Articles tagged with Amyloids
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Researchers at the University of Leeds have visualised the structure of amylin fibrils, a key player in type 2 diabetes, and discovered an intricate architecture that makes some sequences more prone to aggregation. This finding suggests a potential explanation for the rapid onset of disease in individuals with early-onset type 2 diabetes.
Researchers at Korea Brain Research Institute used GANs to analyze bulk RNA-seq data, finding that increased Amyloid-beta in the brain alters cholesterol biosynthesis. This study provides a new approach for projecting biological changes and aiding healthcare industry.
Researchers at Tokyo University of Science used infrared laser irradiation to destroy amyloid fibrils, which are typical of neurodegenerative diseases like Alzheimer's. The study combines experimental and simulation results, showing that the process begins at the core of the fibril, where resonance breaks intermolecular hydrogen bonds.
Studies of alpha-synuclein protein aggregates found variations in elongation rates and fibril structures, depending on cross-seeding and pH levels. High-speed atomic force microscopy enabled visualization of growth over time, shedding light on amyloid-related diseases.
Researchers have identified a blood test target, phosphorylated tau 217, that correlates with the presence of amyloid plaques in the brain. This protein can be detected in the blood of people who have yet to show signs of forgetfulness or confusion, making it a promising tool for early Alzheimer's diagnosis.
A blood test for Alzheimer's disease has shown high accuracy in detecting the disease, with levels of p-tau217 increasing seven-fold in individuals with Alzheimer's. The test detected tau brain changes 20 years before cognitive impairment in those with a genetic predisposition.
Researchers discovered that low-concentration salt crystals can precipitate at nanoscales due to local density fluctuation, accelerating amyloid-β peptide aggregation. This process could provide a permanent solution for Alzheimer's disease treatment.
Researchers at Washington University School of Medicine have developed a technique to detect minute amounts of p-tau-217, a protein fragment linked to Alzheimer's disease in the blood. The levels of this protein are elevated during the early stages of the disease and can accurately predict the presence of amyloid plaques in PET scans.
Researchers discovered that garden peas can form highly stable amyloid protein aggregates, which may aid in seed longevity. Vicilin and its domains were found to co-localize with amyloid-specific dye in pea seeds.
A research team mapped molecular changes in cells near amyloid plaques, finding two co-expression networks that respond to amyloid beta deposition. These networks, expressed by astroglia, microglia, and oligodendrocytes, show both protective and damaging effects on the brain, highlighting the complexity of Alzheimer's disease.
The AHEAD 3-45 study is a Phase III clinical trial aiming to prevent worsening memory and thinking among individuals at risk for future decline. Researchers hope to find that BAN2401 can help prevent Alzheimer's disease.
Research at SNMMI 2020 Annual Meeting found super-agers have lower tau and amyloid pathology associated with neurodegeneration. This enables them to maintain their cognitive skills even at advanced ages. The study suggests a potential pathway for successful aging and developing novel treatments to tackle age-related diseases.
A new study suggests that misfolded protein build-up in the gut may contribute to Alzheimer's-like symptoms in mice, potentially leading to a new treatment approach targeting the gut. The researchers found that beta amyloid proteins injected into the gut traveled to the nervous system and brain, causing cognitive impairments.
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.
Researchers provide new understanding of co-aggregation process between proinflammatory S100A9 protein and Aβ42 peptide in Alzheimer's disease. The study reveals that S100A9 amyloids coat the surface of Aβ42 amyloids, reducing secondary nucleation sites and enhancing cellular toxicity.
A newly discovered gene RBFOX1 may drive the first appearance of amyloid plaques in the brain, contributing to Alzheimer's disease. The study found that variants of RBFOX1 increase protein fragments making up amyloid plaques and disrupt critical connections between neurons.
Researchers found amyloid β protein fibrillation slowed down in microgravity, resulting in distinct morphologies. The study provides fundamental insights into pathological amyloid formation, highlighting the ISS as an ideal experimental environment.
Researchers have created new antiviral molecules by designing synthetic amyloid peptides that can inactivate viral proteins, thereby interfering with viral replication. These 'Pept-ins' specifically target the influenza A and Zika virus proteins.
Researchers develop lab-engineered model of human blood-brain barrier, discovering how APOE4 variant causes amyloid protein plaques to disrupt brain's vasculature. They identify specific vascular cell type and molecular pathway that promotes cerebral amyloid angiopathy pathology.
Researchers developed a single-molecule orientation imaging approach to study amyloid proteins, revealing nanoscale differences in their structures. The method provides insights into the fundamental biological mechanisms of disease, potentially contributing to the development of effective therapeutics.
Researchers have developed an antibody that can accurately detect and quantify toxic amyloid-beta oligomers, a hallmark of Alzheimer's disease. This discovery could lead to improved diagnostic methods and ultimately help monitor the progression of the disease.
Researchers found that acetylation at lysine 16 leads to disordered aggregates with high toxicity, highlighting the importance of protein shape in amyloid beta toxicity. The study aims to better understand the complexity of misfolded proteins and their role in neurodegenerative diseases like Alzheimer's.
Researchers at University of Malaga's BacBio laboratory have identified a new role for an amyloid protein, improving biological control methods in sustainable agriculture. The study reveals the dual functionality of the protein, which helps bacterial cells attach to plant surfaces, combat pathogens and improve fitness.
A study using mouse models of Alzheimer's disease found that high calcium levels in mitochondria are associated with plaque deposition and neuronal death. Researchers propose targeting calcium entry to the mitochondria as a promising new therapeutic approach.
Researchers developed simple molecular reagents that can simultaneously target and modulate various pathogenic factors in Alzheimer's disease. The reagents displayed redox-dependent reactivities against free radicals, metal-free and metal-bound amyloid-beta, and led to chemical modifications that altered its aggregation.
Researchers developed a compound that significantly reduced amyloid plaques, lessened brain inflammation, and diminished molecular markers of Alzheimer's disease. The findings suggest that drugs targeting different regions of amyloid-beta protein fragments and metal ions could improve outcomes for people with Alzheimer's.
Researchers used CRISPR/Cas9 to search for genes related to Alzheimer's disease and found that low levels of CIB1 lead to high amyloid beta production. The study suggests that regulating CIB1 and gamma secretase could be a new target for Alzhemier's disease therapy.
The A4 study found that higher levels of the amyloid protein in the brain are associated with an early stage of Alzheimer's disease. The study analyzed data from 4,486 participants and showed that amyloid burden is linked to a family history of disease, lower cognitive test scores, and reports of daily cognitive decline.
Researchers used high-speed atomic force microscopy to visualize the formation of Sup35NM amyloid fibrils in real time. They discovered that oligomers and fibrils have distinct structural characteristics, challenging previous assumptions about their relationship.
Researchers have identified a gene, endothelin-converting enzyme 2 (ECE2), that significantly increases the risk of Alzheimer's disease. The study found two mutations in ECE2 impairing its ability to break down amyloid beta protein, leading to increased levels and plaque formation.
A study published in eLife found that amyloid plaque formation directly causes brain tissue loss in animals, leading to progressive memory loss and loss of brain matter. However, lithium has been shown to reduce the life-shortening effects of this loss, suggesting a potential strategy to slow Alzheimer's disease progression.
A study reveals that Alzheimer risk genes are linked to microglia's response to amyloid-beta, a key protein in the disease. The researchers identified 11 new risk genes that are upregulated when facing increased amyloid-beta levels.
Researchers suggest that infectious agents may play a role in Alzheimer's disease, challenging the current amyloid hypothesis. Recent studies have linked certain viruses and bacteria to AD pathology, sparking fresh interest in this unorthodox approach.
Researchers have discovered a new role for amyloids in memory storage. They found that Orb2 protein self-aggregates form biochemically active aggregates at synapses, promoting synaptic translation and memory persistence. This finding challenges the traditional view of amyloids as neurotoxic structures.
Researchers have made a groundbreaking finding by using gold nanoparticles to label and visualize amyloid fibrils in their natural state. This breakthrough has significant implications for understanding the mechanisms of Alzheimer's disease and developing new treatments.
Researchers found that interferon triggers a cascade of inflammatory reactions leading to synapse loss and neuronal dysfunction in Alzheimer's disease. The study also suggests that blocking the IFN-triggered cascade could potentially reduce microglia activation and synapse loss.
Researchers developed a small molecule that can modify the coordination sphere of copper bound to amyloid-β, inhibiting its aggregation and toxicity. The study offers insights into chemically modifying neurotoxicity in Alzheimer's disease.
Researchers found that a protein called FRX1 functions in an amyloid form in healthy brains, contradicting the idea that only diseased brains store amyloids. This discovery has significant implications for the treatment of neurodegenerative diseases.
Scientists at Newcastle University have discovered a link between amyloid-beta levels in the blood and cardiovascular disease. Higher levels of amyloid-beta may indicate a higher risk of developing serious heart complications, such as heart failure and progression to heart disease.
Scientists at Chiba University discovered that human cells have a system to capture and degrade aberrant extracellular proteins. The research found that Clusterin, an extracellular molecular chaperone, selectively binds to amyloid β and forms a complex that is taken up by cells via the heparan sulfate receptor.
New research found that the accumulation of tau and amyloid proteins in the brain significantly alters gene expression, particularly in genes related to inflammation. The study provides new insights into the progression of Alzheimer's disease and highlights potential pathways for treatment.
A newly identified compound, C1, is a covalent gamma-secretase inhibitor that blocks the production of amyloids by inhibiting the enzyme's activity on the amyloid precursor protein. This approach avoids traditional enzyme inhibitors' severe side effects and shows promise for treating Alzheimer's disease.
Scientists develop a mathematical model that describes the chemical reactions responsible for amyloid fibril formation, revealing catalytic sites at interfaces and implications for laboratory data interpretation. The model has a simpler mathematical form than previous models, making it more accessible for future studies.
Researchers have identified a new protein called 'aggregatin' that accumulates in brain plaques and may be linked to Alzheimer's disease progression. Suppressing this protein could lead to future treatments aimed at slowing the disease's advance.
Scientists discovered a key mechanism underlying Alzheimer's pathology, revealing how amyloid-beta oligomers hijack norepinephrine signaling to activate GSK3-beta and hyper-phosphorylate tau protein. This rewiring of the alpha-2A adrenergic receptor may explain the failure of previous clinical trials targeting amyloid protein buildup.
A protein associated with ovarian cancer may contribute to the progression of Alzheimer's disease by impairing mitochondria function and causing neuronal damage. Researchers have identified OCIAD1 as a potential therapeutic target for the disease.
A Brazilian research team identified the presence of mutant p53 protein clusters in chemotherapy-resistant glioblastoma cells, which can lead to drug resistance. The study found that these clusters are organized in a way that makes them resistant to temozolomide, a common treatment for the disease.
A new study finds that tau protein is a more reliable predictor of brain atrophy in Alzheimer's patients than amyloid plaques. Tau PET imaging technology has the potential to accelerate clinical trials and improve individualized patient care.
Researchers found that individuals with objective subtle cognitive difficulties accumulated amyloid protein faster than cognitively normal individuals, even before symptoms appeared. This suggests that sensitive neuropsychological measures can detect subtle cognitive changes earlier in the disease process.
Researchers found people with subtle thinking and memory differences had faster amyloid accumulation and thinner brain regions compared to those with normal skills. The study challenges the long-held theory that beta-amyloid is the first sign of Alzheimer's disease.
A new study by McGill University researchers found that APOEε4 carriers have greater levels of tau tangles in memory centers, even after controlling for amyloid plaques. The study provides evidence that the gene's risk of dementia is related to both hallmark pathologies of Alzheimer's disease.
Researchers at Massachusetts General Hospital found that slow spontaneous vessel pulsations drive the clearance of substances from the brain. Targeting vasculature health may prevent or treat Alzheimer's disease.
Researchers at the University of Pittsburgh are using advanced MRI technology to study the connection between small vessel disease and Alzheimer's disease, aiming to identify new prevention and treatment targets. The team will visualize cerebrospinal fluid flow in real-time, shedding light on pathways linking SVD and CSF clearance.
Researchers at Tokyo University of Agriculture and Technology have discovered a novel amyloid protein, lipopolysaccharide binding protein (LBP), that induces amyloidosis in rats. This finding is significant as it may provide insights into the development of human amyloidosis and serve as a disease model for studying this condition.
Research at MIT's Picower Institute has shown that stimulating a specific brain rhythm via light or sound can reduce amyloid buildup and improve memory in Alzheimer's model mice. The technique, called GENUS, also shows promise in reducing inflammation and improving blood vessel function.
Scientists observed how alpha-synuclein protein variants change over time, identifying initial stages of protein aggregates linked to early onset familial cases. They also found evidence of which protein species are important for amyloid filament growth and distinct structures depending on the mutation.
A new study by MIT neuroscientists pinpointed the earliest emergence of amyloid protein plaques in the human brain, finding they correlate strongly with disease progression. The research uses a mouse model to track plaque development and shows that these regions eventually spread throughout the brain.
Researchers have developed a way to track the formation of soluble amyloid beta peptide aggregates implicated in the onset of Alzheimer's disease. The ruthenium-based fluorescent complexes bind to these aggregates, allowing researchers to monitor their progress and movements over time.
Researchers have discovered two short peptides that significantly improved memory and reduced physical changes in the brain of mice with Alzheimer's disease. The treatment uses a process of computer modeling and artificial intelligence to develop an optimized oral version of the drug, which could lead to new treatments for Alzheimer's.
Researchers at Osaka University used X-ray imaging to visualize Lewy bodies in post-mortem brains and found α-synuclein aggregates with cross-β structure. This discovery supports the idea that Parkinson's disease is a systemic amyloidosis, with implications for diagnosis and treatment.