Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses
Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses
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Publisher
London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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Soluble aggregates of the microtubule-associated protein tau have been challenging to assemble and characterize, despite their important role in the development of tauopathies. We found that sequential hyperphosphorylation by protein kinase A in conjugation with either glycogen synthase kinase 3β or stress activated protein kinase 4 enabled recombi...
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Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses
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TN_cdi_doaj_primary_oai_doaj_org_article_bc2803e2004a427bb2eed72cdc9d158e
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bc2803e2004a427bb2eed72cdc9d158e
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-022-30461-x
