Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/116302
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dc.titleDo we know the complete sequence of metalloproteinase and nonenzymatic platelet aggregation inhibitor (disintegrin) precursor proteins?
dc.contributor.authorKini, R.M.
dc.date.accessioned2014-12-12T07:48:12Z
dc.date.available2014-12-12T07:48:12Z
dc.date.issued1995-09
dc.identifier.citationKini, R.M. (1995-09). Do we know the complete sequence of metalloproteinase and nonenzymatic platelet aggregation inhibitor (disintegrin) precursor proteins?. Toxicon 33 (9) : 1151-1160. ScholarBank@NUS Repository.
dc.identifier.issn00410101
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/116302
dc.description.abstractRecent 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. © 1995.
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOSCIENCE CENTRE
dc.description.sourcetitleToxicon
dc.description.volume33
dc.description.issue9
dc.description.page1151-1160
dc.description.codenTOXIA
dc.identifier.isiutNOT_IN_WOS
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