Mad Cow Disease or BSE (bovine spongiform encephalopathy) is a progressive neurological disorder of cattle that results from infection by an unusual transmissible agent called a prion. The nature of the transmissible agent is not well understood. Currently, the most accepted theory is that the agent is a modified form of a normal protein known as prion protein. For reasons that are not yet understood, the normal prion protein changes into a pathogenic (harmful) form that then damages the central nervous system of cattle.
Plastic surgery patients were getting infections with antibiotic resistant bacteria, and no one knew why. UConn microbiologists found the answer in a leech's gut. Their research, published today in mBio, provides proof that tiny levels of antibiotics found in the environment can encourage bacterial resistance.
Chronic wasting disease did not cross the species barrier to infect cynomolgus macaque monkeys during a lengthy investigation by National Institutes of Health scientists exploring risks to humans.
Scientists at the University of Alberta may have found possible targets for therapeutic interventions in the fight against Lou Gehrig's disease.
Postnova Analytics reports that the Department of Molecular Biology & Biotechnology at the University of Sheffield is using their AF2000 Field Flow Fractionation system to investigate the mechanism of amyloid formation, a protein mis-folding process implicated to be the cause of Alzheimer’s and other neurodegenerative diseases.
Creutzfeldt-Jakob disease (CJD)- the human equivalent of mad cow disease- is caused by rogue, misfolded protein aggregates termed prions, which are infectious and cause fatal damages in the patient's brain. CJD patients develop signature microscopic sponge-like holes in their brains.
Research carried out at the University of Kent has the potential to influence the future search for treatment of neurodegenerative diseases that are linked to a family of protein molecules known as 'amyloid'.
A new kind of antibody targets a feature shared by proteins thought to cause the most damage in Alzheimer's disease, Parkinson's disease, and related conditions, creating potential for a unified treatment approach.
Recent research on Parkinson's disease has focused on the gut-brain connection, examining patients' gut bacteria, and even how severing the vagus nerve connecting the stomach and brain might protect some people from the debilitating disease.
A new study has uncovered a molecular mechanism in the prion protein, a protein responsible for neurodegenerative diseases, which may explain why nerve cells degenerate in these disorders.
Prion diseases are scary, incurable and fatal. They first gained notoriety when cows became infected by prion proteins and, in turn, infected people. Fervor surrounding mad cow disease resulted in the U.S. banning imports of beef from the European Union for 15 years.
The highly pathogenic Staphylococcus aureus bacteria is one of the five most common causes of hospital-acquired infections. In the US alone, approximately 500,000 patients at hospitals contract a staph infection. It is the bacteria responsible for MRSA, for which there is no vaccine.
The detection of prions in the blood of patients with variant Creutzfeldt-Jakob disease could lead to a noninvasive diagnosis prior to symptoms and a way to identify prion contamination of the donated blood supply, according to researchers at McGovern Medical School at The University of Texas Health Science Center at Houston.
As demand for the widely used blood thinning drug heparin continues to grow, experts worry of possible shortages of the essential medication.
Prion proteins, best known as the agents of deadly brain disorders like mad cow disease, can help yeast survive hard times and pass the advantageous traits down to their offspring, according to a new study by researchers at the Stanford University School of Medicine.
Groundbreaking research from the University of Alberta has identified the structure of the infectious prion protein, the cause of "mad cow disease" or BSE, chronic wasting disease in deer and elk and Creutzfeldt-Jakob disease in humans, which has long remained a mystery.
Ever since the prion gene was discovered in 1985, its role and biological impact on the neurons has remained a mystery.
Scientists have clarified details in understanding the beneficial function of a type of protein normally associated with prion diseases of the brain, such as bovine spongiform encephalopathy (commonly known as mad cow disease) and its human counterpart, variant Creutzfeldt-Jakob disease.
Led by Claudio Soto, Ph.D., researchers from McGovern Medical School at The University of Texas Health Science Center at Houston have been awarded $11 million from the National Institute of Allergy and Infectious Diseases to study the pathogenesis, transmission and detection of prion diseases - such as chronic wasting disease in deer - that can potentially spread to humans.
Thank the little "muscles" in your neurons for allowing you to remember where you live, what your friends and family look like and a lot more.
Transmissible spongiform encephalopathies (TSEs), or prion diseases, are a family of rare progressive, neurodegenerative illnesses that affect both humans and animals. TSE surveillance is important for public health and food safety because TSEs have the potential of crossing from animals to humans, as seen with the spread of mad cow disease, or bovine spongiform encephalopathy (BSE). A study in The Journal of Molecular Diagnostics describes an advanced assay that offers better sensitivity than currently available tests for detecting a prion disease affecting elk.