AbstractPrions are self-propagating protein conformations. Recent research brought insight into prion propagation, but how they first appear is unknown. We previously established that the yeast non-Mendelian trait [PIN+] is required for the de novo appearance of the [PSI+] prion. Here, we show that the presence of prions formed by Rnq1 or Ure2 is sufficient to make cells [PIN+]. Thus, [PIN+] can be caused by more than one prion. Furthermore, an unbiased functional screen for [PIN+] prions uncovered the known prion gene, URE2, the proposed prion gene, NEW1, and nine novel candidate prion genes all carrying prion domains. Importantly, the de novo appearance of Rnq1::GFP prion aggregates also requires the presence of other prions, suggesting t...
<div><p>Prions are transmissible, propagating alternative states of proteins. Prions in budding yeas...
Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propag...
Protein conformational disorders are a hallmark of protein aggregation and understanding these disea...
AbstractPrions are self-propagating protein conformations. Recent research brought insight into prio...
Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are excepti...
Amyloidogenic proteins associated with a variety of unrelated diseases are typically capable of form...
<div><p>Many proteins can misfold into β-sheet-rich, self-seeding polymers (amyloids). Prions are ex...
Prions are self-perpetuating aggregated proteins that are not limited to mammalian systems but also ...
Prion strains (or variants) are structurally distinct amyloid conformations arising from a single po...
Prion strains (or variants) are structurally distinct amyloid conformations arising from a single po...
AbstractThe yeast prion [PSI+] results from self-propagating aggregates of Sup35p. De novo formation...
Various proteins, like the infectious yeast prions and the noninfectious human Huntingtin protein (w...
The aggregation of the two yeast proteins Sup35p and Ure2p is widely accepted as a model for explain...
Prions are self-perpetuating aggregated proteins that are not limited to mammalian systems but also ...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2011.This electronic versi...
<div><p>Prions are transmissible, propagating alternative states of proteins. Prions in budding yeas...
Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propag...
Protein conformational disorders are a hallmark of protein aggregation and understanding these disea...
AbstractPrions are self-propagating protein conformations. Recent research brought insight into prio...
Many proteins can misfold into beta-sheet-rich, self-seeding polymers (amyloids). Prions are excepti...
Amyloidogenic proteins associated with a variety of unrelated diseases are typically capable of form...
<div><p>Many proteins can misfold into β-sheet-rich, self-seeding polymers (amyloids). Prions are ex...
Prions are self-perpetuating aggregated proteins that are not limited to mammalian systems but also ...
Prion strains (or variants) are structurally distinct amyloid conformations arising from a single po...
Prion strains (or variants) are structurally distinct amyloid conformations arising from a single po...
AbstractThe yeast prion [PSI+] results from self-propagating aggregates of Sup35p. De novo formation...
Various proteins, like the infectious yeast prions and the noninfectious human Huntingtin protein (w...
The aggregation of the two yeast proteins Sup35p and Ure2p is widely accepted as a model for explain...
Prions are self-perpetuating aggregated proteins that are not limited to mammalian systems but also ...
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2011.This electronic versi...
<div><p>Prions are transmissible, propagating alternative states of proteins. Prions in budding yeas...
Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propag...
Protein conformational disorders are a hallmark of protein aggregation and understanding these disea...