Hauptseite > Publikationsdatenbank > Differently Selected D-Enantiomeric Peptides Act on Different A beta Species > print |
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 |
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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 |
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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 |
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980 | _ | _ | |a UNRESTRICTED |
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