CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering-Reference-Cited by-同舟云学术

CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering

Published:2018-12-12 Issue:3 Volume:11 Page:453-462
ISSN:1942-0862
Container-title:mAbs
language:en
Short-container-title:mAbs

Author:

Yageta Seiki¹²³,Imamura Hiroshi¹⁴^ORCID,Shibuya Risa²^ORCID,Honda Shinya¹²³^ORCID

Affiliation:

1. Biomedical Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki, Japan

2. Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, the University of Tokyo, Kashiwa, Chiba, Japan

3. Manufacturing Technology Association of Biologics, Tsukuba, Ibaraki, Japan

4. Department of Applied Chemistry, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, Japan

Funder

Japan Agency for Medical Research and Development

Publisher

Informa UK Limited

Subject

Immunology,Immunology and Allergy

Link

https://www.tandfonline.com/doi/pdf/10.1080/19420862.2018.1546086

Reference82 articles.

1. Developments in therapy with monoclonal antibodies and related proteins

2. Therapeutic antibodies: Market considerations, disease targets and bioprocessing

3. Aglycosylated full-length IgG antibodies: steps toward next-generation immunotherapeutics

4. With or Without Sugar? (A)glycosylation of Therapeutic Antibodies

5. Bypassing glycosylation: engineering aglycosylated full-length IgG antibodies for human therapy

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