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10.3390/v13081439 http://scihub22266oqcxt.onion/10.3390/v13081439 34452305!8402637!34452305     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Viruses 2021 ; 13 (8): ä Nephropedia Template TP {{tp|p=34452305|t=2021. SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity |pdf=|usr=}}{{34452305}} gab.com Text SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity JO: Viruses http://www.kidney.de/pget.php?&tw=1&pmid=34452305 #FOAvip A weak production of INF-beta along with an exacerbated release of pro-inflammatory cytokines have been reported during infection by the novel SARS-CoV-2 virus. SARS-CoV-2 encodes several proteins able to counteract the host immune system, which is believed to be one of the most important features contributing to the viral pathogenesis and development of a severe clinical picture. Previous reports have demonstrated that SARS-CoV-2 N protein, along with some non-structural and accessory proteins, efficiently suppresses INF-beta production by interacting with RIG-I, an important pattern recognition receptor (PRR) involved in the recognition of pathogen-derived molecules. In the present study, we better characterized the mechanism by which the SARS-CoV-2 N counteracts INF-beta secretion and affects RIG-I signaling pathways. In detail, when the N protein was ectopically expressed, we noted a marked decrease in TRIM25-mediated RIG-I activation. The capability of the N protein to bind to, and probably mask, TRIM25 could be the consequence of its antagonistic activity. Furthermore, this interaction occurred at the SPRY domain of TRIM25, harboring the RNA-binding activity necessary for TRIM25 self-activation. Here, we describe new findings regarding the interplay between SARS-CoV-2 and the IFN system, filling some gaps for a better understanding of the molecular mechanisms affecting the innate immune response in COVID-19. Twit Text FOAVip SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity ????Viruses http://www.kidney.de/pget.php?&tw=1&pmid=34452305 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34452305 #FOAvip English Wikipedia <ref>{{Cite pmid|34452305}}</ref> SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppress Innate Immunity #MMPMID34452305 Gori Savellini G; Anichini G; Gandolfo C; Cusi MG Viruses 2021[Jul]; 13 (8): ä PMID34452305show ga A weak production of INF-beta along with an exacerbated release of pro-inflammatory cytokines have been reported during infection by the novel SARS-CoV-2 virus. SARS-CoV-2 encodes several proteins able to counteract the host immune system, which is believed to be one of the most important features contributing to the viral pathogenesis and development of a severe clinical picture. Previous reports have demonstrated that SARS-CoV-2 N protein, along with some non-structural and accessory proteins, efficiently suppresses INF-beta production by interacting with RIG-I, an important pattern recognition receptor (PRR) involved in the recognition of pathogen-derived molecules. In the present study, we better characterized the mechanism by which the SARS-CoV-2 N counteracts INF-beta secretion and affects RIG-I signaling pathways. In detail, when the N protein was ectopically expressed, we noted a marked decrease in TRIM25-mediated RIG-I activation. The capability of the N protein to bind to, and probably mask, TRIM25 could be the consequence of its antagonistic activity. Furthermore, this interaction occurred at the SPRY domain of TRIM25, harboring the RNA-binding activity necessary for TRIM25 self-activation. Here, we describe new findings regarding the interplay between SARS-CoV-2 and the IFN system, filling some gaps for a better understanding of the molecular mechanisms affecting the innate immune response in COVID-19. |COVID-19/genetics/*immunology/virology[MESH] |Coronavirus Nucleocapsid Proteins/genetics/*immunology[MESH] |DEAD Box Protein 58/genetics/*immunology[MESH] |Gene Expression Regulation[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Immunity, Innate[MESH] |Interferon-beta/genetics/immunology[MESH] |Promoter Regions, Genetic[MESH] |Receptors, Immunologic/genetics/*immunology[MESH] |SARS-CoV-2/genetics/*immunology[MESH] |Signal Transduction[MESH] |Transcription Factors/genetics/*immunology[MESH] |Tripartite Motif Proteins/genetics/*immunology[MESH]SARS-CoV-2 N Protein Targets TRIM25-Mediated RIG-I Activation to Suppr(epmc).pdf DeepDyve Pubget Overpricing