Articles tagged with Tau Proteins
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A new gene regulation therapy using zinc finger proteins has shown high efficacy in reducing Tau protein levels in the brain, potentially protecting against Alzheimer's disease. The treatment reduces Tau production by 50-80% and prevents nerve damage without obvious side effects.
Researchers have developed a new animal model of early-stage Alzheimer's disease in rhesus macaques, which could enable better testing of new treatments. The model replicates the spread of misfolded tau proteins through brain circuits, similar to human disease progression.
Tau oligomers form droplets within TIA1 droplets selectively, producing highly lethal effects on neurons. The study provides a tool to screen compounds that can inhibit tau oligomer formation, offering hope for Alzheimer's and frontotemporal dementia treatment.
A study by University of Liège researchers links increased tau protein levels in the brainstem to higher cortical excitability, a hallmark of Alzheimer's disease. The findings suggest that measuring cortical hyperexcitability could help identify people at risk before cognitive symptoms appear.
A new study has made a significant discovery about the origins of TAU protein in Alzheimer's disease, revealing its primary emergence in the rhinal cortex. The automated method, which tracks TAU buildup using PET imaging, suggests targeting this area could slow disease progression.
A study published in Proceedings of the National Academy of Sciences reveals that liquid-liquid phase separation facilitates tau protein aggregation, a hallmark of neurodegenerative disorders. The researchers discovered a novel regulatory mechanism involving different variants of tau protein, which may influence disease clinical outcomes.
Research reveals that tau protein undergoes stepwise chemical modifications over time, correlating with dementia stage in Alzheimer's disease. The discovery suggests that multiple drugs may be necessary to target tau effectively, with early intervention requiring different therapeutics compared to late-stage treatment.
Researchers have developed an antibody fragment that reduces Aú peptide and tau protein levels, alleviating cognitive decline and neuroinflammation in advanced Alzheimer's disease models. This breakthrough therapy shows promise as a potential treatment for the devastating disease.
A study by Tokyo Metropolitan University reveals that a specific MARK4 mutation causes tau protein to aggregate in the brain, leading to Alzheimer's disease. The mutated enzyme makes tau proteins sticky and insoluble, causing neurons to die and memory functions to impair.
Researchers discovered a novel mutation in the VCP gene leading to a buildup of tau proteins and neuronal vacuoles, characteristic of Vacuolar Tauopathy (VT), a rare neurodegenerative disease. The study suggests a new therapeutic target for Alzheimer's disease by boosting VCP activity to break up protein aggregates.
A new mouse model shows that injecting synthetic assembled tau protein causes tau accumulation in wild-type mice, spreading to connected regions. This study establishes that tau assembly does not require mutation or overexpression.
Researchers discovered a novel role of tau specific to FTLD spectrum diseases, contributing to conditions like ALS, PSP, and CBD, but not AD and Pick's disease. The study proposes an imbalanced accumulation of tau model, where FUS and SFPQ regulate MAPT processing, leading to increased 4-repeat tau levels.
Researchers discovered deposits of the tau protein typically found in Alzheimer's patients in the brain of an autistic child with ADNP syndrome. An experimental drug called NAP successfully restored normal function to damaged nerve cells in models of ADNP syndrome, offering new hope for treating this genetic disorder.
A new study has uncovered 12 proteins linked to both tau and Alzheimer's disease, expanding understanding of the molecular interactions driving neurodegeneration. The research analyzed donated brain tissue samples from individuals with Alzheimer's, revealing dozens of other proteins associated with the disease.
A new study sheds light on the molecular factors that render entorhinal brain cells uniquely sensitive to degeneration. Researchers found that a suite of genes is likely involved in making these neurons easy targets for degeneration, with PTBP1 playing a major role.
Researchers found that neurons with high remodeling activity are more vulnerable to Alzheimer's disease and die when their remodeling goes awry. The study, which linked amyloid-beta and tau proteins at the genetic and molecular levels, provides insights into the disease's progression.
A new study from Massachusetts General Hospital reveals that different forms of phosphorylated tau can explain variable effects in Alzheimer's disease. The research found specific molecular characteristics associated with greater tau spread and worse disease progression.
Researchers at Lund University and McGill University found that toxic tau protein spreads in the human brain via connected neurons, facilitated by beta-amyloid. The spread of toxic tau leads to widespread neuronal death and eventual dementia.
A study published in Nature reveals that the low-density lipoprotein receptor-related protein 1 (LRP1) plays a key role in the spread of pathological tau proteins between neurons. By inhibiting LRP1 expression, researchers were able to reduce tau spread in mice, offering new hope for potential treatments.
Researchers from University of Konstanz discover that a molecular chaperone helps form Alzheimer fibrils by exposing a vulnerable area on the protein tau, preventing longer, more toxic fibril formation. The findings suggest a possible defense mechanism against Alzheimer's disease.
A Mayo Clinic study found that genetic variants on chromosomes 1 and 5 were linked to higher tau levels in older adults. Participants with these variants had about 10% higher tau levels than those without them. The research suggests that genes previously linked to Alzheimer's risk may not be associated with tau accumulation.
A study of 754 participants found that specific gene variants on chromosomes 1 and 5 were associated with higher levels of tau protein in the brain. These variants were present in around 2-3% of the group, leading to about 10% higher tau levels than those without.
A new brain scan-blood test panel has been developed to help diagnose brain trauma following battlefield blasts. The panel combines functional assessment with blood tests and brain scans to estimate brain degeneration in human veterans exposed to IED blasts.
The Kong group will investigate how neurons and muscle cells communicate, with the goal of understanding how to reactivate neurons in injured muscle. They will also develop a drug delivery system to target tau proteins responsible for Alzheimer's disease.
A University of South Florida study suggests beta-arrestin-2 can lead to increased accumulation of neurotoxic tau tangles in the brain, causing forms of dementia. The researchers found that oligomerized beta-arrestin-2 disrupts protective clearance processes, leading to disease-causing tau buildup.
Researchers analyzed brain tissue from patients with Alzheimer's and corticobasal degeneration, finding that modifications to the tau protein influence its misfolding behavior. The study reveals key insights into how tau filaments form, grow, and spread throughout the brain, potentially accelerating the fight against neurodegenerative ...
Tau proteins exhibit distinct aggregation behaviors, with phosphorylation influencing their formation of either solid fibrils or disordered clumps. The researchers' findings offer new insights into the causes of Alzheimer's and frontotemporal dementia, potentially leading to the development of therapeutic interventions.
A study on globular glial tauopathy reveals that phosphate groups are not unique to tau protein and can lead to dysfunction in other proteins. Glial cells also play a crucial role in the disease's progression by facilitating the spread of protein inclusions. This research sheds light on potential new drug targets to stop disease progre...
Researchers found that reelin promotes synaptic plasticity and reduces Tau phosphorylation in animal models with tauopathy, potentially reducing neurodegenerative effects. This discovery opens a new perspective for designing future therapeutic targets to combat Alzheimer's and other tauopathies.
Researchers found that inflammatory processes triggered by the NLRP3 inflammasome play a key role in emerging tau pathology, a hallmark of neurodegenerative diseases like Alzheimer's. The study suggests that modulating the immune response could be a promising approach for treating these conditions.
Scientists have linked abnormal tau in the brain to at least 25 neurodegenerative diseases, but current diagnosis requires analyzing brain tissue after death. The new test uses cerebrospinal fluid to detect abnormal tau, offering hope for diagnosing less common neurological diseases like Alzheimer's.
University of Warwick researchers introduce fluorescently labelled Tau oligomers into single brain neurons and observe significant effects on action potential dynamics and synaptic transmission. They find that Tau oligomers interfere with memory storage by mis-localising at synapses.
Researchers at Imperial College London visualized protein 'tangles' associated with dementia in patients who suffered a single head injury, showing collective likelihood of tau tangles and nerve damage. The study may accelerate treatment development by enabling medics to monitor tau protein levels.
Researchers at UC San Francisco have found that Alzheimer's disease directly attacks brain regions responsible for wakefulness during the day, leading to excessive daytime napping. This damage is associated with tau protein buildup, which contributes more directly to brain degeneration than amyloid protein.
A new skin test using ultrasensitive technology may provide an early diagnosis of Alzheimer's and Parkinson's diseases, detecting misfolded proteins in skin samples. The RT-QuIC test is highly sensitive and specific, offering a promising tool for diagnosing and characterizing these neurodegenerative diseases.
The study reveals that Tau controls Fyn nanoclustering in dendrites, leading to altered nerve signals and synapse dysfunction. Single molecule imaging provides unprecedented insights into the organisation of key proteins in living brain cells.
Researchers have identified non-inherited somatic mutations in the brain that could contribute to Alzheimer's disease progression. These mutations were found to be associated with hyperphosphorylation of tau proteins, a hallmark of AD.
Researchers at Temple University Health System discovered that VPS35 clears the brain of a potentially harmful protein called tau, which accumulates in neurodegenerative disorders. The study found that altering VPS35 levels in individual neurons can directly control tau accumulation, implicating VPS35 in tauopathy.
Research finds that older brains have a higher rate of tau protein spread, contributing to Alzheimer's disease progression. The study uses gene vectors to demonstrate this connection in mice, raising questions about therapeutic options and disease mechanisms.
A new study by UC Berkeley psychologists links disrupted sleep in 50s and 60s to increased protein tangles in the aging brain, raising the risk of developing Alzheimer's disease. The research highlights the importance of sleep for maintaining a healthy brain into old age.
A Mayo Clinic study found that people with sleep apnea had higher accumulations of the toxic protein tau in the entorhinal cortex, a part of the brain responsible for memory, navigation, and perception. This association may suggest a link between sleep disruption and an increased risk of dementia.
Researchers at Ohio State University have found that tau protein aggregates in Alzheimer's disease can grow by joining end-to-end, forming longer filaments. This discovery helps explain the formation of toxic aggregates and may inform the development of new drug candidates.
A study examining nearly 300 clinically normal adults found that women showed more tau deposits in the brain than men, associated with greater Aβ plaque deposits, supporting potential reasons for differences in AD risk between men and women. The findings may be limited by the study population's age and demographic characteristics.
A recent study published in Science has found that sleep deprivation increases levels of the key Alzheimer's protein tau, leading to accelerated brain damage and dementia. In mice and people, researchers discovered that disrupted sleep causes tau tangles to spread through the brain, a hallmark of Alzheimer's disease.
A new study finds that sleep deprivation increases tau levels in the brain, a key protein associated with neurodegeneration and Alzheimer's disease. The researchers suggest optimizing the sleep-wake cycle as a potential treatment target to prevent Alzheimer's.
A study from Massachusetts General Hospital reveals that tau protein and amyloid-beta interact to impair brain function. Elevated tau levels were associated with reduced neural activity, regardless of tangle formation.
Excitatory neurons are more susceptible to abnormal tau protein accumulation, a key factor in Alzheimer's disease progression. The study identifies genetic differences between excitatory and inhibitory neurons that may explain their vulnerability.
A new study found that certain neurons protect themselves from Alzheimer's by clearing toxic tau proteins, which accumulate in sluggish cells. The discovery suggests new treatment possibilities to support natural defense mechanisms against neurodegenerative diseases.
Researchers have identified three promising radiopharmaceuticals that bind to tau tangles, a protein associated with neurodegenerative diseases. The tracers were tested in patients with Alzheimer's disease and found to show promise in measuring tau protein accumulation.
A recent study by the University of Helsinki reveals that pathological tau triggers a safety valve mechanism in cell membranes, leading to accelerated neuronal cell death and loss of synapses. Omega-3 fatty acids have been found to modify the microstructure of cell membranes, capturing tau aggregates within cells.
Researchers have found that tau protein interferes with the nucleus's ability to communicate with the cell, disrupting the function of the nuclear pore complex. This alteration accelerates tau aggregation and neurofibrillary tangle formation, leading to neural dysfunction and death in Alzheimer's disease.
Researchers have discovered a signal pathway within cells that could stop degeneration and improve learning and memory in affected patients. The study also invented a potential drug to target tauopathies, a class of diseases caused by misfolding of the tau protein.
New study by Drexel University researchers suggests that tau protein allows microtubules to grow and remain dynamic. This challenges the widely-held theory that tau stabilizes microtubules, which is critical for cognitive function.
Researchers discovered that tau protein mutations can increase cancer risk by up to 3.72 times, highlighting a new association between neurodegenerative disorders and cancer. The study's findings suggest that clinicians should monitor patients with tau mutations for their cancer risk, in addition to attending to neurodegeneration.
Researchers found that tau production and secretion from nerve cells is an active process in the natural course of Alzheimer's disease. This may explain why experimental treatments targeting tau have had disappointing results. The study provides new insights into the role of tau kinetics in neurodegenerative diseases.
A study investigated tau phosphorylation-related targets for Alzheimer's disease treatment, focusing on four kinases and one phosphatase. The model suggests the role of each enzyme in AD pathogenesis and identifies potential targets for therapy. This work builds upon InSysBio's quantitative systems pharmacology (QSP) modeling approach.
A study published in the journal Brain uses a combination of imaging techniques to examine tau build-up in patients with Alzheimer's disease and progressive supranuclear palsy. The findings support the transneuronal spread hypothesis, suggesting that tau starts in one place and spreads throughout the brain.
Researchers have developed small shining molecules that can recognize specific proteins in the brain, such as amyloid beta and tau. These molecules emit light at different wavelengths when bound to their target protein, enabling potential diagnostic tools for neurodegenerative diseases.
The compound anle138b was shown to close harmful openings in the membrane of nerve cells and induce conformational changes that modify pore conductivity. Treatment with anle138b normalized brain activity and improved learning ability in mice affected by Alzheimer's disease, regardless of when treatment started.
Researchers discovered that Tau protein interacts with and disrupts cell membranes, forming toxic complexes that induce neuronal toxicity. The complexes are made up of Tau proteins and phospholipids from the membrane, and can be taken up by neurons more readily than the fibril form of the protein.