{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,11,18]],"date-time":"2023-11-18T15:07:07Z","timestamp":1700320027315},"reference-count":33,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2001,10,25]],"date-time":"2001-10-25T00:00:00Z","timestamp":1003968000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Spinal Cord Research Foundation of the Paralyzed Veterans Association"},{"name":"NIH"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Neuroscience Research"],"published-print":{"date-parts":[[2001,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The neural cell adhesion molecule L1 contains immunoglobulin\u2010like (Ig) domains in its extracellular region that mediate homophilic binding, neurite outgrowth and other activities relevant to CNS development. To correlate conformations of these domains to biological function, several L1\u2010Fc fusion proteins whose bioactivities were previously characterized were analyzed by rotary shadowing electron microscopy. We found that bioactive L1\u2010Fcs containing Ig domains 1\u20134 or 1\u20136 exhibited extended, branched structures. In contrast, inactive L1\u2010Fcs containing only the first two or three Ig domains assumed compact shapes that suggested interactions between the L1 arms of these proteins. Analysis of an untagged L1 fragment composed of Ig domains 1\u20103 demonstrated a mixture of monomeric and dimeric forms. Surprisingly, these dimers were stabilized by intermolecular disulfide bonds. Finally, cell surface L1\u2010GFP fusion proteins containing only the first two or three Ig domains in the extracellular region also engaged in disulfide\u2010mediated dimerization. These results suggest a novel mechanism by which mutations in L1 could interfere with its biological functioning. 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Res. 66:347\u2013355, 2001. \u00a9 2001 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/jnr.1227","type":"journal-article","created":{"date-parts":[[2004,10,28]],"date-time":"2004-10-28T11:58:47Z","timestamp":1098964727000},"page":"347-355","source":"Crossref","is-referenced-by-count":3,"title":["Disulfide\u2010mediated dimerization of L1 Ig domains"],"prefix":"10.1002","volume":"66","author":[{"given":"Jeffrey","family":"Haspel","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gregor","family":"Sch\u00fcrmann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jeffrey","family":"Jacob","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Harold 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