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Structure–function analyses of a pertussis-like toxin from pathogenic Escherichia coli reveal a distinct mechanism of inhibition of trimeric G-proteins

Pertussis-like toxins are secreted by several bacterial pathogens during infection. They belong to the AB(5) virulence factors, which bind to glycans on host cell membranes for internalization. Host cell recognition and internalization are mediated by toxin B subunits sharing a unique pentameric rin...

詳細記述

保存先:
書誌詳細
出版年:J Biol Chem
主要な著者: Littler, Dene R., Ang, Sheng Y., Moriel, Danilo G., Kocan, Martina, Kleifeld, Oded, Johnson, Matthew D., Tran, Mai T., Paton, Adrienne W., Paton, James C., Summers, Roger J., Schembri, Mark A., Rossjohn, Jamie, Beddoe, Travis
フォーマット: Artigo
言語:Inglês
出版事項: American Society for Biochemistry and Molecular Biology 2017
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC5592689/
https://ncbi.nlm.nih.gov/pubmed/28663369
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M117.796094
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