Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1038/s42003-021-02250-7 http://scihub22266oqcxt.onion/10.1038/s42003-021-02250-7 34117354!8196010!34117354     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Commun+Biol 2021 ; 4 (1): 724 Nephropedia Template TP {{tp|p=34117354|t=2021. Structural basis of coronavirus E protein interactions with human PALS1 PDZ domain |pdf=|usr=}}{{34117354}} gab.com Text Structural basis of coronavirus E protein interactions with human PALS1 PDZ domain JO: Commun Biol http://www.kidney.de/pget.php?&tw=1&pmid=34117354 #FOAvip SARS-CoV-2 infection leads to coronavirus disease 2019 (COVID-19), which is associated with severe and life-threatening pneumonia and respiratory failure. However, the molecular basis of these symptoms remains unclear. SARS-CoV-1 E protein interferes with control of cell polarity and cell-cell junction integrity in human epithelial cells by binding to the PALS1 PDZ domain, a key component of the Crumbs polarity complex. We show that C-terminal PDZ binding motifs of SARS-CoV-1 and SARS-CoV-2 E proteins bind the PALS1 PDZ domain with 29.6 and 22.8 muM affinity, whereas the related sequence from MERS-CoV did not bind. We then determined crystal structures of PALS1 PDZ domain bound to both SARS-CoV-1 and SARS-CoV-2 E protein PDZ binding motifs. Our findings establish the structural basis for SARS-CoV-1/2 mediated subversion of Crumbs polarity signalling and serve as a platform for the development of small molecule inhibitors to suppress SARS-CoV-1/2 mediated disruption of polarity signalling in epithelial cells. Twit Text FOAVip Structural basis of coronavirus E protein interactions with human PALS1 PDZ domain ????Commun Biol http://www.kidney.de/pget.php?&tw=1&pmid=34117354 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34117354 #FOAvip English Wikipedia <ref>{{Cite pmid|34117354}}</ref> Structural basis of coronavirus E protein interactions with human PALS1 PDZ domain #MMPMID34117354 Javorsky A; Humbert PO; Kvansakul M Commun Biol 2021[Jun]; 4 (1): 724 PMID34117354show ga SARS-CoV-2 infection leads to coronavirus disease 2019 (COVID-19), which is associated with severe and life-threatening pneumonia and respiratory failure. However, the molecular basis of these symptoms remains unclear. SARS-CoV-1 E protein interferes with control of cell polarity and cell-cell junction integrity in human epithelial cells by binding to the PALS1 PDZ domain, a key component of the Crumbs polarity complex. We show that C-terminal PDZ binding motifs of SARS-CoV-1 and SARS-CoV-2 E proteins bind the PALS1 PDZ domain with 29.6 and 22.8 muM affinity, whereas the related sequence from MERS-CoV did not bind. We then determined crystal structures of PALS1 PDZ domain bound to both SARS-CoV-1 and SARS-CoV-2 E protein PDZ binding motifs. Our findings establish the structural basis for SARS-CoV-1/2 mediated subversion of Crumbs polarity signalling and serve as a platform for the development of small molecule inhibitors to suppress SARS-CoV-1/2 mediated disruption of polarity signalling in epithelial cells. |*PDZ Domains[MESH] |Amino Acid Sequence[MESH] |Coronavirus Envelope Proteins/*chemistry/*metabolism[MESH] |Humans[MESH] |Membrane Proteins/*chemistry/*metabolism[MESH] |Models, Molecular[MESH] |Nucleoside-Phosphate Kinase/*chemistry/*metabolism[MESH]Structural basis of coronavirus E protein interactions with human PALS(epmc).pdf DeepDyve Pubget Overpricing