Naturally occurring structural isomers in serum IgA1 o-glycosylation. - Wikidata - wikimedia - TriplyDB

Naturally occurring structural isomers in serum IgA1 o-glycosylation.

Naturally occurring structural isomers in serum IgA1 o-glycosylation.

http://www.wikidata.org/entity/Q37352215

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Recent Advances in Clinical Glycoproteomics of Immunoglobulins (Igs)The Origin and Activities of IgA1-Containing Immune Complexes in IgA Nephropathy Mass spectrometry of glycans Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy O-linked glycosylation determines the nephritogenic potential of IgA rheumatoid factor.The genetics and immunobiology of IgA nephropathy.IgA N- and O-glycosylation profiling reveals no association with the pregnancy-related improvement in rheumatoid arthritis.Site-specific glycosylation of secretory immunoglobulin A from human colostrum.Identification of distinct glycoforms of IgA1 in plasma from patients with immunoglobulin A (IgA) nephropathy and healthy individuals Primary breast cancer tumours contain high amounts of IgA1 immunoglobulin: an immunohistochemical analysis of a possible carrier of the tumour-associated Tn antigen.Elucidating heterogeneity of IgA1 hinge-region O-glycosylation by use of MALDI-TOF/TOF mass spectrometry: role of cysteine alkylation during sample processing.Targeted biomarker discovery by high throughput glycosylation profiling of human plasma alpha1-antitrypsin and immunoglobulin A.N-acetylgalactosaminide α2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy.Novel lectin-independent approach to detect galactose-deficient IgA1 in IgA nephropathy Site-specific analysis of von Willebrand factor O-glycosylation.Longitudinal monitoring of immunoglobulin A glycosylation during pregnancy by simultaneous MALDI-FTICR-MS analysis of N- and O-glycopeptides New Insights into the Pathogenesis of IgA Nephropathy.Antibodies and their receptors: different potential roles in mucosal defense.Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma.Cytokines alter IgA1 O-glycosylation by dysregulating C1GalT1 and ST6GalNAc-II enzymes.High-sensitivity analytical approaches for the structural characterization of glycoproteins.Glycosylation of IgA1 and pathogenesis of IgA nephropathy.Biomarkers in IgA nephropathy: relationship to pathogenetic hits.Biomarkers in IgA nephropathy.Paradigm shift in activity assessment of IgA nephropathy - optimizing the next generation of diagnostic and therapeutic maneuvers via glycan targeting.Immunoglobulin A nephropathy: a pathophysiology view.Update on immunoglobulin A nephropathy, Part I: Pathophysiology.Analysis of mammalian O-glycopeptides - we have made a good start, but there is a long way to go.Potential diagnostic biomarkers for IgA nephropathy: a comparative study pre- and post-tonsillectomy.Assay for galactose-deficient IgA1 enables mechanistic studies with primary cells from IgA nephropathy patients

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Naturally occurring structural isomers in serum IgA1 o-glycosylation.

http://www.wikidata.org/entity/Q37352215

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 29 December 2011

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Naturally occurring structural isomers in serum IgA1 o-glycosylation.

@en

Naturally occurring structural isomers in serum IgA1 o-glycosylation.

@nl

type

label

Naturally occurring structural isomers in serum IgA1 o-glycosylation.

@en

Naturally occurring structural isomers in serum IgA1 o-glycosylation.

@nl

prefLabel

Naturally occurring structural isomers in serum IgA1 o-glycosylation.

@en

Naturally occurring structural isomers in serum IgA1 o-glycosylation.

@nl

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Journal of Proteome Research

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Naturally occurring structural isomers in serum IgA1 o-glycosylation.

@en

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Archer D Smith

http://www.w3.org/2001/XMLSchema#string

Bruce A Julian

http://www.w3.org/2001/XMLSchema#string

Jan Novak

http://www.w3.org/2001/XMLSchema#string

Jiri Mestecky

http://www.w3.org/2001/XMLSchema#string

Kazuo Takahashi

http://www.w3.org/2001/XMLSchema#string

Knud Poulsen

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P2860

Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2

The pathophysiology of IgA nephropathy

Performance characteristics of electron transfer dissociation mass spectrometry

Mass spectrometry proves under-O-glycosylation of glomerular IgA1 in IgA nephropathy.

Heterogeneity of O-glycosylation in the hinge region of human IgA1.

Human serum IgA1 is substituted with up to six O-glycans as shown by matrix assisted laser desorption ionisation time-of-flight mass spectrometry.

An essential epitope of anti-MUC1 monoclonal antibody KL-6 revealed by focused glycopeptide library.

Combined electron capture and infrared multiphoton dissociation for multistage MS/MS in a Fourier transform ion cyclotron resonance mass spectrometer.

Analysis of the microheterogeneity of the IgA1 hinge glycopeptide having multiple O-linked oligosaccharides by capillary electrophoresis.

Application of matrix-assisted laser desorption ionization time-of-flight mass spectrometry to the analysis of glycopeptide-containing multiple O-linked oligosaccharides.

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692-702

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scholarly article

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10.1021/PR200608Q

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2

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11

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Matthew B. Renfrow

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2011-12-29T00:00:00Z

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22067045

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3844682

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