Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates. - Wikidata - wikimedia - TriplyDB

Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.

Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.

http://www.wikidata.org/entity/Q38208557

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B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan Neurological aspects of human glycosylation disorders The functional O-mannose glycan on α-dystroglycan contains a phospho-ribitol primed for matriglycan addition Mammalian O-mannosylation of cadherins and plexins is independent of protein O-mannosyltransferases 1 and 2.Development of a multifunctional aminoxy-based fluorescent linker for glycan immobilization and analysis.Protein O-Mannosylation in the Murine Brain: Occurrence of Mono-O-Mannosyl Glycans and Identification of New Substrates Chemoenzymatic synthesis of α-dystroglycan core M1 O-mannose glycans.Eukaryotic protein glycosylation: a primer for histochemists and cell biologists Glycosylation-directed quality control of protein folding.What Have We Learned from Glycosyltransferase Knockouts in Mice?Induction of Antibodies Directed Against Branched Core O-Mannosyl Glycopeptides-Selectivity Complimentary to the ConA Lectin.Mannoside recognition and degradation by bacteria.Recent advancements in understanding mammalian O-mannosylation.Functional Similarities between the Protein O-Mannosyltransferases Pmt4 from Bakers' Yeast and Human POMT1.O-mannosylation and N-glycosylation: two coordinated mechanisms regulating the tumour suppressor functions of E-cadherin in cancer.Protein O-Linked Mannose β-1,4-N-Acetylglucosaminyl-transferase 2 (POMGNT2) Is a Gatekeeper Enzyme for Functional Glycosylation of α-Dystroglycan.Muscular Dystrophy with Ribitol-Phosphate Deficiency: A Novel Post-Translational Mechanism in Dystroglycanopathy.Discovery of an O-mannosylation pathway selectively serving cadherins and protocadherins.Rapid screening of sugar-nucleotide donor specificities of putative glycosyltransferases.

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P2860

Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.

http://www.wikidata.org/entity/Q38208557

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Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.

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Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.

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Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.

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Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.

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Jeremy L Praissman

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Lance Wells

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P2860

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

Dystroglycan function requires xylosyl- and glucuronyltransferase activities of LARGE

Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity

Tumor suppressor function of laminin-binding alpha-dystroglycan requires a distinct beta3-N-acetylglucosaminyltransferase

ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and cause Walker-Warburg syndrome

Mutations in ISPD cause Walker-Warburg syndrome and defective glycosylation of α-dystroglycan

SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function

Mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of α-dystroglycan

A comparative study of alpha-dystroglycan glycosylation in dystroglycanopathies suggests that the hypoglycosylation of alpha-dystroglycan does not consistently correlate with clinical severity

Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan.

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3066-3078

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scholarly article

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10.1021/BI500153Y

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19

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53

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2014-05-07T00:00:00Z

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2014-05-20T00:00:00Z

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262017689

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24786756

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Angliavandeniai

regulation of gene expression

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4033628

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