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10.3390/v13010047 http://scihub22266oqcxt.onion/10.3390/v13010047 33396605!7823417!33396605     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 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\33396605.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Viruses 2020 ; 13 (1): � Nephropedia Template TP {{tp|p=33396605|t=2020. SARS-CoV-2 Nucleocapsid Protein Interacts with RIG-I and Represses RIG-Mediated IFN-beta Production |pdf=|usr=}}{{33396605}} gab.com Text SARS-CoV-2 Nucleocapsid Protein Interacts with RIG-I and Represses RIG-Mediated IFN-beta Production JO: Viruses http://www.kidney.de/pget.php?&tw=1&pmid=33396605 #FOAvip SARS-CoV-2 is highly pathogenic in humans and poses a great threat to public health worldwide. Clinical data shows a disturbed type I interferon (IFN) response during the virus infection. In this study, we discovered that the nucleocapsid (N) protein of SARS-CoV-2 plays an important role in the inhibition of interferon beta (IFN-beta) production. N protein repressed IFN-beta production induced by poly(I:C) or upon Sendai virus (SeV) infection. We noted that N protein also suppressed IFN-beta production, induced by several signaling molecules downstream of the retinoic acid-inducible gene I (RIG-I) pathway, which is the crucial pattern recognition receptor (PRR) responsible for identifying RNA viruses. Moreover, our data demonstrated that N protein interacted with the RIG-I protein through the DExD/H domain, which has ATPase activity and plays an important role in the binding of immunostimulatory RNAs. These results suggested that SARS-CoV-2 N protein suppresses the IFN-beta response through targeting the initial step, potentially the cellular PRR-RNA-recognition step in the innate immune pathway. Therefore, we propose that the SARS-CoV-2 N protein represses IFN-beta production by interfering with RIG-I. Twit Text FOAVip SARS-CoV-2 Nucleocapsid Protein Interacts with RIG-I and Represses RIG-Mediated IFN-beta Production ????Viruses http://www.kidney.de/pget.php?&tw=1&pmid=33396605 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33396605 #FOAvip English Wikipedia <ref>{{Cite pmid|33396605}}</ref> SARS-CoV-2 Nucleocapsid Protein Interacts with RIG-I and Represses RIG-Mediated IFN-beta Production #MMPMID33396605 Chen K; Xiao F; Hu D; Ge W; Tian M; Wang W; Pan P; Wu K; Wu J Viruses 2020[Dec]; 13 (1): � PMID33396605show ga SARS-CoV-2 is highly pathogenic in humans and poses a great threat to public health worldwide. Clinical data shows a disturbed type I interferon (IFN) response during the virus infection. In this study, we discovered that the nucleocapsid (N) protein of SARS-CoV-2 plays an important role in the inhibition of interferon beta (IFN-beta) production. N protein repressed IFN-beta production induced by poly(I:C) or upon Sendai virus (SeV) infection. We noted that N protein also suppressed IFN-beta production, induced by several signaling molecules downstream of the retinoic acid-inducible gene I (RIG-I) pathway, which is the crucial pattern recognition receptor (PRR) responsible for identifying RNA viruses. Moreover, our data demonstrated that N protein interacted with the RIG-I protein through the DExD/H domain, which has ATPase activity and plays an important role in the binding of immunostimulatory RNAs. These results suggested that SARS-CoV-2 N protein suppresses the IFN-beta response through targeting the initial step, potentially the cellular PRR-RNA-recognition step in the innate immune pathway. Therefore, we propose that the SARS-CoV-2 N protein represses IFN-beta production by interfering with RIG-I. |A549 Cells[MESH] |Animals[MESH] |COVID-19/*immunology[MESH] |DEAD Box Protein 58/genetics/*metabolism[MESH] |HEK293 Cells[MESH] |HeLa Cells[MESH] |Host-Pathogen Interactions/immunology[MESH] |Humans[MESH] |Interferon-beta/*metabolism[MESH] |Nucleocapsid Proteins/*metabolism[MESH] |Protein Interaction Domains and Motifs[MESH] |Receptors, Immunologic[MESH] |SARS-CoV-2/*metabolism[MESH]SARS-CoV-2 Nucleocapsid Protein Interacts with RIG-I and Represses RIG(epmc).pdf DeepDyve Pubget Overpricing