Yeast cells can sometimes reverse the protein misfolding and clumping associated with diseases such as Alzheimer's, according to new research from the University of Arizona.
Cell & Microbiology
Dec 9, 2014
1
2
(Phys.org)—A team of researchers affiliated with the Whitehead Institute for Biomedical Research, MIT and the Howard Hughes Medical Institute, all in Massachusetts has found a prion-like protein in Arabidopsis thaliana, ...
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 ...
Biochemistry
Oct 3, 2016
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245
Grass plants can bind, uptake and transport infectious prions, according to researchers at The University of Texas Health Science Center at Houston (UTHealth). The research was published online in the latest issue of Cell ...
Cell & Microbiology
May 16, 2015
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1390
In a new study, researchers from the Case Western Reserve University School of Medicine have identified the structure of protein fibrils linked to a hereditary form of human prion disease. This insight, they say, reveals ...
Cell & Microbiology
Sep 12, 2022
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142
(Phys.org) —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 ...
Biochemistry
Aug 16, 2013
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0
"When they are healthy, they look like tiny spheres; when they are malignant, they appear as cubes" stated Giuseppe Legname, principal investigator of the Prion Biology Laboratory at the Scuola Internazionale Superiore di ...
Biochemistry
Jan 24, 2014
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1
New research out of the University of Wisconsin-Madison has, for the first time, detected prions responsible for chronic wasting disease (CWD) in samples taken from sites where deer congregate.
Ecology
May 3, 2018
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40
(PhysOrg.com) -- Antibodies that stick to a brain prion protein called PrP could be the key to treating prion diseases like variant CJD and preventing people accidentally exposed to prions from going on to develop the fatal ...
Feb 12, 2009
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When it comes to infectious agents, it doesn’t get much worse than prions. These misfolded proteins are highly resistant to a wide variety of extreme disinfectant procedures. They have been identified as the culprits ...
Cell & Microbiology
Feb 15, 2012
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0
A prion (pronounced /ˈpriː.ɒn/ ( listen)) is an infectious agent that is composed of protein. To date, all such agents that have been discovered propagate by transmitting a mis-folded protein state; the protein does not itself self-replicate and the process is dependent on the presence of the polypeptide in the host organism. The mis-folded form of the prion protein has been implicated in a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle and Creutzfeldt-Jakob disease (CJD) in humans. All known prion diseases affect the structure of the brain or other neural tissue, and all are currently untreatable and are always fatal. In general usage, prion refers to the theoretical unit of infection. In scientific notation, PrPC refers to the endogenous form of prion protein (PrP), which is found in a multitude of tissues, while PrPSC refers to the misfolded form of PrP, that is responsible for the formation of amyloid plaques that lead to neurodegeneration.
Prions are hypothesized to infect and propagate by refolding abnormally into a structure which is able to convert normal molecules of the protein into the abnormally structured form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This altered structure is extremely stable and accumulates in infected tissue, causing tissue damage and cell death. This stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult.
Proteins showing prion-type behavior are also found in some fungi and this has been important in helping to understand mammalian prions. However, fungal prions do not appear to cause disease in their hosts and may even confer an evolutionary advantage through a form of protein-based inheritance.
The word prion is a compound word derived from the initial letters of the words proteinaceous and infectious, with -on added by analogy to the word virion.
This text uses material from Wikipedia, licensed under CC BY-SA
