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Engineering an autonomous VH domain to modulate intracellular pathways and to interrogate the eIF4F...

Engineering an autonomous VH domain to modulate intracellular pathways and to interrogate the eIF4F...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e93e759ee68a4352930b901a4ebc4c2b

Engineering an autonomous VH domain to modulate intracellular pathways and to interrogate the eIF4F complex

About this item

Full title

Engineering an autonomous VH domain to modulate intracellular pathways and to interrogate the eIF4F complex

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2022-08, Vol.13 (1), p.4854-22, Article 4854

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

An attractive approach to target intracellular macromolecular interfaces and to model putative drug interactions is to design small high-affinity proteins. Variable domains of the immunoglobulin heavy chain (VH domains) are ideal miniproteins, but their development has been restricted by poor intracellular stability and expression. Here we show tha...

Alternative Titles

Full title

Engineering an autonomous VH domain to modulate intracellular pathways and to interrogate the eIF4F complex

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_e93e759ee68a4352930b901a4ebc4c2b

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e93e759ee68a4352930b901a4ebc4c2b

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-022-32463-1

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