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10.1038/s41594-019-0334-7 http://scihub22266oqcxt.onion/10.1038/s41594-019-0334-7 31792450!7097669!31792450     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 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Struct+Mol+Biol 2019 ; 26 (12): 1151-1157 Nephropedia Template TP {{tp|p=31792450|t=2019. Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors |pdf=|usr=}}{{31792450}} gab.com Text Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=31792450 #FOAvip The Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe and often lethal respiratory illness in humans, and no vaccines or specific treatments are available. Infections are initiated via binding of the MERS-CoV spike (S) glycoprotein to sialosides and dipeptidyl-peptidase 4 (the attachment and entry receptors, respectively). To understand MERS-CoV engagement of sialylated receptors, we determined the cryo-EM structures of S in complex with 5-N-acetyl neuraminic acid, 5-N-glycolyl neuraminic acid, sialyl-Lewis(X), alpha2,3-sialyl-N-acetyl-lactosamine and alpha2,6-sialyl-N-acetyl-lactosamine at 2.7-3.0 A resolution. We show that recognition occurs via a conserved groove that is essential for MERS-CoV S-mediated attachment to sialosides and entry into human airway epithelial cells. Our data illuminate MERS-CoV S sialoside specificity and suggest that selectivity for alpha2,3-linked over alpha2,6-linked receptors results from enhanced interactions with the former class of oligosaccharides. This study provides a structural framework explaining MERS-CoV attachment to sialoside receptors and identifies a site of potential vulnerability to inhibitors of viral entry. Twit Text FOAVip Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=31792450 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=31792450 #FOAvip English Wikipedia <ref>{{Cite pmid|31792450}}</ref> Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors #MMPMID31792450 Park YJ; Walls AC; Wang Z; Sauer MM; Li W; Tortorici MA; Bosch BJ; DiMaio F; Veesler D Nat Struct Mol Biol 2019[Dec]; 26 (12): 1151-1157 PMID31792450show ga The Middle East respiratory syndrome coronavirus (MERS-CoV) causes severe and often lethal respiratory illness in humans, and no vaccines or specific treatments are available. Infections are initiated via binding of the MERS-CoV spike (S) glycoprotein to sialosides and dipeptidyl-peptidase 4 (the attachment and entry receptors, respectively). To understand MERS-CoV engagement of sialylated receptors, we determined the cryo-EM structures of S in complex with 5-N-acetyl neuraminic acid, 5-N-glycolyl neuraminic acid, sialyl-Lewis(X), alpha2,3-sialyl-N-acetyl-lactosamine and alpha2,6-sialyl-N-acetyl-lactosamine at 2.7-3.0 A resolution. We show that recognition occurs via a conserved groove that is essential for MERS-CoV S-mediated attachment to sialosides and entry into human airway epithelial cells. Our data illuminate MERS-CoV S sialoside specificity and suggest that selectivity for alpha2,3-linked over alpha2,6-linked receptors results from enhanced interactions with the former class of oligosaccharides. This study provides a structural framework explaining MERS-CoV attachment to sialoside receptors and identifies a site of potential vulnerability to inhibitors of viral entry. |Binding Sites[MESH] |Carbohydrate Conformation[MESH] |Cryoelectron Microscopy[MESH] |Dipeptidyl Peptidase 4/chemistry/metabolism/ultrastructure[MESH] |Hemagglutination, Viral[MESH] |Humans[MESH] |Middle East Respiratory Syndrome Coronavirus/*chemistry[MESH] |Models, Molecular[MESH] |Protein Binding[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Interaction Mapping[MESH] |Sialic Acids/chemistry/*metabolism[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/metabolism/ultrastructure[MESH]Structures of MERS-CoV spike glycoprotein in complex with sialoside at(epmc).pdf DeepDyve Pubget Overpricing