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.
Grass plants can bind, uptake and transport infectious prions, according to researchers at The University of Texas Health Science Center at Houston (UTHealth).
Researchers from the BIOCAPS Area of 'Biomaterials, tissue engineering and regenerative medicine' have managed to obtain bioceramics from shark teeth, which have already tested applications in the regeneration of bone tissue, particularly in the fields of traumatology and odontology.
Chronic wasting disease (CWD) — an infectious disease caused by prions — affects North American elk and deer, but has not been observed in humans. Using a mouse model that expresses an altered form of the normal human prion protein, researchers at University of California, San Diego School of Medicine have determined why the human proteins aren't corrupted when exposed to the elk prions.
Scientists from the Florida campus of The Scripps Research Institute have for the first time discovered a killing mechanism that could underpin a range of the most intractable neurodegenerative diseases such as Alzheimer's, Parkinson's and ALS.
The new study, published recently in the journal Brain, revealed the mechanism of toxicity of a misfolded form of the protein that underlies prion diseases, such as bovine spongiform encephalopathy (“mad cow disease”) and its human equivalent, Creutzfeldt-Jakob disease.
INRA scientists have shown for the first time that the pathogens responsible for scrapie in small ruminants (prions) have the potential to convert the human prion protein from a healthy state to a pathological state. In mice models reproducing the human species barrier, this prion induces a disease similar to Creutzfeldt-Jakob disease.
Researchers at NYU Langone Medical Center and elsewhere say that a vaccination they have developed to fight a brain-based, wasting syndrome among deer and other animals may hold promise on two additional fronts: Protecting U.S. livestock from contracting the disease, and preventing similar brain infections in humans.
Researchers at UC San Francisco and UC Berkeley have teamed up to create an innovative, integrated center for research on neurodegenerative diseases. Supported by a $3 million grant from the Glenn Foundation for Medical Research, the new center aims to pave the way to developing novel treatments for diseases such as Alzheimer's disease and Parkinson's disease by investigating the many ways that proteins can malfunction within cells.
V3 Healthcare Strategies, a Wisconsin-based Accountable Care Strategies company, announced the North American launch of the revolutionary Hypo-tec Needlestick Injury Prevention Product amidst an environment of infectious catastrophic diseases such as Ebola, Hanta & Hemorrhagic Fevers, while simultaneously protecting against all other infectious diseases such as HIV/AIDS, Hepatitis and more.
The misfolded and infectious prion protein that is a marker for variant Creutzfeldt-Jakob disease - linked to the consumption of infected cattle meat - has been detected in the urine of patients with the disease by researchers at The University of Texas Health Science Center at Houston (UTHealth) Medical School.
The prion diseases were originally discovered by Dr Gajdusek and Dr Gibbs. The first disease discovered was Kuru, which was affecting native tribes in the Papua New Guinea highlands in the 1950s.
New research from David Westaway, PhD, of the University of Alberta and Jiri Safar, MD, Case Western Reserve University School of Medicine has uncovered a quality control mechanism in brain cells that may help keep deadly neurological diseases in check for months or years.
New research from David Westaway, PhD, of the University of Alberta and Jiri Safar, PhD, Case Western Reserve University School of Medicine has uncovered a quality control mechanism in brain cells that may help keep deadly neurological diseases in check for months or years.
Creuztfeldt-Jakob disease (CJD) is a rare but fatal disease in humans. For the first time, the presence of infectivity in the blood of patients affected by sporadic and the new variant of CJD was established by scientists from the French National Institute for Agricultural Research (INRA) and the French National Veterinary School (ENVT), in collaboration with European partners.
Researchers at Chalmers University of Technology in Sweden, together with researchers at the Polish Wroclaw University of Technology, have made a discovery that may lead to the curing of diseases such as Alzheimer's, Parkinson's and Creutzfeldt-Jakob disease (the so called mad cow disease) through photo therapy.
Case Western Reserve University researchers today published findings that point to a promising discovery for the treatment and prevention of prion diseases, rare neurodegenerative disorders that are always fatal.
Two leading neurology researchers have proposed a theory that could unify scientists' thinking about several neurodegenerative diseases and suggest therapeutic strategies to combat them.
Scientists at Washington University School of Medicine in St. Louis have found a way that corrupted, disease-causing proteins spread in the brain, potentially contributing to Alzheimer's disease, Parkinson's disease and other brain-damaging disorders.
By directly manipulating a portion of the prion protein-coding gene, Whitehead Institute researchers have 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 these unusual but deadly diseases.
Mad cow disease and its cousin Creutzfeld-Jakob disease cause fatal spongy changes in brain tissue. Today, we know that these diseases are caused by prions, proteins that are folded incorrectly. A team of German researchers have now been able to follow how the diseased proteins aggregate and "infect" healthy ones on the atomic scale. Their report appears in the journal Angewandte Chemie.