| http://purl.uniprot.org/citations/34235568 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/34235568 | http://www.w3.org/2000/01/rdf-schema#comment | "The COVID-19 pandemic is caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Similar to other coronaviruses, its particles are composed of four structural proteins: spike (S), envelope (E), membrane (M), and nucleocapsid (N) proteins. S, E, and M proteins are glycosylated, and the N protein is phosphorylated. The S protein is involved in the interaction with the host receptor human angiotensin-converting enzyme 2 (hACE2), which is also heavily glycosylated. Recent studies have revealed several other potential host receptors or factors that can increase or modulate the SARS-CoV-2 infection. Interestingly, most of these molecules bear carbohydrate residues. While glycans acquired by the viruses through the hijacking of the host machinery help the viruses in their infectivity, they also play roles in immune evasion or modulation. Glycans play complex roles in viral pathobiology, both on their own and in association with carrier biomolecules, such as proteins or glycosaminoglycans (GAGs). Understanding these roles in detail can help in developing suitable strategies for prevention and therapy of COVID-19. In this review, we sought to emphasize the interplay of SARS-CoV-2 glycosylated proteins and their host receptors in viral attachment, entry, replication, and infection. Moreover, the implications for future therapeutic interventions targeting these glycosylated biomolecules are also discussed in detail."xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.org/dc/terms/identifier | "doi:10.1007/s00216-021-03499-x"xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/author | "Azadi P."xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/author | "Shajahan A."xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/author | "Heiss C."xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/author | "Rouhani D.S."xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/author | "Pepi L.E."xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/name | "Anal Bioanal Chem"xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/pages | "7179-7193"xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/title | "Glycosylation of SARS-CoV-2: structural and functional insights."xsd:string |
| http://purl.uniprot.org/citations/34235568 | http://purl.uniprot.org/core/volume | "413"xsd:string |
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