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Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril

Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e31f43f0213d4f06865cd6238d6a6ca0

Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril

About this item

Full title

Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2023-07, Vol.14 (1), p.4293-4293, Article 4293

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Amyloid fibrils have emerged as innovative tools to enhance the transduction efficiency of retroviral vectors in gene therapy strategies. In this study, we used cryo-electron microscopy to analyze the structure of a biotechnologically engineered peptide fibril that enhances retroviral infectivity. Our findings show that the peptide undergoes a time...

Alternative Titles

Full title

Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_e31f43f0213d4f06865cd6238d6a6ca0

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e31f43f0213d4f06865cd6238d6a6ca0

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-023-40042-1

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