001     56233
005     20180211180240.0
024 7 _ |2 DOI
|a 10.2174/092986607780363970
024 7 _ |2 WOS
|a WOS:000246346800012
037 _ _ |a PreJuSER-56233
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Kastenholz, B.
|b 0
|u FZJ
|0 P:(DE-Juel1)129343
245 _ _ |a New hope for the diagnosis and therapy of Alzheimer's disease
260 _ _ |a Schiphol
|b Bentham Science Publ.
|c 2007
300 _ _ |a 389 - 393
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
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 Protein and Peptide Letters
|x 0929-8665
|0 15161
|v 14
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Improperly folded metal cofactor-containing proteins (e.g., copper chaperone for Superoxide dismutase, CCS) are believed to play a key role in several protein-misfolding diseases (e.g., Alzheimer's disease or Amyotrophic Lateral Sclerosis) because Under regular physiological conditions, metallochaperolles activate or stabilize the native conformation of important metalloproteins (e.g., superoxide dismutase) in certain Cellular processes. For an improved diagnosis and therapy of neurodegenerative diseases, new methodologies have to be developed that enable a well-defined differentiation between properly folded and inactive metalloproteins in clinical samples. In the literature it is reported that different high molecular mass metal-containing proteins were isolated in brain samples from Alzheimer's patients and in vegetables by using a 2-dimensional polyacrylamide gel electrophoresis (2-DE) procedure. In the present article, selected results of these studies are Scrutinized and compared with some results obtained by a standardized method termed 'quantitative preparative native continuous polycrylamide gel electrophoresis (QPNC-PAGE)'. Conclusively, QPNC-PAGE is a highly efficient approach used by biochemists to resolve native and denatured metalloproteins (MW 6 - >= 200 kDa) in complex protein Mixtures.
536 _ _ |a Terrestrische Umwelt
|c P24
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK407
|x 0
588 _ _ |a Dataset connected to Web of Science
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a QPNC-PAGE
653 2 0 |2 Author
|a 2-DE
653 2 0 |2 Author
|a GPC
653 2 0 |2 Author
|a NMR
653 2 0 |2 Author
|a CCS
653 2 0 |2 Author
|a Alzheimer's disease
653 2 0 |2 Author
|a isoelectric point
653 2 0 |2 Author
|a native conformation
653 2 0 |2 Author
|a breakthrough method
653 2 0 |2 Author
|a biofluids
653 2 0 |2 Author
|a cadmium protein
653 2 0 |2 Author
|a folding
653 2 0 |2 Author
|a Arabidopsis
653 2 0 |2 Author
|a metal cofactor
653 2 0 |2 Author
|a get structure
773 _ _ |a 10.2174/092986607780363970
|g Vol. 14, p. 389 - 393
|p 389 - 393
|q 14<389 - 393
|0 PERI:(DE-600)2136373-0
|t Protein and peptide letters
|v 14
|y 2007
|x 0929-8665
856 7 _ |u http://dx.doi.org/10.2174/092986607780363970
909 C O |o oai:juser.fz-juelich.de:56233
|p VDB
913 1 _ |k P24
|v Terrestrische Umwelt
|l Terrestrische Umwelt
|b Erde und Umwelt
|0 G:(DE-Juel1)FUEK407
|x 0
914 1 _ |y 2007
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k ICG-3
|l Phytosphäre
|d 31.10.2010
|g ICG
|0 I:(DE-Juel1)ICG-3-20090406
|x 1
970 _ _ |a VDB:(DE-Juel1)88185
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)IBG-2-20101118
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBG-2-20101118
981 _ _ |a I:(DE-Juel1)ICG-3-20090406


LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21