Biglycan is an extracellular MuSK binding protein important for synapse stability - Wikidata - wikimedia - TriplyDB

Biglycan is an extracellular MuSK binding protein important for synapse stability

Biglycan is an extracellular MuSK binding protein important for synapse stability

http://www.wikidata.org/entity/Q35855912

about

Galectin-1 Protein Therapy Prevents Pathology and Improves Muscle Function in the mdx Mouse Model of Duchenne Muscular Dystrophy Soluble biglycan as a biomarker of inflammatory renal diseases.The neuromuscular junction: measuring synapse size, fragmentation and changes in synaptic protein density using confocal fluorescence microscopy.Collagen Q and anti-MuSK autoantibody competitively suppress agrin/LRP4/MuSK signaling.The role of novel and known extracellular matrix and adhesion molecules in the homeostatic and regenerative bone marrow microenvironment Transcriptome-wide regulation of pre-mRNA splicing and mRNA localization by muscleblind proteins.Contaminants in commercial preparations of 'purified' small leucine-rich proteoglycans may distort mechanistic studies.Biglycan: a multivalent proteoglycan providing structure and signals MuSK IgG4 autoantibodies cause myasthenia gravis by inhibiting binding between MuSK and Lrp4.MuSK is a BMP co-receptor that shapes BMP responses and calcium signaling in muscle cells.Structural mechanisms of the agrin-LRP4-MuSK signaling pathway in neuromuscular junction differentiation.Structure of the neuromuscular junction: function and cooperative mechanisms in the synapse.Pathogenic immune mechanisms at the neuromuscular synapse: the role of specific antibody-binding epitopes in myasthenia gravis.Mechanisms controlling neuromuscular junction stability.Biglycan modulates angiogenesis and bone formation during fracture healing Synaptic Homeostasis and Its Immunological Disturbance in Neuromuscular Junction Disorders.De novo expression of circulating biglycan evokes an innate inflammatory tissue response via MyD88/TRIF pathways.Postnatal knockdown of dok-7 gene expression in mice causes structural defects in neuromuscular synapses and myasthenic pathology.Animal models of antimuscle-specific kinase myasthenia.Novel adeno-associated viral vector delivering the utrophin gene regulator jazz counteracts dystrophic pathology in mdx mice.ECM-Related Myopathies and Muscular Dystrophies: Pros and Cons of Protein Therapies.The mouse passive-transfer model of MuSK myasthenia gravis: disrupted MuSK signaling causes synapse failure.Agrin-LRP4-MuSK signaling as a therapeutic target for myasthenia gravis and other neuromuscular disorders.The presence of dysautonomia in different subgroups of myasthenia gravis patients.Non-Glycanated Biglycan and LTBP4: Leveraging the extracellular matrix for Duchenne Muscular Dystrophy therapeutics.

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Biglycan is an extracellular MuSK binding protein important for synapse stability

http://www.wikidata.org/entity/Q35855912

description

2012 nî lūn-bûn

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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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2012年论文

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2012年论文

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name

Biglycan is an extracellular MuSK binding protein important for synapse stability

@ast

Biglycan is an extracellular MuSK binding protein important for synapse stability

@en

type

label

Biglycan is an extracellular MuSK binding protein important for synapse stability

@ast

Biglycan is an extracellular MuSK binding protein important for synapse stability

@en

prefLabel

Biglycan is an extracellular MuSK binding protein important for synapse stability

@ast

Biglycan is an extracellular MuSK binding protein important for synapse stability

@en

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P356

JNEUROSCI.4610-11.2012

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Journal of Neuroscience

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Biglycan is an extracellular MuSK binding protein important for synapse stability

@en

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Alison R Amenta

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

Beatrice E Lechner

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

Beth A McKechnie

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

David J McQuillan

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

Emilio Marrero

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

Hilliary E Creely

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

Hiroki Hagiwara

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

Justin R Fallon

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

Lin Mei

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

Marian F Young

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

P2860

Biglycan binds to alpha- and gamma-sarcoglycan and regulates their expression during development

To build a synapse: signaling pathways in neuromuscular junction assembly

MuSK is required for anchoring acetylcholinesterase at the neuromuscular junction

Distinct domains of MuSK mediate its abilities to induce and to associate with postsynaptic specializations

The small leucine-rich repeat proteoglycan biglycan binds to alpha-dystroglycan and is upregulated in dystrophic muscle

Induction, assembly, maturation and maintenance of a postsynaptic apparatus

Cellular and molecular mechanisms underlying age-related skeletal muscle wasting and weakness

Agrin acts via a MuSK receptor complex

Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice

Assembly of the sarcoglycan complex. Insights for muscular dystrophy

P304

2324-2334

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scholarly article

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10.1523/JNEUROSCI.4610-11.2012

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7

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32

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2012-02-01T00:00:00Z

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221683193

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22396407

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3313673

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