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10.1016/j.isci.2021.103562 http://scihub22266oqcxt.onion/10.1016/j.isci.2021.103562 34901782!8642831!34901782     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34901782&cmd=llinks): Failed to open stream: HTTP request failed! 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SARS-CoV-2 nucleocapsid protein binds host mRNAs and attenuates stress granules to impair host stress response |pdf=|usr=}}{{34901782}} gab.com Text SARS-CoV-2 nucleocapsid protein binds host mRNAs and attenuates stress granules to impair host stress response JO: iScience http://www.kidney.de/pget.php?&tw=1&pmid=34901782 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nucleocapsid (N) protein is essential for viral replication, making it a promising target for antiviral drug and vaccine development. SARS-CoV-2 infected patients exhibit an uncoordinated immune response; however, the underlying mechanistic details of this imbalance remain obscure. Here, starting from a functional proteomics workflow, we cataloged the protein-protein interactions of SARS-CoV-2 proteins, including an evolutionarily conserved specific interaction of N with the stress granule resident proteins G3BP1 and G3BP2. N localizes to stress granules and sequesters G3BPs away from their typical interaction partners, thus attenuating stress granule formation. We found that N binds directly to host mRNAs in cells, with a preference for 3' UTRs, and modulates target mRNA stability. We show that the N protein rewires the G3BP1 mRNA-binding profile and suppresses the physiological stress response of host cells, which may explain the imbalanced immune response observed in SARS-CoV-2 infected patients. Twit Text FOAVip SARS-CoV-2 nucleocapsid protein binds host mRNAs and attenuates stress granules to impair host stress response ????iScience http://www.kidney.de/pget.php?&tw=1&pmid=34901782 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34901782 #FOAvip English Wikipedia <ref>{{Cite pmid|34901782}}</ref> SARS-CoV-2 nucleocapsid protein binds host mRNAs and attenuates stress granules to impair host stress response #MMPMID34901782 Nabeel-Shah S; Lee H; Ahmed N; Burke GL; Farhangmehr S; Ashraf K; Pu S; Braunschweig U; Zhong G; Wei H; Tang H; Yang J; Marcon E; Blencowe BJ; Zhang Z; Greenblatt JF iScience 2022[Jan]; 25 (1): 103562 PMID34901782show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nucleocapsid (N) protein is essential for viral replication, making it a promising target for antiviral drug and vaccine development. SARS-CoV-2 infected patients exhibit an uncoordinated immune response; however, the underlying mechanistic details of this imbalance remain obscure. Here, starting from a functional proteomics workflow, we cataloged the protein-protein interactions of SARS-CoV-2 proteins, including an evolutionarily conserved specific interaction of N with the stress granule resident proteins G3BP1 and G3BP2. N localizes to stress granules and sequesters G3BPs away from their typical interaction partners, thus attenuating stress granule formation. We found that N binds directly to host mRNAs in cells, with a preference for 3' UTRs, and modulates target mRNA stability. We show that the N protein rewires the G3BP1 mRNA-binding profile and suppresses the physiological stress response of host cells, which may explain the imbalanced immune response observed in SARS-CoV-2 infected patients. äSARS-CoV-2 nucleocapsid protein binds host mRNAs and attenuates stress(epmc).pdf DeepDyve Pubget Overpricing