Cargando…
C(H)2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering
The N-linked glycan in immunoglobulin G is critical for the stability and function of the crystallizable fragment (Fc) region. Alteration of these protein properties upon the removal of the N-linked glycan has often been explained by the alteration of the C(H)2 domain orientation in the Fc region. T...
Autores principales: | Yageta, Seiki, Imamura, Hiroshi, Shibuya, Risa, Honda, Shinya |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6512918/ https://www.ncbi.nlm.nih.gov/pubmed/30513259 http://dx.doi.org/10.1080/19420862.2018.1546086 |
Ejemplares similares
-
Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1
por: Arena de Souza, Victoria, et al.
Publicado: (2015) -
Impact of Drug Conjugation on Thermal and Metabolic
Stabilities of Aglycosylated and N-Glycosylated
Antibodies
por: Yamazoe, Sayumi, et al.
Publicado: (2022) -
Aglycosylated antibody-producing mice for aglycosylated antibody-lectin coupled immunoassay for the quantification of tumor markers (ALIQUAT)
por: Lee, Nan-Ee, et al.
Publicado: (2020) -
Cue to Acid-Induced Long-Range Conformational Changes in an Antibody Preceding Aggregation: The Structural Origins of the Subpeaks in Kratky Plots of Small-Angle X-ray Scattering
por: Imamura, Hiroshi, et al.
Publicado: (2023) -
Comparison of the Fc glycosylation of fetal and maternal immunoglobulin G
por: Einarsdottir, Helga K., et al.
Publicado: (2012)