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TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence

TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e3e9e519f6b84b0e8f7d6e0867082a16

TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence

About this item

Full title

TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2024-01, Vol.15 (1), p.244-244, Article 244

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Viruses, as opportunistic intracellular parasites, hijack the cellular machinery of host cells to support their survival and propagation. Numerous viral proteins are subjected to host-mediated post-translational modifications. Here, we demonstrate that the SARS-CoV-2 nucleocapsid protein (SARS2-NP) is SUMOylated on the lysine 65 residue, which effi...

Alternative Titles

Full title

TRIM28-mediated nucleocapsid protein SUMOylation enhances SARS-CoV-2 virulence

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_e3e9e519f6b84b0e8f7d6e0867082a16

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e3e9e519f6b84b0e8f7d6e0867082a16

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-023-44502-6

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