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@ARTICLE{Wiesehan:60107,
      author       = {Wiesehan, K. and Funke, S. A. and Fries, M. and Willbold,
                      D.},
      title        = {{P}urification of recombinantly expressed and cytotoxic
                      human amyloid-beta peptide},
      journal      = {Journal of chromatography / B},
      volume       = {856},
      issn         = {1570-0232},
      address      = {New York, NY [u.a.]},
      publisher    = {Science Direct},
      reportid     = {PreJuSER-60107},
      pages        = {229 - 233},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {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.},
      keywords     = {Amino Acid Sequence / Amyloid beta-Peptides: isolation $\&$
                      purification / Amyloid beta-Peptides: pharmacology / Base
                      Sequence / Chromatography, High Pressure Liquid / DNA
                      Primers / Humans / Molecular Sequence Data / Peptide
                      Fragments: isolation $\&$ purification / Peptide Fragments:
                      pharmacology / Recombinant Proteins: isolation $\&$
                      purification / Recombinant Proteins: pharmacology / Amyloid
                      beta-Peptides (NLM Chemicals) / DNA Primers (NLM Chemicals)
                      / Peptide Fragments (NLM Chemicals) / Recombinant Proteins
                      (NLM Chemicals) / amyloid beta-protein (1-42) (NLM
                      Chemicals) / J (WoSType)},
      cin          = {INB-2 / JARA-SIM},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB805 / I:(DE-Juel1)VDB1045},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemical Research Methods / Chemistry, Analytical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17606418},
      UT           = {WOS:000249615100032},
      doi          = {10.1016/j.jchromb.2007.06.003},
      url          = {https://juser.fz-juelich.de/record/60107},
}