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Distinct differences in prion-like seeding and aggregation between Tau protein variants provide mechanistic insights into tauopathies

Strang, Kevin H., Croft, Cara L., Sorrentino, Zachary A., Chakrabarty, Paramita, Golde, Todd E., Giasson, Benoit I.·2018·Journal of Biological Chemistry
DOI 10.1074/jbc.m117.815357
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  • The tau mutations have confirmed prion properties.

    “Thus, these mutations, that have confirmed prion properties (11), were selected by us as exemplars of different tau conformers that could form tau tangles in an accelerated manner.”

    From Combinatorial model of amyloid β and tau reveals synergy between amyloid deposits and tangle formation (2022) · cites this paper as [11]

    The Discussion reports robust prion-like seeding for specific tau mutants at Pro 301 and Ser 320, supporting the choice of those mutants as aggregation exemplars. It does not establish that tau mutations generally have confirmed prion properties; other mutants tested did not readily aggregate when seeded. Page numbers are unavailable in our copy. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • S320F tau shows self-aggregating properties in cell culture.

    “whereas the S320F tau showed self-aggregating properties in cell culture (11) and in nonTG mice (10).”

    From Combinatorial model of amyloid β and tau reveals synergy between amyloid deposits and tangle formation (2022) · cites this paper as [11]

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Research works printed but not linked: 66

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Metadata

Authors
Strang, K. H., Croft, C. L., Sorrentino, Z. A., Chakrabarty, P., Golde, T. E., & Giasson, B. I.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2018-02
Volume
293
Issue
7
Pages
2408-2421
ISSN
0021-9258
DOI
10.1074/jbc.m117.815357
Cited by
124
References
17
Language
en
Update notices
correction (2018-03-23)
Licence
Funders
National Institutes of Health (R01NS089022)

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