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10.1126/science.abd4251 http://scihub22266oqcxt.onion/10.1126/science.abd4251 32694201!7464562!32694201     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       Science 2020 ; 369 (6511): 1586-1592 Nephropedia Template TP {{tp|p=32694201|t=2020. Distinct conformational states of SARS-CoV-2 spike protein |pdf=|usr=}}{{32694201}} gab.com Text Distinct conformational states of SARS-CoV-2 spike protein JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32694201 #FOAvip Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics. Twit Text FOAVip Distinct conformational states of SARS-CoV-2 spike protein ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32694201 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32694201 #FOAvip English Wikipedia <ref>{{Cite pmid|32694201}}</ref> Distinct conformational states of SARS-CoV-2 spike protein #MMPMID32694201 Cai Y; Zhang J; Xiao T; Peng H; Sterling SM; Walsh RM Jr; Rawson S; Rits-Volloch S; Chen B Science 2020[Sep]; 369 (6511): 1586-1592 PMID32694201show ga Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics. |Angiotensin-Converting Enzyme 2[MESH] |Cryoelectron Microscopy[MESH] |HEK293 Cells[MESH] |Host-Pathogen Interactions/*immunology[MESH] |Humans[MESH] |Peptidyl-Dipeptidase A/chemistry[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |Protein Structure, Secondary[MESH] |Receptors, Virus/chemistry[MESH] |Spike Glycoprotein, Coronavirus/*chemistry[MESH]Distinct conformational states of SARS-CoV-2 spike protein (epmc).pdf DeepDyve Pubget Overpricing