Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-9-4
pubmed:databankReference
pubmed:abstractText
Members of the L1 family of neural cell adhesion molecules consist of multiple extracellular immunoglobulin and fibronectin type III domains that mediate the adhesive properties of this group of transmembrane proteins. In vertebrate genomes, these protein domains are separated by introns, and it has been suggested that L1-type genes might have been subject to exon-shuffling events during evolution. However, comparison of the human L1-CAM and the chicken neurofascin gene with the genomic structure of their Drosophila homologue, neuroglian, indicates that no major rearrangement of protein domains has taken place subsequent to the split of the arthropod and chordate phyla. The Drosophila neuroglian gene appears to have lost most of the introns that have been conserved in the human L1-CAM and the chicken neurofascin gene. Nevertheless, exon shuffling or the generation of new exons by mutational changes might have been responsible for the generation of additional, alternatively spliced exons in L1-type genes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, Neuronal, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Leukocyte L1 Antigen Complex, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/NFASC protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Growth Factors, http://linkedlifedata.com/resource/pubmed/chemical/Neural Cell Adhesion Molecules, http://linkedlifedata.com/resource/pubmed/chemical/Nfasc protein, Gallus gallus, http://linkedlifedata.com/resource/pubmed/chemical/Nrg protein, Drosophila
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
215
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-55
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9666073-Animals, pubmed-meshheading:9666073-Arthropods, pubmed-meshheading:9666073-Base Sequence, pubmed-meshheading:9666073-Cell Adhesion Molecules, pubmed-meshheading:9666073-Cell Adhesion Molecules, Neuronal, pubmed-meshheading:9666073-Chickens, pubmed-meshheading:9666073-Chordata, Nonvertebrate, pubmed-meshheading:9666073-DNA, pubmed-meshheading:9666073-Drosophila, pubmed-meshheading:9666073-Drosophila Proteins, pubmed-meshheading:9666073-Evolution, Molecular, pubmed-meshheading:9666073-Exons, pubmed-meshheading:9666073-Genes, Insect, pubmed-meshheading:9666073-Humans, pubmed-meshheading:9666073-Introns, pubmed-meshheading:9666073-Leukocyte L1 Antigen Complex, pubmed-meshheading:9666073-Membrane Glycoproteins, pubmed-meshheading:9666073-Molecular Sequence Data, pubmed-meshheading:9666073-Nerve Growth Factors, pubmed-meshheading:9666073-Neural Cell Adhesion Molecules, pubmed-meshheading:9666073-Sequence Analysis, DNA, pubmed-meshheading:9666073-Sequence Homology, pubmed-meshheading:9666073-Transcription, Genetic, pubmed-meshheading:9666073-Vertebrates
pubmed:year
1998
pubmed:articleTitle
The analysis of genomic structures in the L1 family of cell adhesion molecules provides no evidence for exon shuffling events after the separation of arthropod and chordate lineages.
pubmed:affiliation
University of Michigan, Department of Anatomy, Cell Biology, Ann Arbor, MI 48109-0616, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.