Cargando…
The Acetyltransferase Activity of the Bacterial Toxin YopJ of Yersinia Is Activated by Eukaryotic Host Cell Inositol Hexakisphosphate
Plague, one of the most devastating diseases in human history, is caused by the bacterium Yersinia pestis. The bacteria use a syringe-like macromolecular assembly to secrete various toxins directly into the host cells they infect. One such Yersinia outer protein, YopJ, performs the task of dampening...
Autores principales: | Mittal, Rohit, Peak-Chew, Sew Yeu, Sade, Robert S., Vallis, Yvonne, McMahon, Harvey T. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2888404/ https://www.ncbi.nlm.nih.gov/pubmed/20430892 http://dx.doi.org/10.1074/jbc.M110.126581 |
Ejemplares similares
-
Structural Requirements for Yersinia YopJ Inhibition of MAP Kinase Pathways
por: Hao, Yi-Heng, et al.
Publicado: (2008) -
Heightened Virulence of Yersinia Is Associated with Decreased Function of the YopJ Protein
por: Mares, Chris A., et al.
Publicado: (2021) -
Secondary-structure switch regulates the substrate binding of a YopJ family acetyltransferase
por: Xia, Yao, et al.
Publicado: (2021) -
Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-κB activation
por: Zhou, Honglin, et al.
Publicado: (2005) -
Differential Distribution, Clustering, and Lateral Diffusion of Subtypes of the Inositol 1,4,5-Trisphosphate Receptor
por: Pantazaka, Evangelia, et al.
Publicado: (2011)