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001     9877
005     20200402205835.0
024 7 _ |2 pmid
|a pmid:19954333
024 7 _ |2 DOI
|a 10.1089/rej.2009.0924
024 7 _ |2 WOS
|a WOS:000277602200017
024 7 _ |a altmetric:21804052
|2 altmetric
037 _ _ |a PreJuSER-9877
041 _ _ |a eng
082 _ _ |a 610
084 _ _ |2 WoS
|a Geriatrics & Gerontology
100 1 _ |a Bartnik, D.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB65461
245 _ _ |a Differently Selected D-Enantiomeric Peptides Act on Different A beta Species
260 _ _ |a Larchmont, NY
|b Liebert
|c 2010
300 _ _ |a
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 Rejuvenation Research
|x 1549-1684
|0 18202
|y 2
|v 13
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Aging is the most significant risk factor for Alzheimer disease (AD). The pathological hallmark of AD is the accumulation of aggregated amyloid-beta (Abeta) forms and insoluble plaques, mainly composed of Abeta, in the brain of the patient. Recently, we reported on the selection of D-enantiomeric, Abeta-binding peptides D1 and D3. D1 was selected against aggregated Abeta species to address diagnosis by in vivo imaging of amyloid plaques, whereas D3 was selected using low-molecular-weight Abeta species, therefore addressing therapeutical studies. Here, we use a surface plasmon resonance method to confirm that both peptides show the desired binding specificities.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
536 _ _ |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|c P45
|0 G:(DE-Juel1)FUEK505
|x 1
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Alzheimer Disease: diagnosis
650 _ 2 |2 MeSH
|a Alzheimer Disease: metabolism
650 _ 2 |2 MeSH
|a Alzheimer Disease: pathology
650 _ 2 |2 MeSH
|a Amyloid: analysis
650 _ 2 |2 MeSH
|a Amyloid: chemistry
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: chemistry
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: drug effects
650 _ 2 |2 MeSH
|a Amyloid beta-Peptides: metabolism
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Oligopeptides: chemistry
650 _ 2 |2 MeSH
|a Oligopeptides: metabolism
650 _ 2 |2 MeSH
|a Oligopeptides: pharmacology
650 _ 2 |2 MeSH
|a Peptide Fragments: chemistry
650 _ 2 |2 MeSH
|a Peptide Fragments: isolation & purification
650 _ 2 |2 MeSH
|a Peptide Fragments: metabolism
650 _ 2 |2 MeSH
|a Peptide Fragments: pharmacology
650 _ 2 |2 MeSH
|a Plaque, Amyloid: chemistry
650 _ 2 |2 MeSH
|a Plaque, Amyloid: drug effects
650 _ 2 |2 MeSH
|a Plaque, Amyloid: metabolism
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Isoforms: analysis
650 _ 2 |2 MeSH
|a Protein Isoforms: chemistry
650 _ 2 |2 MeSH
|a Protein Multimerization: drug effects
650 _ 2 |2 MeSH
|a Substrate Specificity
650 _ 2 |2 MeSH
|a Surface Plasmon Resonance
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid
650 _ 7 |0 0
|2 NLM Chemicals
|a Amyloid beta-Peptides
650 _ 7 |0 0
|2 NLM Chemicals
|a D3 peptide
650 _ 7 |0 0
|2 NLM Chemicals
|a Oligopeptides
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptide Fragments
650 _ 7 |0 0
|2 NLM Chemicals
|a Protein Isoforms
650 _ 7 |a J
|2 WoSType
700 1 _ |a Funke, S. A.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB65869
700 1 _ |a Andrei-Selmer, L.C.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Bacher, M.
|b 3
|0 P:(DE-HGF)0
700 1 _ |a Dodel, R.
|b 4
|0 P:(DE-HGF)0
700 1 _ |a Willbold, D.
|b 5
|u FZJ
|0 P:(DE-Juel1)132029
773 _ _ |a 10.1089/rej.2009.0924
|g Vol. 13
|q 13
|0 PERI:(DE-600)2155984-3
|t Rejuvenation research
|v 13
|y 2010
|x 1549-1684
909 C O |o oai:juser.fz-juelich.de:9877
|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
913 1 _ |k P45
|v BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung
|l Biologische Informationsverarbeitung
|b Schlüsseltechnologien
|0 G:(DE-Juel1)FUEK505
|x 1
913 2 _ |a DE-HGF
|b Key Technologies
|l BioSoft Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences
|1 G:(DE-HGF)POF3-550
|0 G:(DE-HGF)POF3-553
|2 G:(DE-HGF)POF3-500
|v Physical Basis of Diseases
|x 0
914 1 _ |y 2010
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |d 31.12.2010
|g ISB
|k ISB-3
|l Strukturbiochemie
|0 I:(DE-Juel1)VDB942
|x 0
920 1 _ |0 I:(DE-82)080012_20140620
|k JARA-HPC
|l Jülich Aachen Research Alliance - High-Performance Computing
|g JARA
|x 1
970 _ _ |a VDB:(DE-Juel1)119984
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a I:(DE-82)080012_20140620
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)VDB1346

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