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000020882 0247_ $$2pmid$$apmid:22533419
000020882 0247_ $$2DOI$$a10.1089/rej.2011.1262
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000020882 041__ $$aeng
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000020882 084__ $$2WoS$$aGeriatrics & Gerontology
000020882 1001_ $$0P:(DE-Juel1)VDB101069$$aFunke, S.A.$$b0$$uFZJ
000020882 245__ $$aIdentification and characterization of an Aß; oligomer precipitating peptide that may be useful to explore gene therapeutic approaches to Alzheimer's disease
000020882 260__ $$aLarchmont, NY$$bLiebert$$c2012
000020882 300__ $$a144 - 147
000020882 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000020882 440_0 $$018202$$aRejuvenation Research$$v15$$x1549-1684$$y2
000020882 500__ $$aThe authors gratefully acknowledge support from the "Helmholtz-CSC (China Scholarship Council) Junior Scientists Exchange Program" for Hongmei Liu.
000020882 520__ $$aA 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.
000020882 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000020882 536__ $$0G:(DE-Juel1)FUEK505$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000020882 588__ $$aDataset connected to Web of Science, Pubmed
000020882 650_2 $$2MeSH$$aAlzheimer Disease: genetics
000020882 650_2 $$2MeSH$$aAlzheimer Disease: therapy
000020882 650_2 $$2MeSH$$aAmyloid beta-Peptides: chemistry
000020882 650_2 $$2MeSH$$aAnimals
000020882 650_2 $$2MeSH$$aCell Line, Tumor
000020882 650_2 $$2MeSH$$aCentrifugation, Density Gradient
000020882 650_2 $$2MeSH$$aDisease Models, Animal
000020882 650_2 $$2MeSH$$aGene Therapy: methods
000020882 650_2 $$2MeSH$$aHumans
000020882 650_2 $$2MeSH$$aMice
000020882 650_2 $$2MeSH$$aNephelometry and Turbidimetry
000020882 650_2 $$2MeSH$$aNeurons: metabolism
000020882 650_2 $$2MeSH$$aPeptides: chemistry
000020882 650_2 $$2MeSH$$aSequence Analysis, DNA
000020882 650_2 $$2MeSH$$aThiazoles: chemistry
000020882 650_7 $$00$$2NLM Chemicals$$aAmyloid beta-Peptides
000020882 650_7 $$00$$2NLM Chemicals$$aPeptides
000020882 650_7 $$00$$2NLM Chemicals$$aThiazoles
000020882 650_7 $$02390-54-7$$2NLM Chemicals$$athioflavin T
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000020882 7001_ $$0P:(DE-Juel1)VDB4104$$aLiu, H.$$b1$$uFZJ
000020882 7001_ $$0P:(DE-Juel1)VDB86041$$aSehl, T.$$b2$$uFZJ
000020882 7001_ $$0P:(DE-Juel1)VDB65461$$aBartnik, D.$$b3$$uFZJ
000020882 7001_ $$0P:(DE-Juel1)VDB89561$$aBrener, O.$$b4$$uFZJ
000020882 7001_ $$0P:(DE-Juel1)VDB72731$$aNagel-Steger, L.$$b5$$uFZJ
000020882 7001_ $$0P:(DE-Juel1)VDB15437$$aWiesehan, K.$$b6$$uFZJ
000020882 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b7$$uFZJ
000020882 773__ $$0PERI:(DE-600)2155984-3$$a10.1089/rej.2011.1262$$gVol. 15, p. 144 - 147$$p144 - 147$$q15<144 - 147$$tRejuvenation research$$v15$$x1549-1684$$y2012
000020882 8567_ $$uhttp://dx.doi.org/10.1089/rej.2011.1262
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000020882 9141_ $$y2012
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