Infectious prions or PrPSc -- misfolded versions ... data reveal a four-rung ß-solenoid architecture as the basic element for the structure of the mammalian prion GPI-anchorless PrPSc.

"This discovery is very interesting from a basic scientific point of view ... or conformation, of the prion's protein structure. Building on research that identified the part of the prion protein ...

Although the mammalian prion protein (PrP) induces a fatal neurodegenerative disease following conformational conversion, changes in the structure ... of these factors on basic cellular physiology ...

Prions, mysterious shape-shifting proteins, can lead to brain disorders such as Creutzfeldt-Jakob disease in humans and ...

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.

The model enables the study of the fundamental interactions that underlie neurodegenerative disease. Researchers from ...

In a new study, researchers have identified the structure of protein fibrils linked to a hereditary form of human prion disease ... of amino acids -- the basic building blocks of each protein.

And finally, what is the atomic structure of the prion agent ... make a significant impact on human medicine and basic science. The cellular prion protein (PrP C) is highly conserved and is ...

At first, they cause memory deficits and difficulties in walking, finally they inhibit elementary motor skills and destroy basic brain ... "The structure of prions typically shows two subdomains ...

This altered water structure influences the protein's ability to adopt its abnormal shape. The study, "Water-directed pinning is key to tau prion formation," is published in the Proceedings of the ...

In a new study, researchers from Case Western Reserve University School of Medicine have identified the structure ... basic building blocks of each protein. “It appears that the barriers—or lack ...

CLEVELAND—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.