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Metamorphism in TDP-43 prion-like domain determines chaperone recognition

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_9a9166e33ea74700a35643c8927458e0

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

About this item

Full title

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2023-01, Vol.14 (1), p.466-15, Article 466

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The RNA binding protein TDP-43 forms cytoplasmic inclusions via its C-terminal prion-like domain in several neurodegenerative diseases. Aberrant TDP-43 aggregation arises upon phase de-mixing and transitions from liquid to solid states, following still unknown structural conversions which are primed by oxidative stress and chaperone inhibition. Des...

Alternative Titles

Full title

Metamorphism in TDP-43 prion-like domain determines chaperone recognition

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_9a9166e33ea74700a35643c8927458e0

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_9a9166e33ea74700a35643c8927458e0

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-023-36023-z

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