Post-translational modifications of tau protein: implications for Alzheimer's disease.

By Ludovic Martin, X. Latypova, F. Terro. Neurochemistry International, 2011

610 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/24a930836fc2b629d4640177adc54b57131638cd

How researchers see this paper

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In Cellular and Molecular Neuroscience

1. V. Lee
2. John Q. Trojanowski
3. Dennis W. Dickson

In Molecular Biology

1. John Q. Trojanowski
2. Dennis W. Dickson
3. V. Lee

In Physiology

1. V. Lee
2. Jing L Guo
3. John Q. Trojanowski
4. Brittany N. Dugger
5. Bin Zhang
6. Dennis W. Dickson
7. E. Mandelkow
8. D. Selkoe

Citations in the corpus

• Pathology of Neurodegenerative Diseases. (2017, background): “In addition to phosphorylation, tau undergoes other posttranslational modifications, such as ubiquitination, nitration, glycation, and acetylation, all of which have been linked to abnormal tau that accumulates in degenerative tauopathies (Morishima and Ihara 1994; Alonso et al. 2008; Martin et al. ”
• Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer’s-like Tauopathy (2013, background): “…affinity of tau is regulated by various posttranslational modifications, including phosphorylation (Lee et al., 1991), acetylation (Min et al., 2010; Cohen et al., 2011; Irwin et al., 2012), and glycosylation (for review, see Gong et al., 2005; Ballatore et al., 2007; Martin et al., 2011).”