| pubmed-article:9751164 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9751164 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9751164 | pubmed:dateCreated | 1998-10-14 | lld:pubmed |
| pubmed-article:9751164 | pubmed:abstractText | Neurexins are neuronal cell-surface proteins with up to thousands of isoforms. These isoforms are generated by alternative splicing of transcripts from six promoters in three genes. The structure of neurexins resembles cell-surface receptors with a modular architecture suggestive of a sequential assembly during evolution. Neurexins probably perform multiple functions in the brain. They participate in intercellular junctions in which beta-neurexins tightly bind to a second class of neuronal cell-surface receptors called neuroligins. Intracellularly, the neurexin/neuroligin junction is bound by CASK on the neurexin side and PSD95 on the neuroligin side. CASK and PSD95 are homologous membrane-associated guanylate kinases that bind to the neurexin/neuroligin junction via PDZ domains, creating an asymmetric junction (neurexin/neuroligin) with similar intracellular binding partners. In addition to a function as cell-adhesion molecules, neurexins may also serve as a signalling receptor, because a class of ligands for alpha-neurexins called neurexophilins is similar to peptide hormones. Finally, at least one neurexin isoform, neurexin Ialpha, represents a high-affinity receptor for alpha-latrotoxin, which is a potent excitatory neurotoxin. Thus, neurexins constitute a large family of neuronal receptors that may be involved in multiple interactive functions between neurons. | lld:pubmed |
| pubmed-article:9751164 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9751164 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9751164 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9751164 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9751164 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9751164 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9751164 | pubmed:issn | 0022-3042 | lld:pubmed |
| pubmed-article:9751164 | pubmed:author | pubmed-author:MisslerMM | lld:pubmed |
| pubmed-article:9751164 | pubmed:author | pubmed-author:SüdhofT CTC | lld:pubmed |
| pubmed-article:9751164 | pubmed:author | pubmed-author:Fernandez-Cha... | lld:pubmed |
| pubmed-article:9751164 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9751164 | pubmed:volume | 71 | lld:pubmed |
| pubmed-article:9751164 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9751164 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9751164 | pubmed:pagination | 1339-47 | lld:pubmed |
| pubmed-article:9751164 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9751164 | pubmed:meshHeading | pubmed-meshheading:9751164-... | lld:pubmed |
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| pubmed-article:9751164 | pubmed:meshHeading | pubmed-meshheading:9751164-... | lld:pubmed |
| pubmed-article:9751164 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9751164 | pubmed:articleTitle | The making of neurexins. | lld:pubmed |
| pubmed-article:9751164 | pubmed:affiliation | Department of Molecular Genetics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235, USA. | lld:pubmed |
| pubmed-article:9751164 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9751164 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9751164 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9751164 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:9751164 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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