Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments

By A. Alonso, T. Zaidi, M. Novák, I. Grundke‐Iqbal, K. Iqbal. Proceedings of the National Academy of Sciences of the United States of America, 2001

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Tau pathology in Alzheimer disease and other tauopathies. (2005, background): “[58]).”
Tau in Alzheimer Disease and Related Tauopathies (2010, background): “Both the amino terminal and the carboxy terminal flanking regions to the microtubule binding repeats in normal tau appear to inhibit its self-aggregation into filaments and on AD type abnormal hyperphosphorylation, i.e., the phosphorylation of the amino terminal and the carboxy terminal flanking reg”
Role of tau protein in both physiological and pathological conditions. (2004, background): “Indeed, strong evidence exists that the phosphorylation of tau promotes its self-assembly (5).”
Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation (2005, background): “…hyperphosphorylation of tau is believed to be responsible for its loss of biological activity, for its gain of toxic activity and for its aggregation into PHFs (Iqbal et al., 1986; Alonso et al., 1994; 2001a,b; Lucas et al., 2001; Fath et al., 2002; Jackson et al., 2002; Perez et al., 2002).”
Mechanisms of tau-induced neurodegeneration (2009, neutral): “PHF/SF in vitro under physiological conditions of protein concentration, pH, ionic strength, and reducing conditions [6].”