| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10797721 | Biochimica et Biophysica Acta (BBA) - Biomembranes | 2011 | 10 Pages |
Abstract
⺠Lipase activity of bacterial phospholipases. ⺠Combination of in-silico and in-vitro studies. ⺠α-toxin aspecifically hydrolyses a wide variety of phospholipids. ⺠This helps the bacterium to infect a greater variety of host tissues.
Keywords
Rac1N-domainPLCHLamarckian genetic algorithm31P-NMRDOPGDOPCMLVLGAdHPCP-groupRMSDGTPCHOLBSAdioleoylphosphatidylglycerolEF handTIM barrelAsparagineAspartic acidalaninebovine serum albuminsphingomyelinsphingomyelinaseglutamic acidisoleucinelarge unilamellar vesicleC-terminalTryptophaneTyrosineamino-terminal domainDockingdioleoylphosphatidylcholineRas-related C3 botulinum toxin substrate 1SerineCell membranephosphatidylinositolphosphatidylcholinephosphatidylglycerolphosphatidylethanolaminePhosphatidylserinePhospholipidZincLUVLysineroot mean square deviationhistidinePathogenicityMultilamellar vesicleProlineDeuterated chloroformcholesterolGlycineGuanosine triphosphate
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Authors
Patricia Urbina, M. Isabel Collado, Alicia Alonso, Félix M. Goñi, Marietta Flores-DÃaz, Alberto Alape-Girón, Jean-Marie Ruysschaert, Marc F. Lensink,