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.

10.1021/acs.analchem.0c03173 http://scihub22266oqcxt.onion/10.1021/acs.analchem.0c03173 33406838!7805595!33406838     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       Anal+Chem 2021 ; 93 (4): 2003-2009 Nephropedia Template TP {{tp|p=33406838|t=2021. N- and O-Glycosylation of the SARS-CoV-2 Spike Protein |pdf=|usr=}}{{33406838}} gab.com Text N- and O-Glycosylation of the SARS-CoV-2 Spike Protein JO: Anal Chem http://www.kidney.de/pget.php?&tw=1&pmid=33406838 #FOAvip Covid-19 pandemic outbreak is the reason of the current world health crisis. The development of effective antiviral compounds and vaccines requires detailed descriptive studies of SARS-CoV-2 proteins. The SARS-CoV-2 spike (S) protein mediates virion binding to the human cells through its interaction with the ACE2 cell surface receptor and is one of the prime immunization targets. A functional virion is composed of three S1 and three S2 subunits created by furin cleavage of the spike protein at R682, a polybasic cleavage site that differs from the SARS-CoV spike protein of 2002. By analysis of the protein produced in HEK293 cells, we observe that the spike is O-glycosylated on a threonine (T678) near the furin cleavage site occupied by core-1 and core-2 structures. In addition, we have identified eight additional O-glycopeptides on the spike glycoprotein and confirmed that the spike protein is heavily N-glycosylated. Our recently developed liquid chromatography-mass spectrometry methodology allowed us to identify LacdiNAc structural motifs on all occupied N-glycopeptides and polyLacNAc structures on six glycopeptides of the spike protein. In conclusion, our study substantially expands the current knowledge of the spike protein's glycosylation and enables the investigation of the influence of O-glycosylation on its proteolytic activation. Twit Text FOAVip N- and O-Glycosylation of the SARS-CoV-2 Spike Protein ????Anal Chem http://www.kidney.de/pget.php?&tw=1&pmid=33406838 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33406838 #FOAvip English Wikipedia <ref>{{Cite pmid|33406838}}</ref> N- and O-Glycosylation of the SARS-CoV-2 Spike Protein #MMPMID33406838 Sanda M; Morrison L; Goldman R Anal Chem 2021[Feb]; 93 (4): 2003-2009 PMID33406838show ga Covid-19 pandemic outbreak is the reason of the current world health crisis. The development of effective antiviral compounds and vaccines requires detailed descriptive studies of SARS-CoV-2 proteins. The SARS-CoV-2 spike (S) protein mediates virion binding to the human cells through its interaction with the ACE2 cell surface receptor and is one of the prime immunization targets. A functional virion is composed of three S1 and three S2 subunits created by furin cleavage of the spike protein at R682, a polybasic cleavage site that differs from the SARS-CoV spike protein of 2002. By analysis of the protein produced in HEK293 cells, we observe that the spike is O-glycosylated on a threonine (T678) near the furin cleavage site occupied by core-1 and core-2 structures. In addition, we have identified eight additional O-glycopeptides on the spike glycoprotein and confirmed that the spike protein is heavily N-glycosylated. Our recently developed liquid chromatography-mass spectrometry methodology allowed us to identify LacdiNAc structural motifs on all occupied N-glycopeptides and polyLacNAc structures on six glycopeptides of the spike protein. In conclusion, our study substantially expands the current knowledge of the spike protein's glycosylation and enables the investigation of the influence of O-glycosylation on its proteolytic activation. |Chromatography, Liquid[MESH] |Glycosylation[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Mass Spectrometry[MESH] |SARS-CoV-2/*metabolism[MESH]N- and O-Glycosylation of the SARS-CoV-2 Spike Protein (epmc).pdf DeepDyve Pubget Overpricing