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NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_04c38fed278645e2a4a1f52a4ea229f4

NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

About this item

Full title

NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2022-06, Vol.13 (1), p.3380-17, Article 3380

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

A G4C2 hexanucleotide repeat expansion in the
C9orf72
gene is the most common genetic cause of ALS and FTLD (C9-ALS/FTLD) with cytoplasmic TDP-43 inclusions observed in regions of neurodegeneration. The accumulation of repetitive RNAs and dipeptide repeat protein (DPR) are two proposed mechanisms of toxicity in C9-ALS/FTLD and linked to impai...

Alternative Titles

Full title

NUP62 localizes to ALS/FTLD pathological assemblies and contributes to TDP-43 insolubility

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_04c38fed278645e2a4a1f52a4ea229f4

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_04c38fed278645e2a4a1f52a4ea229f4

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-022-31098-6

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