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- W2010635265 abstract "Abstract Phospholipases are enzymes that hydrolyze different phospholipids within biomembranes to produce messenger molecules for the cellular signal transduction. Their activity is highly dependent on the lipid membrane structure as described in this review. In particular, the secretory phospholipase A 2 (sPLA 2 ) is activated through liquid–liquid phase boundaries and membrane curvature on a nanometer-length scale. The local enrichment of lipid activators within membrane domains has been shown to efficiently enhance the activity of sPLA 2 as well as of bacterial phospholipase D (PLD). Thus, phospholipase activity has been correlated to the underlying lipid phase diagrams. This allows the use of phospholipases as molecular probes to unravel model membrane structure with very high resolution." @default.
- W2010635265 created "2016-06-24" @default.
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- W2010635265 date "2008-02-01" @default.
- W2010635265 modified "2023-09-23" @default.
- W2010635265 title "Phospholipases to recognize model membrane structures on a molecular length scale" @default.
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- W2010635265 doi "https://doi.org/10.1016/j.cocis.2007.08.009" @default.
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