Engineered Sialylation of Pathogenic Antibodies In Vivo Attenuates Autoimmune Disease
- 1 January 2018
- Vol. 172 (3) , 564-577.e13
Abstract
No abstract availableKeywords
Funding Information
- NIAMS/NIH (DP2AR068272)
- Lupus Research Alliance
- H.M. Goodman Fellowship
This publication has 81 references indexed in Scilit:
- Anti-inflammatory IgG Production Requires Functional P1 Promoter in β-Galactoside α2,6-Sialyltransferase 1 (ST6Gal-1) GeneJournal of Biological Chemistry, 2012
- Unique carbohydrate–carbohydrate interactions are required for high affinity binding between FcγRIII and antibodies lacking core fucoseProceedings of the National Academy of Sciences, 2011
- Platelets Amplify Inflammation in Arthritis via Collagen-Dependent Microparticle ProductionScience, 2010
- Impaired inhibitory Fcγ receptor IIB expression on B cells in chronic inflammatory demyelinating polyneuropathyProceedings of the National Academy of Sciences, 2009
- DC-SIGN and α2,6-sialylated IgG Fc interaction is dispensable for the anti-inflammatory activity of IVIg on human dendritic cellsProceedings of the National Academy of Sciences, 2009
- Identification of a receptor required for the anti-inflammatory activity of IVIGProceedings of the National Academy of Sciences, 2008
- In vivo enzymatic modulation of IgG glycosylation inhibits autoimmune disease in an IgG subclass-dependent mannerProceedings of the National Academy of Sciences, 2008
- Proteolytic Shedding of ST6Gal-I by BACE1 Regulates the Glycosylation and Function of α4β1 IntegrinsJournal of Biological Chemistry, 2008
- Recapitulation of IVIG Anti-Inflammatory Activity with a Recombinant IgG FcScience, 2008
- Diagnosis and management of goutBMJ, 2006