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10.1038/s41564-020-0759-0 http://scihub22266oqcxt.onion/10.1038/s41564-020-0759-0 32690955!ä!32690955 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       Nat+Microbiol 2020 ; 5 (11): 1361-1373 Nephropedia Template TP {{tp|p=32690955|t=2020. Inhibition of the integrated stress response by viral proteins that block p-eIF2-eIF2B association |pdf=|usr=}}{{32690955}} gab.com Text Inhibition of the integrated stress response by viral proteins that block p-eIF2-eIF2B association JO: Nat Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=32690955 #FOAvip Eukaryotic cells, when exposed to environmental or internal stress, activate the integrated stress response (ISR) to restore homeostasis and promote cell survival. Specific stress stimuli prompt dedicated stress kinases to phosphorylate eukaryotic initiation factor 2 (eIF2). Phosphorylated eIF2 (p-eIF2) in turn sequesters the eIF2-specific guanine exchange factor eIF2B to block eIF2 recycling, thereby halting translation initiation and reducing global protein synthesis. To circumvent stress-induced translational shutdown, viruses encode ISR antagonists. Those identified so far prevent or reverse eIF2 phosphorylation. We now describe two viral proteins-one from a coronavirus and the other from a picornavirus-that have independently acquired the ability to counteract the ISR at its very core by acting as a competitive inhibitor of p-eIF2-eIF2B interaction. This allows continued formation of the eIF2-GTP-Met-tRNAi ternary complex and unabated global translation at high p-eIF2 levels that would otherwise cause translational arrest. We conclude that eIF2 and p-eIF2 differ in their interaction with eIF2B to such effect that p-eIF2-eIF2B association can be selectively inhibited. Twit Text FOAVip Inhibition of the integrated stress response by viral proteins that block p-eIF2-eIF2B association ????Nat Microbiol http://www.kidney.de/pget.php?&tw=1&pmid=32690955 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32690955 #FOAvip English Wikipedia <ref>{{Cite pmid|32690955}}</ref> Inhibition of the integrated stress response by viral proteins that block p-eIF2-eIF2B association #MMPMID32690955 Rabouw HH; Visser LJ; Passchier TC; Langereis MA; Liu F; Giansanti P; van Vliet ALW; Dekker JG; van der Grein SG; Saucedo JG; Anand AA; Trellet ME; Bonvin AMJJ; Walter P; Heck AJR; de Groot RJ; van Kuppeveld FJM Nat Microbiol 2020[Nov]; 5 (11): 1361-1373 PMID32690955show ga Eukaryotic cells, when exposed to environmental or internal stress, activate the integrated stress response (ISR) to restore homeostasis and promote cell survival. Specific stress stimuli prompt dedicated stress kinases to phosphorylate eukaryotic initiation factor 2 (eIF2). Phosphorylated eIF2 (p-eIF2) in turn sequesters the eIF2-specific guanine exchange factor eIF2B to block eIF2 recycling, thereby halting translation initiation and reducing global protein synthesis. To circumvent stress-induced translational shutdown, viruses encode ISR antagonists. Those identified so far prevent or reverse eIF2 phosphorylation. We now describe two viral proteins-one from a coronavirus and the other from a picornavirus-that have independently acquired the ability to counteract the ISR at its very core by acting as a competitive inhibitor of p-eIF2-eIF2B interaction. This allows continued formation of the eIF2-GTP-Met-tRNAi ternary complex and unabated global translation at high p-eIF2 levels that would otherwise cause translational arrest. We conclude that eIF2 and p-eIF2 differ in their interaction with eIF2B to such effect that p-eIF2-eIF2B association can be selectively inhibited. |Animals[MESH] |Binding Sites[MESH] |Chlorocebus aethiops[MESH] |Eukaryotic Cells/metabolism[MESH] |Eukaryotic Initiation Factor-2/*antagonists & inhibitors/metabolism[MESH] |Eukaryotic Initiation Factor-2B/*antagonists & inhibitors/metabolism[MESH] |Gene Knockout Techniques[MESH] |HEK293 Cells[MESH] |HeLa Cells[MESH] |Humans[MESH] |Phosphorylation[MESH] |Picornaviridae/metabolism[MESH] |Protein Binding[MESH] |Stress, Physiological/*physiology[MESH] |Vero Cells[MESH]Inhibition of the integrated stress response by viral proteins that bl(epmc).pdf DeepDyve Pubget Overpricing