<p>(A) The lysates of [<i>PSI</i><sup>+</sup>] yeast cells producing full-sized or truncated Sup35 were analyzed by SDD-AGE. (B, C) Lysates were heated in the presence of sample buffer containing 2% SDS at different temperatures and analyzed by SDD-AGE. The thermal denaturation curves were derived from densitometric analysis of the stained blot images.</p
<p>(<b>A</b>) Polymers of Sup35 visualized by SDD-AGE. 74-D694 [<i>psi</i><sup>−</sup>] [<i>PIN</i><...
The yeast prion [PSI+] is caused by the self-propagation of beta-sheet rich aggregates of the transl...
The yeast [PSI+] prion, formed by the Sup35 (eRF3) protein, has multiple structural variants differi...
<p>(A) PK-digested anchored and anchorless RML prions were heated to temperatures from 25–99°C and m...
<p>(A) Lysates of 74-D694/ΔS35 [<i>PIN</i><sup>+</sup>] cells producing QX proteins of different len...
Fungal prions are protein-based genetic elements. Sup35 and Ure2p constitute the best-characterized ...
The use of yeast systems to study the propagation of prions and amyloids has emerged as a crucial as...
Prions, or infectious proteins, are self-templating ordered aggregates capable of replication. One ...
The yeast cytoplasmically inherited genetic determinant [PSI1] is presumed to be a manifestation of ...
When yeast are energy depleted, Sup35 prion protein phase separates into condensates with very diffe...
S. cerevisiae Sup35p inhabits two metastable states: functional translation termination factor; and ...
Prion is an infectious isoform of a normal cellular protein which is capable of converting the non-p...
<div><p>(A) The metabolic stability of Sup35-GFP was analyzed in [<i>PSI<sup>+</sup></i>] (SY81) or ...
Certain yeast cells contain proteins that behave like the mammalian prion PrP and are called yeast p...
Self-replicating 'proteinaceous infectious particles' or prions are responsible for complex heritabl...
<p>(<b>A</b>) Polymers of Sup35 visualized by SDD-AGE. 74-D694 [<i>psi</i><sup>−</sup>] [<i>PIN</i><...
The yeast prion [PSI+] is caused by the self-propagation of beta-sheet rich aggregates of the transl...
The yeast [PSI+] prion, formed by the Sup35 (eRF3) protein, has multiple structural variants differi...
<p>(A) PK-digested anchored and anchorless RML prions were heated to temperatures from 25–99°C and m...
<p>(A) Lysates of 74-D694/ΔS35 [<i>PIN</i><sup>+</sup>] cells producing QX proteins of different len...
Fungal prions are protein-based genetic elements. Sup35 and Ure2p constitute the best-characterized ...
The use of yeast systems to study the propagation of prions and amyloids has emerged as a crucial as...
Prions, or infectious proteins, are self-templating ordered aggregates capable of replication. One ...
The yeast cytoplasmically inherited genetic determinant [PSI1] is presumed to be a manifestation of ...
When yeast are energy depleted, Sup35 prion protein phase separates into condensates with very diffe...
S. cerevisiae Sup35p inhabits two metastable states: functional translation termination factor; and ...
Prion is an infectious isoform of a normal cellular protein which is capable of converting the non-p...
<div><p>(A) The metabolic stability of Sup35-GFP was analyzed in [<i>PSI<sup>+</sup></i>] (SY81) or ...
Certain yeast cells contain proteins that behave like the mammalian prion PrP and are called yeast p...
Self-replicating 'proteinaceous infectious particles' or prions are responsible for complex heritabl...
<p>(<b>A</b>) Polymers of Sup35 visualized by SDD-AGE. 74-D694 [<i>psi</i><sup>−</sup>] [<i>PIN</i><...
The yeast prion [PSI+] is caused by the self-propagation of beta-sheet rich aggregates of the transl...
The yeast [PSI+] prion, formed by the Sup35 (eRF3) protein, has multiple structural variants differi...