Title : Cellular aspartyl proteases promote the unconventional secretion of biologically active HIV-1 matrix protein p17.

Pub. Date : 2016 Dec 1

PMID : 27905556






2 Functional Relationships(s)
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1 Here we show that in Gag-expressing cells, secretion of biologically active p17 takes place at the plasma membrane and occurs following its interaction with phosphatidylinositol-(4,5)-bisphosphate and its subsequent cleavage from the precursor Gag (Pr55Gag) operated by cellular aspartyl proteases. Glycosaminoglycans family with sequence similarity 72 member B Homo sapiens
2 Here we show that in Gag-expressing cells, secretion of biologically active p17 takes place at the plasma membrane and occurs following its interaction with phosphatidylinositol-(4,5)-bisphosphate and its subsequent cleavage from the precursor Gag (Pr55Gag) operated by cellular aspartyl proteases. Glycosaminoglycans family with sequence similarity 72 member B Homo sapiens