期刊
BIOCHEMICAL SOCIETY TRANSACTIONS
卷 38, 期 -, 页码 1006-1011出版社
PORTLAND PRESS LTD
DOI: 10.1042/BST0381006
关键词
Alzheimer's disease; heparin; nuclear magnetic resonance spectroscopy (NMR spectroscopy); phosphorylation; tau
资金
- Agence Nationale de la Recherche [ANR-05-blanc-6320-01]
- Region Nord, CNRS (Centre National de la Recherche Scientifique) Pasteur Institute of Lille
- European Community (Fondo Europeo de Desarrollo Regional)
- French Research Ministry
- University of Sciences and Technologies of Lille
- CNRS/Region Nord-Pas de Calais (France)
NMR spectroscopy was used to explore the different aspects of the normal and pathological functions of tau, but proved challenging because the protein contains 441 amino acids and has poor signal dispersion. We have set out to dissect the phosphorylation patterns of tau in order to understand better its role in the aggregation process and microtubule-binding regulation. Our current knowledge on the functional consequences of specific phosphorylations is still limited, mainly because producing and assessing quantitatively phosphorylated tau samples is far from straightforward, even in vitro. We use NMR spectroscopy as a proteonnics tool to characterize the phosphorylation patterns of tau, after in vitro phosphorylation by recombinant kinases. The phosphorylated tau can next be use for functional assays or interaction assays with phospho-dependent protein partners, such as the prolyl cis-trans isomerase Pin1.
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