pubmed-article:1472994 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C2700455 | lld:lifeskim |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C0031603 | lld:lifeskim |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C0597162 | lld:lifeskim |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C1158884 | lld:lifeskim |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C1947974 | lld:lifeskim |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
pubmed-article:1472994 | lifeskim:mentions | umls-concept:C1720655 | lld:lifeskim |
pubmed-article:1472994 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:1472994 | pubmed:dateCreated | 1993-2-3 | lld:pubmed |
pubmed-article:1472994 | pubmed:abstractText | We performed phosphate analysis of tau proteins isolated from normal human brain, tau proteins associated with paired helical filaments (PHF-tau), and Alzheimer tau not associated with PHF. These tau fractions were of high purity. Normal and Alzheimer tau were purified by heat treatment, acid extraction and calmodulin-affinity chromatography with or without HPLC. Fractions containing primarily PHF-tau polypeptides of 60, 64 and 68 kDa and their degraded fragments were purified either on a sucrose density gradient as filaments (PHF) or by heat treatment and acid extraction as amorphous proteins (PHF-tau). PHF and PHF-tau were found to contain 6-8 mol phosphate/mol protein while normal and Alzheimer tau proteins contained 1.9 and 2.6 mol phosphate/mol protein, respectively. Upon 2-h incubation with alkaline phosphatase, PHF lost two of the phosphate groups without apparent changes in the stability and morphology of PHF. The released phosphate originated from the N-terminal half of PHF-tau as determined by immunoblotting with antibodies to epitopes blocked by phosphorylation. Tau-1 and E-2, and by a prominent shift in the electrophoretic mobility of some fragments of PHF-tau. The shift in mobility was not observed with the C-terminal fragments of 25-26 kDa, which retained the epitope to Tau 46. The results suggest that the phosphorylation sites not affected by phosphatase may be located in the 25-26 kDa C-terminal region of PHF-tau and may play a role in structural stability of PHF. | lld:pubmed |
pubmed-article:1472994 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1472994 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1472994 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1472994 | pubmed:language | eng | lld:pubmed |
pubmed-article:1472994 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1472994 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1472994 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1472994 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1472994 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1472994 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1472994 | pubmed:month | Dec | lld:pubmed |
pubmed-article:1472994 | pubmed:issn | 0006-8993 | lld:pubmed |
pubmed-article:1472994 | pubmed:author | pubmed-author:RaoL MLM | lld:pubmed |
pubmed-article:1472994 | pubmed:author | pubmed-author:LiuW KWK | lld:pubmed |
pubmed-article:1472994 | pubmed:author | pubmed-author:Ksiezak-Redin... | lld:pubmed |
pubmed-article:1472994 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1472994 | pubmed:day | 4 | lld:pubmed |
pubmed-article:1472994 | pubmed:volume | 597 | lld:pubmed |
pubmed-article:1472994 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1472994 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1472994 | pubmed:pagination | 209-19 | lld:pubmed |
pubmed-article:1472994 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:1472994 | pubmed:meshHeading | pubmed-meshheading:1472994-... | lld:pubmed |
pubmed-article:1472994 | pubmed:meshHeading | pubmed-meshheading:1472994-... | lld:pubmed |
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pubmed-article:1472994 | pubmed:meshHeading | pubmed-meshheading:1472994-... | lld:pubmed |
pubmed-article:1472994 | pubmed:year | 1992 | lld:pubmed |
pubmed-article:1472994 | pubmed:articleTitle | Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments. | lld:pubmed |
pubmed-article:1472994 | pubmed:affiliation | Department of Pathology, Albert Einstein College of Medicine, Bronx, NY 10461. | lld:pubmed |
pubmed-article:1472994 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1472994 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1472994 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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