Structural Basis of Tau Interaction With BIN1 and Regulation by Tau Phosphorylation-Reference-Cited by-同舟云学术

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Structural Basis of Tau Interaction With BIN1 and Regulation by Tau Phosphorylation

Published:2018-11-14 Issue: Volume:11 Page:
ISSN:1662-5099
Container-title:Frontiers in Molecular Neuroscience
language:
Short-container-title:Front. Mol. Neurosci.

Author:

Lasorsa Alessia,Malki Idir,Cantrelle François-Xavier,Merzougui Hamida,Boll Emmanuelle,Lambert Jean-Charles,Landrieu Isabelle

Funder

Agence Nationale de la Recherche

Alzheimer’s Association

Publisher

Frontiers Media SA

Subject

Cellular and Molecular Neuroscience,Molecular Biology

Reference49 articles.

1. Proline conformation in a functional tau fragment.;Ahuja;J. Mol. Biol.,2016

2. Abnormal Alzheimer-like phosphorylation of tau-protein by cyclin-dependent kinases cdk2 and cdk5.;Baumann;FEBS Lett.,1993

3. Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry.;Braak;Acta Neuropathol.,2006

4. Loss of bin1 promotes the propagation of tau pathology.;Calafate;Cell Rep.,2016

5. Increased expression of BIN1 mediates Alzheimer genetic risk by modulating tau pathology.;Chapuis;Mol. Psychiatry,2013

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