The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation
Masison, Daniel C., Maddelein, Marie-Lise, Wickner, Reed B.
The genetic properties of the non-Mendelian element, [URE3], suggest that it is a prion (infectious protein) form of Ure2p, a mediator of nitrogen regulation in Saccharomyces cerevisiae. Into a...
A novel Rtg2p activity regulates nitrogen catabolism in yeast
Pierce, Michael M., Maddelein, Marie-Lise, Roberts, B. Tibor, Wickner, Reed B.
The inactivity of Ure2p, caused by either a ure2 mutation or the presence of the [URE3] prion, increases DAL5 transcription and thus enables Saccharomyces cerevisiae to take up ureidosuccinate...
Prions in Saccharomyces and Podospora spp.: Protein-Based Inheritance
Wickner, Reed B., Taylor, Kimberly L., Edskes, Herman K., Maddelein, Marie-Lise, Moriyama, Hiromitsu, Roberts, B. Tibor
Genetic evidence showed two non-Mendelian genetic elements of Saccharomyces cerevisiae, called [URE3] and [PSI], to be prions of Ure2p and Sup35p, respectively. [URE3] makes cells derepressed for...
Two Prion-Inducing Regions of Ure2p Are Nonoverlapping
Maddelein, Marie-Lise, Wickner, Reed B.
Ure2p of Saccharomyces cerevisiae normally functions in blocking utilization of a poor nitrogen source when a good nitrogen source is available. The non-Mendelian genetic element [URE3] is a prion...
Amyloid aggregates of the HET-s prion protein are infectious
Maddelein, Marie-Lise, Dos Reis, Suzana, Duvezin-Caubet, Stéphane, Coulary-Salin, Bénédicte, Saupe, Sven J.
The [Het-s] infectious element of the filamentous fungus Podospora anserina is a prion. We have recently reported that recombinant HET-s protein aggregates in vitro into amyloid fibers. In vivo, the...
The prion model for [URE3] of yeast: Spontaneous generation and requirements for propagation
Masison, Daniel C., Maddelein, Marie-Lise, Wickner, Reed B.
The genetic properties of the non-Mendelian element, [URE3], suggest that it is a prion (infectious protein) form of Ure2p, a mediator of nitrogen regulation in Saccharomyces cerevisiae. Into a...
A novel Rtg2p activity regulates nitrogen catabolism in yeast
Pierce, Michael M., Maddelein, Marie-Lise, Roberts, B. Tibor, Wickner, Reed B.
The inactivity of Ure2p, caused by either a ure2 mutation or the presence of the [URE3] prion, increases DAL5 transcription and thus enables Saccharomyces cerevisiae to take up ureidosuccinate...
Prions in Saccharomyces and Podospora spp.: Protein-Based Inheritance
Wickner, Reed B., Taylor, Kimberly L., Edskes, Herman K., Maddelein, Marie-Lise, Moriyama, Hiromitsu, Roberts, B. Tibor
Genetic evidence showed two non-Mendelian genetic elements of Saccharomyces cerevisiae, called [URE3] and [PSI], to be prions of Ure2p and Sup35p, respectively. [URE3] makes cells derepressed for...
Two Prion-Inducing Regions of Ure2p Are Nonoverlapping
Maddelein, Marie-Lise, Wickner, Reed B.
Ure2p of Saccharomyces cerevisiae normally functions in blocking utilization of a poor nitrogen source when a good nitrogen source is available. The non-Mendelian genetic element [URE3] is a prion...
Amyloid aggregates of the HET-s prion protein are infectious
Maddelein, Marie-Lise, Dos Reis, Suzana, Duvezin-Caubet, Stéphane, Coulary-Salin, Bénédicte, Saupe, Sven J.
The [Het-s] infectious element of the filamentous fungus Podospora anserina is a prion. We have recently reported that recombinant HET-s protein aggregates in vitro into amyloid fibers. In vivo, the...