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| 001 | 138852 | ||
| 005 | 20240524120323.0 | ||
| 024 | 7 | _ | |a 10.1186/s40478-016-0381-9 |2 doi |
| 024 | 7 | _ | |a pmid:27724899 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC5057504 |2 pmc |
| 024 | 7 | _ | |a altmetric:12565012 |2 altmetric |
| 037 | _ | _ | |a DZNE-2020-05174 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 610 |
| 100 | 1 | _ | |a Mazzitelli, Sonia |0 P:(DE-2719)2812690 |b 0 |e First author |u dzne |
| 245 | _ | _ | |a Amyloid-β 1-24 C-terminal truncated fragment promotes amyloid-β 1-42 aggregate formation in the healthy brain. |
| 260 | _ | _ | |a London |c 2016 |b Biomed Central |
| 264 | _ | 1 | |3 online |2 Crossref |b Springer Science and Business Media LLC |c 2016-10-10 |
| 264 | _ | 1 | |3 print |2 Crossref |b Springer Science and Business Media LLC |c 2016-12-01 |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1716542636_5216 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Substantial data indicate that amyloid-β (Aβ), the major component of senile plaques, plays a central role in Alzheimer's Disease and indeed the assembly of naturally occurring amyloid peptides into cytotoxic aggregates is linked to the disease pathogenesis. Although Aβ42 is a highly aggregating form of Aβ, the co-occurrence of shorter Aβ peptides might affect the aggregation potential of the Aβ pool. In this study we aimed to assess whether the structural behavior of human Aβ42 peptide inside the brain is influenced by the concomitant presence of N-terminal fragments produced by the proteolytic activity of glial cells. We show that the occurrence of the human C-terminal truncated 1-24 Aβ fragment impairs Aβ42 clearance through blood brain barrier and promotes the formation of Aβ42 aggregates even in the healthy brain. By showing that Aβ1-24 has seeding properties for aggregate formation in intracranially injected wild type mice, our study provide the proof-of-concept that peptides produced upon Aβ42 cleavage by activated glial cells may cause phenotypic defects even in the absence of genetic mutations associated with Alzheimer's Disease, possibly contributing to the development of the sporadic form of the pathology. |
| 536 | _ | _ | |a 345 - Population Studies and Genetics (POF3-345) |0 G:(DE-HGF)POF3-345 |c POF3-345 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a Amyloid beta-Peptides |2 NLM Chemicals |
| 650 | _ | 7 | |a Peptide Fragments |2 NLM Chemicals |
| 650 | _ | 7 | |a amyloid beta-peptide (1-24) |2 NLM Chemicals |
| 650 | _ | 7 | |a amyloid beta-protein (1-42) |2 NLM Chemicals |
| 650 | _ | 7 | |a Matrix Metalloproteinase 9 |0 EC 3.4.24.35 |2 NLM Chemicals |
| 650 | _ | 7 | |a Mmp9 protein, mouse |0 EC 3.4.24.35 |2 NLM Chemicals |
| 650 | _ | 2 | |a Alzheimer Disease: metabolism |2 MeSH |
| 650 | _ | 2 | |a Alzheimer Disease: pathology |2 MeSH |
| 650 | _ | 2 | |a Amyloid beta-Peptides: administration & dosage |2 MeSH |
| 650 | _ | 2 | |a Amyloid beta-Peptides: metabolism |2 MeSH |
| 650 | _ | 2 | |a Animals |2 MeSH |
| 650 | _ | 2 | |a Brain: metabolism |2 MeSH |
| 650 | _ | 2 | |a Brain: pathology |2 MeSH |
| 650 | _ | 2 | |a Disease Models, Animal |2 MeSH |
| 650 | _ | 2 | |a Humans |2 MeSH |
| 650 | _ | 2 | |a Learning Disabilities: metabolism |2 MeSH |
| 650 | _ | 2 | |a Learning Disabilities: pathology |2 MeSH |
| 650 | _ | 2 | |a Matrix Metalloproteinase 9: genetics |2 MeSH |
| 650 | _ | 2 | |a Matrix Metalloproteinase 9: metabolism |2 MeSH |
| 650 | _ | 2 | |a Memory Disorders: metabolism |2 MeSH |
| 650 | _ | 2 | |a Memory Disorders: pathology |2 MeSH |
| 650 | _ | 2 | |a Mice |2 MeSH |
| 650 | _ | 2 | |a Mice, Inbred BALB C |2 MeSH |
| 650 | _ | 2 | |a Mice, Inbred C57BL |2 MeSH |
| 650 | _ | 2 | |a Mice, Knockout |2 MeSH |
| 650 | _ | 2 | |a Mice, Transgenic |2 MeSH |
| 650 | _ | 2 | |a Microglia: metabolism |2 MeSH |
| 650 | _ | 2 | |a Microglia: pathology |2 MeSH |
| 650 | _ | 2 | |a Motor Activity: physiology |2 MeSH |
| 650 | _ | 2 | |a Peptide Fragments: administration & dosage |2 MeSH |
| 650 | _ | 2 | |a Peptide Fragments: metabolism |2 MeSH |
| 650 | _ | 2 | |a Plaque, Amyloid: metabolism |2 MeSH |
| 650 | _ | 2 | |a Plaque, Amyloid: pathology |2 MeSH |
| 650 | _ | 2 | |a Protein Folding |2 MeSH |
| 650 | _ | 2 | |a Protein Multimerization |2 MeSH |
| 650 | _ | 2 | |a Social Behavior |2 MeSH |
| 700 | 1 | _ | |a Filipello, Fabia |b 1 |
| 700 | 1 | _ | |a Rasile, Marco |b 2 |
| 700 | 1 | _ | |a Lauranzano, Eliana |b 3 |
| 700 | 1 | _ | |a Starvaggi-Cucuzza, Chiara |b 4 |
| 700 | 1 | _ | |a Tamborini, Matteo |b 5 |
| 700 | 1 | _ | |a Pozzi, Davide |b 6 |
| 700 | 1 | _ | |a Barajon, Isabella |b 7 |
| 700 | 1 | _ | |a Giorgino, Toni |b 8 |
| 700 | 1 | _ | |a Natalello, Antonino |b 9 |
| 700 | 1 | _ | |a Matteoli, Michela |0 P:(DE-HGF)0 |b 10 |e Corresponding author |
| 773 | 1 | 8 | |a 10.1186/s40478-016-0381-9 |b : Springer Science and Business Media LLC, 2016-10-10 |n 1 |p 110 |3 journal-article |2 Crossref |t Acta Neuropathologica Communications |v 4 |y 2016 |x 2051-5960 |
| 773 | _ | _ | |a 10.1186/s40478-016-0381-9 |g Vol. 4, no. 1, p. 110 |0 PERI:(DE-600)2715589-4 |n 1 |q 4:1<110 |p 110 |t Acta Neuropathologica Communications |v 4 |y 2016 |x 2051-5960 |
| 856 | 4 | _ | |y OpenAccess |u https://pub.dzne.de/record/138852/files/DZNE-2020-05174.pdf |
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| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5057504 |
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