Missense tau mutations identified in FTDP-17 have a small effect on tau–microtubule interactions-Reference-Cited by-同舟云学术

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Missense tau mutations identified in FTDP-17 have a small effect on tau–microtubule interactions

Published:2000-01 Issue:1 Volume:853 Page:5-14
ISSN:0006-8993
Container-title:Brain Research
language:en
Short-container-title:Brain Research

Author:

DeTure Michael,Ko Li-wen,Yen Samuel,Nacharaju Parimala,Easson Colin,Lewis Jada,van Slegtenhorst Marjon,Hutton Michael,Yen Shu-Hui

Publisher

Elsevier BV

Subject

Developmental Biology,Clinical Neurology,Molecular Biology,General Neuroscience

Reference35 articles.

1. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer Disease;Alonso;Proc. Natl. Acad. Sci. U. S. A.,1994

2. The tau mutation (val337met) disrupts cytoskeletal networks of microtubules;Arawaka;NeuroReport,1999

3. Polymerization and colchicine binding. Two independent properties of tubulin;Barton;Biochim. Biophys. Acta,1978

4. Straight and paired helical filaments in Alzheimer Disease have a common structural unit;Crowther;Proc. Natl. Acad. Sci. U. S. A.,1991

5. The microtubule binding repeats of tau protein assemble into filaments like those found in Alzheimer's Disease;Crowther;FEBS Lett.,1992

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1. Tau‐targeting nanoparticles for treatment of Alzheimer's disease;Exploration;2024-06-21

2. The disease-causing tau V337M mutation induces tau hypophosphorylation and perturbs axon morphology pathways;2024-06-06

3. Tau filaments with the Alzheimer fold in cases withMAPTmutations V337M and R406W;2024-04-30

4. Impaired tau–microtubule interactions are prevalent among pathogenic tau variants arising from missense mutations;Journal of Biological Chemistry;2019-11

5. Pathological Progression Induced by the Frontotemporal Dementia-Associated R406W Tau Mutation in Patient-Derived iPSCs;Stem Cell Reports;2019-10

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