Articles tagged with Prions
A new theory explains how prion diseases get started and kill neurons by showing that small amounts of misfolded PrP in the cytosol can cause cell death. The research also reveals a mechanism for the conversion of normal PrP to its toxic form, which can then spread and aggregate.
Researchers at Ohio State University and MIT found that a specific protein misfolding in an organelle leads to the transmission of transmissible spongiform encephalopathies. The misfolded proteins accumulate in the cytosol, altering cell metabolism and killing neural cells.
Researchers have developed a potential treatment for Creutzfeldt-Jakob disease (CJD) by using CpG oligodeoxynucleotides to stimulate the immune system. Studies on mice infected with scrapie prions showed improved survival times, suggesting a possible therapeutic approach for human CJD patients.
A vaccine has been shown to delay symptoms of prion brain disease in mice by inducing an immune response and producing antibodies. This breakthrough could potentially lead to a therapeutic response and prevent the disease in animals at risk.
Researchers found high levels of prions in skeletal muscle of mice, which may lead to transmission in cattle. The team suggests investigating the distribution of prions in the muscles of animals with prion diseases to improve diagnostic tools and disease understanding.
Researchers create antibody Fab D18, which blocks prion propagation and clears infectious prions from cell cultures. This breakthrough provides a potential therapeutic target for a human drug to cure established infection.
Researchers at UCSF have found that two existing drugs, quinacrine and chlorpromazine, can effectively treat mouse cells infected with prions, which cause rare neurodegenerative diseases. The study suggests that these drugs may also be effective in patients with advanced disease, paving the way for potential new treatment options.
Researchers at the University of Illinois Chicago have discovered a new way to identify prions, the causative agents of mad-cow and Creutzfeldt-Jakob diseases. The study used yeast to pinpoint unidentified prions, which may be related to the sudden appearance of CJD in older adults.
Researchers developed a highly sensitive immunoblot method to detect PrPSc in vCJD tissues, revealing its presence in lymphoid tissues and high concentrations in tonsil. The findings suggest new models for risk-management and highlight the need for further investigation into peripheral tissue transmission.
Researchers discovered that misfolded yeast prion proteins can alter protein synthesis and unveil silent genes, generating novel traits. By ignoring natural genetic stop signals, yeast may gain advantageous properties such as increased antibiotic resistance.
Researchers at the University of Chicago found that prions enable yeast to acquire multiple genetic changes simultaneously, leading to novel characteristics and growth properties. This discovery has broad implications for understanding evolutionary processes and how organisms respond to environmental fluctuations.
Researchers have discovered that normal prions may fine-tune neuronal functions at the cellular level through a signaling pathway. This discovery could provide new insights into how brain-degenerating diseases occur and potentially lead to treatments.
Researchers have identified a new mechanism by which prions replicate their structures in yeast, suggesting a general model for understanding protein aggregation in human diseases. The finding offers potential pathways to treatment and sheds light on the novel mode of inheritance used by yeast prions.
Scientists at UCSF have shown that deformed prion proteins can trigger normal proteins to change shape and become infectious. The researchers used a new system to introduce prions into yeast, eliminating the possibility of non-prion molecules contributing to infection.
Researchers have developed a novel diagnostic technique to directly detect prions in the cerebrospinal fluid, which is easily accessible for diagnostic purposes. This breakthrough method uses dual-color scanning for intensely fluorescent targets to identify single prion particles with high sensitivity.
Researchers at NIAID's Rocky Mountain Laboratories have identified a new class of compounds that slow the development of prion diseases in mice. The compounds, which include drugs used in cancer therapy, block the conversion of normal prion protein to an altered form, delaying disease progression. If successful in humans, this treatmen...
HHMI researchers found that yeast prions can transmit phenotypes through protein-protein interactions, hinting at the presence of undiscovered protein-based 'genetic elements'. This discovery offers a powerful new technique for exploring cells' machinery by selectively turning off specific proteins.
Researchers at UCSF discovered that prions, known for being deadly to cattle and humans, might serve a beneficial role in some organisms, including humans. They found evidence of prion-forming proteins in yeast species spanning 300 million years of evolution, suggesting prions aid survival.
Researchers establish direct link between prions causing mad cow disease and new-variant Creutzfeldt-Jakob disease in humans, challenging the species barrier theory. The study used transgenic mice to demonstrate that the strain of prion responsible for mad cow disease also causes new-variant CJD.
UCSF researchers developed a highly sensitive, rapid technique for detecting infectious prions causing prion diseases like 'mad cow' disease and Creutzfeldt-Jakob's disease. The assay reveals unique shapes of the protein strains, providing new insights into their biology.
Researchers have discovered a chaperone protein from yeast that controls a new, protein-only form of inheritance called a yeast prion. The discovery links the mechanism responsible for this new form of inheritance to neurodegenerative diseases such as Alzheimer's and Creutzfeld-Jakob disease.
Researchers have made a major breakthrough in understanding prion diseases by fully decoding the three-dimensional structure of the normal prion protein. This discovery may play a key role in the conversion of normal to disease-inducing prions, potentially leading to new treatments for BSE and Creutzfeld-Jacob disease.
Researchers weigh evidence for and against prion theory behind rare fatal diseases. A 24 researcher interview draws on interviews with all sides of the issue.