The University of Southampton
University of Southampton Institutional Repository

Yeast screening platform identifies FDA-approved drugs that reduce Aβ oligomerization

Yeast screening platform identifies FDA-approved drugs that reduce Aβ oligomerization
Yeast screening platform identifies FDA-approved drugs that reduce Aβ oligomerization
The older the average person alive today becomes, the more instances of neuro degeneration are observed worldwide. Alzheimer's disease is the most common neuro degenerative disorder preferentially affecting older individuals with 26.6 million cases recorded in 2006. It is estimated that worldwide prevalence will rise to 100 millioncases by 2050 [1]. There is currently no effective treatmentnor preventative therapy for Alzheimer's disease, and nodefinitive diagnosis besides post-mortem pathology. Diagnosis is based on the presence of intracellular inclusions of hyper phosphorylated microtubule associated protein tauand extracellular plaques consisting of amyloid beta (Aβ)peptide [2]. Aβ is a small peptide 40-42 aa in length, formed via amyloid precursor protein (APP) cleavage that results in Aβ release into the extracellular space. Aβ is normally observed circulating in the cerebrospinal fluid of mammals, and is produced mostly in the central nervous system [3]. Although Aβ aggregates are the major pathological hallmark of Alzheimer’s disease, the mechanisms ofAβ induced neurotoxicity is not well understood, and even less is known about the physiological function of Aβ peptide. Absence of APP results in embryonic development defects due to irregular migration of cerebral cortex neurons [4]. Recent work also indicates that Aβ peptide concentrations in the CNS modulate synaptic transmission and synaptic hyperactivity via direct binding to APP [5].
2311-2638
97-100
Amen, Triana
388dc540-e819-4d07-8f1e-ee0f3949a54b
Kaganovich, Daniel
ebb13f4e-e925-4aef-88e7-ddc25ef52d8f
Amen, Triana
388dc540-e819-4d07-8f1e-ee0f3949a54b
Kaganovich, Daniel
ebb13f4e-e925-4aef-88e7-ddc25ef52d8f

Amen, Triana and Kaganovich, Daniel (2016) Yeast screening platform identifies FDA-approved drugs that reduce Aβ oligomerization. Microbial Cell, 3 (3), 97-100. (doi:10.15698/mic2016.03.482).

Record type: Article

Abstract

The older the average person alive today becomes, the more instances of neuro degeneration are observed worldwide. Alzheimer's disease is the most common neuro degenerative disorder preferentially affecting older individuals with 26.6 million cases recorded in 2006. It is estimated that worldwide prevalence will rise to 100 millioncases by 2050 [1]. There is currently no effective treatmentnor preventative therapy for Alzheimer's disease, and nodefinitive diagnosis besides post-mortem pathology. Diagnosis is based on the presence of intracellular inclusions of hyper phosphorylated microtubule associated protein tauand extracellular plaques consisting of amyloid beta (Aβ)peptide [2]. Aβ is a small peptide 40-42 aa in length, formed via amyloid precursor protein (APP) cleavage that results in Aβ release into the extracellular space. Aβ is normally observed circulating in the cerebrospinal fluid of mammals, and is produced mostly in the central nervous system [3]. Although Aβ aggregates are the major pathological hallmark of Alzheimer’s disease, the mechanisms ofAβ induced neurotoxicity is not well understood, and even less is known about the physiological function of Aβ peptide. Absence of APP results in embryonic development defects due to irregular migration of cerebral cortex neurons [4]. Recent work also indicates that Aβ peptide concentrations in the CNS modulate synaptic transmission and synaptic hyperactivity via direct binding to APP [5].

This record has no associated files available for download.

More information

Published date: 3 March 2016

Identifiers

Local EPrints ID: 475600
URI: http://eprints.soton.ac.uk/id/eprint/475600
ISSN: 2311-2638
PURE UUID: 4d54e7a4-4ece-4f94-a465-f3f233685325
ORCID for Triana Amen: ORCID iD orcid.org/0000-0003-4808-7806
ORCID for Daniel Kaganovich: ORCID iD orcid.org/0000-0003-2398-1596

Catalogue record

Date deposited: 22 Mar 2023 17:36
Last modified: 17 Mar 2024 04:22

Export record

Altmetrics

Contributors

Author: Triana Amen ORCID iD
Author: Daniel Kaganovich ORCID iD

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×