[URE3] Prion formation by the Candida albicans Ure2p (but not by C. glabrata Ure2p)
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[URE3] Prion formation by the Candida albicans Ure2p (but not by C. glabrata Ure2p)-ScUre2. Saccharomyces cerevisiae
[URE3] is a prion (infectious protein) of the Saccharomyces cerevisiae Ure2p, a regulator of nitrogen catabolism. We find that the Ure2p of Candida albicans and C. glabrata also regulate nitrogen cata
NIAID Data Ecosystem40
Prion Formation and Polyglutamine Aggregation Are Controlled by Two Classes of Genes
Prions are self-perpetuating aggregated proteins that are not limited to mammalian systems but also exist in lower eukaryotes including yeast. While much work has focused around chaperones involved in
NIAID Data Ecosystem20
Amyloid aggregates of the HET-s prion protein are infectious
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 p
PubMed Central2002-05-21 更新10
[URE3] Prion formation by the Candida albicans Ure2p (but not by C. glabrata Ure2p)
This SuperSeries is composed of the SubSeries listed below. Refer to individual Series
NIAID Data Ecosystem20
RTG-dependent Mitochondria-to-Nucleus Signaling Is Regulated by MKS1 and Is Linked to Formation of Yeast Prion [URE3]
An important function of the RTG signaling pathway is maintenance of intracellular glutamate supplies in yeast cells with dysfunctional mitochondria. Herein, we report that MKS1 is a negative regulato
PubMed Central10
