Structural Impact of Heparin Binding to Full-Length Tau As Studied by NMR Spectroscopy-Reference-Cited by-同舟云学术

Structural Impact of Heparin Binding to Full-Length Tau As Studied by NMR Spectroscopy

Published:2006-09-20 Issue:41 Volume:45 Page:12560-12572
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sibille Nathalie¹,Sillen Alain¹,Leroy Arnaud¹,Wieruszeski Jean-Michel¹,Mulloy Barbara¹,Landrieu Isabelle¹,Lippens Guy¹

Affiliation:

1. CNRS UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle, Université des Sciences et Technologies de Lille 1, 59655, Villeneuve d'Ascq Cedex, France, Laboratoire de biochimie appliquée, Faculté de Pharmacie (Paris XI), 5 rue Jean-Baptiste Clément, 92296 Chatenay-Malabry Cedex, France, and Laboratory of Molecular Structure, National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Herts EN63QG, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi060964o

Reference63 articles.

1. Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.

2. Alzheimer's disease: Tau proteins, the promoting factors of microtubule assembly, are major components of paired helical filaments

3. Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

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