ArticleActa crystallographica. Section F, Structural biology communications2019
Crystal structure of the Fab region of a neutralizing antibody against granulocyte-macrophage colony-stimulating factor.
Article in Acta crystallographica. Section F, Structural biology communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 2 citations in OpenAlex.
- Multifunctional human monoclonal antibody combination mediates protection against Rift Valley fever virus at low doses.Nature communications · 2023Article
- Evolution of surrogate light chain in tetrapods and the relationship between lengths of CDR H3 and VpreB tails.Frontiers in immunology · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
An increased level of granulocyte-macrophage colony-stimulating factor has a potential role in the development of autoimmune diseases, and the neutralization of its activity by monoclonal antibodies is a promising therapy for some diseases. Here, the crystal structure of the Fab region of EV1007, a fully human antibody expressed in Chinese hamster ovary cells that was developed from human peripheral blood mononuclear cells, is described. The structure closely resembles that of MB007, which is the Fab region of the same antibody expressed in Escherichia coli [Blech et al. (2012), Biochem. J. 447, 205-215], except at the hinge regions between the immunoglobulin domains and the H3 loop region. This paper presents evidence for the flexibility of the hinge and H3 loop regions of the antibody based on the comparison of two independently solved crystal structures.
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