| pubmed-article:8641271 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C0084710 | lld:lifeskim |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C1441547 | lld:lifeskim |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C1283195 | lld:lifeskim |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C0449830 | lld:lifeskim |
| pubmed-article:8641271 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8641271 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:8641271 | pubmed:dateCreated | 1996-7-18 | lld:pubmed |
| pubmed-article:8641271 | pubmed:abstractText | The neuronal cell adhesion molecule axonin-1 is composed of six immunoglobulin and four fibronectin type III domains. Axonin-1 promotes neurite outgrowth, when presented as a substratum for neurons in vitro, via a neuronal receptor that has been identified as the neuron-glia cell adhesion molecule, NgCAM, based on the blocking effect of polyclonal antibodies directed to NgCAM. Here we report the identification of axonin-1 domains involved in NgCAM binding. NgCAM-conjugated microspheres were tested for binding to COS cells expressing domain deletion mutants of axonin-1. In addition, monoclonal antibodies directed to axonin-1 were assessed for their ability to block the axonin-1-NgCAM interaction, and their epitopes were mapped using the domain deletion mutants. The results suggest that the four amino-terminal immunoglobulin domains of axonin-1 form a domain conglomerate which is necessary and sufficient for NgCAM binding. Surprisingly, NgCAM binding to membrane-bound axonin-1 was increased strongly by deletion of the fifth or sixth immunoglobulin domains of axonin-1. Based on these results and on negative staining electron microscopy, we propose a horseshoe-shaped domain arrangement of axonin-1 that obscures the NgCAM binding site. Neurite outgrowth studies with truncated forms of axonin-1 show that axonin-1 is a neurite outgrowth-promoting substratum in the absence of the NgCAM binding site. | lld:pubmed |
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| pubmed-article:8641271 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8641271 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8641271 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8641271 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8641271 | pubmed:month | May | lld:pubmed |
| pubmed-article:8641271 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8641271 | pubmed:author | pubmed-author:GrossHH | lld:pubmed |
| pubmed-article:8641271 | pubmed:author | pubmed-author:KunzBB | lld:pubmed |
| pubmed-article:8641271 | pubmed:author | pubmed-author:SondereggerPP | lld:pubmed |
| pubmed-article:8641271 | pubmed:author | pubmed-author:BergerPP | lld:pubmed |
| pubmed-article:8641271 | pubmed:author | pubmed-author:RadevGG | lld:pubmed |
| pubmed-article:8641271 | pubmed:author | pubmed-author:GigerR JRJ | lld:pubmed |
| pubmed-article:8641271 | pubmed:author | pubmed-author:TittmannPP | lld:pubmed |
| pubmed-article:8641271 | pubmed:author | pubmed-author:LierheimerRR | lld:pubmed |
| pubmed-article:8641271 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8641271 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8641271 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:8641271 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8641271 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8641271 | pubmed:pagination | 2056-68 | lld:pubmed |
| pubmed-article:8641271 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:8641271 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8641271 | pubmed:articleTitle | Implications for the domain arrangement of axonin-1 derived from the mapping of its NgCAM binding site. | lld:pubmed |
| pubmed-article:8641271 | pubmed:affiliation | Institute of Biochemistry, University of Zurich, Switzerland. | lld:pubmed |
| pubmed-article:8641271 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8641271 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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