Topic prions

News prions

• 'Good' prion-like proteins boost immune response, UT Southwestern scientists report

  A person's ability to battle viruses at the cellular level remarkably resembles the way deadly infectious agents called prions misfold and cluster native proteins to cause disease, UT Southwestern Medical Center researchers report.This study marks the first discovery of so-called "good" prion-like p more

• Multitarget Drugs against Prion Diseases

  The central nervous systems of humans and cattle alike are attacked by prions (abnormal insoluble amyloidogenic proteins) when they suffer from Creutzfeldt–Jakob disease (CJD) or bovine spongiform encephalopathy (BSE). This causes a steady deterioration of neurological function and ultimately leads more

• BSE pathogens can be transmitted by air

  Airborne prions are also infectious and can induce mad cow disease or Creutzfeldt-Jakob disorder. This is the surprising conclusion of researchers at the University of Zurich, the University Hospital Zurich and the University of Tübingen. They recommend precautionary measures for scientific labs, sl more

Publications prions

• Editors' Choice

  Astrophysics: Planetary Confinement | Molecular Biology: Prions: A New Part to Play | Chemistry: Making Methanol | Genetics: Isoform Identification | Biomedicine: Aiming Even Lower | Entomology: A Toast to Fruitfly Health | Ecology: Fluctuating Forests more

• Ultrasensitive detection of scrapie prion protein derived from ARQ and AHQ homozygote sheep by interspecies in vitro amplification

  ABSTRACT Prions, infectious agents causing transmissible spongiform encephalopathies (TSEs), are composed primarily of the pathogenic form (PrPSc) of the host‐encoded prion protein (PrPC). The susceptibility of sheep to scrapie is determined by polymorphisms in the coding region of the prion prot more

• De novo design of synthetic prion domains [Biochemistry]

  Prions are important disease agents and epigenetic regulatory elements. Prion formation involves the structural conversion of proteins from a soluble form into an insoluble amyloid form. In many cases, this structural conversion is driven by a glutamine/asparagine (Q/N)-rich prion-forming domain. Ho more

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