Articles tagged with Prions
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The new molecules are formed by a chain of 7 amino acids, each composed of only two different amino acids. These peptides have numerous applications, including generating electrical nanoconductors and fibrillar mini enzymes capable of acting as catalysts in the formation of organic nanomaterials.
CWRU School of Medicine researchers synthesized the first artificial human prion, offering hope for treatment and cure of brain-wasting diseases. The discovery provides a basis for understanding how mis-folded protein structure affects prion transmissibility and manifestation in humans.
Researchers discovered that microglia can defend against prion infections by trapping and destroying aggregated prion proteins. Eliminating microglia with a specific drug accelerated disease progression in infected mice. The findings suggest targeting microglia to slow the course of prion diseases, including Alzheimer's and Parkinson's.
Researchers at the University of Wisconsin-Madison have detected CWD prions in soil and water samples from sites where deer congregate. The study suggests that environmental reservoirs of prions could serve as an additional transmission route for CWD, highlighting the need for further research on the disease's spread and persistence.
Scientists from NIAID exposed research mice to brain samples from three people who died from a familial prion disease. Two mutations, Y226X and G131V, were found to be transmissible to mice. The finding highlights the hardiness of prion infectivity and potential risks associated with prion transmission.
Researchers found that soils with more than 18% clay are associated with a steep drop in cases of chronic wasting disease. Additionally, soils with pH above 6.6 also show higher incidence rates of the disease. These findings could inform future management schemes to prevent disease transmission.
Researchers discovered that a yeast protein's prion domain acts like a stress sensor, triggering the formation of protective droplets and gels to help cells recover from stress. This finding suggests that prion domains have a positive function beyond their association with disease-causing aggregates.
Researchers analyze brain slices from patients with Alzheimer's and cerebral amyloid angiopathy, finding distinct amyloid-beta prion strains associated with different disease types. Mutant amyloid-beta adopts self-propagating prion structure, imparting pathological conformation to normal amyloid-beta.
Case Western Reserve University researchers found infectious prions in CJD patient skin, which are 1,000-100,000 times lower than in brain tissue. This discovery raises concerns about potential disease transmission through surgeries and may pave the way for less invasive diagnostic techniques.
Researchers discover misfolded prion proteins in skin samples from Creutzfeldt-Jakob disease patients, but find lower amounts in the skin compared to brain tissue. The study raises concerns about possible transmission of prion diseases through surgical procedures involving the skin.
Researchers detected abnormal prion protein in the skin of nearly two dozen CJD patients and found that healthy mice infected with skin extracts developed prion disease. The study raises questions about potential surgical instrument contamination and the use of skin samples as a diagnostic test for human and animal prion diseases.
Researchers have developed a new system to study Creutzfeldt-Jakob disease in the laboratory, using brain cells derived from human stem cells. The method enables scientists to infect human cells with prions and replicate the proteins in the lab, providing valuable information for potential treatments.
A single amino acid change determines which species are vulnerable to a hereditary brain disease. The human, mouse and hamster forms of the protein have distinct three-dimensional structures at the atomic level.
Scientists have created a first simple and standardized research tool to study protein aggregation in live cells. The tool, called yTRAP, allows researchers to quantify, manipulate, and track protein aggregates in yeast cells.
A recent study has discovered an unexpected link between Parkinson's disease and prion diseases, revealing a complex interaction between α-synuclein and the prion protein. The findings suggest that α-synuclein deposits in brain cells can slow the progression of prion diseases.
Researchers have discovered a molecular mechanism behind prion protein's role in neurodegenerative diseases, including Creutzfeldt-Jakob and Alzheimer's. The study found that copper biases the prion protein towards its 'off' state, which reduces toxic signals to nerve cells.
Researchers at Michigan State University have discovered that altering pH levels can prevent prion proteins from aggregating and forming deadly diseases. The study used a laser technique to measure the speed at which proteins rearrange before clumping, and found that an antihistamine called astemizole was effective in reducing prion ag...
Researchers at Emory University School of Medicine and Georgia Tech found that the yeast protein Lsb2 forms a 'metastable' prion in response to elevated temperatures as a protective mechanism against stress. This discovery suggests that prions may play an adaptive role in cell survival.
A reliable blood test can identify prion disease before symptoms appear, allowing for non-invasive diagnosis and potentially preventing transmission through blood transfusions. Researchers successfully detected abnormal proteins in the blood of presymptomatic donors with 100% accuracy.
Researchers at UTHealth have developed a blood test that can detect Creutzfeldt-Jakob disease with 100% sensitivity and specificity. The test uses a protein misfolding cyclic amplification assay to identify prions, which are infectious proteins responsible for the disease.
Researchers found that prion diseases can infect the gut through contaminated meat, and that M cells are key to whether or not the infection takes hold. The study suggests that factors like inflammation and ageing may influence a person's risk of contracting prion diseases.
A team of researchers at Colorado State University is investigating the use of a test developed to detect early-stage chronic wasting disease in deer to identify the onset of brain disorders, including concussion-related trauma, in humans. The test may also be used to detect misfolded proteins found in people with Alzheimer's, Parkinso...
Researchers have made a breakthrough discovery on the formation and dissociation of pathogenic α-synuclein fibrils in Parkinson's disease, providing new insights into its progression. The study shows how high hydrostatic pressure breaks apart these toxic fibrils, shedding light on potential strategies for treating PD.
A team of scientists has isolated a mutated prion protein that can multiply in the lab but not in living animals. The mutant scrapie prion lacks a crucial stretch of amino acids necessary for animal infection, providing new insights into the mechanisms behind prion infectiousness.
Two new studies describe the function of PrPC, the physiological form of the prion protein. The protein promotes neurite growth and guides nerve impulses through homophilic interactions with neural cell adhesion molecules (NCAM).
Scientists at the University of Cambridge have developed a genetically modified fruit fly that can detect infectious prions in blood, leading to a potential breakthrough in diagnosing and preventing variant Creutzfeldt-Jakob disease (vCJD). This new test could be faster, more versatile, and more sensitive than current methods.
Researchers have discovered that prion proteins, previously known for causing fatal diseases, may also transmit beneficial traits from cell to cell. These intrinsically disordered proteins can adapt yeast cells to stressful environments and are conserved over millions of years in human cognates.
A Stanford University School of Medicine study suggests that prion proteins can help yeast survive hard times and pass advantageous traits down to their offspring. The researchers found that protein-based inheritance is more widespread than previously believed and could play a role in evolution.
A team of researchers has discovered the three-dimensional structure of infectious prions, revealing a four-rung β-solenoid architecture that allows for replication. This finding rules out existing theories and proposes a novel templating mechanism involving protein-protein interactions.
Scientists at the University of Alberta have identified the structure of the infectious prion protein, a misfolded protein causing BSE, Chronic Wasting Disease, and Creutzfeldt-Jakob Disease. The breakthrough study uses electron cryomicroscopy technology to reveal how infectious prions replicate and propagate.
Researchers describe distinct stages of prion disease in the mouse retina and define a model to test therapeutic approaches. They found that misfolded prion protein accumulation and inflammatory responses occur at specific time points, allowing for potential therapy evaluation.
Scientists have identified how prion proteins dock onto Schwann cells to maintain nerve integrity. The discovery resolves a 30-year-old question and holds promise for future treatments of Creutzfeld-Jakob disease and peripheral neuropathy.
Researchers have clarified the beneficial function of a brain protein associated with prion diseases, revealing its role in maintaining nerve cell insulation. The study found that properly folded proteins play a crucial role in keeping axons insulated, enabling rapid nerve signal propagation.
Researchers have developed a system to quickly screen millions of yeast cells for protein aggregates, offering new ways to explore their causes and potential therapies. The technology was used to study prions, Huntington's disease, and prion-switching, providing insights into the toxic effects of misfolded proteins.
Iowa State researchers discovered copper-induced misfolding of prion proteins, leading to inflammation and damage in brain tissue from a mouse model. The study's findings have major implications for understanding the role of metals in protein misfolding diseases, including Alzheimer's and Parkinson's.
Researchers at UTHealth will investigate the zoonotic potential of CWD and environmental prion contamination. The team aims to develop efficient detection methods for prion diseases, which are fatal brain disorders with long incubation periods.
A new neuronal culture system has been developed to study the early stages of prion neurotoxicity, specifically targeting dendritic spines. The research found that prions cause rapid and dramatic changes in spine density, leading to reduced neuron function before actual death.
A new timed amyloid seeding assay achieves or surpasses the sensitivity of currently available tests for transmissible spongiform encephalopathies, according to a report in The Journal of Molecular Diagnostics. This advanced assay offers better detection capabilities, allowing for clinical applications and surveillance programs.
Researchers examine the efficacy profile of anti-prion antibodies, finding that toxicity depends on factors such as antibody dose and binding region. The study suggests that antibodies targeting the flexible tail region of PrP may be more promising candidates for immunotherapy.
Scientists at SISSA create synthetic prion series for the first time, allowing precise control over their pathogenic behavior. The study verifies that these synthetic prions cause illness comparable to natural ones, paving the way for potential treatments for neurodegenerative diseases.
A new SISSA study uncovers a critical cofactor in prion protein transformation from 'good' to 'bad', revealing the role of copper in triggering the process. The study suggests a new potential target for treating prion diseases, including Creutzfeldt-Jakob disease and mad cow disease.
Researchers at NIAID can detect infectious prion protein in mouse brains within a week of inoculation, surpassing prior detection times of six weeks. The study found that the protein was generated outside blood vessels in a specific brain region where drug treatment could be targeted.
Researchers have identified a new type of prion causing Multiple System Atrophy (MSA), a neurodegenerative disorder with similarities to Parkinson's disease. The discovery raises concerns about treatments and research involving contact with brain tissue from MSA patients.
A recent study proposes that sequestered prion protein may be involved in depression by modulating monoaminergic systems and causing desensitization of dopamine receptors. The research found increased levels of serotonin receptors and dopamine in mice lacking normal prions, leading to depressive-like behavior.
Researchers tested transgenic mice and rabbits for susceptibility to prions from various species, revealing that rabbits are susceptible to TSE after exposure to prions from other animals. The studies also showed that rabbit PRNP gene and its normal PrPC protein product do not provide absolute resistance to prion disease.
Researchers at University of Edinburgh's Roslin Institute discovered that prions build up in Peyer's patches before spreading to the brain. This finding could enable earlier detection and treatment of prion diseases, including variant Creutzfeldt-Jakob disease and bovine spongiform encephalopathy.
Scientists confirm neuroprotective function of PrPC against epilepsy using four animal models, revealing its crucial role in preventing seizures. The study's precision and collaboration between international institutes make it a significant reference point in the field.
Scientists develop synthetic prions to study prion disease, demonstrating similarity with natural disease-causing prions. The researchers also explore the transmission capabilities of human prion mutations in mice, revealing the importance of expressing mutant human PrP for infection.
Research by Eric Kandel's lab shows prion-like proteins, like those causing mad cow disease, are critical for maintaining long-term memories in mice. These proteins work by creating aggregated structures that turn on protein synthesis necessary to maintain the memory.
University of Alberta scientists investigate physical principles underlying prion protein formation, with potential applications for diseases like Alzheimer's and Parkinson's. Their recent discovery sheds light on microscopic mechanisms governing protein misfolding, offering a new step towards developing therapeutics.
Researchers at UTHealth discovered that grass plants can bind, uptake and transport infectious prions, which can act as carriers of the disease. The study suggests that plants may play an important role in environmental prion contamination and horizontal transmission of diseases like CWD.
A study published in the Journal of Clinical Investigation reveals a small loop in the human prion protein confers resistance to chronic wasting disease. The discovery provides a potential therapeutic target for developing new treatments for prion diseases, which are currently fatal and have no effective treatment.
Researchers have discovered the N-terminal domain of Hsp104 plays a crucial role in its ability to dissolve prions and other misfolded proteins. This finding opens up new research directions for designing and engineering Hsp104 to combat human disease proteins.
Scientists at NYU Langone Health successfully vaccinated deer against chronic wasting disease (CWD), a fatal brain disorder caused by prions. The vaccine holds promise against similar brain infections in humans and may prevent the spread of CWD to U.S. livestock.
Researchers discovered that yeast cells can clear themselves of misfolded prion proteins by activating a stress response and producing specific heat-shock proteins. This finding suggests a new approach to treating diseases associated with prion misfolding, such as Alzheimer's, Huntington's, and Parkinson's.
Researchers will explore protein quality-control decline in dementias, illnesses. Badly formed proteins can lead to devastating physiological consequences by acting as templates, spreading misfolding like an infection.
Researchers discovered a biochemical communication system behind 'stuck fermentation,' enabling bacteria to switch yeast from sugar to other food sources without altering its DNA. Winemakers can now avoid stuck fermentations by altering sulfur dioxide levels or adding yeast strains that overpower bacteria.
A self-repairing mechanism known as neurogenesis partially counteracts neuronal loss in neurodegenerative diseases. Newborn neurons generated in the dentate gyrus integrate into brain circuitry, maintaining some functions at early stages of disease progression.
A new assay can detect toxic prions in blood samples from humans with variant Creutzfeldt-Jakob Disease (vCJD) and asymptomatic animals. The test, developed by French researchers, was tested on vCJD patients and non-infected controls, accurately identifying infected individuals.
Researchers found that bank vole PrP is a universal acceptor for prions, making it an intrinsic property of the protein. This discovery has broader implications for understanding prion disease transmission and developing strategies to prevent its spread.