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10.15252/embj.2020106478 http://scihub22266oqcxt.onion/10.15252/embj.2020106478 33200826!7737613!33200826     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       EMBO+J 2020 ; 39 (24): e106478 Nephropedia Template TP {{tp|p=33200826|t=2020. SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs |pdf=|usr=}}{{33200826}} gab.com Text SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs JO: EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=33200826 #FOAvip Tightly packed complexes of nucleocapsid protein and genomic RNA form the core of viruses and assemble within viral factories, dynamic compartments formed within the host cells associated with human stress granules. Here, we test the possibility that the multivalent RNA-binding nucleocapsid protein (N) from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) condenses with RNA via liquid-liquid phase separation (LLPS) and that N protein can be recruited in phase-separated forms of human RNA-binding proteins associated with SG formation. Robust LLPS with RNA requires two intrinsically disordered regions (IDRs), the N-terminal IDR and central-linker IDR, as well as the folded C-terminal oligomerization domain, while the folded N-terminal domain and the C-terminal IDR are not required. N protein phase separation is induced by addition of non-specific RNA. In addition, N partitions in vitro into phase-separated forms of full-length human hnRNPs (TDP-43, FUS, hnRNPA2) and their low-complexity domains (LCs). These results provide a potential mechanism for the role of N in SARS-CoV-2 viral genome packing and in host-protein co-opting necessary for viral replication and infectivity. Twit Text FOAVip SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs ????EMBO J http://www.kidney.de/pget.php?&tw=1&pmid=33200826 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33200826 #FOAvip English Wikipedia <ref>{{Cite pmid|33200826}}</ref> SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs #MMPMID33200826 Perdikari TM; Murthy AC; Ryan VH; Watters S; Naik MT; Fawzi NL EMBO J 2020[Dec]; 39 (24): e106478 PMID33200826show ga Tightly packed complexes of nucleocapsid protein and genomic RNA form the core of viruses and assemble within viral factories, dynamic compartments formed within the host cells associated with human stress granules. Here, we test the possibility that the multivalent RNA-binding nucleocapsid protein (N) from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) condenses with RNA via liquid-liquid phase separation (LLPS) and that N protein can be recruited in phase-separated forms of human RNA-binding proteins associated with SG formation. Robust LLPS with RNA requires two intrinsically disordered regions (IDRs), the N-terminal IDR and central-linker IDR, as well as the folded C-terminal oligomerization domain, while the folded N-terminal domain and the C-terminal IDR are not required. N protein phase separation is induced by addition of non-specific RNA. In addition, N partitions in vitro into phase-separated forms of full-length human hnRNPs (TDP-43, FUS, hnRNPA2) and their low-complexity domains (LCs). These results provide a potential mechanism for the role of N in SARS-CoV-2 viral genome packing and in host-protein co-opting necessary for viral replication and infectivity. |COVID-19/pathology/*virology[MESH] |Coronavirus Nucleocapsid Proteins/*chemistry/metabolism[MESH] |Cytoplasmic Granules/virology[MESH] |DNA-Binding Proteins/chemistry/metabolism[MESH] |Heterogeneous-Nuclear Ribonucleoprotein Group A-B/chemistry/metabolism[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Phosphoproteins/chemistry/metabolism[MESH] |RNA-Binding Protein FUS/chemistry/metabolism[MESH] |SARS-CoV-2/*chemistry/metabolism[MESH]SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with huma(epmc).pdf DeepDyve Pubget Overpricing