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- W2040391028 endingPage "864" @default.
- W2040391028 startingPage "848" @default.
- W2040391028 abstract "Protein ubiquitination plays indispensable roles in the regulation of cell homeostasis and pathogenesis of neoplastic, infectious, and neurodegenerative diseases. Given the importance of this modification, it is to be expected that several pathogenic bacteria have developed the ability to utilize the host ubiquitin system for their own benefit. Modulation of the host ubiquitin system by bacterial effector proteins inhibits innate immune responses and hijacks central signaling pathways. Bacterial effectors mimic enzymes of the host ubiquitin system, but may or may not be structurally similar to the mammalian enzymes. Other effectors bind and modify components of the host ubiquitin system, and some are themselves subject to ubiquitination. This review will describe recent findings, based on structural analyses, regarding how pathogens use post-translational modifications of proteins to establish an infection." @default.
- W2040391028 created "2016-06-24" @default.
- W2040391028 creator A5028070594 @default.
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- W2040391028 creator A5064206219 @default.
- W2040391028 creator A5086693282 @default.
- W2040391028 creator A5088028110 @default.
- W2040391028 date "2014-08-18" @default.
- W2040391028 modified "2023-10-18" @default.
- W2040391028 title "Bacterial Effectors and Their Functions in the Ubiquitin-Proteasome System: Insight from the Modes of Substrate Recognition" @default.
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- W2040391028 doi "https://doi.org/10.3390/cells3030848" @default.
- W2040391028 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4197628" @default.
- W2040391028 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25257025" @default.