sub:provenance { beldoc:dce:description "Approximately 61,000 statements." ; dce:rights "Copyright (c) 2011-2012, Selventa. All rights reserved." ; dce:title "BEL Framework Large Corpus Document" ; pav:authoredBysub:_6 ; pav:version "1.4" . sub:_5prov:value "Site-directed mutagenesis, electron microscopy, and X-ray crystallography were used to probe the structural basis of annexin IV-induced membrane aggregation and the inhibition of this property by protein kinase C phosphorylation. Site-directed mutants that either mimic (Thr6Asp, T6D) or prevent (Thr6Ala, T6A) phosphorylation of threonine 6 were produced for these studies and compared with wild-type annexin IV. In vitro assays showed that unmodified wild-type annexin IV and the T6A mutant, but not PKC-phosphorylated wild-type or the T6D mutant, promote vesicle aggregation. " ; prov:wasQuotedFrompubmed:11300800 . sub:_6rdfs:label "Selventa" . sub:assertionprov:hadPrimarySourcepubmed:11300800 ; prov:wasDerivedFrombeldoc: , sub:_5 . }