ArticleThe EMBO journal2003
The mechanisms of [URE3] prion elimination demonstrate that large aggregates of Ure2p are dead-end products.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- The p53 DNA-Binding (Core) Domain can form a prion that seeds prion formation in full-length p53.Microbial cell (Graz, Austria) · 2026Article
- Variant-specific and reciprocal Hsp40 functions in Hsp104-mediated prion elimination.Molecular microbiology · 2018Article
- Real-time imaging of yeast cells reveals several distinct mechanisms of curing of the [URE3] prion.The Journal of biological chemistry · 2018Article
- Article
- The involvement of mRNA processing factors TIA-1, TIAR, and PABP-1 during mammalian hibernation.Cell stress & chaperones · 2014Article
- Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability.PLoS genetics · 2013Article
- Methionine oxidation of Sup35 protein induces formation of the [PSI+] prion in a yeast peroxiredoxin mutant.The Journal of biological chemistry · 2011Article
- [SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.PLoS genetics · 2011Article
- Prion dynamics and the quest for the genetic determinant in protein-only inheritance.Current opinion in microbiology · 2009Review
- Increased [PSI+] appearance by fusion of Rnq1 with the prion domain of Sup35 in Saccharomyces cerevisiae.Eukaryotic cell · 2009Article
- The cellular concentration of the yeast Ure2p prion protein affects its propagation as a prion.Molecular biology of the cell · 2009Article
- Application of GFP-labeling to study prions in yeast.Protein and peptide letters · 2009Review
- Specificity of the J-protein Sis1 in the propagation of 3 yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Role of Hsp104 in the propagation and inheritance of the [Het-s] prion.Molecular biology of the cell · 2007Article
- Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.Molecular cell · 2006Article
- Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Article
- Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication.Eukaryotic cell · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The yeast prion [URE3] is a self-propagating inactive form (the propagon) of the Ure2 protein. Ure2p is composed of two domains: residues 1-93--the prion-forming domain (PFD)--and the remaining C-terminal part of the protein, which forms the functional domain involved in nitrogen catabolite repression. Guanidine hydrochloride, and the overproduction of Ure2p 1-65 or Ure2-GFP have been shown to induce the elimination of [URE3]. We demonstrate here, two different curing mechanisms: the inhibition of [URE3] replication by guanidine hydrochloride and its destruction by Ure2p aggregation. Such aggregation is observed if PFD or Ure2-GFP are overproduced and in heterozygous URE2/URE2-GFP, [URE3] diploids. We found that the GFP foci associated with the presence of the prion were dead-end products, the propagons remaining soluble. Surprisingly, [URE3] propagated via the Ure2-GFP fusion protein alone is resistant to these two curing mechanisms and cannot promote the formation of foci. The relationship between aggregation, prion and Hsp104 gives rise to a model in which the propagon is in equilibrium with larger aggregates and functional protein.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.