Linked Life Data

8585085

Source:http://linkedlifedata.com/resource/pubmed/id/8585085

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1996-3-20
pubmed:abstractText
Recent evidence indicates that metalloproteinases and disintegrins, nonenzymatic inhibitors of platelet aggregation, are derived by proteolysis from common precursors. Although proteins and polypeptides with various domain structures have been identified, proteins containing proprotein domains or the complete mature precursors have not yet been isolated. This prompted a closer examination of the putative start codon, signal peptide and the segment upstream of these regions. A critical evaluation of sequence information of these precursors indicates that the putative signal peptide identified in these precursors may be an internal hydrophobic segment within the precursor. There is also evidence to indicate that C-type lectin-related proteins are also derived from these precursors. Thus the available sequence data of the precursors appear to be incomplete.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1151-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Do we know the complete sequence of metalloproteinase and nonenzymatic platelet aggregation inhibitor (disintegrin) precursor proteins?
pubmed:affiliation
Bioscience Centre, Faculty of Science, National University of Singapore, Singapore.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't