Agrin and the organization of the neuromuscular junction

Agrin is a component of the synaptic extracellular matrix and may regulate the organization of acetylcholine receptors and other synaptic molecules in both synapse regeneration and development. Analyses of cDNAs encoding agrin define a number of structural domains, including regions of homology to l...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Current opinion in neurobiology 1992-02, Vol.2 (1), p.88-93
Hauptverfasser: Rupp, Fabio, Hoch, Werner, Campanelli, James T., Kreiner, Thane, Scheller, Richard H.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 93
container_issue 1
container_start_page 88
container_title Current opinion in neurobiology
container_volume 2
creator Rupp, Fabio
Hoch, Werner
Campanelli, James T.
Kreiner, Thane
Scheller, Richard H.
description Agrin is a component of the synaptic extracellular matrix and may regulate the organization of acetylcholine receptors and other synaptic molecules in both synapse regeneration and development. Analyses of cDNAs encoding agrin define a number of structural domains, including regions of homology to laminin, Kazal protease inhibitors, and epidermal growth factor repeats.
doi_str_mv 10.1016/0959-4388(92)90168-K
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_73082419</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>095943889290168K</els_id><sourcerecordid>73082419</sourcerecordid><originalsourceid>FETCH-LOGICAL-c349k-8859696e7d51df601e477786ce3a331bbe2910d58bf9a9839d48b2a3360158b33</originalsourceid><addsrcrecordid>eNqFkE1Lw0AQhhdRaq3-A4WcRA_R_Ug2uxehFL9owYuel83upG5Nk7qbCPrrTZqiNz0NvO8zM_AgdErwFcGEX2OZyjhhQlxIeim7RMTzPTQmImMxF4Luo_EPcoiOQlhhjDkTbIRGhFFKsRwjMV16V0W6slHzClHtl7pyX7pxdRXVxTaroPX1ug2mLbWPVm1l-vYYHRS6DHCymxP0cnf7PHuIF0_3j7PpIjYskW-xEKnkkkNmU2ILjgkkWZYJboBpxkieA5UE21TkhdRSMGkTkdOu6tAuZGyCzoe7G1-_txAatXbBQFnqCuo2qIxhQRMi_wUJp4RSgTswGUDj6xA8FGrj3Vr7T0Ww6s2qXpvqtSlJ1dasmndrZ7v7bb4G-7s0qOz6m6GHzsaHA6-CcVAZsM6DaZSt3d8PvgEl_YZg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16212280</pqid></control><display><type>article</type><title>Agrin and the organization of the neuromuscular junction</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Rupp, Fabio ; Hoch, Werner ; Campanelli, James T. ; Kreiner, Thane ; Scheller, Richard H.</creator><creatorcontrib>Rupp, Fabio ; Hoch, Werner ; Campanelli, James T. ; Kreiner, Thane ; Scheller, Richard H.</creatorcontrib><description>Agrin is a component of the synaptic extracellular matrix and may regulate the organization of acetylcholine receptors and other synaptic molecules in both synapse regeneration and development. Analyses of cDNAs encoding agrin define a number of structural domains, including regions of homology to laminin, Kazal protease inhibitors, and epidermal growth factor repeats.</description><identifier>ISSN: 0959-4388</identifier><identifier>EISSN: 1873-6882</identifier><identifier>DOI: 10.1016/0959-4388(92)90168-K</identifier><identifier>PMID: 1322209</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Agrin ; Animals ; Extracellular Matrix - physiology ; Humans ; Nerve Tissue Proteins - physiology ; Neuromuscular Junction - physiology ; Neuromuscular Junction - ultrastructure ; Receptors, Cholinergic - physiology</subject><ispartof>Current opinion in neurobiology, 1992-02, Vol.2 (1), p.88-93</ispartof><rights>1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c349k-8859696e7d51df601e477786ce3a331bbe2910d58bf9a9839d48b2a3360158b33</citedby><cites>FETCH-LOGICAL-c349k-8859696e7d51df601e477786ce3a331bbe2910d58bf9a9839d48b2a3360158b33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0959-4388(92)90168-K$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1322209$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rupp, Fabio</creatorcontrib><creatorcontrib>Hoch, Werner</creatorcontrib><creatorcontrib>Campanelli, James T.</creatorcontrib><creatorcontrib>Kreiner, Thane</creatorcontrib><creatorcontrib>Scheller, Richard H.</creatorcontrib><title>Agrin and the organization of the neuromuscular junction</title><title>Current opinion in neurobiology</title><addtitle>Curr Opin Neurobiol</addtitle><description>Agrin is a component of the synaptic extracellular matrix and may regulate the organization of acetylcholine receptors and other synaptic molecules in both synapse regeneration and development. Analyses of cDNAs encoding agrin define a number of structural domains, including regions of homology to laminin, Kazal protease inhibitors, and epidermal growth factor repeats.</description><subject>Agrin</subject><subject>Animals</subject><subject>Extracellular Matrix - physiology</subject><subject>Humans</subject><subject>Nerve Tissue Proteins - physiology</subject><subject>Neuromuscular Junction - physiology</subject><subject>Neuromuscular Junction - ultrastructure</subject><subject>Receptors, Cholinergic - physiology</subject><issn>0959-4388</issn><issn>1873-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1Lw0AQhhdRaq3-A4WcRA_R_Ug2uxehFL9owYuel83upG5Nk7qbCPrrTZqiNz0NvO8zM_AgdErwFcGEX2OZyjhhQlxIeim7RMTzPTQmImMxF4Luo_EPcoiOQlhhjDkTbIRGhFFKsRwjMV16V0W6slHzClHtl7pyX7pxdRXVxTaroPX1ug2mLbWPVm1l-vYYHRS6DHCymxP0cnf7PHuIF0_3j7PpIjYskW-xEKnkkkNmU2ILjgkkWZYJboBpxkieA5UE21TkhdRSMGkTkdOu6tAuZGyCzoe7G1-_txAatXbBQFnqCuo2qIxhQRMi_wUJp4RSgTswGUDj6xA8FGrj3Vr7T0Ww6s2qXpvqtSlJ1dasmndrZ7v7bb4G-7s0qOz6m6GHzsaHA6-CcVAZsM6DaZSt3d8PvgEl_YZg</recordid><startdate>199202</startdate><enddate>199202</enddate><creator>Rupp, Fabio</creator><creator>Hoch, Werner</creator><creator>Campanelli, James T.</creator><creator>Kreiner, Thane</creator><creator>Scheller, Richard H.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7X8</scope></search><sort><creationdate>199202</creationdate><title>Agrin and the organization of the neuromuscular junction</title><author>Rupp, Fabio ; Hoch, Werner ; Campanelli, James T. ; Kreiner, Thane ; Scheller, Richard H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c349k-8859696e7d51df601e477786ce3a331bbe2910d58bf9a9839d48b2a3360158b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Agrin</topic><topic>Animals</topic><topic>Extracellular Matrix - physiology</topic><topic>Humans</topic><topic>Nerve Tissue Proteins - physiology</topic><topic>Neuromuscular Junction - physiology</topic><topic>Neuromuscular Junction - ultrastructure</topic><topic>Receptors, Cholinergic - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rupp, Fabio</creatorcontrib><creatorcontrib>Hoch, Werner</creatorcontrib><creatorcontrib>Campanelli, James T.</creatorcontrib><creatorcontrib>Kreiner, Thane</creatorcontrib><creatorcontrib>Scheller, Richard H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Current opinion in neurobiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rupp, Fabio</au><au>Hoch, Werner</au><au>Campanelli, James T.</au><au>Kreiner, Thane</au><au>Scheller, Richard H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Agrin and the organization of the neuromuscular junction</atitle><jtitle>Current opinion in neurobiology</jtitle><addtitle>Curr Opin Neurobiol</addtitle><date>1992-02</date><risdate>1992</risdate><volume>2</volume><issue>1</issue><spage>88</spage><epage>93</epage><pages>88-93</pages><issn>0959-4388</issn><eissn>1873-6882</eissn><abstract>Agrin is a component of the synaptic extracellular matrix and may regulate the organization of acetylcholine receptors and other synaptic molecules in both synapse regeneration and development. Analyses of cDNAs encoding agrin define a number of structural domains, including regions of homology to laminin, Kazal protease inhibitors, and epidermal growth factor repeats.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>1322209</pmid><doi>10.1016/0959-4388(92)90168-K</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0959-4388
ispartof Current opinion in neurobiology, 1992-02, Vol.2 (1), p.88-93
issn 0959-4388
1873-6882
language eng
recordid cdi_proquest_miscellaneous_73082419
source MEDLINE; Access via ScienceDirect (Elsevier)
subjects Agrin
Animals
Extracellular Matrix - physiology
Humans
Nerve Tissue Proteins - physiology
Neuromuscular Junction - physiology
Neuromuscular Junction - ultrastructure
Receptors, Cholinergic - physiology
title Agrin and the organization of the neuromuscular junction
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-14T03%3A19%3A54IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Agrin%20and%20the%20organization%20of%20the%20neuromuscular%20junction&rft.jtitle=Current%20opinion%20in%20neurobiology&rft.au=Rupp,%20Fabio&rft.date=1992-02&rft.volume=2&rft.issue=1&rft.spage=88&rft.epage=93&rft.pages=88-93&rft.issn=0959-4388&rft.eissn=1873-6882&rft_id=info:doi/10.1016/0959-4388(92)90168-K&rft_dat=%3Cproquest_cross%3E73082419%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=16212280&rft_id=info:pmid/1322209&rft_els_id=095943889290168K&rfr_iscdi=true