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N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell li...

N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell li...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_93a8586e551741e0bef6fe5c6e66c9f0

N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line

About this item

Full title

N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2024-01, Vol.15 (1), p.393-393, Article 393

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

IgG secreted by B cells carry asparagine N(297)-linked glycans in the fragment crystallizable (Fc) region. Changes in Fc glycosylation are related to health or disease and are functionally relevant, as IgG without Fc glycans cannot bind to Fcɣ receptors or complement factors. However, it is currently unknown whether ɣ-heavy chain (ɣHC) glycans also...

Alternative Titles

Full title

N-linked Fc glycosylation is not required for IgG-B-cell receptor function in a GC-derived B-cell line

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_93a8586e551741e0bef6fe5c6e66c9f0

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_93a8586e551741e0bef6fe5c6e66c9f0

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-023-44468-5

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