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Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approac...

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approac...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_fc5801f1b98b49f29a52e09a1075880f

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

About this item

Full title

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

Publisher

England: BioMed Central Ltd

Journal title

Molecular neurodegeneration, 2024-02, Vol.19 (1), p.20-32, Article 20

Language

English

Formats

Publication information

Publisher

England: BioMed Central Ltd

More information

Scope and Contents

Contents

The conversion of native peptides and proteins into amyloid aggregates is a hallmark of over 50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence implicates misfolded protein oligomers produced during the amyloid formation process as the primary cytotoxic agents in many of these devastating conditions. In this rev...

Alternative Titles

Full title

Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_fc5801f1b98b49f29a52e09a1075880f

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_fc5801f1b98b49f29a52e09a1075880f

Other Identifiers

ISSN

1750-1326

E-ISSN

1750-1326

DOI

10.1186/s13024-023-00651-2

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