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The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibr...

The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibr...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10533390

The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils

About this item

Full title

The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils

Publisher

London: Nature Publishing Group UK

Journal title

Nature chemistry, 2023-10, Vol.15 (10), p.1340-1349

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The maturation of liquid-like protein condensates into amyloid fibrils has been associated with several neurodegenerative diseases. However, the molecular mechanisms underlying this liquid-to-solid transition have remained largely unclear. Here we analyse the amyloid formation mediated by condensation of the low-complexity domain of hnRNPA1, a prot...

Alternative Titles

Full title

The interface of condensates of the hnRNPA1 low-complexity domain promotes formation of amyloid fibrils

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10533390

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10533390

Other Identifiers

ISSN

1755-4330

E-ISSN

1755-4349

DOI

10.1038/s41557-023-01289-9

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