Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
about
Form and function: the laminin family of heterotrimersApoptosis inhibitors and mini-agrin have additive benefits in congenital muscular dystrophy miceDevelopmental and pathogenic mechanisms of basement membrane assemblyProteoglycans in liver cancerDecoding the Matrix: Instructive Roles of Proteoglycan ReceptorsPhysiological roles of aquaporin-4 in brainExpression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathiesThe Structure of the T190M Mutant of Murine α-Dystroglycan at High Resolution: Insight into the Molecular Basis of a Primary DystroglycanopathyAsparagine of z8 insert is critical for the affinity, conformation, and acetylcholine receptor-clustering activity of neural agrinCharacterization of the secreted proteome of rat hepatocytes cultured in collagen sandwiches.Duplication of the dystroglycan gene in most branches of teleost fish.A synthetic peptide corresponding to the 550-585 region of alpha-dystroglycan binds beta-dystroglycan as revealed by NMR spectroscopy.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.The process-inducing activity of transmembrane agrin requires follistatin-like domainsAmelioration of laminin-alpha2-deficient congenital muscular dystrophy by somatic gene transfer of miniagrin.Still more complexity in mammalian basement membranes.Design and screening of a glial cell-specific, cell penetrating peptide for therapeutic applications in multiple sclerosis.Basement membranes: cell scaffoldings and signaling platforms.Dystroglycan in the diagnosis of FSGS.Perlecan is recruited by dystroglycan to nodes of Ranvier and binds the clustering molecule gliomedin.Disruption of glomerular basement membrane charge through podocyte-specific mutation of agrin does not alter glomerular permselectivityLinker molecules between laminins and dystroglycan ameliorate laminin-alpha2-deficient muscular dystrophy at all disease stagesStructure-function analysis of endogenous lectin mind-the-gap in synaptogenesisAgrin can mediate acetylcholine receptor gene expression in muscle by aggregation of muscle-derived neuregulins.A PDZ-containing scaffold related to the dystrophin complex at the basolateral membrane of epithelial cells.Role of extracellular matrix proteins and their receptors in the development of the vertebrate neuromuscular junctionExtracellular matrix and matrix receptors in blood-brain barrier formation and stroke.Schwann cell myelination requires integration of laminin activities.Agrin mediates chondrocyte homeostasis and requires both LRP4 and α-dystroglycan to enhance cartilage formation in vitro and in vivoScaffold-forming and Adhesive Contributions of Synthetic Laminin-binding Proteins to Basement Membrane AssemblyDystroglycan receptor is involved in integrin activation in intestinal epitheliaThe synaptic CT carbohydrate modulates binding and expression of extracellular matrix proteins in skeletal muscle: Partial dependence on utrophin.Enhanced laminin binding by alpha-dystroglycan after enzymatic deglycosylation.A transcriptome-based assessment of the astrocytic dystrophin-associated complex in the developing human brain.Glomerular basement membrane heparan sulfate in health and disease: A regulator of local complement activation.The nature and biology of basement membranes.Anomalous dystroglycan in carcinoma cell lines.Mutation of a basic sequence in the laminin alpha2LG3 module leads to a lack of proteolytic processing and has different effects on beta1 integrin-mediated cell adhesion and alpha-dystroglycan binding.Recombinant domain IV of perlecan binds to nidogens, laminin-nidogen complex, fibronectin, fibulin-2 and heparin.Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins.
P2860
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P2860
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@ast
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@en
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@en-gb
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@nl
type
label
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@ast
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@en
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@en-gb
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@nl
prefLabel
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@ast
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@en
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@en-gb
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@nl
P2093
P356
P1476
Agrin is a high-affinity binding protein of dystroglycan in non-muscle tissue
@en
P2093
B Schumacher
M Gesemann
P304
P356
10.1074/JBC.273.1.600
P407
P577
1998-01-01T00:00:00Z