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https://doi.org/10.1038/srep15231
DC Field | Value | |
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dc.title | Identification of disulfide cross-linked tau dimer responsible for tau propagation | |
dc.contributor.author | Kim, D | |
dc.contributor.author | Lim, S | |
dc.contributor.author | Haque, M.M | |
dc.contributor.author | Ryoo, N | |
dc.contributor.author | Hong, H.S | |
dc.contributor.author | Rhim, H | |
dc.contributor.author | Lee, D.-E | |
dc.contributor.author | Chang, Y.-T | |
dc.contributor.author | Lee, J.-S | |
dc.contributor.author | Cheong, E | |
dc.contributor.author | Kim, D.J | |
dc.contributor.author | Kim, Y.K | |
dc.date.accessioned | 2020-10-26T08:55:44Z | |
dc.date.available | 2020-10-26T08:55:44Z | |
dc.date.issued | 2015 | |
dc.identifier.citation | Kim, D, Lim, S, Haque, M.M, Ryoo, N, Hong, H.S, Rhim, H, Lee, D.-E, Chang, Y.-T, Lee, J.-S, Cheong, E, Kim, D.J, Kim, Y.K (2015). Identification of disulfide cross-linked tau dimer responsible for tau propagation. Scientific Reports 5 : 15231. ScholarBank@NUS Repository. https://doi.org/10.1038/srep15231 | |
dc.identifier.issn | 2045-2322 | |
dc.identifier.uri | https://scholarbank.nus.edu.sg/handle/10635/180425 | |
dc.description.abstract | Recent evidence suggests that tau aggregates are not only neurotoxic, but also propagate in neurons acting as a seed for native tau aggregation. Prion-like tau transmission is now considered as an important pathogenic mechanism driving the progression of tau pathology in the brain. However, prion-like tau species have not been clearly characterized. To identify infectious tau conformers, here we prepared diverse tau aggregates and evaluated the effect on inducing intracellular tau-aggregation. Among tested, tau dimer containing P301L-mutation is identified as the most infectious form to induce tau pathology. Biochemical analysis reveals that P301L-tau dimer is covalently cross-linked with a disulfide bond. The relatively small and covalently cross-linked tau dimer induced tau pathology efficiently in primary neurons and also in tau-transgenic mice. So far, the importance of tau disulfide cross-linking has been overlooked in the study of tau pathology. Here our results suggested that tau disulfide cross-linking might play critical role in tau propagation by producing structurally stable and small tau conformers. | |
dc.publisher | Nature Publishing Group | |
dc.rights | Attribution 4.0 International | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.source | Unpaywall 20201031 | |
dc.subject | disulfide | |
dc.subject | tau protein | |
dc.subject | animal | |
dc.subject | brain | |
dc.subject | cell culture | |
dc.subject | chemistry | |
dc.subject | cytology | |
dc.subject | dimerization | |
dc.subject | fluorescence microscopy | |
dc.subject | genetics | |
dc.subject | HEK293 cell line | |
dc.subject | human | |
dc.subject | metabolism | |
dc.subject | mouse | |
dc.subject | mutagenesis | |
dc.subject | nerve cell | |
dc.subject | pathology | |
dc.subject | rat | |
dc.subject | transgenic mouse | |
dc.subject | transmission electron microscopy | |
dc.subject | Animals | |
dc.subject | Brain | |
dc.subject | Cells, Cultured | |
dc.subject | Dimerization | |
dc.subject | Disulfides | |
dc.subject | HEK293 Cells | |
dc.subject | Humans | |
dc.subject | Mice | |
dc.subject | Mice, Transgenic | |
dc.subject | Microscopy, Electron, Transmission | |
dc.subject | Microscopy, Fluorescence | |
dc.subject | Mutagenesis | |
dc.subject | Neurons | |
dc.subject | Rats | |
dc.subject | tau Proteins | |
dc.type | Article | |
dc.contributor.department | CHEMISTRY | |
dc.description.doi | 10.1038/srep15231 | |
dc.description.sourcetitle | Scientific Reports | |
dc.description.volume | 5 | |
dc.description.page | 15231 | |
dc.published.state | published | |
Appears in Collections: | Elements Staff Publications |
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