about
Agrin binds to the nerve-muscle basal lamina via lamininCrosstalk between Agrin and Wnt signaling pathways in development of vertebrate neuromuscular junctionA targeted glycan-related gene screen reveals heparan sulfate proteoglycan sulfation regulates WNT and BMP trans-synaptic signalingThe role of agrin in synaptic development, plasticity and signaling in the central nervous systemAgrin is a heparan sulfate proteoglycanA brain-enriched polypyrimidine tract-binding protein antagonizes the ability of Nova to regulate neuron-specific alternative splicingAgrin mediates a rapid switch from electrical coupling to chemical neurotransmission during synaptogenesisAgrin isoforms with distinct amino termini: differential expression, localization, and functionInduction of myasthenia by immunization against muscle-specific kinase.Xenopus muscle-specific kinase: molecular cloning and prominent expression in neural tissues during early embryonic development.Collagen XVIII is a basement membrane heparan sulfate proteoglycan.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.Formation of the neuromuscular junction. Agrin and its unusual receptors.Regulation and functional significance of utrophin expression at the mammalian neuromuscular synapse.Electron microscopic structure of agrin and mapping of its binding site in laminin-1Still more complexity in mammalian basement membranes.A single EGF-like motif of laminin is responsible for high affinity nidogen binding.Differential heparin inhibition of skeletal muscle alpha-dystroglycan binding to laminins.The agrin/muscle-specific kinase pathway: new targets for autoimmune and genetic disorders at the neuromuscular junction.AChR phosphorylation and aggregation induced by an agrin fragment that lacks the binding domain for alpha-dystroglycanEvolution and comparative genomics of subcellular specializations: EST sequencing of Torpedo electric organ.Structure-function analysis of endogenous lectin mind-the-gap in synaptogenesisSynaptic activity and connective tissue remodeling in denervated frog muscle.Regulation of the interaction of nicotinic acetylcholine receptors with the cytoskeleton by agrin-activated protein tyrosine kinase.Distribution of alpha-dystroglycan during embryonic nerve-muscle synaptogenesis.An amino-terminal extension is required for the secretion of chick agrin and its binding to extracellular matrix.Agrin-induced acetylcholine receptor clustering in mammalian muscle requires tyrosine phosphorylation.Laminin-induced acetylcholine receptor clustering: an alternative pathway.Role of extracellular matrix proteins and their receptors in the development of the vertebrate neuromuscular junctionAcetylcholine receptor-aggregating activity of agrin isoforms and mapping of the active siteImmobilization of nicotinic acetylcholine receptors in mouse C2 myotubes by agrin-induced protein tyrosine phosphorylationNeural regulation of muscle acetylcholine receptor epsilon- and alpha-subunit gene promoters in transgenic miceKinase domain of the muscle-specific receptor tyrosine kinase (MuSK) is sufficient for phosphorylation but not clustering of acetylcholine receptors: required role for the MuSK ectodomain?New gene, nel, encoding a M(r) 93 K protein with EGF-like repeats is strongly expressed in neural tissues of early stage chick embryos.Identification of an agrin mutation that causes congenital myasthenia and affects synapse function.Schwann cells promote synaptogenesis at the neuromuscular junction via transforming growth factor-beta1Substrate-bound agrin induces expression of acetylcholine receptor epsilon-subunit gene in cultured mammalian muscle cellsHeparin inhibits acetylcholine receptor aggregation at two distinct steps in the agrin-induced pathway.Anti-agrin staining is absent at abandoned synaptic sites of frog neuromuscular junctions.Expression, distribution and ultrastructural localization of the synapse-organizing molecule agrin in the mature avian retina.
P2860
Q24321436-C114B047-2FF2-4482-92C5-569FD7048088Q27013130-49A83612-5D16-40C8-A497-69198ECBC773Q27330302-18888B9D-828A-4E17-88AF-64A5C8727665Q27690239-33C5A89C-858A-4C32-845B-8DD1923B8183Q28307146-68E4C81D-9776-4A83-A150-FE20EB6BEB4DQ28512596-5F6F46B9-23C0-4B76-89CD-1874DC077DE0Q28566547-4E889C6F-C6B3-4C12-950C-7D0E545C6C09Q28592146-FE0ABEB9-991C-4FED-90D1-149D374D057DQ30476990-0169EA10-3F14-40BD-BCF4-08C3F99EBBF9Q30650686-1F97BDB8-B8D3-4840-B659-4E7EB97706E2Q32021258-6FA1CC80-FA25-4398-A97A-3A1856152B69Q33294705-8E145A6C-B01E-45E5-A46F-8771F1117127Q33734614-CC9862D2-B41A-47FD-9C80-EF1AF45441E6Q33887124-1C7C770E-9927-4D4B-82AF-2D83DCC853B8Q33888037-B2181D4A-769B-4F96-81CA-49FFF37166CDQ34035427-0E0D55CC-F453-49AD-ACC4-212964A2172AQ34050043-60B2FC42-CDE7-4038-813E-C28891DB6A57Q34379897-59450CE8-ACA7-41E9-AA68-D3451EAE26F1Q34468998-C60FB740-2ACF-4793-8DBB-28726BD415B4Q35850798-56AEA638-F414-4DF4-B146-4291891D5FB4Q36141028-9FA321A9-8E46-44E9-90CD-831E71E983E0Q36160060-588E25C8-B755-4A96-BD62-654ECD88DFC1Q36234922-B77755F9-0EEF-40F8-89B6-220EB1F63E6EQ36235442-48530404-ED15-4705-8922-06B3A463FF57Q36235647-D2288668-1221-4B75-9155-992F2721799AQ36236246-D0675579-D5C1-4D93-AF8C-15AB7E7D0D3AQ36236530-82B30C9A-AFBD-428D-B7EC-C5EA1C182999Q36273941-CBD2D7D3-B92A-4FEB-8909-DC53B5E9A39DQ36321503-38C054D3-2BDB-48AE-B369-C1523C47E39AQ36382434-CB42983F-6763-4359-AAAB-6496BB5E02DCQ36382764-5B5B9BD0-9E07-45F9-A78D-912A5D2698B3Q36534824-B2223B4A-FE37-4D9E-8574-D3983864B928Q36563500-74D43696-3134-48BC-92A5-CB33531DCA1FQ36692178-C810BD05-533A-4179-9EA3-E8472B4CB8B0Q37301198-500BA90E-6609-40C2-B5F6-3183D7780CFBQ37352517-FDEEDC97-B28A-4109-9764-68566FB85421Q37566944-C34ECFF6-933F-4F2E-AB98-3B6D1587FC89Q38345407-8984370D-C38D-49D8-A14C-1DC41CF6B3A7Q39228953-C97318F9-2183-4009-9ED9-7797F77EF0E2Q39749508-5BA71053-FDBA-4C18-B942-FABEA4D86499
P2860
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
cDNA that encodes active agrin.
@en
type
label
cDNA that encodes active agrin.
@en
prefLabel
cDNA that encodes active agrin.
@en
P2093
P1433
P1476
cDNA that encodes active agrin.
@en
P2093
P304
P356
10.1016/0896-6273(92)90089-V
P407
P577
1992-04-01T00:00:00Z