Prions are infectious, self-propagating protein aggregates that have been identified in evolutionarily divergent members of the eukaryotic domain of life. Nevertheless, it is not yet known whether prokaryotes can support the formation of prion aggregates. Here we demonstrate that the yeast prion protein Sup35 can access an infectious conformation in Escherichia coli cells and that formation of this material is greatly stimulated by the presence of a transplanted [PSI+] inducibility factor, a distinct prion that is required for Sup35 to undergo spontaneous conversion to the prion form in yeast. Our results establish that the bacterial cytoplasm can support the formation of infectious prion aggregates, providing a heterologous system in which...
Prion is an infectious isoform of a normal cellular protein which is capable of converting the non-p...
Prions are classically understood as infectious agents capable of transmission by a mechanism of con...
<div><p>Many proteins can misfold into β-sheet-rich, self-seeding polymers (amyloids). Prions are ex...
ABSTRACT The yeast Saccharomyces cerevisiae harbors several prions that constitute powerful models t...
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015.Cataloged from PD...
ABSTRACT The yeast Saccharomyces cerevisiae harbors several prions that constitute powerful models t...
The yeast cytoplasmically inherited genetic determinant [PSI1] is presumed to be a manifestation of ...
Background Prions were first identified as infectious proteins associated with fatal brain diseases ...
Prions, or infectious proteins, are self-templating ordered aggregates capable of replication. One ...
Prions are proteins that can access multiple conformations, at least one of which is β-sheet rich, i...
Prions are self-propagating protein aggregates that are characteristically transmissible. In mammals...
Prions are infectious, self-propagating amyloid-like protein aggregates of mammals and fungi. We hav...
Prion proteins can adopt multiple infectious strain conformations. Here we investigate how the seque...
AbstractThe discovery of prion disease transmission in mammals, as well as a non-Mendelian type of i...
The term prion, proteinaceus infectious particle, was first used to describe the causative agent of ...
Prion is an infectious isoform of a normal cellular protein which is capable of converting the non-p...
Prions are classically understood as infectious agents capable of transmission by a mechanism of con...
<div><p>Many proteins can misfold into β-sheet-rich, self-seeding polymers (amyloids). Prions are ex...
ABSTRACT The yeast Saccharomyces cerevisiae harbors several prions that constitute powerful models t...
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015.Cataloged from PD...
ABSTRACT The yeast Saccharomyces cerevisiae harbors several prions that constitute powerful models t...
The yeast cytoplasmically inherited genetic determinant [PSI1] is presumed to be a manifestation of ...
Background Prions were first identified as infectious proteins associated with fatal brain diseases ...
Prions, or infectious proteins, are self-templating ordered aggregates capable of replication. One ...
Prions are proteins that can access multiple conformations, at least one of which is β-sheet rich, i...
Prions are self-propagating protein aggregates that are characteristically transmissible. In mammals...
Prions are infectious, self-propagating amyloid-like protein aggregates of mammals and fungi. We hav...
Prion proteins can adopt multiple infectious strain conformations. Here we investigate how the seque...
AbstractThe discovery of prion disease transmission in mammals, as well as a non-Mendelian type of i...
The term prion, proteinaceus infectious particle, was first used to describe the causative agent of ...
Prion is an infectious isoform of a normal cellular protein which is capable of converting the non-p...
Prions are classically understood as infectious agents capable of transmission by a mechanism of con...
<div><p>Many proteins can misfold into β-sheet-rich, self-seeding polymers (amyloids). Prions are ex...