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- W2004406780 endingPage "330" @default.
- W2004406780 startingPage "311" @default.
- W2004406780 abstract "SUMMARY Proteolytic cleavage of proteins that are permanently or transiently associated with the cytoplasmic membrane is crucially important for a wide range of essential processes in bacteria. This applies in particular to the secretion of proteins and to membrane protein quality control. Major progress has been made in elucidating the structure-function relationships of many of the responsible membrane proteases, including signal peptidases, signal peptide hydrolases, FtsH, the rhomboid protease GlpG, and the site 1 protease DegS. These enzymes employ very different mechanisms to cleave substrates at the cytoplasmic and extracytoplasmic membrane surfaces or within the plane of the membrane. This review highlights the different ways that bacterial membrane proteases degrade their substrates, with special emphasis on catalytic mechanisms and substrate delivery to the respective active sites." @default.
- W2004406780 created "2016-06-24" @default.
- W2004406780 creator A5049078993 @default.
- W2004406780 creator A5053610737 @default.
- W2004406780 creator A5070787254 @default.
- W2004406780 date "2012-06-01" @default.
- W2004406780 modified "2023-10-16" @default.
- W2004406780 title "Membrane Proteases in the Bacterial Protein Secretion and Quality Control Pathway" @default.
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