001     20882
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024 7 _ |2 pmid
|a pmid:22533419
024 7 _ |2 DOI
|a 10.1089/rej.2011.1262
024 7 _ |2 WOS
|a WOS:000303383600008
037 _ _ |a PreJuSER-20882
041 _ _ |a eng
082 _ _ |a 610
084 _ _ |2 WoS
|a Geriatrics & Gerontology
100 1 _ |a Funke, S.A.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB101069
245 _ _ |a Identification and characterization of an Aß; oligomer precipitating peptide that may be useful to explore gene therapeutic approaches to Alzheimer's disease
260 _ _ |a Larchmont, NY
|b Liebert
|c 2012
300 _ _ |a 144 - 147
336 7 _ |a Journal Article
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336 7 _ |a article
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440 _ 0 |a Rejuvenation Research
|x 1549-1684
|0 18202
|y 2
|v 15
500 _ _ |a The authors gratefully acknowledge support from the "Helmholtz-CSC (China Scholarship Council) Junior Scientists Exchange Program" for Hongmei Liu.
520 _ _ |a A key feature of Alzheimer disease (AD) is the pathologic self-association of the amyloid-β (Aβ) peptide, leading to the formation of diffusible toxic Aβ oligomers and extracellular amyloid plaques. Next to extracellular Aβ, intraneuronal Aβ has important pathological functions in AD. Agents that specifically interfere with the oligomerization processes either outside or inside of neurons are highly desired for the elucidation of the pathologic mechanisms of AD and might even pave the way for new AD gene therapeutic approaches. Here, we characterize the Aβ binding peptide L3 and its influence on Aβ oligomerization in vitro. Preliminary studies in cell culture demonstrate that stably expressed L3 reduces cell toxicity of externally added Aβ in neuroblastoma cells.
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588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Alzheimer Disease: genetics
650 _ 2 |2 MeSH
|a Alzheimer Disease: therapy
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: chemistry
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Cell Line, Tumor
650 _ 2 |2 MeSH
|a Centrifugation, Density Gradient
650 _ 2 |2 MeSH
|a Disease Models, Animal
650 _ 2 |2 MeSH
|a Gene Therapy: methods
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Mice
650 _ 2 |2 MeSH
|a Nephelometry and Turbidimetry
650 _ 2 |2 MeSH
|a Neurons: metabolism
650 _ 2 |2 MeSH
|a Peptides: chemistry
650 _ 2 |2 MeSH
|a Sequence Analysis, DNA
650 _ 2 |2 MeSH
|a Thiazoles: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid beta-Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptides
650 _ 7 |0 0
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|a Thiazoles
650 _ 7 |0 2390-54-7
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650 _ 7 |a J
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700 1 _ |a Liu, H.
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700 1 _ |a Sehl, T.
|b 2
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700 1 _ |a Bartnik, D.
|b 3
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700 1 _ |a Brener, O.
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700 1 _ |a Nagel-Steger, L.
|b 5
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700 1 _ |a Wiesehan, K.
|b 6
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|0 P:(DE-Juel1)VDB15437
700 1 _ |a Willbold, D.
|b 7
|u FZJ
|0 P:(DE-Juel1)132029
773 _ _ |a 10.1089/rej.2011.1262
|g Vol. 15, p. 144 - 147
|p 144 - 147
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|0 PERI:(DE-600)2155984-3
|t Rejuvenation research
|v 15
|y 2012
|x 1549-1684
856 7 _ |u http://dx.doi.org/10.1089/rej.2011.1262
909 C O |o oai:juser.fz-juelich.de:20882
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913 1 _ |b Gesundheit
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914 1 _ |y 2012
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