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Structural basis for receptor binding and broader interspecies receptor recognition of currently cir...

Structural basis for receptor binding and broader interspecies receptor recognition of currently cir...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_9c7ccb952a7d4249a69ee47d1977771a

Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants

About this item

Full title

Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2023-07, Vol.14 (1), p.4405-4405, Article 4405

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Multiple SARS-CoV-2 Omicron sub-variants, such as BA.2, BA.2.12.1, BA.4, and BA.5, emerge one after another. BA.5 has become the dominant strain worldwide. Additionally, BA.2.75 is significantly increasing in some countries. Exploring their receptor binding and interspecies transmission risk is urgently needed. Herein, we examine the binding capaci...

Alternative Titles

Full title

Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_9c7ccb952a7d4249a69ee47d1977771a

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_9c7ccb952a7d4249a69ee47d1977771a

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-023-39942-z

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