Agalactosyl glycoforms of IgG autoantibodies are pathogenic. - Wikidata - wikimedia - TriplyDB

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

http://www.wikidata.org/entity/Q35555049

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The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a Mechanisms involved in antibody- and complement-mediated allograft rejection Modeling human arthritic diseases in nonhuman primates.Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies EndoS, a novel secreted protein from Streptococcus pyogenes with endoglycosidase activity on human IgG The p68 autoantigen characteristic of rheumatoid arthritis is reactive with carbohydrate epitope specific autoantibodies Human IgG/Fc gamma R interactions are modulated by streptococcal IgG glycan hydrolysis Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy Pairing of oligosaccharides in the Fc region of immunoglobulin G.IgG glycan hydrolysis by a bacterial enzyme as a therapy against autoimmune conditions.Mechanisms of action of intravenous immunoglobulins.Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: results from a large prospective cohort study Does it take sugar? A clinical role for measuring the glycosylation of IgG?Favorable Response to Long-term Nucleos(t)ide Analogue Therapy in HBeAg-positive Patients with High Serum Fucosyl-Agalactosyl IgG.Mechanisms of Autoantibody-Induced Pathology.Glycobiology: 'the function of sugar in the IgG molecule'.Lectin-reactive anti-α-gal in patients with Crohn's disease: correlation with clinical phenotypes Aberrant IgG galactosylation precedes disease onset, correlates with disease activity, and is prevalent in autoantibodies in rheumatoid arthritis.Clustered O-glycans of IgA1: defining macro- and microheterogeneity by use of electron capture/transfer dissociation.Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes Reversibility of membrane N-glycome of HeLa cells upon treatment with epigenetic inhibitors.Change in IgG1 Fc N-linked glycosylation in human lung cancer: age- and sex-related diagnostic potential.Elucidating heterogeneity of IgA1 hinge-region O-glycosylation by use of MALDI-TOF/TOF mass spectrometry: role of cysteine alkylation during sample processing.Fc-glycosylation of IgG1 is modulated by B-cell stimuli.The role of FcgammaRIIa as an inflammatory mediator in rheumatoid arthritis and systemic lupus erythematosus.Rheumatoid arthritis and pregnancy: evolution of disease activity and pathophysiological considerations for drug use.Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity.Pro-inflammatory pattern of IgG1 Fc glycosylation in multiple sclerosis cerebrospinal fluid.Changes in antigen-specific IgG1 Fc N-glycosylation upon influenza and tetanus vaccination Multiple juvenile idiopathic arthritis subtypes demonstrate proinflammatory IgG glycosylation Hypogalactosylation of serum N-glycans fails to predict clinical response to methotrexate and TNF inhibition in rheumatoid arthritis Characterization of IgG glycosylation in rheumatoid arthritis patients by MALDI-TOF-MSn and capillary electrophoresis.Sialylation determines the nephritogenicity of IgG3 cryoglobulins.Carbohydrate recognition systems in autoimmunity.Antibody-induced arthritis: disease mechanisms and genes involved at the effector phase of arthritis.Sialylation converts arthritogenic IgG into inhibitors of collagen-induced arthritis.Glycoengineering of human IgG1-Fc through combined yeast expression and in vitro chemoenzymatic glycosylation.T cell-independent B cell activation induces immunosuppressive sialylated IgG antibodies.Anti-rhesus D prophylaxis in pregnant women is based on sialylated IgG antibodies Fibrinogen-specific antibody induces abdominal aortic aneurysm in mice through complement lectin pathway activation.

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P2860

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

http://www.wikidata.org/entity/Q35555049

description

1994 nî lūn-bûn

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1994年の論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

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1994年論文

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1994年论文

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1994年论文

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1994年论文

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name

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

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Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

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type

label

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

@ast

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

@en

prefLabel

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

@ast

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

@en

P1433

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PNAS.91.13.6123

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Agalactosyl glycoforms of IgG autoantibodies are pathogenic.

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P2093

Dwek RA

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Rademacher TW

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Williams P

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P2860

Agalactosyl IgG in inflammatory bowel disease: correlation with C-reactive protein.

Type II collagen-induced arthritis in mice. I. Major histocompatibility complex (I region) linkage and antibody correlates

Serum transfer of collagen-induced arthritis in mice.

Age-related galactosylation of the N-linked oligosaccharides of human serum IgG.

Network theory of glycosylation--etiologic and pathogenic implications of changes in IgG glycoform levels in autoimmunity.

A monoclonal antibody raised by immunising mice with group A streptococci binds to agalactosyl IgG from rheumatoid arthritis

The role of IgG glycoforms in the pathogenesis of rheumatoid arthritis.

Mechanisms of disruption of the articular cartilage surface in inflammation. Neutrophil elastase increases availability of collagen type II epitopes for binding with antibody on the surface of articular cartilage.

Enhanced production of interleukin-6 in mice with type II collagen-induced arthritis.

Induction of arthritis with monoclonal antibodies to collagen.

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6123-6127

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10.1073/PNAS.91.13.6123

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8016124

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44150

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