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].
97-100
Amen, Triana
388dc540-e819-4d07-8f1e-ee0f3949a54b
Kaganovich, Daniel
ebb13f4e-e925-4aef-88e7-ddc25ef52d8f
3 March 2016
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), .
(doi:10.15698/mic2016.03.482).
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].
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Published date: 3 March 2016
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Local EPrints ID: 475600
URI: http://eprints.soton.ac.uk/id/eprint/475600
ISSN: 2311-2638
PURE UUID: 4d54e7a4-4ece-4f94-a465-f3f233685325
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Date deposited: 22 Mar 2023 17:36
Last modified: 17 Mar 2024 04:22
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Author:
Triana Amen
Author:
Daniel Kaganovich
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