001     60107
005     20200402210439.0
024 7 _ |2 pmid
|a pmid:17606418
024 7 _ |2 DOI
|a 10.1016/j.jchromb.2007.06.003
024 7 _ |2 WOS
|a WOS:000249615100032
037 _ _ |a PreJuSER-60107
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Biochemical Research Methods
084 _ _ |2 WoS
|a Chemistry, Analytical
100 1 _ |a Wiesehan, K.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB15437
245 _ _ |a Purification of recombinantly expressed and cytotoxic human amyloid-beta peptide
260 _ _ |a New York, NY [u.a.]
|b Science Direct
|c 2007
300 _ _ |a 229 - 233
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Journal of Chromatography B
|x 1570-0232
|0 3155
|v 856
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a The 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.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: isolation & purification
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: pharmacology
650 _ 2 |2 MeSH
|a Base Sequence
650 _ 2 |2 MeSH
|a Chromatography, High Pressure Liquid
650 _ 2 |2 MeSH
|a DNA Primers
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Peptide Fragments: isolation & purification
650 _ 2 |2 MeSH
|a Peptide Fragments: pharmacology
650 _ 2 |2 MeSH
|a Recombinant Proteins: isolation & purification
650 _ 2 |2 MeSH
|a Recombinant Proteins: pharmacology
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid beta-Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a DNA Primers
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptide Fragments
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a amyloid beta-protein (1-42)
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a purification
653 2 0 |2 Author
|a amyloid-beta peptide
653 2 0 |2 Author
|a cytotoxicity
653 2 0 |2 Author
|a aggregation
653 2 0 |2 Author
|a Alzheimer's disease
700 1 _ |a Funke, S. A.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB65869
700 1 _ |a Fries, M.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Willbold, D.
|b 3
|u FZJ
|0 P:(DE-Juel1)132029
773 _ _ |a 10.1016/j.jchromb.2007.06.003
|g Vol. 856, p. 229 - 233
|p 229 - 233
|q 856<229 - 233
|0 PERI:(DE-600)1491259-4
|t Journal of chromatography / B
|v 856
|y 2007
|x 1570-0232
856 7 _ |u http://dx.doi.org/10.1016/j.jchromb.2007.06.003
909 C O |o oai:juser.fz-juelich.de:60107
|p VDB
913 1 _ |k P33
|v Funktion und Dysfunktion des Nervensystems
|l Funktion und Dysfunktion des Nervensystems
|b Gesundheit
|0 G:(DE-Juel1)FUEK409
|x 0
914 1 _ |y 2007
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k INB-2
|l Molekulare Biophysik
|d 31.12.2008
|g INB
|0 I:(DE-Juel1)VDB805
|x 0
920 1 _ |k JARA-SIM
|l Jülich-Aachen Research Alliance - Simulation Sciences
|g JARA
|0 I:(DE-Juel1)VDB1045
|x 1
970 _ _ |a VDB:(DE-Juel1)94303
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a I:(DE-Juel1)VDB1045
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)VDB1045
981 _ _ |a I:(DE-Juel1)ICS-6-20110106


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