Tau-mediated neurodegeneration in Alzheimer's disease and related disorders

By C. Ballatore, V. Lee, John Q. Trojanowski. Nature Reviews Neuroscience, 2007

2,152 citations recorded by the source corpus.

Subfields: Neurology, Pharmacology, Physiology

View Paper: https://www.semanticscholar.org/paper/950aecf4d265cd2cb4df98bfd268b3407ad00827

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Neurology

1. V. Lee
2. J. Götz
3. L. Ittner
4. D. Holtzman
5. E. Mandelkow
6. Jing L Guo
7. John Q. Trojanowski
8. E. Masliah

In Pharmacology

1. E. Mandelkow
2. Rudolph E. Tanzi
3. J. Götz
4. L. Ittner
5. E. Masliah
6. Bradley T. Hyman
7. D. Holtzman
8. G. Bu

In Physiology

1. D. Holtzman
2. E. Mandelkow
3. V. Lee
4. L. Ittner
5. A. Goate
6. Rudolph E. Tanzi
7. J. Götz
8. D. Selkoe

Citations in the corpus

• Animal models of Alzheimer's disease and frontotemporal dementia (2008, background): “cgi?id=600274">Frontotemporal dementia (FTD) is less common, but makes up 50% of dementia cases presenting before age 60 (Ref”
• Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer’s-like Tauopathy (2013, background): “Pathological tau protein is hyperphosphorylated, conformationally altered, and aggregated into insoluble neurofibrillary tangles (NFTs) in perikarya as well as in processes as neuropil threads, which are the signature pathological hallmarks of tauopathies (for review, see Ballatore et al., 2007).”
• Aβ Oligomers Cause Localized Ca2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines (2010, background): “These include loss of synapses and neurons, deficiency in neurotransmitters and metabolism, aggregation of amyloid- (A )-peptides into extracellular “amyloid plaques” and Tau protein into intracellular “neurofibrillary tangles” (Selkoe, 2004; Binder et al., 2005; Ballatore et al., 2007).”
• Parkinson's disease: genetics and pathogenesis. (2011, background): “several other neurodegenerative disorders, collectively termed tauopathies (25, 95).”
• Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. (2010, positive): “Tau can also form aggregates in the absence of an overt Ab pathology, for example in frontotemporal dementia (FTD), where familial mutations have been identified in the tau-encoding MAPT gene (Ballatore et al., 2007).”
• RNA Editing with CRISPR-Cas13 (2017, background): “Phosphorylation of these residues in disease-relevant proteins affects disease progression for many disorders including Alzheimer’s disease and multiple neurodegenerative conditions (30).”
• Alzheimer’s Disease: The Challenge of the Second Century (2011, background): “It is a major component and a primary constituent of NFTs that are found in AD as well as in a host of other neurodegenerative diseases such as certain frontotemporal dementias and progressive supranuclear palsy (168).”
• Propagation of tau pathology in a model of early Alzheimer’s disease (2012, positive): “It has been reported that glial tau pathology occurs in tauopathies (Ballatore et al., 2007; Chin and Goldman, 1996) and in AD (Nakano et al.”
• Acetylation of tau inhibits its degradation and contributes to tauopathy. (2010, positive): “However, the accumulation of soluble forms of aberrantly phosphorylated tau (p-tau) may underlie tau-mediated neurodegeneration by disrupting the ability of tau to bind microtubules and promoting tau aggregation and fibrillization (Ballatore et al., 2007).”
• Amyloid-β and tau — a toxic pas de deux in Alzheimer's disease (2011, background): “The tau-encoding microtubule-associated protein tau ( MAPT ; also known as tau ) gene carries mutations in a subset of familial forms of FT”
• Mechanisms Underlying Inflammation in Neurodegeneration (2010, neutral): “Inducers and Sensors of Inflammation in AD NFTs are composed of hyperphosphorylated forms of the microtubule-binding protein tau, which under normal physiological conditions regulates cytoskeletal changes.”
• Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice (2011, background): “Although the importance of tau in AD and other tauopathies is well-established [ 5-7 ], unanswered is whether NFTs are the primary neurotoxic factor.”