Characterization of the novel protein P9TLDR (temporal lobe down-regulated) with a brain-site-specific gene expression modality in Alzheimer's disease brain
DC Field | Value | Language |
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dc.contributor.author | Yokota, Tomoko | - |
dc.contributor.author | Akatsu, Hiroyasu | - |
dc.contributor.author | Miyauchi, Takashi | - |
dc.contributor.author | Heese, Klaus | - |
dc.date.accessioned | 2022-07-16T12:39:54Z | - |
dc.date.available | 2022-07-16T12:39:54Z | - |
dc.date.created | 2021-05-12 | - |
dc.date.issued | 2012-12 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/164087 | - |
dc.description.abstract | Alzheimer's disease (AD) is an aging-related neurodegenerative disorder characterized by irreversible loss of higher cognitive functions. The disease is characterized by the presence of amyloid plaques and neurofibrillary tangles (NFT). In the current study we isolated from an intra-cerebral brain-site-specific (AD temporal lobe vs. AD occipital lobe) polymerase chain reaction (PCR)-select cDNA suppression subtractive hybridization (PCR-cDNA-SSH) expression analysis the novel gene P9TLDR, potentially a microtubule-associated protein involved in neuronal migration, with an altered expression pattern: down-regulated in the temporal lobe cortex of early stage AD brains. In an in vitro AD-related cell model, amyloid-beta peptide (A beta)-treated neurons, reduced P9TLDR expression correlated with increased tau protein phosphorylation. In conclusion, interference with the P9TLDR signalling pathways might be a therapeutic strategy for the treatment of AD. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | Elsevier B.V. | - |
dc.title | Characterization of the novel protein P9TLDR (temporal lobe down-regulated) with a brain-site-specific gene expression modality in Alzheimer's disease brain | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Heese, Klaus | - |
dc.identifier.doi | 10.1016/j.febslet.2012.10.050 | - |
dc.identifier.scopusid | 2-s2.0-84870565960 | - |
dc.identifier.wosid | 000312004400017 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.586, no.24, pp.4357 - 4361 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 586 | - |
dc.citation.number | 24 | - |
dc.citation.startPage | 4357 | - |
dc.citation.endPage | 4361 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | SUPPRESSION SUBTRACTIVE HYBRIDIZATION | - |
dc.subject.keywordAuthor | Alzheimer&apos | - |
dc.subject.keywordAuthor | s disease | - |
dc.subject.keywordAuthor | Amyloid | - |
dc.subject.keywordAuthor | Brain | - |
dc.subject.keywordAuthor | Mapt | - |
dc.subject.keywordAuthor | Neurotoxicity | - |
dc.subject.keywordAuthor | Neurodegeneration | - |
dc.subject.keywordAuthor | Tau | - |
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