Articles tagged with Tau Proteins
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Researchers discovered compounds that interact with tau protein in three specific ways, which could lead to early diagnosis and treatment of Alzheimer's disease. These compounds may bind to tau filaments, inhibit filament formation, or drive tau protein to form filaments.
Research finds Pin1, previously thought to help with Alzheimer's, actually worsens frontotemporal dementia due to specific tau mutations. This study suggests alternative therapeutic approaches and proper animal models are needed.
Researchers at USF Health found that Akt protein can influence tau protein, leading to nerve cell death in Alzheimer's disease. The study suggests regulating Akt levels may be beneficial for treating diseases of aging, including cancer and diabetes.
Researchers led by Dr. Shaohua Xu propose a new theory on the origin of Alzheimer's Disease, suggesting that abnormal tau protein molecules form tangled fibers that accumulate and kill brain cells. The three-step process involves spherical clusters, linear chains, and uniform filaments.
A new study reveals a mechanism of regulating protein transport in neurons, where tau proteins act as smart speed bumps to regulate the movement of dynein and kinesin proteins. This finding provides insight into neurodegenerative diseases like Alzheimer's, which arise from impaired shipping systems.
Researchers uncovered new details about how proteins orchestrate cell division and how curcumin boosts the immune system to fight cancer. Additionally, scientists provided new insights into the toxic effects of tau protein aggregation in Alzheimer's disease.
Researchers have identified a complex of proteins that plays a key role in alleviating tau accumulation in mice and cultured human cells. The study's findings suggest a pivotal role for Hsp90 in aberrant tau degradation, making an Hsp90 inhibitor like EC102 a promising therapeutic candidate for Alzheimer's disease.
A study of 14 Swedish amateur boxers found higher levels of certain chemicals in their cerebrospinal fluid indicating injuries to neurons and astroglia after a bout. The findings suggest that amateur boxing is associated with acute neuronal and astroglial injury, warranting further investigation for medical counseling of athletes.
The study reveals that tau protein undergoes a stepwise folding and truncation process in the formation of neurofibrillary tangles in Alzheimer's disease. Dr. Binder's research contributes to diagnostic and therapeutic strategies for AD patients, marking an important milestone in understanding the disease.
Researchers found that immune therapy against Alzheimer's disease not only removes the toxic amyloid plaque but also clears protein tangles, suggesting a broad assault on the disease. The treatment was shown to clear both hallmark lesions of AD by alleviating interference in the cell's protein garbage disposal system.
Researchers found a link between olfactory dysfunction and excess tau proteins in brain structures important for smelling. The study used genetically engineered mice to evaluate the effect of tau protein overexpression on smell perception.
Researchers discovered that tau and alpha-synuclein proteins interact to form brain lesions in both diseases, potentially leading to effective treatments for both conditions. The study found that inhibiting the formation of one type of amyloid lesion may also prevent the other.
A study led by Dr. Jeffery M. Vance found significant evidence of linkage between the tau gene and late-onset Parkinson's in three single nucleotide polymorphisms. The research suggests that normal variations in the tau protein may make individuals more susceptible to the disease.
A new double transgenic mouse model has been developed to study Alzheimer's disease, featuring both brain plaques and tangles associated with the condition. The model is expected to contribute significantly to knowledge about the course of the disease and aid in further development and testing of potential therapies.
A team of scientists led by Li-Huei Tsai found that the enzyme calpain triggers neurodegeneration in brain cells, similar to Alzheimer's disease. The discovery proposes a common mechanistic link between toxic insults and brain cell injury, offering potential targets for drugs to slow or stop progression.
Researchers identified a molecule that triggers the formation of deadly protein snarls in Alzheimer's disease. High levels of a shortened, malfunctioning version of the protein p35 in brains lead to hyperphosphorylation of tau protein, causing neurofibrillary tangles.
Researchers identify three mutations in tau gene causing hereditary neurodegenerative diseases, providing new direction for exploring Alzheimer's disease. The findings suggest that abnormal tau protein accumulation kills brain cells, potentially leading to the development of treatments for related diseases.