Results 171 to 180 of about 243,600 (356)

Involvement of T-complex protein 1-ring complex/chaperonin containing T-complex protein 1 (TRiC/CCT) in retrograde axonal transport through tau phosphorylation

, 2019
Xu‐Qiao Chen
openalex   +1 more source

Specific post-translational modifications of soluble tau protein distinguishes Alzheimer’s disease and primary tauopathies [PDF]

, 2023
Nathalie Kyalu Ngoie Zola, Clémence Balty, Sébastien Pyr dit Ruys, Axelle Vanparys, Nicolas D. Huyghe, Gaëtan Herinckx, Manuel Johanns, Emilien Boyer, Pascal Kienlen‐Campard, Mark H. Rider, Didier Vertommen, Bernard Hanseeuw   +11 more
openalex   +1 more source

Electrical Control of the Transduction Channels’ Gating Force in Mechanosensory Hair Cells

Advanced Science, EarlyView.
The inner ear's hair cells rely on mechanosensitive ion channels to convert vibrations of their hair‐bundle into electrical signals. We show that varying the electrical potential (U) across the sensory epithelium modulates a key determinant of mechanosensitivity—the gating force (FG)—by modulating the gating swing (d), ranging from the size of the ...
Achille Joliot, Laure Stickel, Pascal Martin   +2 more
wiley   +1 more source

Live-cell visualization of tau aggregation in human neurons

Communications Biology
Alzheimer’s disease (AD) and more than twenty other dementias, termed tauopathies, are pathologically defined by insoluble aggregates of the microtubule-associated protein tau (MAPT). Although tau aggregation correlates with AD symptomology, the specific
Bryan Hurtle, Christopher J. Donnelly, Xin Zhang, Amantha Thathiah   +3 more
doaj   +1 more source

Role of Tau Protein in Both Physiological and Pathological Conditions [PDF]

, 2004
Jesús Ávila, José J. Lucas, Mar Pérez, Félix Hernández   +3 more
openalex   +1 more source

Tau protein in Alzheimer’s disease.

Current Alzheimer research, 2011
1
openaire   +5 more sources

Morphological and Hyperphosphorylation Transitions of Nanoscale Tau Aggregates in Alzheimer's Disease

Advanced Science, EarlyView.
Super‐resolution microscopy identifies nano‐sized tau aggregates (nano‐aggregates) and reveals distinct transitions in their morphology and phosphorylation profiles across control, Primary Age‐Related Tauopathy, and Alzheimer's disease brains. Morphology and hyperphosphorylation signatures distinguish physiological from pathological forms, with nano ...
Adriana N. Santiago‐Ruiz, Siewert Hugelier, Gabriela L. Correa, Charles R. Bond, Edward B. Lee, Melike Lakadamyali   +5 more
wiley   +1 more source

TBK1 Induces the Formation of Optineurin Filaments That Condensate with Polyubiquitin and LC3 for Cargo Sequestration

Advanced Science, EarlyView.
Phosphorylation of Optineurin by TBK1 induces the formation of filaments that condensate upon binding to linear polyubiquitin. Membrane‐anchored LC3 partitions into these condensates, suggesting that phase separation of filamentous Optineurin with ubiquitylated cargo promotes the sequestration of cargo and its subsequent alignment with LC3‐positive ...
Maria G. Herrera, Lena Kühn, Lisa Jungbluth, Verian Bader, Laura J. Krause, David Kartte, Elias Adriaenssens, Sascha Martens, Jörg Tatzelt, Carsten Sachse, Konstanze F. Winklhofer   +10 more
wiley   +1 more source

The Regulatory Ser262 of Microtubule-associated Protein Tau Is Phosphorylated by Phosphorylase Kinase

, 1997
Hemant K. Paudel
openalex   +1 more source

Genetic background modifies neurodegeneration and neuroinflammation driven by misfolded human tau protein in rat model of tauopathy: implication for immunomodulatory approach to Alzheimer's disease [PDF]

, 2010
Zuzana Stožická, Norbert Žilka, Petr Novák, Branislav Kováčech, Ondrej Bugos, Michal Novák   +5 more
openalex   +1 more source