O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding. - Wikidata - wikimedia - TriplyDB

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

http://www.wikidata.org/entity/Q34090655

about

Fukutin-related protein resides in the Golgi cisternae of skeletal muscle fibres and forms disulfide-linked homodimers via an N-terminal interaction Skeletal muscle laminin and MDC1A: pathogenesis and treatment strategies.Mutations in GDP-mannose pyrophosphorylase B cause congenital and limb-girdle muscular dystrophies associated with hypoglycosylation of α-dystroglycan 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 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 SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function Mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of α-dystroglycan Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression Mouse fukutin deletion impairs dystroglycan processing and recapitulates muscular dystrophy Post-translational maturation of dystroglycan is necessary for pikachurin binding and ribbon synaptic localization Glycan Engineering for Cell and Developmental Biology The potential of sarcospan in adhesion complex replacement therapeutics for the treatment of muscular dystrophy Neurological aspects of human glycosylation disorders Mammalian O-mannosylation: unsolved questions of structure/function O-Mannosylation and human disease The secretory pathway kinases Enzymatic reactions on immobilised substrates Autosomal recessive dilated cardiomyopathy due to DOLK mutations results from abnormal dystroglycan O-mannosylation 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 AGO61-dependent GlcNAc modification primes the formation of functional glycans on α-dystroglycan LARGE glycans on dystroglycan function as a tunable matrix scaffold to prevent dystrophy LARGE2 generates the same xylose- and glucuronic acid-containing glycan structures as LARGE Xylosyl- and glucuronyltransferase functions of LARGE in α-dystroglycan modification are conserved in LARGE2 Development of rabbit monoclonal antibodies for detection of alpha-dystroglycan in normal and dystrophic tissue.Biochemical correlation of activity of the α-dystroglycan-modifying glycosyltransferase POMGnT1 with mutations in muscle-eye-brain disease.Fer kinase regulates cell migration through α-dystroglycan glycosylation POMK mutations disrupt muscle development leading to a spectrum of neuromuscular presentations Structural basis of laminin binding to the LARGE glycans on dystroglycan.The Muscular Dystrophy Gene TMEM5 Encodes a Ribitol β1,4-Xylosyltransferase Required for the Functional Glycosylation of Dystroglycan.The functional O-mannose glycan on α-dystroglycan contains a phospho-ribitol primed for matriglycan addition Mammalian protein glycosylation--structure versus function.Dystroglycan mediates homeostatic synaptic plasticity at GABAergic synapses Efficacy of Gene Therapy Is Dependent on Disease Progression in Dystrophic Mice with Mutations in the FKRP Gene Neurexins.Transgenic overexpression of LARGE induces α-dystroglycan hyperglycosylation in skeletal and cardiac muscle Large induces functional glycans in an O-mannosylation dependent manner and targets GlcNAc terminals on alpha-dystroglycan Mammalian O-mannosylation of cadherins and plexins is independent of protein O-mannosyltransferases 1 and 2.

P2860

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P2860

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

http://www.wikidata.org/entity/Q34090655

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@ast

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@en

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@nl

type

label

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@ast

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@en

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@nl

prefLabel

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@ast

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@en

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding.

@nl

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SCIENCE.1180512

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P1476

O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding

@en

P2093

Harry Schachter

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

Lance Wells

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

Michael B A Oldstone

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

Michael Madson

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

Sarah Davis

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

Stephanie H Stalnaker

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

Takako Yoshida-Moriguchi

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

P2860

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

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

An ancient retrotransposal insertion causes Fukuyama-type congenital muscular dystrophy

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.

Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome

Ethnically diverse causes of Walker-Warburg syndrome (WWS): FCMD mutations are a more common cause of WWS outside of the Middle East

POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome

Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan

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

Molecular recognition by LARGE is essential for expression of functional dystroglycan

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88-92

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scholarly article

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10.1126/SCIENCE.1180512

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5961

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327

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Kevin P Campbell

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2010-01-01T00:00:00Z

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40821808

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20044576

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phosphorylation

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2978000

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