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10.1093/glycob/cwab044 http://scihub22266oqcxt.onion/10.1093/glycob/cwab044 33997890!8241430!33997890     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Glycobiology 2021 ; 31 (9): 1080-1092 Nephropedia Template TP {{tp|p=33997890|t=2021. Variable posttranslational modifications of severe acute respiratory syndrome coronavirus 2 nucleocapsid protein |pdf=|usr=}}{{33997890}} gab.com Text Variable posttranslational modifications of severe acute respiratory syndrome coronavirus 2 nucleocapsid protein JO: Glycobiology http://www.kidney.de/pget.php?&tw=1&pmid=33997890 #FOAvip Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which causes coronavirus disease 2019 (COVID-19), started in 2019 in China and quickly spread into a global pandemic. Nucleocapsid protein (N protein) is highly conserved and is the most abundant protein in coronaviruses and is thus a potential target for both vaccine and point-of-care diagnostics. N Protein has been suggested in the literature as having posttranslational modifications (PTMs), and accurately defining these PTMs is critical for its potential use in medicine. Reports of phosphorylation of N protein have failed to provide detailed site-specific information. We have performed comprehensive glycomics, glycoproteomics and proteomics experiments on two different N protein preparations. Both were expressed in HEK293 cells; one was in-house expressed and purified without a signal peptide (SP) sequence, and the other was commercially produced with a SP channeling it through the secretory pathway. Our results show completely different PTMs on the two N protein preparations. The commercial product contained extensive N- and O-linked glycosylation as well as O-phosphorylation on site Thr393. Conversely, the native N Protein model had O-phosphorylation at Ser176 and no glycosylation, highlighting the importance of knowing the provenance of any commercial protein to be used for scientific or clinical studies. Recent studies have indicated that N protein can serve as an important diagnostic marker for COVID-19 and as a major immunogen by priming protective immune responses. Thus, detailed structural characterization of N protein may provide useful insights for understanding the roles of PTMs on viral pathogenesis, vaccine design and development of point-of-care diagnostics. Twit Text FOAVip Variable posttranslational modifications of severe acute respiratory syndrome coronavirus 2 nucleocapsid protein ????Glycobiology http://www.kidney.de/pget.php?&tw=1&pmid=33997890 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33997890 #FOAvip English Wikipedia <ref>{{Cite pmid|33997890}}</ref> Variable posttranslational modifications of severe acute respiratory syndrome coronavirus 2 nucleocapsid protein #MMPMID33997890 Supekar NT; Shajahan A; Gleinich AS; Rouhani DS; Heiss C; Chapla DG; Moremen KW; Azadi P Glycobiology 2021[Sep]; 31 (9): 1080-1092 PMID33997890show ga Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which causes coronavirus disease 2019 (COVID-19), started in 2019 in China and quickly spread into a global pandemic. Nucleocapsid protein (N protein) is highly conserved and is the most abundant protein in coronaviruses and is thus a potential target for both vaccine and point-of-care diagnostics. N Protein has been suggested in the literature as having posttranslational modifications (PTMs), and accurately defining these PTMs is critical for its potential use in medicine. Reports of phosphorylation of N protein have failed to provide detailed site-specific information. We have performed comprehensive glycomics, glycoproteomics and proteomics experiments on two different N protein preparations. Both were expressed in HEK293 cells; one was in-house expressed and purified without a signal peptide (SP) sequence, and the other was commercially produced with a SP channeling it through the secretory pathway. Our results show completely different PTMs on the two N protein preparations. The commercial product contained extensive N- and O-linked glycosylation as well as O-phosphorylation on site Thr393. Conversely, the native N Protein model had O-phosphorylation at Ser176 and no glycosylation, highlighting the importance of knowing the provenance of any commercial protein to be used for scientific or clinical studies. Recent studies have indicated that N protein can serve as an important diagnostic marker for COVID-19 and as a major immunogen by priming protective immune responses. Thus, detailed structural characterization of N protein may provide useful insights for understanding the roles of PTMs on viral pathogenesis, vaccine design and development of point-of-care diagnostics. |Amino Acid Motifs[MESH] |Amino Acid Sequence[MESH] |Binding Sites[MESH] |Coronavirus Nucleocapsid Proteins/chemistry/*metabolism[MESH] |Glycosylation[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Phosphorylation[MESH] |Protein Processing, Post-Translational/*physiology[MESH]Variable posttranslational modifications of severe acute respiratory s(epmc).pdf DeepDyve Pubget Overpricing