Tau Protein
Tau Protein - Related Videos
09:22
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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Cited by 21 •
2015
Unmodified and hyperphosphorylated tau proteins were used in two in vitro aggregation assays to reveal the hyperphosphorylation-dependent fast aggregation kinetics. These assays pave the way for future screens for compounds that can modulate the propensity of hyperphosphorylated tau to form fibrils that underlie the progression of Alzheimer’s disease.
02:19
Lentiviral-Mediated Transduction of Human Neurons for Tau Protein Aggregation Analysis
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2025
This video demonstrates the process of transducing human neuronal cells with a lentivirus encoding a mutant human tau protein tagged with yellow fluorescent protein (YFP) to study protein aggregation. It outlines the steps from viral entry to mutant tau expression, culminating in the formation of visible cytoplasmic tau aggregates in the neurons.
05:22
A Cell-Based Assay to Assess the Tau Protein Uptake by Microglia
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2025
This video showcases a cell-based assay quantifying Tau uptake by murine microglia using pH-sensitive fluorescent-labeled Tau aggregates, analyzed via fluorescence-activated cell sorting for a quantitative assessment.
12:55
Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
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Cited by 11 •
2017
This manuscript describes standard protocols for measuring tau hyperphosphorylation, measuring tau binding to microtubules, and localization of intracellular tau following drug treatments. These protocols can be used repetitively for screening drugs or other compounds that target tau hyperphosphorylation or microtubule binding.
01:25
Detection of Phosphorylated Tau Proteins in Mouse Brain Samples Using Western Blot Analysis
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2025
Homogenize the tissue to release proteins into the buffer. The protease inhibitors block protease activity, preventing protein degradation.
FAQs
Abnormal phosphorylation changes tau’s relationship with microtubules. When tau becomes abnormally phosphorylated, its ability to bind these structural tracks can be reduced. This weakens the organization that supports axonal transport and may promote tau misfolding. The sequence connects a molecular modification with neuronal dysfunction and provides a target for investigating disease mechanisms.
Misfolded tau can assemble into aggregates called neurofibrillary tangles. These structures are characteristic of Alzheimer’s disease and other neurodegenerative tauopathies, but their importance extends beyond being disease markers: they are associated with neuronal dysfunction and loss. Consequently, research examines aggregation as part of the process linking abnormal tau behavior to declining neuronal integrity.
Microtubules provide the structural framework associated with axonal organization and intracellular transport. Tau binding helps maintain this arrangement in healthy neurons. If abnormal phosphorylation reduces that binding, transport-related support may be compromised, offering a mechanistic explanation for why a molecular change in tau can affect neuronal function.
Tau research supports development of fluid and imaging biomarkers for Alzheimer’s disease and other tauopathies. These approaches can help investigators study disease-related tau changes and examine processes involving abnormal modification, aggregation, or spread. The specific samples, imaging methods, and interpretation criteria depend on the research design and are not specified here.
Potential therapies can target several stages of tau pathology, including abnormal modification, aggregation, and spread. A modification-focused strategy addresses changes that may disrupt tau’s microtubule binding, whereas anti-aggregation or anti-spread approaches address later disease-associated behavior. Studying these targets helps researchers evaluate different ways to prevent or limit neuronal damage.
Within biology, tau connects molecular changes with cell-level outcomes. Its association with neuronal microtubules relates protein behavior to axonal structure and intracellular transport, while abnormal phosphorylation, misfolding, and aggregation relate those changes to neuronal dysfunction and loss. This makes tau useful for studying how altered proteins contribute to neurodegenerative disease.