1992
DOI: 10.1016/s0021-9258(18)48531-6
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Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau.

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Cited by 482 publications
(55 citation statements)
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“…By MS, we observe that Tau from PrP-CAA (Q160X) is phosphorylated at S 199 and S 202 , while Tau from GSS (F198S) is phosphorylated at S 202 ; however, Tau deposits were immunoreactive for the AT8 phosphoepitope (phosphorylation at residues S 202 and T 205 but also other epitopes, including S 199 and S 208 ) [ 41 ] by immunohistochemistry, immunoblotting, and immuno-EM methods. PHF-1 also decorates Tau aggregates in PrP-CAA (Q160X) and GSS (F198S) (not shown), and by MS, we are able to detect the phosphorylated residues S 396 and S 404 , which constitute the epitope recognized by antibody PHF-1 (directed against the doubly phosphorylated epitope S 396 and S 404 ) [ 29 , 32 ]. The MS data also show deamidation of N 279 , which has been suggested to contribute to the AD folds as opposed to the folds seen in CBD [ 3 , 7 ].…”
Section: Discussionmentioning
confidence: 99%
“…By MS, we observe that Tau from PrP-CAA (Q160X) is phosphorylated at S 199 and S 202 , while Tau from GSS (F198S) is phosphorylated at S 202 ; however, Tau deposits were immunoreactive for the AT8 phosphoepitope (phosphorylation at residues S 202 and T 205 but also other epitopes, including S 199 and S 208 ) [ 41 ] by immunohistochemistry, immunoblotting, and immuno-EM methods. PHF-1 also decorates Tau aggregates in PrP-CAA (Q160X) and GSS (F198S) (not shown), and by MS, we are able to detect the phosphorylated residues S 396 and S 404 , which constitute the epitope recognized by antibody PHF-1 (directed against the doubly phosphorylated epitope S 396 and S 404 ) [ 29 , 32 ]. The MS data also show deamidation of N 279 , which has been suggested to contribute to the AD folds as opposed to the folds seen in CBD [ 3 , 7 ].…”
Section: Discussionmentioning
confidence: 99%
“…It was also found to be stable when purified using TCA (data not shown) ( 62 ). Heat stability is an inherent property of tau as an aggregation-prone and intrinsically unstructured protein without a hydrophobic core ( 63 , 64 , 65 ) and is widely used as a method for separation of tau from other abundant proteins ( 2 , 63 , 64 ). In contrast to tau, other synaptic proteins were not heat stable.…”
Section: Discussionmentioning
confidence: 99%
“…Mouse anti-phopsho-Tau (ser 396/404) PHF-1 was a kind gift from Dr. Peter Davies, Albert Einstein College of Medicine, New York, NY (Greenberg et al, 1992). The following commercial primary antibodies were used: anti-Reelin (clone G10) (Chemicon); anti-phospho-Tau (ser202/thr205, clone AT8, Innogenetics); anti-total Tau (clone Tau-5, Millipore); anti-total Tau K9JA (DAKO, A0024); anti-actin (Chemicon, MAB1501); anti-phospho-Tau T205 (ThermoFisher, 44-738G); antineurofilament (NF200, Sigma, N4142); anti-calbindin (Swant, CB38); anti-MAP2 (Sigma, M1406); anti-human Tau HT7 (Thermofisher, MN1000); and anti-β Galactosidase (AB986, Millipore).…”
Section: Antibodiesmentioning
confidence: 99%