Identification and characterization of CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase in IgA1-producing cells - sprookjes - yvandenbroek - TriplyDB

Identification and characterization of CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase in IgA1-producing cells

Identification and characterization of CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase in IgA1-producing cells

http://www.wikidata.org/entity/Q24680134

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The Origin and Activities of IgA1-Containing Immune Complexes in IgA Nephropathy The pathophysiology of IgA nephropathy Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy The genetics and immunobiology of IgA nephropathy.Genetic studies of IgA nephropathy: past, present, and future.Identification of distinct glycoforms of IgA1 in plasma from patients with immunoglobulin A (IgA) nephropathy and healthy individuals Aberrantly glycosylated IgA1 as a factor in the pathogenesis of IgA nephropathy Role of aberrant glycosylation of IgA1 molecules in the pathogenesis of IgA nephropathy N-acetylgalactosaminide α2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy.IgA1-secreting cell lines from patients with IgA nephropathy produce aberrantly glycosylated IgA1 IgA glycosylation and IgA immune complexes in the pathogenesis of IgA nephropathy.Aberrant O-glycosylation and anti-glycan antibodies in an autoimmune disease IgA nephropathy and breast adenocarcinoma.Pathogenesis of Henoch-Schönlein purpura nephritis.The IgA1 immune complex-mediated activation of the MAPK/ERK kinase pathway in mesangial cells is associated with glomerular damage in IgA nephropathy.Cytokines alter IgA1 O-glycosylation by dysregulating C1GalT1 and ST6GalNAc-II enzymes.The Tn antigen-structural simplicity and biological complexity.Glycosylation of IgA1 and pathogenesis of IgA nephropathy.Paradigm shift in activity assessment of IgA nephropathy - optimizing the next generation of diagnostic and therapeutic maneuvers via glycan targeting.IgA nephropathy enigma.New insights into the pathogenesis of IgA nephropathy.

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Identification and characterization of CMP-NeuAc:GalNAc-IgA1 alpha2,6-sialyltransferase in IgA1-producing cells

http://www.wikidata.org/entity/Q24680134

description

2007 nî lūn-bûn

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2007 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2007 թվականի մայիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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Identification and characteriz ...... ferase in IgA1-producing cells

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Identification and characteriz ...... ferase in IgA1-producing cells

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Identification and characteriz ...... ferase in IgA1-producing cells

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Identification and characteriz ...... ferase in IgA1-producing cells

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Identification and characteriz ...... ferase in IgA1-producing cells

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Identification and characteriz ...... ferase in IgA1-producing cells

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Identification and characteriz ...... ferase in IgA1-producing cells

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Identification and characteriz ...... ferase in IgA1-producing cells

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J.JMB.2007.03.002

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Journal of Molecular Biology

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Identification and characteriz ...... ferase in IgA1-producing cells

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Bruce A Julian

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Fredric Carlsson

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Gunnar Lindahl

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Hitoshi Suzuki

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Huong L Vu

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Jan Novak

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Jiri Mestecky

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Judit Andrasi

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Milan Raska

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Milan Tomana

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P2860

Cloning and expression of a human gene encoding an N-acetylgalactosamine-alpha2,6-sialyltransferase (ST6GalNAc I): a candidate for synthesis of cancer-associated sialyl-Tn antigens

Cloning and expression of human core 1 beta1,3-galactosyltransferase

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

A unique molecular chaperone Cosmc required for activity of the mammalian core 1 beta 3-galactosyltransferase

Ultrastructural studies of human lymphoid cells. mu and J chain expression as a function of B cell differentiation

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.

Molecular cloning and characterization of a novel UDP-Gal:GalNAc(alpha) peptide beta 1,3-galactosyltransferase (C1Gal-T2), an enzyme synthesizing a core 1 structure of O-glycan.

Glomerulonephritis.

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