Identification of agrin, a synaptic organizing protein from Torpedo electric organ. - Wikidata - wikimedia - TriplyDB

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

http://www.wikidata.org/entity/Q36217149

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Proteoglycan form and function: A comprehensive nomenclature of proteoglycans Agrin binds to the nerve-muscle basal lamina via laminin Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate Ultrastructure of acetylcholine receptor aggregates parallels mechanisms of aggregation Proteoglycans in the central nervous system: role in development, neural repair, and Alzheimer's disease The Wnt and BMP families of signaling morphogens at the vertebrate neuromuscular junction Alterations of cAMP-dependent signaling in dystrophic skeletal muscle Crosstalk between Agrin and Wnt signaling pathways in development of vertebrate neuromuscular junction Glutamatergic neurons induce expression of functional glutamatergic synapses in primary myotubes The neurogenetics of alternative splicing Reduced glycosaminoglycan sulfation diminishes the agrin signal transduction pathway Agrin is a heparan sulfate proteoglycan Subacute developmental exposure of zebrafish to the organophosphate pesticide metabolite, chlorpyrifos-oxon, results in defects in Rohon-Beard sensory neuron development.Regulation of synaptic growth and maturation by a synapse-associated E3 ubiquitin ligase at the neuromuscular junction Agrin mediates a rapid switch from electrical coupling to chemical neurotransmission during synaptogenesis An investigation of the activity of recombinant rat skeletal muscle cytosolic sialidase Asparagine of z8 insert is critical for the affinity, conformation, and acetylcholine receptor-clustering activity of neural agrin Agrin in Alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma Essential roles of the acetylcholine receptor gamma-subunit in neuromuscular synaptic patterning.Xenopus muscle-specific kinase: molecular cloning and prominent expression in neural tissues during early embryonic development.MAGI-1c: a synaptic MAGUK interacting with muSK at the vertebrate neuromuscular junction.Collagen XVIII is a basement membrane heparan sulfate proteoglycan.Chondroitin sulfate proteoglycans are structural renewable constituents of the rabbit vitreous body.The proteome survey of an electricity-generating organ (Torpedo californica electric organ).C. elegans agrin is expressed in pharynx, IL1 neurons and distal tip cells and does not genetically interact with genes involved in synaptogenesis or muscle function.Genetics and cell biology of building specific synaptic connectivity.Processing of ARIA and release from isolated nerve terminals.Dynamic light scattering: a practical guide and applications in biomedical sciences.Formation of the neuromuscular junction. Agrin and its unusual receptors.Electron microscopic structure of agrin and mapping of its binding site in laminin-1 New role for Agrin in T cells and its potential importance in immune system regulation Collagen XIX is expressed by interneurons and contributes to the formation of hippocampal synapses.Still more complexity in mammalian basement membranes.Agrin expression during synaptogenesis induced by traumatic brain injury Basement membrane proteins: structure, assembly, and cellular interactions.Skeletal muscle tissue engineering: methods to form skeletal myotubes and their applications.The heparan sulfate proteoglycan agrin contributes to barrier properties of mouse brain endothelial cells by stabilizing adherens junctions.The agrin/muscle-specific kinase pathway: new targets for autoimmune and genetic disorders at the neuromuscular junction.Effect of agrin on the distribution of acetylcholine receptors and sodium channels on adult skeletal muscle fibers in culture.Integrated genomics and proteomics of the Torpedo californica electric organ: concordance with the mammalian neuromuscular junction

P2860

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P2860

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

http://www.wikidata.org/entity/Q36217149

description

1987 nî lūn-bûn

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1987年の論文

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1987年論文

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1987年論文

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1987年論文

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1987年論文

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1987年論文

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1987年论文

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1987年论文

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1987年论文

@zh-cn

name

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

@ast

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

@en

type

label

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

@ast

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

@en

prefLabel

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

@ast

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

@en

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Journal of Cell Biology

P1476

Identification of agrin, a synaptic organizing protein from Torpedo electric organ.

@en

P2093

B G Wallace

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

C Magill

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

J R Fallon

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M A Smith

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R M Nitkin

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U J McMahan

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Y M Yao

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P2860

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity

Lateral motion of fluorescently labeled acetylcholine receptors in membranes of developing muscle fibers.

Dispersal and reformation of acetylcholine receptor clusters of cultured rat myotubes treated with inhibitors of energy metabolism

Brain extract causes acetylcholine receptor redistribution which mimics some early events at developing neuromuscular junctions

The influence of basal lamina on the accumulation of acetylcholine receptors at synaptic sites in regenerating muscle

Components of Torpedo electric organ and muscle that cause aggregation of acetylcholine receptors on cultured muscle cells

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2471-2478

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scholarly article

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10.1083/JCB.105.6.2471

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P433

6 Pt 1

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105

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1987-12-01T00:00:00Z

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2826489

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2114709

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