Matches in SemOpenAlex for { <https://semopenalex.org/work/W2981596073> ?p ?o ?g. }
- W2981596073 abstract "Trimeric autotransporter adhesins (TAAs) are specialized bacterial outer membrane proteins consisting of three identical subunits. TAAs contain large extracellular domains that trimerize and promote virulence, but the mechanism by which they are secreted is poorly understood. We found that the extracellular domains of a native TAA were secreted rapidly but that disordered and artificially folded polypeptides fused to native passenger domains were secreted in a slow, sequential fashion. Our results strongly suggest that the efficient secretion of native extracellular domains is driven by their trimerization following export but that alternative energy sources can be harnessed to secrete nonnative polypeptides. Furthermore, we obtained evidence that TAA extracellular domains are secreted before the assembly of the linked membrane spanning domain is completed." @default.
- W2981596073 created "2019-11-01" @default.
- W2981596073 creator A5015142148 @default.
- W2981596073 creator A5062522223 @default.
- W2981596073 date "2019-10-29" @default.
- W2981596073 modified "2023-10-18" @default.
- W2981596073 title "Sequential Translocation of Polypeptides across the Bacterial Outer Membrane through the Trimeric Autotransporter Pathway" @default.
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- W2981596073 doi "https://doi.org/10.1128/mbio.01973-19" @default.
- W2981596073 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6805991" @default.
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