Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils
The authors present a method for the conversion of full-length tau protein into seeding-competent amyloid fibrils without heparin or other negatively charged co-factors, which could be useful for studying the effects of post-translational modifications on Tau aggregation as well as to identify poten...
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2021-07-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-24362-8 |
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doaj-4ae08ea82f3e4f1da86a83d9dfe205fb2021-07-11T11:43:11ZengNature Publishing GroupNature Communications2041-17232021-07-0112111210.1038/s41467-021-24362-8Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrilsPijush Chakraborty0Gwladys Rivière1Shu Liu2Alain Ibáñez de Opakua3Rıza Dervişoğlu4Alina Hebestreit5Loren B. Andreas6Ina M. Vorberg7Markus Zweckstetter8German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)Department for NMR-based Structural Biology, Max Planck Institute for Biophysical ChemistryGerman Center for Neurodegenerative Diseases (DZNE)Department for NMR-based Structural Biology, Max Planck Institute for Biophysical ChemistryGerman Center for Neurodegenerative Diseases (DZNE)German Center for Neurodegenerative Diseases (DZNE)The authors present a method for the conversion of full-length tau protein into seeding-competent amyloid fibrils without heparin or other negatively charged co-factors, which could be useful for studying the effects of post-translational modifications on Tau aggregation as well as to identify potential inhibitors of tau aggregation. Biochemical experiments and solid-state NMR spectroscopy measurements show that these co-factor-free tau fibrils have similar properties as amyloid fibrils isolated from brain tissue but differ from those of commonly used heparin-induced tau fibrils.https://doi.org/10.1038/s41467-021-24362-8 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
Pijush Chakraborty Gwladys Rivière Shu Liu Alain Ibáñez de Opakua Rıza Dervişoğlu Alina Hebestreit Loren B. Andreas Ina M. Vorberg Markus Zweckstetter |
| spellingShingle |
Pijush Chakraborty Gwladys Rivière Shu Liu Alain Ibáñez de Opakua Rıza Dervişoğlu Alina Hebestreit Loren B. Andreas Ina M. Vorberg Markus Zweckstetter Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils Nature Communications |
| author_facet |
Pijush Chakraborty Gwladys Rivière Shu Liu Alain Ibáñez de Opakua Rıza Dervişoğlu Alina Hebestreit Loren B. Andreas Ina M. Vorberg Markus Zweckstetter |
| author_sort |
Pijush Chakraborty |
| title |
Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils |
| title_short |
Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils |
| title_full |
Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils |
| title_fullStr |
Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils |
| title_full_unstemmed |
Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils |
| title_sort |
co-factor-free aggregation of tau into seeding-competent rna-sequestering amyloid fibrils |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2021-07-01 |
| description |
The authors present a method for the conversion of full-length tau protein into seeding-competent amyloid fibrils without heparin or other negatively charged co-factors, which could be useful for studying the effects of post-translational modifications on Tau aggregation as well as to identify potential inhibitors of tau aggregation. Biochemical experiments and solid-state NMR spectroscopy measurements show that these co-factor-free tau fibrils have similar properties as amyloid fibrils isolated from brain tissue but differ from those of commonly used heparin-induced tau fibrils. |
| url |
https://doi.org/10.1038/s41467-021-24362-8 |
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