The Glycosylation of Human Serum IgD and IgE and the Accessibility of Identified Oligomannose Structures for Interaction with Mannan-Binding Lectin-Reference-Cited by-同舟云学术

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The Glycosylation of Human Serum IgD and IgE and the Accessibility of Identified Oligomannose Structures for Interaction with Mannan-Binding Lectin

Published:2004-11-19 Issue:11 Volume:173 Page:6831-6840
ISSN:0022-1767
Container-title:The Journal of Immunology
language:en
Short-container-title:J Immunol

Author:

Arnold James N.,Radcliffe Catherine M.,Wormald Mark R.,Royle Louise,Harvey David J.,Crispin Max,Dwek Raymond A.,Sim Robert B.,Rudd Pauline M.

Publisher

The American Association of Immunologists

Subject

Immunology,Immunology and Allergy

Reference57 articles.

1. Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis

2. Secretory IgA N- and O-Glycans Provide a Link between the Innate and Adaptive Immune Systems

3. The Glycosylation and Structure of Human Serum IgA1, Fab, and Fc Regions and the Role of N-Glycosylation on Fcα Receptor Interactions

4. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG

5. Glycosylation changes of IgG associated with rheumatooid arthritis can activate complement via the mannose-binding protein

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