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10.1016/j.redox.2022.102388 http://scihub22266oqcxt.onion/10.1016/j.redox.2022.102388 35792438!9239706!35792438     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Redox+Biol 2022 ; 54 (ä): 102388 Nephropedia Template TP {{tp|p=35792438|t=2022. SARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with ER oxidoreductases |pdf=|usr=}}{{35792438}} gab.com Text SARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with ER oxidoreductases JO: Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=35792438 #FOAvip The replication machinery of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is closely associated with the endoplasmic reticulum (ER) in host cells. Activation of the unfolded protein response (UPR) is a strategy hijacked by coronavirus to facilitate its replication and suppress host innate immunity. Here, we have found that SARS-CoV-2 ORF8 protein accumulates in the ER and escapes the degradation system by forming mixed disulfide complexes with ER oxidoreductases. ORF8 induces the activation of three UPR pathways through targeting key UPR components, remodels ER morphology and accelerates protein trafficking. Moreover, small molecule reducing agents release ORF8 from the mixed disulfide complexes and facilitate its degradation, therefore mitigate ER stress. Our study reveals a unique mechanism by which SARS-CoV-2 ORF8 escapes degradation by host cells and regulates ER reshaping. Targeting ORF8-involved mixed disulfide complexes could be a new strategy to alleviate SARS-CoV-2 induced ER stress and related diseases. Twit Text FOAVip SARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with ER oxidoreductases ????Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=35792438 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35792438 #FOAvip English Wikipedia <ref>{{Cite pmid|35792438}}</ref> SARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with ER oxidoreductases #MMPMID35792438 Liu P; Wang X; Sun Y; Zhao H; Cheng F; Wang J; Yang F; Hu J; Zhang H; Wang CC; Wang L Redox Biol 2022[Aug]; 54 (ä): 102388 PMID35792438show ga The replication machinery of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is closely associated with the endoplasmic reticulum (ER) in host cells. Activation of the unfolded protein response (UPR) is a strategy hijacked by coronavirus to facilitate its replication and suppress host innate immunity. Here, we have found that SARS-CoV-2 ORF8 protein accumulates in the ER and escapes the degradation system by forming mixed disulfide complexes with ER oxidoreductases. ORF8 induces the activation of three UPR pathways through targeting key UPR components, remodels ER morphology and accelerates protein trafficking. Moreover, small molecule reducing agents release ORF8 from the mixed disulfide complexes and facilitate its degradation, therefore mitigate ER stress. Our study reveals a unique mechanism by which SARS-CoV-2 ORF8 escapes degradation by host cells and regulates ER reshaping. Targeting ORF8-involved mixed disulfide complexes could be a new strategy to alleviate SARS-CoV-2 induced ER stress and related diseases. |*Disulfides/metabolism[MESH] |*Endoplasmic Reticulum/metabolism[MESH] |*SARS-CoV-2[MESH] |*Viral Proteins/metabolism[MESH] |COVID-19[MESH] |Humans[MESH]SARS-CoV-2 ORF8 reshapes the ER through forming mixed disulfides with (epmc).pdf DeepDyve Pubget Overpricing