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000060107 0247_ $$2DOI$$a10.1016/j.jchromb.2007.06.003
000060107 0247_ $$2WOS$$aWOS:000249615100032
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000060107 041__ $$aeng
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000060107 084__ $$2WoS$$aBiochemical Research Methods
000060107 084__ $$2WoS$$aChemistry, Analytical
000060107 1001_ $$0P:(DE-Juel1)VDB15437$$aWiesehan, K.$$b0$$uFZJ
000060107 245__ $$aPurification of recombinantly expressed and cytotoxic human amyloid-beta peptide
000060107 260__ $$aNew York, NY [u.a.]$$bScience Direct$$c2007
000060107 300__ $$a229 - 233
000060107 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000060107 440_0 $$03155$$aJournal of Chromatography B$$v856$$x1570-0232
000060107 500__ $$aRecord converted from VDB: 12.11.2012
000060107 520__ $$aThe amyloid cascade hypothesis assigns the amyloid-beta peptide (Abeta) a central role in the pathogenesis of Alzheimer's disease (AD). Although there are strong efforts to biophysically characterize formation of Abeta aggregates and fibrils, as well as their prevention, progress is still severly hampered by the availability of tens of milligrams of recombinant Abeta(1-42). Here, we describe a reliable and easy procedure to recombinantly express and purify Abeta(1-42), which is fully cytotoxic and able to form fibrils without any further refolding steps. The yield of the procedure is 5-8 mg of tag-less peptide per liter culture volume.
000060107 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000060107 588__ $$aDataset connected to Web of Science, Pubmed
000060107 650_2 $$2MeSH$$aAmino Acid Sequence
000060107 650_2 $$2MeSH$$aAmyloid beta-Peptides: isolation & purification
000060107 650_2 $$2MeSH$$aAmyloid beta-Peptides: pharmacology
000060107 650_2 $$2MeSH$$aBase Sequence
000060107 650_2 $$2MeSH$$aChromatography, High Pressure Liquid
000060107 650_2 $$2MeSH$$aDNA Primers
000060107 650_2 $$2MeSH$$aHumans
000060107 650_2 $$2MeSH$$aMolecular Sequence Data
000060107 650_2 $$2MeSH$$aPeptide Fragments: isolation & purification
000060107 650_2 $$2MeSH$$aPeptide Fragments: pharmacology
000060107 650_2 $$2MeSH$$aRecombinant Proteins: isolation & purification
000060107 650_2 $$2MeSH$$aRecombinant Proteins: pharmacology
000060107 650_7 $$00$$2NLM Chemicals$$aAmyloid beta-Peptides
000060107 650_7 $$00$$2NLM Chemicals$$aDNA Primers
000060107 650_7 $$00$$2NLM Chemicals$$aPeptide Fragments
000060107 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000060107 650_7 $$00$$2NLM Chemicals$$aamyloid beta-protein (1-42)
000060107 650_7 $$2WoSType$$aJ
000060107 65320 $$2Author$$apurification
000060107 65320 $$2Author$$aamyloid-beta peptide
000060107 65320 $$2Author$$acytotoxicity
000060107 65320 $$2Author$$aaggregation
000060107 65320 $$2Author$$aAlzheimer's disease
000060107 7001_ $$0P:(DE-Juel1)VDB65869$$aFunke, S. A.$$b1$$uFZJ
000060107 7001_ $$0P:(DE-HGF)0$$aFries, M.$$b2
000060107 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b3$$uFZJ
000060107 773__ $$0PERI:(DE-600)1491259-4$$a10.1016/j.jchromb.2007.06.003$$gVol. 856, p. 229 - 233$$p229 - 233$$q856<229 - 233$$tJournal of chromatography / B$$v856$$x1570-0232$$y2007
000060107 8567_ $$uhttp://dx.doi.org/10.1016/j.jchromb.2007.06.003
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000060107 9141_ $$y2007
000060107 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000060107 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
000060107 9201_ $$0I:(DE-Juel1)VDB1045$$gJARA$$kJARA-SIM$$lJülich-Aachen Research Alliance - Simulation Sciences$$x1
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