Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin
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- J Coburn
- Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.
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- S T Dillon
- Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.
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- B H Iglewski
- Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.
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- D M Gill
- Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.
書誌事項
- 公開日
- 1989-03
- 権利情報
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- https://journals.asm.org/non-commercial-tdm-license
- DOI
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- 10.1128/iai.57.3.996-998.1989
- 公開者
- American Society for Microbiology
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説明
<jats:p>Exoenzyme S, which had been thought to be unselective, catalyzes the ADP-ribosylation of only a subset of cellular proteins. The intermediate filament protein vimentin is one of the more abundant substrates. Disassembled vimentin, and proteolytic fragments of vimentin that cannot form filaments, is more readily ADP-ribosylated than is filamentous vimentin.</jats:p>
収録刊行物
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- Infection and Immunity
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Infection and Immunity 57 (3), 996-998, 1989-03
American Society for Microbiology