| A new method to measure cellular toxicity of non-fibrillar and fibrillar Alzheimer's Abeta using yeast. | |
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MedLine Citation:
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PMID: 18376056 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The 42 amino acid amyloid-beta (Abeta) can exist in multiple physical states including oligomers and fibrils. This study shows that fibril formation is hastened by the biological buffers required to support the growth of mammalian cells, but is prevented if Abeta is maintained in water. Here we describe a method to produce Abeta in oligomeric form and the comparison of stable fibrillar and non-fibrillar forms in cell toxicity studies in water, achieved through the use of yeast. We show that extracellular, non-fibrillar Abeta causes a dose dependent loss of cell viability while fibrillar Abeta has low toxicity. |
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Authors:
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Prashant Bharadwaj; Lynne Waddington; Jose Varghese; Ian G Macreadie |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Journal of Alzheimer's disease : JAD Volume: 13 ISSN: 1387-2877 ISO Abbreviation: J. Alzheimers Dis. Publication Date: 2008 Mar |
Date Detail:
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Created Date: 2008-03-31 Completed Date: 2008-06-10 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9814863 Medline TA: J Alzheimers Dis Country: Netherlands |
Other Details:
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Languages: eng Pagination: 147-50 Citation Subset: IM |
Affiliation:
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CSIRO Molecular and Health Technologies and P-Health Flagship, Parkville, VIC, Australia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Aged Alzheimer Disease / metabolism*, physiopathology* Amyloid / metabolism*, ultrastructure Amyloid beta-Protein / metabolism* Candida glabrata / metabolism*, ultrastructure Cells, Cultured Humans Microscopy, Electron Peptide Fragments / toxicity* Solubility |
| Chemical | |
Reg. No./Substance:
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0/Amyloid; 0/Amyloid beta-Protein; 0/Peptide Fragments |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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