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Showing 1-6 of 6 results for "PP0520" within Papers
Florian Cambay et al.
Current research in immunology, 1, 23-37 (2020-06-27)
The effector functions of the IgGs are modulated by the N-glycosylation of their Fc region. Particularly, the absence of core fucosylation is known to increase the affinity of IgG1s for the Fcγ receptor IIIa expressed by immune cells, in turn
Separation of 2-aminobenzamide labeled glycans using hydrophilic interaction chromatography columns packed with 1.7 mum sorbent
Ahn J, et al.
Journal of Chromatography. B, Biomedical Sciences and Applications, 878(3-4), 403-408 (2010)
Expression and biochemical characterization of recombinant human epididymis protein 4
Hua L, et al.
Protein Expression and Purification, 102, 52-62 (2014)
Céline Raymond et al.
mAbs, 7(3), 571-583 (2015-04-16)
The presence of α2,6-sialic acids on the Fc N-glycan provides anti-inflammatory properties to the IgGs through a mechanism that remains unclear. Fc-sialylated IgGs are rare in humans as well as in industrial host cell lines such as Chinese hamster ovary
Belinda L Spillings et al.
Cell reports, 38(5), 110296-110296 (2022-02-03)
Here, we present ultrastructural analyses showing that incoming HIV are captured near the lymphocyte surface in a virion-glycan-dependent manner. Biophysical analyses show that removal of either virion- or cell-associated N-glycans impairs virus-cell binding, and a similar glycan-dependent relationship is observed
Enhancing the antiviral potency of ER alpha-glucosidase inhibitor IHVR-19029 against hemorrhagic fever viruses in vitro and in vivo
Ma J, et al.
Antiviral research, 150, 112-122 (2018)
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