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• W3121306688 startingPage "126" @default.
• W3121306688 abstract "Abstract Intraneuronal accumulation of hyperphosphorylated tau is a pathological hallmark of several neurodegenerative disorders, including Alzheimer's disease. Phosphorylation plays a crucial role in modulating the tau‐microtubule interaction and the ability of the protein to aggregate, but despite efforts during the past decades, the real identity of the kynases involved in vivo remains uncertain. Here, for the first time, we demonstrate that the cGMP‐dependent protein kinase G (PKG) phosphorylates tau in both in vitro and in vivo models. More intriguingly, we provide evidence that PKG phosphorylates tau at Ser214 but not at Ser202, a condition that could reduce the pathological aggregation of the protein shifting tau from a pro‐aggregant to a neuroprotective anti‐aggregant conformation." @default.
• W3121306688 created "2021-02-01" @default.
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• W3121306688 date "2021-01-01" @default.
• W3121306688 modified "2023-09-30" @default.
• W3121306688 title "Protein kinase G phosphorylates the Alzheimer's disease‐associated tau protein at distinct Ser/Thr sites" @default.
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• W3121306688 doi "https://doi.org/10.1002/biof.1705" @default.
• W3121306688 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33469985" @default.
• W3121306688 hasPublicationYear "2021" @default.
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