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10.1080/22221751.2020.1850183 http://scihub22266oqcxt.onion/10.1080/22221751.2020.1850183 33179566!7751432!33179566     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Emerg+Microbes+Infect 2020 ; 9 (1): 2663-2672 Nephropedia Template TP {{tp|p=33179566|t=2020. Human coronavirus dependency on host heat shock protein 90 reveals an antiviral target |pdf=|usr=}}{{33179566}} gab.com Text Human coronavirus dependency on host heat shock protein 90 reveals an antiviral target JO: Emerg Microbes Infect http://www.kidney.de/pget.php?&tw=1&pmid=33179566 #FOAvip Rapid accumulation of viral proteins in host cells render viruses highly dependent on cellular chaperones including heat shock protein 90 (Hsp90). Three highly pathogenic human coronaviruses, including MERS-CoV, SARS-CoV and SARS-CoV-2, have emerged in the past 2 decades. However, there is no approved antiviral agent against these coronaviruses. We inspected the role of Hsp90 for coronavirus propagation. First, an Hsp90 inhibitor, 17-AAG, significantly suppressed MERS-CoV propagation in cell lines and physiological-relevant human intestinal organoids. Second, siRNA depletion of Hsp90beta, but not Hsp90alpha, significantly restricted MERS-CoV replication and abolished virus spread. Third, Hsp90beta interaction with MERS-CoV nucleoprotein (NP) was revealed in a co-immunoprecipitation assay. Hsp90beta is required to maintain NP stability. Fourth, 17-AAG substantially inhibited the propagation of SARS-CoV and SARS-CoV-2. Collectively, Hsp90 is a host dependency factor for human coronavirus MERS-CoV, SARS-CoV and SARS-COV-2. Hsp90 inhibitors can be repurposed as a potent and broad-spectrum antiviral against human coronaviruses. Twit Text FOAVip Human coronavirus dependency on host heat shock protein 90 reveals an antiviral target ????Emerg Microbes Infect http://www.kidney.de/pget.php?&tw=1&pmid=33179566 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33179566 #FOAvip English Wikipedia <ref>{{Cite pmid|33179566}}</ref> Human coronavirus dependency on host heat shock protein 90 reveals an antiviral target #MMPMID33179566 Li C; Chu H; Liu X; Chiu MC; Zhao X; Wang D; Wei Y; Hou Y; Shuai H; Cai J; Chan JF; Zhou J; Yuen KY Emerg Microbes Infect 2020[Dec]; 9 (1): 2663-2672 PMID33179566show ga Rapid accumulation of viral proteins in host cells render viruses highly dependent on cellular chaperones including heat shock protein 90 (Hsp90). Three highly pathogenic human coronaviruses, including MERS-CoV, SARS-CoV and SARS-CoV-2, have emerged in the past 2 decades. However, there is no approved antiviral agent against these coronaviruses. We inspected the role of Hsp90 for coronavirus propagation. First, an Hsp90 inhibitor, 17-AAG, significantly suppressed MERS-CoV propagation in cell lines and physiological-relevant human intestinal organoids. Second, siRNA depletion of Hsp90beta, but not Hsp90alpha, significantly restricted MERS-CoV replication and abolished virus spread. Third, Hsp90beta interaction with MERS-CoV nucleoprotein (NP) was revealed in a co-immunoprecipitation assay. Hsp90beta is required to maintain NP stability. Fourth, 17-AAG substantially inhibited the propagation of SARS-CoV and SARS-CoV-2. Collectively, Hsp90 is a host dependency factor for human coronavirus MERS-CoV, SARS-CoV and SARS-COV-2. Hsp90 inhibitors can be repurposed as a potent and broad-spectrum antiviral against human coronaviruses. |A549 Cells[MESH] |Animals[MESH] |Antiviral Agents/*pharmacology[MESH] |Benzoquinones/*pharmacology[MESH] |COVID-19 Drug Treatment[MESH] |Cell Line[MESH] |Chlorocebus aethiops[MESH] |HEK293 Cells[MESH] |HSP90 Heat-Shock Proteins/*antagonists & inhibitors/*genetics[MESH] |Host Microbial Interactions/*drug effects[MESH] |Humans[MESH] |Intestines/virology[MESH] |Lactams, Macrocyclic/*pharmacology[MESH] |Middle East Respiratory Syndrome Coronavirus/*drug effects[MESH] |Organ Culture Techniques[MESH] |RNA, Small Interfering[MESH] |SARS-CoV-2/drug effects[MESH] |Severe acute respiratory syndrome-related coronavirus/drug effects[MESH] |Vero Cells[MESH]Human coronavirus dependency on host heat shock protein 90 reveals an (epmc).pdf DeepDyve Pubget Overpricing