Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1988-5-4
pubmed:databankReference
pubmed:abstractText
Leukosialin is one of the major glycoproteins of thymocytes and T lymphocytes and is notable for a very high content of O-linked carbohydrate structures. The full protein sequence for rat leukosialin as translated from cDNA clones is now reported. The molecule contains 371 amino acids with 224 residues outside the cell, one transmembrane sequence and 124 cytoplasmic residues. Data from the peptide sequence and carbohydrate composition suggest that one in three of the extracellular amino acids may be O-glycosylated with no N-linked glycosylation sites. The cDNA sequence contained a CpG rich region in the 3' coding sequence and a large 3' non-coding region which included tandem repeats of the sequence GGAT.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-1251186, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-192730, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-2440674, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-2943740, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-2943741, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-2956090, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-303545, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-310389, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3104900, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3115291, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3158393, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3159821, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3511446, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3514613, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3572301, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3600778, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3656447, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3711098, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3714490, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-374095, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3779101, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3849540, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3873337, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3932064, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-3940888, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-518835, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6310323, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6547160, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6571704, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6575390, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6609831, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6773668, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6965465, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6970130, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6970337, http://linkedlifedata.com/resource/pubmed/commentcorrection/2965006-6980823
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4029-34
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
The sequence of rat leukosialin (W3/13 antigen) reveals a molecule with O-linked glycosylation of one third of its extracellular amino acids.
pubmed:affiliation
MRC Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't