Glycomic analyses of mouse models of congenital muscular dystrophy - Wikidata - wikimedia - TriplyDB

Glycomic analyses of mouse models of congenital muscular dystrophy

Glycomic analyses of mouse models of congenital muscular dystrophy

http://www.wikidata.org/entity/Q35065134

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B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function Neurological aspects of human glycosylation disorders Mammalian O-mannosylation: unsolved questions of structure/function O-Mannosylation and human disease Dystroglycan organizes axon guidance cue localization and axonal pathfinding Whoa man! Unexpected protein O-mannosylation pathways in mammals Glycoproteomic characterization of recombinant mouse α-dystroglycan.Neurology of inherited glycosylation disorders.Human natural killer-1 sulfotransferase (HNK-1ST)-induced sulfate transfer regulates laminin-binding glycans on α-dystroglycan.A role for Galgt1 in skeletal muscle regeneration.Synthetic, structural, and biosynthetic studies of an unusual phospho-glycopeptide derived from α-dystroglycan.Neurons and glia modify receptor protein-tyrosine phosphatase ζ (RPTPζ)/phosphacan with cell-specific O-mannosyl glycans in the developing brain.Glycosylation of α-dystroglycan: O-mannosylation influences the subsequent addition of GalNAc by UDP-GalNAc polypeptide N-acetylgalactosaminyltransferases.Protein O-Mannosylation in the Murine Brain: Occurrence of Mono-O-Mannosyl Glycans and Identification of New Substrates Developmental expression of the neuron-specific N-acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V The N's and O's of Drosophila glycoprotein glycobiology.ISPD gene mutations are a common cause of congenital and limb-girdle muscular dystrophies.The o-mannosylation pathway: glycosyltransferases and proteins implicated in congenital muscular dystrophy.ISPD produces CDP-ribitol used by FKTN and FKRP to transfer ribitol phosphate onto α-dystroglycan.Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of α-dystroglycan Sparing of the dystrophin-deficient cranial sartorius muscle is associated with classical and novel hypertrophy pathways in GRMD dogs Protein O-mannosylation is crucial for E-cadherin-mediated cell adhesion.Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins.Vertebrate protein glycosylation: diversity, synthesis and function.Dissecting the molecular basis of the role of the O-mannosylation pathway in disease: α-dystroglycan and forms of muscular dystrophy.Protein O-mannosylation in metazoan organisms.Mammalian O-mannosylation pathway: glycan structures, enzymes, and protein substrates.Finding the sweet spot: assembly and glycosylation of the dystrophin-associated glycoprotein complex.Matriglycan: a novel polysaccharide that links dystroglycan to the basement membrane.Recent advancements in understanding mammalian O-mannosylation.RPTPζ/phosphacan is abnormally glycosylated in a model of muscle-eye-brain disease lacking functional POMGnT1 Dystroglycan binding to α-neurexin competes with neurexophilin-1 and neuroligin in the brain.O-glycosylation of the non-canonical T-cadherin from rabbit skeletal muscle by single mannose residues.

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P2860

Glycomic analyses of mouse models of congenital muscular dystrophy

http://www.wikidata.org/entity/Q35065134

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2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Glycomic analyses of mouse models of congenital muscular dystrophy

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Glycomic analyses of mouse models of congenital muscular dystrophy

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Glycomic analyses of mouse models of congenital muscular dystrophy

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Glycomic analyses of mouse models of congenital muscular dystrophy

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Glycomic analyses of mouse models of congenital muscular dystrophy

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Glycomic analyses of mouse models of congenital muscular dystrophy

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JBC.M110.203281

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Journal of Biological Chemistry

P1476

Glycomic analyses of mouse models of congenital muscular dystrophy

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P2093

David Live

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Huaiyu Hu

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Jae-Min Lim

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Jakob S Satz

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Lance Wells

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Mian Liu

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

Michael Tiemeyer

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

Mindy Porterfield

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Peng Zhang

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Sean Buskirk

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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

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

Molecular recognition by LARGE is essential for expression of functional dystroglycan

Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus

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

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21180-21190

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10.1074/JBC.M110.203281

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24

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286

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Kevin P Campbell

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21460210

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