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- W2078010265 endingPage "784" @default.
- W2078010265 startingPage "771" @default.
- W2078010265 abstract "The cell envelope of Gram-negative bacteria is a complex macromolecular structure that is essential for their viability. Little is known on how the proteins which are secreted to the envelope fold into their unique three-dimensional structure. Several folding factors, including chaperones and protein folding catalysts involved in disulfide bond formation, have been identified in the periplasm. The characterization of these proteins has advanced our understanding of envelope biogenesis, although many fundamental questions remain unanswered. In particular, we still do not know how beta-barrel proteins are transported through the periplasm and inserted into the outer membrane. Here, we discuss the recent discoveries that have shed new light on the mechanisms that ensure the correct folding of envelope proteins. We have paid particular attention to the significant contribution of proteomic studies." @default.
- W2078010265 created "2016-06-24" @default.
- W2078010265 creator A5040498940 @default.
- W2078010265 creator A5084609492 @default.
- W2078010265 creator A5085210292 @default.
- W2078010265 date "2010-02-01" @default.
- W2078010265 modified "2023-10-16" @default.
- W2078010265 title "Contribution of proteomics toward solving the fascinating mysteries of the biogenesis of the envelope of Escherichia coli" @default.
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