Articles tagged with Prions
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Researchers found that heparin interactions with the terminal domains of murine prion protein stabilize the protein, preventing aggregation. This stabilization prevents prion conversion and disease. Heparin may establish groundwork for therapeutic use against prion diseases.
Scientists at the Stowers Institute for Medical Research have identified a protein that is essential for creating and maintaining long-term memories. The protein, Orb2A, must be tightly regulated to form only in specific neural circuits, and its conversion into a prion-like state can be triggered by nerve cell stimulation.
A GW researcher has found a connection between the pathogenesis of prion disease and HIV, discovering that impairment of cellular cholesterol metabolism is key to their development. The study suggests that stimulation of ABCA1, a cellular cholesterol transporter, could inhibit conversion of prions into a pathogenic form.
Researchers at SISSA investigated the structural elements of prion proteins, finding that misfolding originates in the N-terminal region. This knowledge is crucial for developing drugs and therapeutic strategies against diseases like Creutzfeldt-Jakob disease.
Scientists have discovered a natural protective response in brain cells that can minimize the production of diseased prion proteins, potentially helping to prevent or delay neurological diseases such as Creutzfeldt-Jakob disease. The study also found that this mechanism may be relevant to other neurodegenerative diseases like Alzheimer's.
Researchers found that prion protein misfolding is a key trigger for spongiform encephalopathy and neurodegeneration. The study proposes an effective model and testing method for cytosolic forms of prion protein, highlighting the complex intracellular environment as a contributing factor.
A survey of over 32,000 appendix samples found abnormal prion protein in 16 people, indicating a prevalence of 493 per million population. Researchers estimate one in 2,000 people are likely to be carriers, with no particular age group or geographic region affected.
Researchers at Case Western Reserve University discovered that recombinant human prion protein inhibits the propagation of prions, which cause fatal brain diseases. The study's findings have significant implications for treating prion diseases, including Creutzfeldt–Jakob disease and mad cow disease.
Researchers Charles Weissmann and Adriano Aguzzi received the prestigious Hartwig Piepenbrock-DZNE Prize for their groundbreaking work on prion diseases. Their findings shed light on fundamental mechanisms of neurodegenerative disorders, including Alzheimer's and Parkinson's disease.
Researchers at WashU Medicine found that corrupted proteins spread in the brain through a specific type of receptor called heparan sulfate proteoglycans (HSPGs). Blocking this receptor may aid treatment of Alzheimer's and Parkinson's diseases, potentially unifying understanding and treatment of multiple neurodegenerative conditions.
Researchers at Whitehead Institute created mouse models of two neurodegenerative diseases that are fatal in humans. The highly accurate reproduction of disease pathology seen with these models should advance the study of prion diseases, including Creutzfeldt-Jakob disease and fatal familial insomnia.
University of Alberta researchers have made a breakthrough in understanding prion protein interactions, paving the way for designing molecules that can block prion infection. The discovery opens up possibilities for treating human victims and preventing livestock diseases such as BSE.
Researchers discover that prion protein has a 'switch' controlling its toxicity, which can be triggered by antibodies targeting the flexible tail. The study finds that only antibodies targeting the tail are suitable for use as potential drugs, while those triggering the switch are harmful.
Researchers developed a modified prion protein that resists changing its shape, preventing the propagation of neurodegenerative diseases. The study provides a novel pharmacologic strategy to develop new drugs targeting prion protein and stabilizing its normal shape.
Researchers at Uppsala University have identified the ribosome as a key player in prion diseases, such as mad cow disease and Creutzfeldt-Jakob disease. The discovery suggests that antiprion medicines targeting the ribosome's protein folding activity may be effective in treating these fatal neurodegenerative diseases.
Scientists have identified two compounds, tacrolimus and astemizole, that show anti-prion activity and promise in treating human prion diseases. Astemizole, an antihistamine, stimulates autophagy, a process involved in protein misfolding neurodegenerative diseases like Alzheimer's and Parkinson's.
A team of scientists has identified a prion that triggers epigenetic changes in yeast, leading to the adoption of a multicellular structure for improved survival. This finding suggests that prions may play a role in beneficial traits and could have implications for understanding human diseases such as cancer.
Researchers at Case Western Reserve University found that normal prion protein PrPc plays a crucial role in regulating iron metabolism, which may contribute to neuronal death in CJD. Iron imbalance caused by prion aggregation leads to neurotoxicity and brain cell death.
Researchers at the University of Alberta have made a breakthrough in understanding how prion diseases spread between different types of animals. By studying the adaptation process, they aim to determine why certain strains can infect one type of animal but not another.
Research shows that crows can ingest and excrete infectious prions without being destroyed, posing a risk for the geographic spread of diseases. Crows may play a role in the transmission of prion-caused diseases through their feces.
Scientists at the University of Leeds found that prion protein regulates zinc absorption in brain cells, linking it to memory and learning capabilities. The study may lead to new treatments for neurodegenerative diseases like Alzheimer's.
Researchers found reducing copper in mice with prion disease delays onset by 20 days, with less abnormal protein in brains. However, study does not advocate for copper depletion as therapy and aims to learn more about copper function and prion disease biochemical workings.
University of Alberta researchers have identified a new class of compounds that can clear prions from infected cells. These compounds demonstrate promise in treating prion-induced brain disorders, such as Creutzfeldt-Jakob disease.
Researchers found that prions can accumulate in the gut and infect the autonomic nervous system (ANS) before affecting the central nervous system (CNS). The study identified three possible routes for BSE prion ascension to the brain, shedding light on the pathogenesis of the disease.
A study published in Cell reveals that follicular dendritic cells (FDCs) originate from perivascular precursor cells, which decorate blood vessel walls. This discovery sheds light on the development of lymphoid follicles and has implications for understanding chronic inflammatory conditions and prion infections.
A new study suggests that the toxic effects of the huntingtin protein on cells may not be driven exclusively by its length, but also by which other proteins are present in the cell. The researchers found that yeast cells containing human huntingtin protein with an expanded region exhibited toxicity differences based on the presence of ...
Researchers at Linköping University have discovered that homing molecules can render toxic prions harmless, decreasing their toxicity and infectibility. This breakthrough could lead to the treatment of diseases such as Alzheimer's, which is caused by amyloid plaque with a similar but slower course.
Researchers at RIKEN Brain Science Institute discovered a yeast prion called Mod5 that confers survival advantages by granting cellular resistance to antifungal agents. The study reveals the active role of prion conversion in cellular fitness adaptation, providing new insights into the broader function of prions in living organisms.
A University of Alberta research team discovered that ozone-treated water can eradicate infectious proteins from cattle brain matter, providing a potential solution for decontaminating wastewater and sterilizing neurosurgical equipment. This breakthrough technique offers improved prion removal methods in meat processing plants and surg...
Researchers found prions in one-third of wild yeast strains, creating diverse new traits, nearly half of which are beneficial. This discovery suggests that prions may be an inherent survival mechanism, helping yeasts adapt to changing environments and evolve in response to stress.
Scientists at Scripps Research Institute have identified a single prion protein that causes neuronal death similar to 'mad cow' disease, with toxic effects up to 10 times more potent than larger prion species. The study opens new avenues for exploring neurodegenerative disorders like Alzheimer's and Parkinson's diseases.
Medical researchers have discovered a hidden process that erases the shadoo protein in infected brains, up to seven months before physical symptoms of prion diseases like BSE or mad cow disease appear. This new understanding opens up research opportunities into attenuating the disease.
Scientists found an antidepressant and antipsychotic that effectively combat prion infections in mice, potentially treating human prion diseases like Creutzfeldt-Jakob disease. The compounds also reduced disease symptoms and delayed symptom onset.
Researchers found that MAVS proteins, similar to deadly prions, play a crucial role in innate immunity by forming clusters on mitochondrial membranes to defend against viral assault. This discovery may deepen our knowledge of host defense and provide insights into the development of new treatments for prion-related diseases.
Research in yeast reveals that cellular stress can induce the formation of infectious protein particles called prions, which are associated with neurodegenerative disorders. The study identifies a protein called Lsb2 that promotes spontaneous prion formation under stress conditions.
Researchers at University of Western Ontario will investigate whether prion protein is a therapeutic target in Alzheimer's disease. The team aims to test their hypothesis on the interaction between prion protein and amyloid beta, which could lead to novel therapeutics for both Prion diseases and Alzheimer
Researchers have identified two gene classes associated with new prion formation in yeast, which may provide a genetic key to understanding neurodegenerative disorders like Creutzfeldt-Jakob and Huntington's disease. The study found that genes important for prion generation also increased toxicity in the presence of certain proteins.
USGS research suggests that certain lichens can break down the infectious proteins responsible for chronic wasting disease, a prion disease fatal to wild deer and elk. The study found that some lichen species contain a protease enzyme capable of significantly breaking down prions in the lab.
Researchers at the National Institute of Allergy and Infectious Diseases (NIAID) have developed a highly sensitive blood test for detecting human prion diseases, which are fatal brain disorders. The new method improves upon previous tests by being 10,000 times more sensitive and can rapidly detect abnormal prion proteins in blood plasma.
Researchers at Brown University have discovered that mutant prions can aid cells in overcoming harmful protein misfolding, a process thought to be catastrophic. The findings suggest that targeted interventions at various stages of the misfolding process can enable cells to overcome the problem.
Researchers have discovered that polymers of amino acid lysine can block the propagation of prions, halting their spread in test tubes and cultured cells. In animal models, mice treated with polylysines showed improved symptoms, longer survival, and lower prion levels
A study published in Cell identified the motors driving non-infectious prion proteins up and down long neuronal transport pathways. The research sheds light on how these proteins interact with infectious forms to cause disease, potentially aiding therapies for neurodegenerative diseases like Alzheimer's.
Researchers have developed a new assay test that can detect minute amounts of Creutzfeldt-Jakob disease-causing prions in human blood, making it possible to screen donated blood before acceptance. This could lead to improved and earlier diagnosis for patients and a better understanding of the prevalence of the disease.
Researchers found that prion-tainted aerosols can induce disease in mice by transferring to the brain and colonizing it. The study suggests airborne transmission of prions may be a risk, prompting potential regulations to minimize infection risks.
Researchers found that inhalation of prion-tainted aerosols induced disease with frightening efficiency in mice, infecting all within a single minute. This discovery challenges the widely held view that prions are not airborne and suggests precautionary measures for scientific labs, slaughterhouses, and animal feed plants.
Researchers at the University of Kentucky have discovered that plasminogen accelerates prion disease progression. The study identifies plasminogen as a potential therapeutic target for prion diseases, which could improve treatment options for patients.
Researchers found that prions can adapt and change their properties when transferred between cell lines, evolving into more effective strains. The study suggests the normal prion protein may be an effective therapeutic target for diseases like BSE and CWD.
A new test method has been developed to detect and measure infectious agents called prions that cause devastating brain-damaging conditions. The real time quaking induced conversion assay (RT-QuIC) can detect miniscule amounts of infectious prions, potentially leading to early treatment and prevention.
Researchers have discovered that plasminogen, a protein that breaks down blood clots, accelerates the progression of prion diseases by putting rogue prion proteins into overdrive. This finding presents a promising new target for anti-prion therapy, which could improve treatment options for patients suffering from prion diseases.
A team of researchers at Brown University found that the size of prion protein aggregates, not their number, determines their efficiency in spreading in yeast cells. The study suggests that controlling aggregate size may be a more effective strategy for developing treatments for prion infection and potentially other neurodegenerative d...
Researchers at Case Western Reserve University have discovered a new sporadic prion protein disease, Variably protease-sensitive prionopathy (VPSPr), which shares genotype characteristics with Creutzfeldt-Jakob disease. The abnormal prion protein in VPSPr exhibits distinct characteristics different from other prion diseases.
Scientists discovered that abnormal prions, a type of infectious protein, can suddenly appear in healthy brain tissue when coated onto metal surfaces. This finding raises questions about the origin of these deadly proteins and their potential role in neurodegenerative diseases.
A study by Adriano Aguzzi and Christina Sigurdson found that the local structure of PrPC protein influenced prion transmissibility between different species. The researchers identified a molecular switch controlling interspecies prion disease transmission in mice, providing new insight into food safety risks associated with BSE.
Researchers at CIC bioGUNE and Universidad de Kentucky have discovered a new method to control the stability of prions responsible for transmissible spongiform encephalopathies in deer. This finding has significant implications for controlling the epidemic affecting deer in the USA and Canada.
Researchers discovered that thin-billed prions visit the Antarctic waters for 90% of their molting period, while some individuals moulting further north off South America's coast. This flexibility allows them to adapt to unpredictable weather conditions and survive in vast ocean areas.
Scientists have discovered a new form of prion disease that causes brain artery damage, distinct from the typical sponge-like brain deterioration. The study may hold clues for treating Alzheimer's disease, as researchers found that removing a specific anchor from prion protein could prevent plaque accumulation and block fluid drainage.
A new report reveals that a prion-like protein called CPEB may participate in memory in higher eukaryotes, including sea slugs. The protein's ability to switch between distinct conformational states suggests it could maintain stable states with unstable biological molecules.
Scientists have determined how a normal protein can be converted into a prion, an infectious agent causing fatal brain diseases in humans and mammals. The study provides the strongest evidence yet to prove the prion hypothesis and offers insights into molecular mechanism and potential therapeutic targets for these diseases.
Researchers developed a rapid-acting disinfectant that kills bacteria, viruses and fungi on surgical instruments, including those resistant to conventional disinfectants. The new formula is safer, cheaper and more effective than existing treatments against prions, which cause deadly illnesses.
Prions, infectious protein particles devoid of DNA, can develop mutations and adapt through natural selection, leading to drug resistance. The study suggests that normal prion proteins may be more effective therapeutic targets than their abnormal forms, offering new hope for treating deadly neurodegenerative diseases.