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Categories: Biology: Microbiology, Mathematics: Statistics
Published The shape of infectious prions
(via sciencedaily.com) Prions are unique infective agents -- unlike viruses, bacteria, fungi and other parasites, prions do not contain either DNA or RNA. Despite their seemingly simple structure, they can propagate their pathological effects like wildfire, by "infecting" normal proteins. PrPSc (the pathological form of the prion protein) can induce normal prion proteins (PrPC) to acquire the wrong conformation and convert into further disease-causing agents.
Published Breakthrough in understanding secret life of prion molecules
(via sciencedaily.com) New research has uncovered a quality control mechanism in brain cells that may help keep deadly neurological diseases in check for months or years.
Published Targeted culling of deer controls disease with little effect on hunting
(via sciencedaily.com) Chronic wasting disease, the deer-equivalent of mad cow disease, has crept across the US landscape from west to east, and was first detected in the Midwest in 2002. Little is known about its potential to infect humans. Now researchers offer a first look at the long-term effectiveness of the practice of culling deer in areas affected by CWD to keep the disease in check.
Published New models advance the study of deadly human prion diseases
(via sciencedaily.com) By directly altering the gene coding for the prion protein (PrP), researchers have created mouse models of two neurodegenerative prion diseases, each of which manifests in different regions of the brain. These new models for fatal familial insomnia (FFI) and Creutzfeldt-Jakob disease (CJD) accurately reflect the distinct patterns of destruction caused by the these diseases in humans.
Published Flexible tail of the prion protein poisons brain cells
(via sciencedaily.com) Prion proteins are the infectious pathogens that cause Mad Cow Disease and Creutzfeldt-Jakob disease. They occur when a normal prion protein becomes deformed and clumped. The naturally occurring prion protein is harmless and can be found in most organisms. In humans, it is found in our brain cell membrane. By contrast, the abnormally deformed prion protein is poisonous for the brain cells. Scientists have now discovered that the prion protein has a kind of switch that controls its toxicity.
Published The ribosome: New target for antiprion medicines
(via sciencedaily.com) The key to treating neurodegenerative prion diseases such as mad cow disease and Creutzfeldt-Jakob disease may lie in the ribosome, the protein synthesis machinery of the cell. Prion diseases are fatal neurodegenerative diseases caused by misfolding of prion proteins. Examples of prion diseases are scrapie in sheep, mad cow disease and Creutzfeldt-Jakob disease in human.
Published Potential therapy for human prion disease
(via sciencedaily.com) Scientists have for the first time identified a pair of drugs already approved for human use that show anti-prion activity and, for one of them, great promise in treating rare and universally fatal disorders, such as Creutzfeldt-Jakob disease, caused by misfolded proteins called prions.
Published Protective prion keeps yeast cells from going it alone
(via sciencedaily.com) A team of scientists has added markedly to the job description of prions as agents of change, identifying a prion capable of triggering a transition in yeast from its conventional single-celled form to a cooperative, multicellular structure. This change, which appears to improve yeast's chances for survival in the face of hostile environmental conditions, is an epigenetic phenomenon -- a heritable alteration brought about without any change to the organism’s underlying genome.
Published Normal prion protein regulates iron metabolism
(via sciencedaily.com) An iron imbalance caused by prion proteins collecting in the brain is a likely cause of cell death in Creutzfeldt-Jakob disease, researchers have found. The breakthrough follows discoveries that certain proteins found in the brains of Alzheimer's and Parkinson's patients also regulate iron.
Published Discovery may explain how prion diseases spread between different types of animals
(via sciencedaily.com) Medical researchers have made a discovery that may explain how prion diseases, like chronic wasting disease and mad cow disease, adapt in order to spread between various types of animals.
Published Brain inflammation likely key initiator to Prion and Parkinson's disease
(via sciencedaily.com) Researchers have shown that neuro-inflammation plays a crucial role in initiating prion disease.
Published Crows don't digest prions, may transport them to other locations
(via sciencedaily.com) Crows fed on prion-infected brains from mice can transmit these infectious agents in their feces and may play a role in the geographic spread of diseases caused by prions, such as chronic wasting disease or scrapie.
Published 'Mad Cow' blood test now on the horizon
(via sciencedaily.com) A simple blood test for Creutzfeldt-Jakob Disease and Mad Cow disease is a step closer, following a breakthrough by medical researchers in Australia.
Published Copper facilitates prion disease, scientists show
(via sciencedaily.com) Many of us are familiar with prion disease from its most startling and unusual incarnations —- the outbreaks of “mad cow” disease (bovine spongiform encephalopathy) that created a crisis in the global beef industry. Or the strange story of Kuru, a fatal illness affecting a tribe in Papua New Guinea known for its cannibalism. Both are forms of prion disease, caused by the abnormal folding of a protein and resulting in progressive neurodegeneration and death.
Published New compounds inhibit prion infection
(via sciencedaily.com) Researchers have identified a new class of compounds that inhibit the spread of prions, misfolded proteins in the brain that trigger lethal neurodegenerative diseases in humans and animals. Scientists have now developed compounds that clear prions from infected cells derived from the brain.
Published 'Mad cow disease' in cattle can spread widely in autonomic nervous system before detectable in the central nervous system
(via sciencedaily.com) Bovine spongiform encephalopathy (BSE, or "mad cow disease") is a fatal disease in cattle that causes portions of the brain to turn sponge-like. This transmissible disease is caused by the propagation of a misfolded form of protein known as a prion, rather than by a bacterium or virus. Previous research has reported that the autonomic nervous system (ANS) becomes affected by the disease only after the central nervous system (CNS) has been infected. In a new study researchers found that the ANS can show signs of infection prior to involvement of the CNS.
Published Prions in the brain eliminated by homing molecules
(via sciencedaily.com) Toxic prions in the brain can be detected with self-illuminating polymers. The originators, at Linköping University in Sweden, has now shown that the same molecules can also render the prions harmless, and potentially cure fatal nerve-destroying illnesses.
Published New yeast prion helps cells survive
(via sciencedaily.com) One of the greatest mysterious in cellular biology has been given a new twist. Researchers now show that prions, proteins that transmit heritable information without DNA or RNA, can contribute to drug resistance and cellular adaptation. Their discovery of a yeast prion with these properties demonstrates the active role of the prion conversion in cellular fitness adaptation, providing new insights into the potentially broader function of prions in living organisms.
Published Most lethal known species of prion protein identified
(via sciencedaily.com) Scientists have identified a single prion protein that causes neuronal death similar to that seen in "mad cow" disease, but is at least 10 times more lethal than larger prion species.
Published New findings about the prion protein and its interaction with the immune system
(via sciencedaily.com) Scrapie is a neurodegenerative disease which can function as a model for other diseases caused by an accumulation of proteins resulting in tissue malformations (proteinpathies), such as Alzheimer's and Parkinson's disease. Many questions regarding these diseases still remain unanswered. A new study has uncovered a number of factors relating to the uptake of the prion protein (PrPSc) associated with the development of this disease and how this protein interacts with the immune cells in the intestines.