pubmed-article:1769655 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:1769655 | lifeskim:mentions | umls-concept:C0026383 | lld:lifeskim |
pubmed-article:1769655 | lifeskim:mentions | umls-concept:C0950625 | lld:lifeskim |
pubmed-article:1769655 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:1769655 | lifeskim:mentions | umls-concept:C0039593 | lld:lifeskim |
pubmed-article:1769655 | lifeskim:mentions | umls-concept:C1416769 | lld:lifeskim |
pubmed-article:1769655 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
pubmed-article:1769655 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:1769655 | pubmed:dateCreated | 1992-2-21 | lld:pubmed |
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pubmed-article:1769655 | pubmed:abstractText | The rodent, avian, and insect L1-like cell adhesion molecules are members of the immunoglobulin superfamily that have been implicated in axon growth. We have isolated an L1-like molecule from human brain and found that it also supports neurite growth in vitro. We have also cloned and sequenced the entire coding region of human L1CAM and found that it shows a very high degree of homology to mouse L1cam, with 92% identity at the amino acid level. This similarity suggests that L1CAM is an important molecule in normal human nervous system development and nerve regeneration. Overall, there is substantially less homology to chick Ng-CAM; they are 40% identical at the amino acid level but many regions are highly conserved. Comparison of the sequences from human, mouse, chick, and Drosophila indicates that the L1 immunoglobulin domain 2 and fibronectin type III domain 2 are strongly conserved and thus are likely functionally important. | lld:pubmed |
pubmed-article:1769655 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1769655 | pubmed:language | eng | lld:pubmed |
pubmed-article:1769655 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1769655 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1769655 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1769655 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1769655 | pubmed:month | Oct | lld:pubmed |
pubmed-article:1769655 | pubmed:issn | 0888-7543 | lld:pubmed |
pubmed-article:1769655 | pubmed:author | pubmed-author:LemmonVV | lld:pubmed |
pubmed-article:1769655 | pubmed:author | pubmed-author:HlavinM LML | lld:pubmed |
pubmed-article:1769655 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1769655 | pubmed:volume | 11 | lld:pubmed |
pubmed-article:1769655 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1769655 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1769655 | pubmed:pagination | 416-23 | lld:pubmed |
pubmed-article:1769655 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:1769655 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1769655 | pubmed:articleTitle | Molecular structure and functional testing of human L1CAM: an interspecies comparison. | lld:pubmed |
pubmed-article:1769655 | pubmed:affiliation | Department of Neurosurgery, Case Western Reserve University, Cleveland, Ohio 44106. | lld:pubmed |
pubmed-article:1769655 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1769655 | pubmed:publicationType | In Vitro | lld:pubmed |
pubmed-article:1769655 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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