Publications by authors named "Timo Piechatzek"
Molecular basis for diversification of yeast prion strain conformation.
Proc Natl Acad Sci U S A
March 2018
Article Synopsis
- Amyloid fibers are linked to various diseases and cellular issues, with different conformations leading to varying levels of toxicity.
- Researchers explore how changes in the structural balance of disordered proteins can create alternative amyloid forms, impacting their effects on cells.
- A study on Sup35NM showed that hidden local structures in the protein can influence its amyloid shape when altered, revealing a new mechanism by which proteins can diversify their aggregate forms and phenotypic outcomes.
The still elusive structural difference of non-infectious and infectious amyloid of the mammalian prion protein (PrP) is a major pending milestone in understanding protein-mediated infectivity in neurodegenerative diseases. Preparations of PrP-amyloid proven to be infectious have never been investigated with a high-resolution technique. All available models to date have been based on low-resolution data.
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