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The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the...

The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_08be2b23ecf04e69a5cf2cce0b6b8737

The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the Prognosis of Alzheimer’s Disease

About this item

Full title

The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the Prognosis of Alzheimer’s Disease

Publisher

Switzerland: MDPI AG

Journal title

Biomolecules (Basel, Switzerland), 2023-06, Vol.13 (7), p.1051

Language

English

Formats

Publication information

Publisher

Switzerland: MDPI AG

More information

Scope and Contents

Contents

Functional changes in chaperone systems play a major role in the decline of cognition and contribute to neurological pathologies, such as Alzheimer’s disease (AD). While such a decline may occur naturally with age or with stress or trauma, the mechanisms involved have remained elusive. The current models suggest that amyloid-β (Aβ) plaque formation...

Alternative Titles

Full title

The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by Which LA1011 May Improve the Prognosis of Alzheimer’s Disease

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_08be2b23ecf04e69a5cf2cce0b6b8737

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_08be2b23ecf04e69a5cf2cce0b6b8737

Other Identifiers

ISSN

2218-273X

E-ISSN

2218-273X

DOI

10.3390/biom13071051

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