Glycoproteomic characterization of recombinant mouse α-dystroglycan. - Wikidata - wikimedia - TriplyDB

Glycoproteomic characterization of recombinant mouse α-dystroglycan.

Glycoproteomic characterization of recombinant mouse α-dystroglycan.

http://www.wikidata.org/entity/Q34126184

about

B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan Mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of α-dystroglycan Glycan analysis of therapeutic glycoproteins A Method to Produce and Purify Full-Length Recombinant Alpha Dystroglycan: Analysis of N- and O-Linked Monosaccharide Composition in CHO Cells with or without LARGE Overexpression Insights from molecular dynamics simulations: structural basis for the V567D mutation-induced instability of zebrafish alpha-dystroglycan and comparison with the murine model The Structure of the T190M Mutant of Murine α-Dystroglycan at High Resolution: Insight into the Molecular Basis of a Primary Dystroglycanopathy Mammalian O-mannosylation of cadherins and plexins is independent of protein O-mannosyltransferases 1 and 2.Insertion of a myc-tag within α-dystroglycan domains improves its biochemical and microscopic detection.Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2011-2012.Probing the stability of the "naked" mucin-like domain of human α-dystroglycan Glycosylation of α-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases.The zebrafish galectins Drgal1-L2 and Drgal3-L1 bind in vitro to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and reduce viral adhesion to fish epithelial cells Targeting the glycoproteome The o-mannosylation pathway: glycosyltransferases and proteins implicated in congenital muscular dystrophy.Mapping the complete glycoproteome of virion-derived HIV-1 gp120 provides insights into broadly neutralizing antibody binding.Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins.Dissecting the molecular basis of the role of the O-mannosylation pathway in disease: α-dystroglycan and forms of muscular dystrophy.The challenge and promise of glycomics.Protein O-mannosylation in metazoan organisms.The sweet tooth of biopharmaceuticals: importance of recombinant protein glycosylation analysis.Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.Recent advancements in understanding mammalian O-mannosylation.Dystroglycan binding to α-neurexin competes with neurexophilin-1 and neuroligin in the brain.Glycoproteomic studies of IgE from a novel hyper IgE syndrome linked to PGM3 mutation.Enhanced glycan nanoprofiling by weak anion exchange preparative chromatography, mild acid desialylation, and nanoliquid chromatography-mass spectrometry with nanofluorescence detection.Protein O-Linked Mannose β-1,4-N-Acetylglucosaminyl-transferase 2 (POMGNT2) Is a Gatekeeper Enzyme for Functional Glycosylation of α-Dystroglycan.The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site.

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P2860

Glycoproteomic characterization of recombinant mouse α-dystroglycan.

http://www.wikidata.org/entity/Q34126184

description

2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2012 թվականի հունվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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type

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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prefLabel

Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

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P2093

Anne Dell

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

David Mekhaiel

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

Howard R Morris

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

Jane E Hewitt

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Maria Panico

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

Paul G Hitchen

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

Rebecca Harrison

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Richard J Pleass

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Stuart M Haslam

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P2860

Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1

Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2

A stoichiometric complex of neurexins and dystroglycan in brain

Distinct requirements for heparin and alpha-dystroglycan binding revealed by structure-based mutagenesis of the laminin alpha2 LG4-LG5 domain pair

Refining genotype phenotype correlations in muscular dystrophies with defective glycosylation of dystroglycan

Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor

Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix

Distribution of dystroglycan in normal adult mouse tissues

A genetic model for muscle-eye-brain disease in mice lacking protein O-mannose 1,2-N-acetylglucosaminyltransferase (POMGnT1)

Membrane organization of the dystrophin-glycoprotein complex

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662-675

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10.1093/GLYCOB/CWS002

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5

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22

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