To elucidate the role cAMP-dependent protein kinase (PKA) phosphorylations on tau play in
Alzheimer's disease, we have generated highly specific monoclonal antibodies, CP-3 and …

Microtubule-associated protein tau from Alzheimer brain has been shown to be
phosphorylated at several ser/thr-pro and ser/thr-X sites (Hasegawa, M. et al., J. Biol. Chem …

Phosphorylation of tau protein at Ser-262 has been shown to diminish its ability to bind to
taxol-stabilized microtubules. The paired helical filaments (PHFs) found in Alzheimer's …

Of 21 phosphorylation sites identified in PHF-tau 11 are on ser/thr-X motifs and are probably
phosphorylated by non-proline-dependent protein kinases (non-PDPKs). The identities of …

Hyperphosphorylation of tau is a hallmark of Alzheimer's disease and other tauopathies.
Although the mechanisms underlying hyperphosphorylation are not fully understood …

Tau protein from Alzheimer disease (AD) brain is phosphorylated at eleven Ser/Thr‐Pro and
nine Ser/Thr‐X sites. The former sites are phosphorylated by proline‐dependent protein …

We have shown earlier that certain proline‐directed kinases such as MAP kinase or GSK‐3
can phosphorylate tau protein in an abnormal manner reminiscent of tau from Alzheimer …

Previously, we determined sites of tau protein phosphorylation by tau protein kinase (TPK)
I/glycogen synthase kinase 3β (GSK-3β) and TPKII/(cyclin-dependent kinase 5 (CDK5)+ …

Tau protein is an integral component of paired helical filaments, a pathological feature of
Alzheimer's disease. tau extracted from these filaments displays decreased electrophoretic …

Alterations in the status of microtubules contribute tothe cytoskeletal rearrangements that
occur during apoptosis. Themicrotubule‐associated protein tau regulates microtubule …