Results 11 to 20 of about 104,850 (261)

Autophagy and Tau Protein [PDF]

International Journal of Molecular Sciences, 2021
Neurofibrillary tangles, which consist of highly phosphorylated tau protein, and senile plaques (SPs) are pathological hallmarks of Alzheimer’s disease (AD). In swollen axons, many autophagic vacuoles are observed around SP in the AD brain. This suggests that autophagy function is disturbed in AD.
Tadanori Hamano, Soichi Enomoto, Norimichi Shirafuji, Masamichi Ikawa, Osamu Yamamura, Shu-Hui Yen, Yasunari Nakamoto   +6 more
openaire   +2 more sources

Amyloidogenesis of Tau protein [PDF]

Protein Science, 2017
AbstractThe role of microtubule‐associated protein Tau in neurodegeneration has been extensively investigated since the discovery of Tau amyloid aggregates in the brains of patients with Alzheimer's disease (AD). The process of formation of amyloid fibrils is known as amyloidogenesis and attracts much attention as a potential target in the prevention ...
Bartosz Nizynski, Wojciech Dzwolak, Krzysztof Nieznanski   +2 more
openaire   +3 more sources

Tau: A Signaling Hub Protein [PDF]

Frontiers in Molecular Neuroscience, 2021
Over four decades ago,in vitroexperiments showed that tau protein interacts with and stabilizes microtubules in a phosphorylation-dependent manner. This observation fueled the widespread hypotheses that these properties extend to living neurons and that reduced stability of microtubules represents a major disease-driving event induced by pathological ...
Rebecca L. Mueller, Rebecca L. Mueller, Benjamin Combs, Mohammed M. Alhadidy, Mohammed M. Alhadidy, Scott T. Brady, Scott T. Brady, Gerardo A. Morfini, Gerardo A. Morfini, Nicholas M. Kanaan, Nicholas M. Kanaan, Nicholas M. Kanaan   +11 more
openaire   +4 more sources

Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau. [PDF]

PLoS ONE, 2012
BACKGROUND: The misfolding of amyloidogenic proteins including human Tau protein, human prion protein, and human α-synuclein is involved in neurodegenerative diseases such as Alzheimer disease, prion disease, and Parkinson disease.
Sheng-Rong Meng, Ying-Zhu Zhu, Tong Guo, Xiao-Ling Liu, Jie Chen, Yi Liang   +5 more
doaj   +1 more source

EFhd2 Affects Tau Liquid–Liquid Phase Separation

Frontiers in Neuroscience, 2019
The transition of tau proteins from its soluble physiological conformation to the pathological aggregate forms found in Alzheimer’s disease and related dementias, is poorly understood.
Irving E. Vega, Irving E. Vega, Irving E. Vega, Andrew Umstead, Nicholas M. Kanaan, Nicholas M. Kanaan, Nicholas M. Kanaan   +6 more
doaj   +1 more source

The Molecular Chaperone Artemin Efficiently Blocks Fibrillization of TAU Protein In Vitro

Cell Journal, 2017
Objective: Aggregation of the TAU proteins in the form of neurofibrillary tangles (NFTs) in the brain is a common risk factor in tauopathies including Alzheimer’s disease (AD).
Zahra Khosravi, Mohammad Ali Nasiri Khalili, Sharif Moradi, Reza Hassan Sajedi, Mehdi Zeinoddini   +4 more
doaj   +1 more source

TTBK2: A Tau Protein Kinase beyond Tau Phosphorylation [PDF]

BioMed Research International, 2015
Tau tubulin kinase 2 (TTBK2) is a kinase known to phosphorylate tau and tubulin. It has recently drawn much attention due to its involvement in multiple important cellular processes. Here, we review the current understanding of TTBK2, including its sequence, structure, binding sites, phosphorylation substrates, and cellular processes involved.
Liao, Jung-Chi, Yang, T. Tony, Weng, Rueyhung Roc, Kuo, Ching-Te, Chang, Chih-Wei   +4 more
openaire   +2 more sources

Folding of the Tau Protein on Microtubules

Angewandte Chemie International Edition, 2015
Abstract Microtubules are regulated by microtubule‐associated proteins. However, little is known about the structure of microtubule‐associated proteins in complex with microtubules. Herein we show that the microtubule‐associated protein Tau, which is intrinsically disordered in solution, locally folds into a stable structure upon ...
Kadavath, H., Jaremko, M., Jaremko, L., Biernat, J., Mandelkow, E., Zweckstetter, M.   +5 more
openaire   +6 more sources

Quantitative flow cytometric selection of tau conformational nanobodies specific for pathological aggregates

Frontiers in Immunology, 2023
Single-domain antibodies, also known as nanobodies, are broadly important for studying the structure and conformational states of several classes of proteins, including membrane proteins, enzymes, and amyloidogenic proteins.
Jennifer M. Zupancic, Jennifer M. Zupancic, Matthew D. Smith, Matthew D. Smith, Hanna Trzeciakiewicz, Mary E. Skinner, Sean P. Ferris, Emily K. Makowski, Emily K. Makowski, Michael J. Lucas, Michael J. Lucas, Michael J. Lucas, Nikki McArthur, Ravi S. Kane, Henry L. Paulson, Henry L. Paulson, Henry L. Paulson, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier, Peter M. Tessier   +22 more
doaj   +1 more source

The regulatory effect of Tau protein on polymerization of MCF7 microtubules in vitro

Biochemistry and Biophysics Reports, 2019
Growing evidence continues to point toward the critical role of beta tubulin isotypes in regulating some intracellular functions. Changes that were observed in the microtubules’ intrinsic dynamics, the way they interact with some chemotherapeutic agents,
Mitra Shojania Feizabadi, Marcos A.V. Hernandez, Jane B. Breslin, Ibukunoluwa I. Akintola   +3 more
doaj   +1 more source