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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2003-12-25
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pubmed:abstractText |
NMR spectroscopy of the full-length neuronal Tau protein has proved to be difficult due to the length of the protein and the unfavorable amino acid composition. We show that the random-coil chemical shift values and their dependence on the presence of a proline residue in the (i+1) position can successfully be exploited to assign all proline-directed phosphorylation sites. This is a first step toward the study of the phosphorylation of Tau by NMR spectroscopy.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1439-4227
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
73-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
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pubmed:year |
2004
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pubmed:articleTitle |
Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites.
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pubmed:affiliation |
CNRS-Université de Lille 2 UMR 8525, Institut Pasteur de Lille, BP 245 59019 Lille Cedex, France. Guy.Lippens@pasteur-lille.fr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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