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Role of glutathionylation in infection and inflammation
Full text linkGlutathionylation, that is, the formation of mixed disulfides between protein cysteines and
glutathione (GSH) cysteines, is a reversible post-translational modification catalyzed by dierent
cellular oxidoreductases, by which the redox state of the cell modulates protein function. So far, most
studies on the identification of glutathionylated proteins have focused on cellular proteins, including
proteins involved in host response to infection, but there is a growing number of reports showing
that microbial proteins also undergo glutathionylation, with modification of their characteristics and
functions. In the present review, we highlight the signaling role of GSH through glutathionylation,
particularly focusing on microbial (viral and bacterial) glutathionylated proteins (GSSPs) and host
GSSPs involved in the immune/inflammatory response to infection; moreover, we discuss the
biological role of the process in microbial infections and related host responses
Role of glutathione and Bcl-2 interaction in the control of influenza A virus replication in neuroblastoma cells.
No full textPurification and characterization of Alpha-Fetoprotein from the human hepatoblastoma HepG2 cell line in serum-free medium
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Influenza virus and intracellular redox state: characterization of redox-sensitive molecular targets for innovative antiviral strategies.
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