Linked Life Data

7744365

Source:http://linkedlifedata.com/resource/pubmed/id/7744365

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-6-9
pubmed:abstractText
We have isolated peptides bound to HLA-DR4, DR53 molecules obtained from HLA homozygous cell line cells, EBV-Wa (DRB1*0405, DRB4*0101), and determined amino acid sequences of the peptides. Amino acid sequences of 19 peptides were obtained and identified as peptide fragments of known proteins. Of those, macrophage migration inhibitory factor (MIF), beta 2 microglobulin (beta 2m), pyruvate kinase M2 (PKM2) and cathepsin C are considered to be endogenously derived, while transferrin and apolipoprotein B-100 are exogenous proteins. Peptides corresponding to each protein have a shared sequence with amino terminal or carboxy terminal protrusions. Based on the core sequences, putative DR4, DR53-binding motifs were suggested as Y----T/V--D or Y----T--D.
pubmed:language
jpn
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0367-6102
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
175-81
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
[Analysis of naturally processed peptides bound to HLA-DR4, DR53 (DRB1*0405, DRB4*0101)].
pubmed:affiliation
Second Department of Pathology, Asahikawa Medical College, Japan.
pubmed:publicationType
Journal Article, English Abstract