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10.1016/j.celrep.2021.109806 http://scihub22266oqcxt.onion/10.1016/j.celrep.2021.109806 34644561!8558842!34644561     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Rep 2021 ; 37 (2): 109806 Nephropedia Template TP {{tp|p=34644561|t=2021. Proteomics reveal cap-dependent translation inhibitors remodel the translation machinery and translatome |pdf=|usr=}}{{34644561}} gab.com Text Proteomics reveal cap-dependent translation inhibitors remodel the translation machinery and translatome JO: Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=34644561 #FOAvip Tactical disruption of protein synthesis is an attractive therapeutic strategy, with the first-in-class eIF4A-targeting compound zotatifin in clinical evaluation for cancer and COVID-19. The full cellular impact and mechanisms of these potent molecules are undefined at a proteomic level. Here, we report mass spectrometry analysis of translational reprogramming by rocaglates, cap-dependent initiation disruptors that include zotatifin. We find effects to be far more complex than simple "translational inhibition" as currently defined. Translatome analysis by TMT-pSILAC (tandem mass tag-pulse stable isotope labeling with amino acids in cell culture mass spectrometry) reveals myriad upregulated proteins that drive hitherto unrecognized cytotoxic mechanisms, including GEF-H1-mediated anti-survival RHOA/JNK activation. Surprisingly, these responses are not replicated by eIF4A silencing, indicating a broader translational adaptation than currently understood. Translation machinery analysis by MATRIX (mass spectrometry analysis of active translation factors using ribosome density fractionation and isotopic labeling experiments) identifies rocaglate-specific dependence on specific translation factors including eEF1epsilon1 that drive translatome remodeling. Our proteome-level interrogation reveals that the complete cellular response to these historical "translation inhibitors" is mediated by comprehensive translational landscape remodeling. Twit Text FOAVip Proteomics reveal cap-dependent translation inhibitors remodel the translation machinery and translatome ????Cell Rep http://www.kidney.de/pget.php?&tw=1&pmid=34644561 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34644561 #FOAvip English Wikipedia <ref>{{Cite pmid|34644561}}</ref> Proteomics reveal cap-dependent translation inhibitors remodel the translation machinery and translatome #MMPMID34644561 Ho JJD; Cunningham TA; Manara P; Coughlin CA; Arumov A; Roberts ER; Osteen A; Kumar P; Bilbao D; Krieger JR; Lee S; Schatz JH Cell Rep 2021[Oct]; 37 (2): 109806 PMID34644561show ga Tactical disruption of protein synthesis is an attractive therapeutic strategy, with the first-in-class eIF4A-targeting compound zotatifin in clinical evaluation for cancer and COVID-19. The full cellular impact and mechanisms of these potent molecules are undefined at a proteomic level. Here, we report mass spectrometry analysis of translational reprogramming by rocaglates, cap-dependent initiation disruptors that include zotatifin. We find effects to be far more complex than simple "translational inhibition" as currently defined. Translatome analysis by TMT-pSILAC (tandem mass tag-pulse stable isotope labeling with amino acids in cell culture mass spectrometry) reveals myriad upregulated proteins that drive hitherto unrecognized cytotoxic mechanisms, including GEF-H1-mediated anti-survival RHOA/JNK activation. Surprisingly, these responses are not replicated by eIF4A silencing, indicating a broader translational adaptation than currently understood. Translation machinery analysis by MATRIX (mass spectrometry analysis of active translation factors using ribosome density fractionation and isotopic labeling experiments) identifies rocaglate-specific dependence on specific translation factors including eEF1epsilon1 that drive translatome remodeling. Our proteome-level interrogation reveals that the complete cellular response to these historical "translation inhibitors" is mediated by comprehensive translational landscape remodeling. |Animals[MESH] |Benzofurans/pharmacology[MESH] |Cell Line, Tumor[MESH] |Eukaryotic Initiation Factor-4A/drug effects/metabolism[MESH] |Humans[MESH] |Male[MESH] |Mice[MESH] |Mice, Inbred NOD[MESH] |Primary Cell Culture[MESH] |Protein Biosynthesis/*drug effects/physiology[MESH] |Protein Synthesis Inhibitors/*pharmacology[MESH] |Proteomics/methods[MESH] |Ribosomes/metabolism[MESH] |Transcriptome/drug effects/genetics[MESH]Proteomics reveal cap-dependent translation inhibitors remodel the tra(epmc).pdf DeepDyve Pubget Overpricing