Brady Kevin¹,Hold Adam¹,Smith Alan³,Knight Michael³,Howard Conor¹,van den Elsen Jean²,Lawson Alastair D.G.¹,Macpherson Alex¹^ORCID

Affiliation:

1. Early Solutions UCB Biopharma UK, Slough, UK

2. Department of Biology and Biochemistry, University of Bath, Bath, UK

3. Biotech Solutions, UCB Biopharma UK, Slough, UK

Funder

funding associated with the work featured in this article

Publisher

Informa UK Limited

Subject

Immunology,Immunology and Allergy

Link

https://www.tandfonline.com/doi/pdf/10.1080/19420862.2022.2076295

Reference29 articles.

1. Conservation and diversity in the ultralong third heavy-chain complementarity-determining region of bovine antibodies

2. Reshaping Antibody Diversity

3. Structural basis of broad HIV neutralization by a vaccine-induced cow antibody

4. The allosteric modulation of complement C5 by knob domain peptides

5. Isolation of antigen-specific, disulphide-rich knob domain peptides from bovine antibodies

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