Organization of myelinated axons by Caspr and Caspr2 requires the cytoskeletal adapter protein 4.1B - sprookjes - yvandenbroek - TriplyDB

Organization of myelinated axons by Caspr and Caspr2 requires the cytoskeletal adapter protein 4.1B

Organization of myelinated axons by Caspr and Caspr2 requires the cytoskeletal adapter protein 4.1B

http://www.wikidata.org/entity/Q33720640

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Protein 4.1B contributes to the organization of peripheral myelinated axons Candidate autism gene screen identifies critical role for cell-adhesion molecule CASPR2 in dendritic arborization and spine development Mechanisms of sodium channel clustering and its influence on axonal impulse conduction Neuro-glial interactions at the nodes of Ranvier: implication in health and diseases Connecting the CNTNAP2 Networks with Neurodevelopmental Disorders Whirlin, a cytoskeletal scaffolding protein, stabilizes the paranodal region and axonal cytoskeleton in myelinated axons A glial signal consisting of gliomedin and NrCAM clusters axonal Na+ channels during the formation of nodes of Ranvier Caspr and caspr2 are required for both radial and longitudinal organization of myelinated axons.Function and mechanism of axonal targeting of voltage-sensitive potassium channels.Electron tomography of paranodal septate-like junctions and the associated axonal and glial cytoskeletons in the central nervous system.Analysis of protein dynamics within the septate junction reveals a highly stable core protein complex that does not include the basolateral polarity protein Discs large Axonal ensheathment and intercellular barrier formation in Drosophila.Organization and maintenance of molecular domains in myelinated axons Characterization of the axon initial segment (AIS) of motor neurons and identification of a para-AIS and a juxtapara-AIS, organized by protein 4.1B.Clustered K+ channel complexes in axons Composition, assembly, and maintenance of excitable membrane domains in myelinated axons.Glial ankyrins facilitate paranodal axoglial junction assembly The cytoskeletal adaptor protein band 4.1B is required for the maintenance of paranodal axoglial septate junctions in myelinated axons.The cytoskeletal adapter protein 4.1G organizes the internodes in peripheral myelinated nerves.Paranodal reorganization results in the depletion of transverse bands in the aged central nervous system.Deep intron elements mediate nested splicing events at consecutive AG dinucleotides to regulate alternative 3' splice site choice in vertebrate 4.1 genes.Band 4.1 proteins regulate integrin-dependent cell spreading The 4.1B cytoskeletal protein regulates the domain organization and sheath thickness of myelinated axons.Kainate receptor post-translational modifications differentially regulate association with 4.1N to control activity-dependent receptor endocytosis Axonal spectrins: all-purpose fences Axons and myelinating glia: An intimate contact.Pathogenic and physiological autoantibodies in the central nervous system.The making of a node: a co-production of neurons and glia.The node of Ranvier in CNS pathology Tumor suppressor role of protein 4.1B/DAL-1.Subcellular patterning: axonal domains with specialized structure and function.The Nodes of Ranvier: Molecular Assembly and Maintenance.Axonal domain disorganization in Caspr1 and Caspr2 mutant myelinated axons affects neuromuscular junction integrity, leading to muscle atrophy.Assembly of CNS Nodes of Ranvier in Myelinated Nerves Is Promoted by the Axon Cytoskeleton.DAL-1 attenuates epithelial-to mesenchymal transition in lung cancer.Axonal transport deficits in multiple sclerosis: spiraling into the abyss.The Axonal Cytoskeleton and the Assembly of Nodes of Ranvier.Intragenic CNTNAP2 Deletions: A Bridge Too Far?4.1G promotes arborization and tight junction formation of oligodendrocyte cell line OLN-93.Contactin-associated protein 1 (Caspr1) regulates the traffic and synaptic content of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors.

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P2860

Organization of myelinated axons by Caspr and Caspr2 requires the cytoskeletal adapter protein 4.1B

http://www.wikidata.org/entity/Q33720640

description

2010 nî lūn-bûn

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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Organization of myelinated axo ...... oskeletal adapter protein 4.1B

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Organization of myelinated axo ...... oskeletal adapter protein 4.1B

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Organization of myelinated axo ...... oskeletal adapter protein 4.1B

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Organization of myelinated axo ...... oskeletal adapter protein 4.1B

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Organization of myelinated axo ...... oskeletal adapter protein 4.1B

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Organization of myelinated axo ...... oskeletal adapter protein 4.1B

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JNEUROSCI.5225-09.2010

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Journal of Neuroscience

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Organization of myelinated axo ...... oskeletal adapter protein 4.1B

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Ido Horresh

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

Joseph L Kissil

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Vered Bar

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P2860

Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels

The local differentiation of myelinated axons at nodes of Ranvier

Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues

Direct association of TSLC1 and DAL-1, two distinct tumor suppressor proteins in lung cancer

Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions.

Juxtaparanodal clustering of Shaker-like K+ channels in myelinated axons depends on Caspr2 and TAG-1

Caspr regulates the processing of contactin and inhibits its binding to neurofascin

Association of TAG-1 with Caspr2 is essential for the molecular organization of juxtaparanodal regions of myelinated fibers

Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction

Protein 4.1B associates with both Caspr/paranodin and Caspr2 at paranodes and juxtaparanodes of myelinated fibres

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10.1523/JNEUROSCI.5225-09.2010

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7

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