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10.1016/j.cell.2020.06.034 http://scihub22266oqcxt.onion/10.1016/j.cell.2020.06.034 32645325!7321036!32645325     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       Cell 2020 ; 182 (3): 685-712.e19 Nephropedia Template TP {{tp|p=32645325|t=2020. The Global Phosphorylation Landscape of SARS-CoV-2 Infection |pdf=|usr=}}{{32645325}} gab.com Text The Global Phosphorylation Landscape of SARS-CoV-2 Infection JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=32645325 #FOAvip The causative agent of the coronavirus disease 2019 (COVID-19) pandemic, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has infected millions and killed hundreds of thousands of people worldwide, highlighting an urgent need to develop antiviral therapies. Here we present a quantitative mass spectrometry-based phosphoproteomics survey of SARS-CoV-2 infection in Vero E6 cells, revealing dramatic rewiring of phosphorylation on host and viral proteins. SARS-CoV-2 infection promoted casein kinase II (CK2) and p38 MAPK activation, production of diverse cytokines, and shutdown of mitotic kinases, resulting in cell cycle arrest. Infection also stimulated a marked induction of CK2-containing filopodial protrusions possessing budding viral particles. Eighty-seven drugs and compounds were identified by mapping global phosphorylation profiles to dysregulated kinases and pathways. We found pharmacologic inhibition of the p38, CK2, CDK, AXL, and PIKFYVE kinases to possess antiviral efficacy, representing potential COVID-19 therapies. Twit Text FOAVip The Global Phosphorylation Landscape of SARS-CoV-2 Infection ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=32645325 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32645325 #FOAvip English Wikipedia <ref>{{Cite pmid|32645325}}</ref> The Global Phosphorylation Landscape of SARS-CoV-2 Infection #MMPMID32645325 Bouhaddou M; Memon D; Meyer B; White KM; Rezelj VV; Correa Marrero M; Polacco BJ; Melnyk JE; Ulferts S; Kaake RM; Batra J; Richards AL; Stevenson E; Gordon DE; Rojc A; Obernier K; Fabius JM; Soucheray M; Miorin L; Moreno E; Koh C; Tran QD; Hardy A; Robinot R; Vallet T; Nilsson-Payant BE; Hernandez-Armenta C; Dunham A; Weigang S; Knerr J; Modak M; Quintero D; Zhou Y; Dugourd A; Valdeolivas A; Patil T; Li Q; Huttenhain R; Cakir M; Muralidharan M; Kim M; Jang G; Tutuncuoglu B; Hiatt J; Guo JZ; Xu J; Bouhaddou S; Mathy CJP; Gaulton A; Manners EJ; Felix E; Shi Y; Goff M; Lim JK; McBride T; O'Neal MC; Cai Y; Chang JCJ; Broadhurst DJ; Klippsten S; De Wit E; Leach AR; Kortemme T; Shoichet B; Ott M; Saez-Rodriguez J; tenOever BR; Mullins RD; Fischer ER; Kochs G; Grosse R; Garcia-Sastre A; Vignuzzi M; Johnson JR; Shokat KM; Swaney DL; Beltrao P; Krogan NJ Cell 2020[Aug]; 182 (3): 685-712.e19 PMID32645325show ga The causative agent of the coronavirus disease 2019 (COVID-19) pandemic, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has infected millions and killed hundreds of thousands of people worldwide, highlighting an urgent need to develop antiviral therapies. Here we present a quantitative mass spectrometry-based phosphoproteomics survey of SARS-CoV-2 infection in Vero E6 cells, revealing dramatic rewiring of phosphorylation on host and viral proteins. SARS-CoV-2 infection promoted casein kinase II (CK2) and p38 MAPK activation, production of diverse cytokines, and shutdown of mitotic kinases, resulting in cell cycle arrest. Infection also stimulated a marked induction of CK2-containing filopodial protrusions possessing budding viral particles. Eighty-seven drugs and compounds were identified by mapping global phosphorylation profiles to dysregulated kinases and pathways. We found pharmacologic inhibition of the p38, CK2, CDK, AXL, and PIKFYVE kinases to possess antiviral efficacy, representing potential COVID-19 therapies. |A549 Cells[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Antiviral Agents/pharmacology[MESH] |Axl Receptor Tyrosine Kinase[MESH] |Betacoronavirus/*metabolism[MESH] |COVID-19[MESH] |Caco-2 Cells[MESH] |Casein Kinase II/antagonists & inhibitors/metabolism[MESH] |Chlorocebus aethiops[MESH] |Coronavirus Infections/*metabolism/virology[MESH] |Cyclin-Dependent Kinases/antagonists & inhibitors/metabolism[MESH] |Drug Evaluation, Preclinical/*methods[MESH] |HEK293 Cells[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/genetics/metabolism[MESH] |Phosphatidylinositol 3-Kinases/metabolism[MESH] |Phosphoinositide-3 Kinase Inhibitors/pharmacology[MESH] |Phosphorylation[MESH] |Pneumonia, Viral/*metabolism/virology[MESH] |Protein Kinase Inhibitors/pharmacology[MESH] |Proteomics/*methods[MESH] |Proto-Oncogene Proteins/antagonists & inhibitors/metabolism[MESH] |Receptor Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism[MESH] |SARS-CoV-2[MESH] |Spike Glycoprotein, Coronavirus/metabolism[MESH] |Vero Cells[MESH]The Global Phosphorylation Landscape of SARS-CoV-2 Infection (epmc).pdf DeepDyve Pubget Overpricing