The Rapidly Expanding Nexus of Immunoglobulin G N-Glycomics, Suboptimal Health Status, and Precision Medicine [0.03%]
免疫球蛋白G岩藻糖基化不足与亚健康状态和精准医学的迅速扩展关系论述
Alyce Russell,Wei Wang
Alyce Russell
Immunoglobulin G is a prevalent glycoprotein, whose downstream immune responses are partially mediated by the N-glycans within the fragment crystallisable domain. Collectively termed the N-glycome, it is considered a complex intermediate ph...
Kathrin Göritzer,Richard Strasser
Kathrin Göritzer
Many economically important protein-based therapeutics like monoclonal antibodies are glycosylated. Due to the recognized importance of this type of posttranslational modification, glycoengineering of expression systems to obtain highly act...
Yusuke Mimura,Radka Saldova,Yuka Mimura-Kimura et al.
Yusuke Mimura et al.
The complex diantennary-type oligosaccharides at Asn297 residues of the IgG heavy chains have a profound impact on the safety and efficacy of therapeutic IgG monoclonal antibodies (mAbs). Fc glycosylation of a mAb is an established critical...
Alyssa L Hansen,Colin Reily,Jan Novak et al.
Alyssa L Hansen et al.
Human IgA is comprised of two subclasses, IgA1 and IgA2. Monomeric IgA (mIgA), polymeric IgA (pIgA), and secretory IgA (SIgA) are the main molecular forms of IgA. The production of IgA rivals all other immunoglobulin isotypes. The large qua...
Marija Pezer
Marija Pezer
Changes in immunoglobulin G (IgG) glycosylation pattern have been observed in a vast array of auto- and alloimmune, infectious, cardiometabolic, malignant, and other diseases. This chapter contains an updated catalog of over 140 studies wit...
Falk Nimmerjahn,Anja Werner
Falk Nimmerjahn
Antibodies produced upon infections with pathogenic microorganisms are essential for clearing primary infections and for providing the host with long-lasting immunity. Moreover, antibodies have become the most widely used platform for devel...
Kaitlyn A Lagattuta,Peter A Nigrovic
Kaitlyn A Lagattuta
Glycosylation within the immunoglobulin G (IgG) Fc region modulates its ability to engage complement and Fc receptors, affording the opportunity to fine-tune effector functions. Mechanisms regulating IgG Fc glycans remain poorly understood....
Immunoglobulin G Glycosylation Changes in Aging and Other Inflammatory Conditions [0.03%]
老龄化和其他炎症条件下免疫球蛋白G的糖基化改变
Fabio Dall&#x;Olio,Nadia Malagolini
Fabio Dall&#x;Olio
Among the multiple roles played by protein glycosylation, the fine regulation of biological interactions is one of the most important. The asparagine 297 (Asn297) of IgG heavy chains is decorated by a diantennary glycan bearing a number of ...
Marija Klasić,Vlatka Zoldoš
Marija Klasić
Alternative glycosylation of immunoglobulin G (IgG) affects its effector functions during the immune response. IgG glycosylation is altered in many diseases, but also during a healthy life of an individual. Currently, there is limited knowl...
Azra Frkatovic,Olga O Zaytseva,Lucija Klaric
Azra Frkatovic
Defining the genetic components that control glycosylation of the human immunoglobulin G (IgG) is an ongoing effort, which has so far been addressed by means of heritability, linkage and genome-wide association studies (GWAS). Unlike the sy...