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10.1016/j.celrep.2016.02.066 http://scihub22266oqcxt.onion/10.1016/j.celrep.2016.02.066 C4930247!4930247 !26997275     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26997275 &cmd=llinks): Failed to open stream: HTTP request failed! 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Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity |pdf=|usr=}}{{26997275 }} gab.com Text Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=26997275 #FOAvip The thiol-disulfide oxidoreductase CXXC catalytic domain of thioredoxin contributes to antioxidant defense in phylogenetically diverse organisms. We find that although the oxidoreductase activity of thioredoxin-1 protects Salmonella enterica serovar Typhimurium from hydrogen peroxide in vitro, it does not appear to contribute to Salmonella's antioxidant defenses in vivo. Nonetheless, thioredoxin-1 defends Salmonella from oxidative stress resulting from NADPH phagocyte oxidase macrophage expression during the innate immune response in mice. Thioredoxin-1 binds to the flexible linker, which connects the receiver and effector domains of SsrB, thereby keeping this response regulator in the soluble fraction. Thioredoxin-1, independently of thiol-disulfide exchange, activates intracellular SPI2 gene transcription required for Salmonella resistance to both reactive species generated by NADPH phagocyte oxidase and oxygen-independent lysosomal host defenses. These findings suggest that the horizontally acquired virulence determinant SsrB is regulated post-translationally by ancestrally present thioredoxin. Twit Text FOAVip Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=26997275 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26997275 #FOAvip English Wikipedia <ref>{{Cite pmid|26997275 }}</ref> Antioxidant Defense by Thioredoxin Can Occur Independently of Canonical Thiol-Disulfide Oxidoreductase Enzymatic Activity #MMPMID26997275 Song M ; Kim JS ; Liu L ; Husain M ; Vázquez-Torres A Cell Rep 2016[Mar]; 14 (12 ): 2901-11 PMID26997275 show ga The thiol-disulfide oxidoreductase CXXC catalytic domain of thioredoxin contributes to antioxidant defense in phylogenetically diverse organisms. We find that although the oxidoreductase activity of thioredoxin-1 protects Salmonella enterica serovar Typhimurium from hydrogen peroxide in vitro, it does not appear to contribute to Salmonella's antioxidant defenses in vivo. Nonetheless, thioredoxin-1 defends Salmonella from oxidative stress resulting from NADPH phagocyte oxidase macrophage expression during the innate immune response in mice. Thioredoxin-1 binds to the flexible linker, which connects the receiver and effector domains of SsrB, thereby keeping this response regulator in the soluble fraction. Thioredoxin-1, independently of thiol-disulfide exchange, activates intracellular SPI2 gene transcription required for Salmonella resistance to both reactive species generated by NADPH phagocyte oxidase and oxygen-independent lysosomal host defenses. These findings suggest that the horizontally acquired virulence determinant SsrB is regulated post-translationally by ancestrally present thioredoxin. |Animals [MESH] |Antioxidants/*metabolism [MESH] |Bacterial Proteins/chemistry/genetics/*metabolism [MESH] |Blotting, Western [MESH] |Catalytic Domain [MESH] |Cell Line [MESH] |HeLa Cells [MESH] |Humans [MESH] |Hydrogen Peroxide/toxicity [MESH] |Immunity, Innate [MESH] |Liver/microbiology [MESH] |Macrophages/cytology/enzymology/immunology [MESH] |Membrane Proteins/genetics/metabolism [MESH] |Mice [MESH] |Mice, Inbred C57BL [MESH] |Mice, Knockout [MESH] |Microscopy, Fluorescence [MESH] |Models, Animal [MESH] |NADPH Oxidases/metabolism [MESH] |Phagocytosis/drug effects [MESH] |Protein Binding [MESH] |Protein Disulfide Reductase (Glutathione)/metabolism [MESH] |RAW 264.7 Cells [MESH] |Reactive Nitrogen Species/metabolism [MESH] |Reactive Oxygen Species/metabolism [MESH] |Salmonella typhi/drug effects/enzymology/growth & development [MESH] |Thioredoxins/chemistry/*metabolism [MESH]Antioxidant Defense by Thioredoxin Can Occur Independently of Canonica(epmc).pdf DeepDyve Pubget Overpricing