guest ::
| Home > Publications database > Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide A beta(1-42) by mirror image phage display > print |
| Home > Publications database > Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide A beta(1-42) by mirror image phage display > print |
| 001 | 29871 | ||
| 005 | 20200402210511.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:12898626 |
| 024 | 7 | _ | |2 DOI |a 10.1002/cbic.200300631 |
| 024 | 7 | _ | |2 WOS |a WOS:000184660400010 |
| 024 | 7 | _ | |a altmetric:21809985 |2 altmetric |
| 037 | _ | _ | |a PreJuSER-29871 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Chemistry, Medicinal |
| 100 | 1 | _ | |a Wiesehan, K. |b 0 |u FZJ |0 P:(DE-Juel1)VDB15437 |
| 245 | _ | _ | |a Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide A beta(1-42) by mirror image phage display |
| 260 | _ | _ | |a Weinheim |b Wiley-VCH |c 2003 |
| 300 | _ | _ | |a 748 - 753 |
| 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 ChemBioChem |x 1439-4227 |0 8962 |v 4 |
| 500 | _ | _ | |a Record converted from VDB: 12.11.2012 |
| 520 | _ | _ | |a A mirror image phage display approach was used to identify novel and highly specific ligands for Alzheimer's disease amyloid peptide Abeta(1-42). A randomized 12-mer peptide library presented on M13 phages was screened for peptides with binding affinity for the mirror image of Abeta(1-42). After four rounds of selection and amplification the peptides were enriched with a dominating consensus sequence. The mirror image of the most representative peptide (D-pep) was shown to bind Abeta(1-42) with a dissociation constant in the submicromolar range. Furthermore, in brain tissue sections derived from patients that suffered from Alzheimer's disease, amyloid plaques and leptomeningeal vessels containing Abeta amyloid were stained specifically with a fluorescence-labeled derivative of D-pep. Fibrillar deposits derived from other amyloidosis were not labeled by D-pep. Possible applications of this novel and highly specific Abeta ligand in diagnosis and therapy of Alzheimer's disease are discussed. |
| 536 | _ | _ | |a Neurowissenschaften |c L01 |2 G:(DE-HGF) |0 G:(DE-Juel1)FUEK255 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Alzheimer Disease: metabolism |
| 650 | _ | 2 | |2 MeSH |a Amino Acid Sequence |
| 650 | _ | 2 | |2 MeSH |a Amyloid beta-Peptides: chemistry |
| 650 | _ | 2 | |2 MeSH |a Amyloid beta-Peptides: genetics |
| 650 | _ | 2 | |2 MeSH |a Amyloid beta-Peptides: metabolism |
| 650 | _ | 2 | |2 MeSH |a Amyloidosis: metabolism |
| 650 | _ | 2 | |2 MeSH |a Brain: metabolism |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Ligands |
| 650 | _ | 2 | |2 MeSH |a Molecular Sequence Data |
| 650 | _ | 2 | |2 MeSH |a Peptide Fragments: chemistry |
| 650 | _ | 2 | |2 MeSH |a Peptide Fragments: genetics |
| 650 | _ | 2 | |2 MeSH |a Peptide Fragments: metabolism |
| 650 | _ | 2 | |2 MeSH |a Peptide Library |
| 650 | _ | 2 | |2 MeSH |a Plaque, Amyloid: genetics |
| 650 | _ | 2 | |2 MeSH |a Plaque, Amyloid: metabolism |
| 650 | _ | 2 | |2 MeSH |a Protein Binding: physiology |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Amyloid beta-Peptides |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Ligands |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Peptide Fragments |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Peptide Library |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a amyloid beta-protein (1-40) |
| 650 | _ | 7 | |a J |2 WoSType |
| 653 | 2 | 0 | |2 Author |a Alzheimer's disease |
| 653 | 2 | 0 | |2 Author |a amyloid peptide |
| 653 | 2 | 0 | |2 Author |a enantiomers |
| 653 | 2 | 0 | |2 Author |a ligand design |
| 653 | 2 | 0 | |2 Author |a phage display |
| 700 | 1 | _ | |a Buder, K. |b 1 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Linke, R. P. |b 2 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Patt, S. |b 3 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Stoldt, M. |b 4 |u FZJ |0 P:(DE-Juel1)VDB21601 |
| 700 | 1 | _ | |a Unger, E. |b 5 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Schmitt, B. |b 6 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Bucci, E. |b 7 |0 P:(DE-HGF)0 |
| 700 | 1 | _ | |a Willbold, D. |b 8 |u FZJ |0 P:(DE-Juel1)132029 |
| 773 | _ | _ | |a 10.1002/cbic.200300631 |g Vol. 4, p. 748 - 753 |p 748 - 753 |q 4<748 - 753 |0 PERI:(DE-600)2020469-3 |t ChemBioChem |v 4 |y 2003 |x 1439-4227 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1002/cbic.200300631 |
| 909 | C | O | |o oai:juser.fz-juelich.de:29871 |p VDB |
| 913 | 1 | _ | |k L01 |v Neurowissenschaften |l Funktion und Dysfunktion des Nervensystems |b Leben |0 G:(DE-Juel1)FUEK255 |x 0 |
| 914 | 1 | _ | |y 2003 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |k IBI-2 |l Biologische Strukturforschung |d 31.12.2006 |g IBI |0 I:(DE-Juel1)VDB58 |x 0 |
| 970 | _ | _ | |a VDB:(DE-Juel1)27086 |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a ConvertedRecord |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-Juel1)ISB-2-20090406 |
| 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)ICS-6-20110106 |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|