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10.1042/BCJ20210110 http://scihub22266oqcxt.onion/10.1042/BCJ20210110 34003254!ä!34003254 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\34003254.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochem+J 2021 ; 478 (10): 1853-1859 Nephropedia Template TP {{tp|p=34003254|t=2021. Opposing forces fight over the same ground to regulate interferon signaling |pdf=|usr=}}{{34003254}} gab.com Text Opposing forces fight over the same ground to regulate interferon signaling JO: Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=34003254 #FOAvip The current SARS-CoV-2 pandemic has spurred new interest in interferon signaling in response to viral pathogens. Much of what we know about the signaling molecules and associated signal transduction induced during the host cellular response to viral pathogens has been gained from research conducted from the 1990's to the present day, but certain intricacies of the mechanisms involved, still remain unclear. In a recent study by Vaughn et al. the authors examine one of the main mechanisms regulating interferon induction following viral infection, the RIG-I/MAVS/IRF3 pathway, and find that similar to PKR both DICER interacting proteins, PACT and TRBP, regulate RIG-I signaling in an opposing manner. More specifically, the reported findings demonstrate, like others, that PACT stimulates RIG-I-mediated signaling in a manner independent of PACT dsRNA-binding ability or phosphorylation at sites known to be important for PACT-dependent PKR activation. In contrast, they show for the first time that TRBP inhibits RIG-I-mediated signaling. RIG-I inhibition by TRBP did not require phosphorylation of sites shown to be important for inhibiting PKR, nor did it involve PACT or PKR, but it did require the dsRNA-binding ability of TRBP. These findings open the door to a complex co-regulation of RIG-I, PKR, MDA5, miRNA processing, and interferon induction. Twit Text FOAVip Opposing forces fight over the same ground to regulate interferon signaling ????Biochem J http://www.kidney.de/pget.php?&tw=1&pmid=34003254 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34003254 #FOAvip English Wikipedia <ref>{{Cite pmid|34003254}}</ref> Opposing forces fight over the same ground to regulate interferon signaling #MMPMID34003254 Blalock WL Biochem J 2021[May]; 478 (10): 1853-1859 PMID34003254show ga The current SARS-CoV-2 pandemic has spurred new interest in interferon signaling in response to viral pathogens. Much of what we know about the signaling molecules and associated signal transduction induced during the host cellular response to viral pathogens has been gained from research conducted from the 1990's to the present day, but certain intricacies of the mechanisms involved, still remain unclear. In a recent study by Vaughn et al. the authors examine one of the main mechanisms regulating interferon induction following viral infection, the RIG-I/MAVS/IRF3 pathway, and find that similar to PKR both DICER interacting proteins, PACT and TRBP, regulate RIG-I signaling in an opposing manner. More specifically, the reported findings demonstrate, like others, that PACT stimulates RIG-I-mediated signaling in a manner independent of PACT dsRNA-binding ability or phosphorylation at sites known to be important for PACT-dependent PKR activation. In contrast, they show for the first time that TRBP inhibits RIG-I-mediated signaling. RIG-I inhibition by TRBP did not require phosphorylation of sites shown to be important for inhibiting PKR, nor did it involve PACT or PKR, but it did require the dsRNA-binding ability of TRBP. These findings open the door to a complex co-regulation of RIG-I, PKR, MDA5, miRNA processing, and interferon induction. |Adaptor Proteins, Signal Transducing/genetics/metabolism[MESH] |COVID-19/*immunology/virology[MESH] |DEAD Box Protein 58/genetics/metabolism[MESH] |Gene Expression Regulation/immunology[MESH] |Humans[MESH] |Interferon Regulatory Factor-3/genetics/metabolism[MESH] |Interferon-Induced Helicase, IFIH1/genetics/metabolism[MESH] |Interferons/genetics/*metabolism[MESH] |MicroRNAs/genetics/metabolism[MESH] |Nuclear Receptor Coactivators/genetics/metabolism[MESH] |RNA-Binding Proteins/genetics/metabolism[MESH] |Receptors, Immunologic/genetics/metabolism[MESH] |SARS-CoV-2/*immunology[MESH]Opposing forces fight over the same ground to regulate interferon sign(epmc).pdf DeepDyve Pubget Overpricing