An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix.
about
Form and function: the laminin family of heterotrimersA single pulse of agrin triggers a pathway that acts to cluster acetylcholine receptorsAgrin is a major heparan sulfate proteoglycan in the human glomerular basement membraneAgrin binds to the nerve-muscle basal lamina via lamininThe dystroglycan complex is necessary for stabilization of acetylcholine receptor clusters at neuromuscular junctions and formation of the synaptic basement membraneAn interdomain disulfide bridge links the NtA and first FS domain in agrinAugmented synthesis and differential localization of heparan sulfate proteoglycans in Duchenne muscular dystrophyThe C-terminal domain V of perlecan promotes beta1 integrin-mediated cell adhesion, binds heparin, nidogen and fibulin-2 and can be modified by glycosaminoglycansAcetylcholine receptors are required for agrin-induced clustering of postsynaptic proteins.Agrin is a chimeric proteoglycan with the attachment sites for heparan sulfate/chondroitin sulfate located in two multiple serine-glycine clustersThe COOH-terminal domain of agrin signals via a synaptic receptor in central nervous system neuronsInhibition of synapse assembly in mammalian muscle in vivo by RNA interferenceAgrin isoforms with distinct amino termini: differential expression, localization, and functionMapping of the laminin-binding site of the N-terminal agrin domain (NtA).Local induction of acetylcholine receptor clustering in myotube cultures using microfluidic application of agrin.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.Electron microscopic structure of agrin and mapping of its binding site in laminin-1Agrin expression during synaptogenesis induced by traumatic brain injuryRecycling of acetylcholine receptors at ectopic postsynaptic clusters induced by exogenous agrin in living rats.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.Defects in eye development in transgenic mice overexpressing the heparan sulfate proteoglycan agrin.AChR phosphorylation and aggregation induced by an agrin fragment that lacks the binding domain for alpha-dystroglycanInduction by agrin of ectopic and functional postsynaptic-like membrane in innervated muscle.Agrin can mediate acetylcholine receptor gene expression in muscle by aggregation of muscle-derived neuregulins.Dynein disruption perturbs post-synaptic components and contributes to impaired MuSK clustering at the NMJ: implication in ALS.Rescuing Z+ agrin splicing in Nova null mice restores synapse formation and unmasks a physiologic defect in motor neuron firingScaffold-forming and Adhesive Contributions of Synthetic Laminin-binding Proteins to Basement Membrane AssemblySubstrate-bound agrin induces expression of acetylcholine receptor epsilon-subunit gene in cultured mammalian muscle cellsExpression, distribution and ultrastructural localization of the synapse-organizing molecule agrin in the mature avian retina.HIV-1-infected blood mononuclear cells form an integrin- and agrin-dependent viral synapse to induce efficient HIV-1 transcytosis across epithelial cell monolayer.Effects of purified recombinant neural and muscle agrin on skeletal muscle fibers in vivo.Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin.Site specific cleavage mediated by MMPs regulates function of agrin.MuSK induces in vivo acetylcholine receptor clusters in a ligand-independent manner.Muscle activity and muscle agrin regulate the organization of cytoskeletal proteins and attached acetylcholine receptor (AchR) aggregates in skeletal muscle fibers.A minigene of neural agrin encoding the laminin-binding and acetylcholine receptor-aggregating domains is sufficient to induce postsynaptic differentiation in muscle fibres.A Cell Culture System to Investigate the Presynaptic Control of Subsynaptic Membrane Differentiation at the Neuromuscular Junction.Laminin deposition in the extracellular matrix: a complex picture emerges.Agrin is required for posterior development and motor axon outgrowth and branching in embryonic zebrafish.
P2860
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P2860
An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
An amino-terminal extension is ...... nding to extracellular matrix.
@ast
An amino-terminal extension is ...... nding to extracellular matrix.
@en
type
label
An amino-terminal extension is ...... nding to extracellular matrix.
@ast
An amino-terminal extension is ...... nding to extracellular matrix.
@en
prefLabel
An amino-terminal extension is ...... nding to extracellular matrix.
@ast
An amino-terminal extension is ...... nding to extracellular matrix.
@en
P2093
P2860
P356
P1476
An amino-terminal extension is ...... nding to extracellular matrix.
@en
P2093
Gesemann M
Schumacher B
P2860
P304
P356
10.1083/JCB.131.6.1547
P407
P433
P577
1995-12-01T00:00:00Z