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Literature DB >> 16028903

High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.

Alain Sillen¹, Jean-Michel Wieruszeski, Arnaud Leroy, Amena Ben Younes, Isabelle Landrieu, Guy Lippens.

Abstract

HRMAS NMR of tau paired helical fragments assembled with heparin show an intensity decrease for those amino acids that are incorporated into the rigid core region, whereas the N-terminal amino acids maintain their full mobility.

Entities: Chemical Disease Gene

Mesh：

Substances：
tau Proteins

Year: 2005 PMID： 16028903 DOI： 10.1021/ja0516211

Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419

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Cited

10 in total

Review 1. Tau aggregation in Alzheimer's disease: what role for phosphorylation?

Authors: Guy Lippens; Alain Sillen; Isabelle Landrieu; Laziza Amniai; Nathalie Sibille; Pascale Barbier; Arnaud Leroy; Xavier Hanoulle; Jean-Michel Wieruszeski
Journal: Prion Date: 2007-01-23 Impact factor: 3.931

2. Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation.

Authors: Anna Pavlova; Evan R McCarney; Dylan W Peterson; Frederick W Dahlquist; John Lew; Songi Han
Journal: Phys Chem Chem Phys Date: 2009-06-29 Impact factor: 3.676

3. Identification of the Tau phosphorylation pattern that drives its aggregation.

Authors: Clément Despres; Cillian Byrne; Haoling Qi; François-Xavier Cantrelle; Isabelle Huvent; Béatrice Chambraud; Etienne-Emile Baulieu; Yves Jacquot; Isabelle Landrieu; Guy Lippens; Caroline Smet-Nocca
Journal: Proc Natl Acad Sci U S A Date: 2017-08-07 Impact factor: 11.205

4. Structural complexity of a composite amyloid fibril.

Authors: Józef R Lewandowski; Patrick C A van der Wel; Mike Rigney; Nikolaus Grigorieff; Robert G Griffin
Journal: J Am Chem Soc Date: 2011-08-23 Impact factor: 15.419

5. Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy.

Authors: Jonathan J Helmus; Krystyna Surewicz; Witold K Surewicz; Christopher P Jaroniec
Journal: J Am Chem Soc Date: 2010-02-24 Impact factor: 15.419

High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.

Review 1. Tau aggregation in Alzheimer's disease: what role for phosphorylation?

2. Site-specific dynamic nuclear polarization of hydration water as a generally applicable approach to monitor protein aggregation.

3. Identification of the Tau phosphorylation pattern that drives its aggregation.

4. Structural complexity of a composite amyloid fibril.

5. Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy.

Review 6. The Structure Biology of Tau and Clue for Aggregation Inhibitor Design.

Review 7. Prion-like strain effects in tauopathies.

Review 8. The Role of Post-Translational Modifications on the Structure and Function of Tau Protein.

9. Solid-state NMR investigation of the involvement of the P2 region in tau amyloid fibrils.

Review 10. NMR Meets Tau: Insights into Its Function and Pathology.