Identification and characterization of an unexpected isomerization motif in CDRH2 that affects antibody activity-Reference-Cited by-同舟云学术

Identification and characterization of an unexpected isomerization motif in CDRH2 that affects antibody activity

Published:2023-05-25 Issue:1 Volume:15 Page:
ISSN:1942-0862
Container-title:mAbs
language:en
Short-container-title:mAbs

Author:

Yi Meiqi¹,Sun Jian¹,Sun Hanzi²,Wang Yifei¹,Hou Shan¹,Jiang Beibei³,Xie Yuanyuan¹,Ji Ruyue¹,Xue Liu¹,Ding Xiao⁴,Song Xiaomin³,Xu April¹,Huang Chichi¹,Quan Quan¹,Song Jing¹

Affiliation:

1. Department of Biologics, BeiGene (Beijing) Co. Ltd, Beijing, China

2. Department of Molecular Science, BeiGene (Beijing) Co. Ltd, Beijing, China

3. Department of Pharmacology, BeiGene (Beijing) Co. Ltd, Beijing, China

4. Department of Translational Science, BeiGene (Beijing) Co. Ltd, Beijing, China

Funder

there is no funding

Publisher

Informa UK Limited

Subject

Immunology,Immunology and Allergy

Link

https://www.tandfonline.com/doi/pdf/10.1080/19420862.2023.2215364

Reference33 articles.

1. Recombinant Antibodies as Therapeutic Agents

2. Monoclonal antibody successes in the clinic

3. Therapeutic antibodies: successes, limitations and hopes for the future

4. Effect of Trastuzumab–HER2 Complex Formation on Stress-Induced Modifications in the CDRs of Trastuzumab

5. Isomerization of an Aspartic Acid Residue in the Complementarity-Determining Regions of a Recombinant Antibody to Human IgE: Identification and Effect on Binding Affinity

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