LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans. - sprookjes - yvandenbroek - TriplyDB

LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

http://www.wikidata.org/entity/Q37472546

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Recent advancements in understanding mammalian O-mannosylation.

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LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

http://www.wikidata.org/entity/Q37472546

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 22 July 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

@en

LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

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type

label

LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

@en

LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

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prefLabel

LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

@en

LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans.

@nl

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LARGE2-dependent glycosylation confers laminin-binding ability on proteoglycans

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Daniel Beltrán-Valero de Bernabé

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Kei-Ichiro Inamori

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Kevin P Campbell

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Michael E Wright

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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

Endogenous glucuronyltransferase activity of LARGE or LARGE2 required for functional modification of α-dystroglycan in cells and tissues

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

B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan

The glucuronyltransferase B4GAT1 is required for initiation of LARGE-mediated α-dystroglycan functional glycosylation

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

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1284-1296

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scholarly article

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10.1093/GLYCOB/CWW075

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12

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26

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Aaron M. Beedle

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2016-07-22T00:00:00Z

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27496765

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5137251

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