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http://purl.uniprot.org/citations/28119058 | http://www.w3.org/2000/01/rdf-schema#comment | "We examined the distribution pattern of the phosphorylated 40S ribosomal subunit protein S6, a downstream target of the mTOR pathway, in the brains of 24-months-old human tau transgenic pR5 mice, non-transgenic littermates and in human hippocampi. We studied baseline levels of phosphorylated S6 and a possible effect of tau pathology. S6 phosphorylated at Ser235/236 (pS6Ser235/236) or Ser240/244 (pS6Ser240/244) has been used as a read-out of mTOR activity in several studies. The mTOR pathway regulates a wide variety of cellular functions including cell growth, ribosome biosynthesis, translational control and autophagy. Its dysregulation might underlie the neurodegenerative pathology of Alzheimer's disease and other tauopathies. pS6Ser235/236 and pS6Ser240/244 immunoreactivity in the mouse brain were widespread and similar distributed, but intensive pS6Ser235/236 immunoreactivity was more selective, especially highlighting certain brainstem regions. In the human hippocampus mainly granulovacuolar inclusions in neurons displayed pS6Ser235/236 immunoreactivity. In contrast, a considerable number of neurons displayed pS6Ser240/244 immunoreactivity in the cytoplasm without labeling of granulovacuolar inclusions. Except for a tendency of lower numbers of intensely phosphorylated S6-positive neurons in pR5 mice, the pattern of distribution of pS6Ser235/236 and pS6Ser240/244 immunoreactivity was largely unchanged when compared with non-transgenic mice and also when human hippocampi from AD cases and controls were compared. Similar to pR5 mice most neurons with hyper-phosphorylated tau in human hippocampi displayed no or only weak labeling for phosphorylated S6, suggesting that phosphorylated S6 is not especially associated with pathological tau, but is rather a feature of unaffected neurons."xsd:string |
http://purl.uniprot.org/citations/28119058 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.brainres.2017.01.016"xsd:string |
http://purl.uniprot.org/citations/28119058 | http://purl.uniprot.org/core/author | "Kohler C."xsd:string |
http://purl.uniprot.org/citations/28119058 | http://purl.uniprot.org/core/author | "Dinekov M."xsd:string |
http://purl.uniprot.org/citations/28119058 | http://purl.uniprot.org/core/author | "Klingebiel M."xsd:string |
http://purl.uniprot.org/citations/28119058 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/28119058 | http://purl.uniprot.org/core/name | "Brain Res"xsd:string |
http://purl.uniprot.org/citations/28119058 | http://purl.uniprot.org/core/pages | "121-135"xsd:string |
http://purl.uniprot.org/citations/28119058 | http://purl.uniprot.org/core/title | "Analysis of ribosomal protein S6 baseline phosphorylation and effect of tau pathology in the murine brain and human hippocampus."xsd:string |
http://purl.uniprot.org/citations/28119058 | http://purl.uniprot.org/core/volume | "1659"xsd:string |
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