ArticleProceedings of the National Academy of Sciences of the United States of America2007
Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed.
- Extracellular Metabolites fromMicroorganisms · 2026Article
- MIL-CELL: a tool for multi-scale simulation of yeast replication and prion transmission.European biophysics journal : EBJ · 2023Article
- Extracellular Vesicles-Encapsulated Yeast Prions and What They Can Tell Us about the Physical Nature of Propagons.International journal of molecular sciences · 2020Review
- Aggregation of CAT tails blocks their degradation and causes proteotoxicity in S. cerevisiae.PloS one · 2020Article
- Osmolytes ameliorate the effects of stress in the absence of the heat shock protein Hsp104 in Saccharomyces cerevisiae.PloS one · 2019Article
- Natural Genetic Variation in Yeast Reveals That NEDD4 Is a Conserved Modifier of Mutant Polyglutamine Aggregation.G3 (Bethesda, Md.) · 2018Article
- The life of [PSI].Current genetics · 2018Review
- Evidence of a Prion-Like Transmission of p53 Amyloid in Saccharomyces cerevisiae.Molecular and cellular biology · 2017Article
- Article
- The copper transport-associated protein Ctr4 can form prion-like epigenetic determinants inMicrobial cell (Graz, Austria) · 2017Article
- A mathematical model of the dynamics of prion aggregates with chaperone-mediated fragmentation.Journal of mathematical biology · 2016Article
- Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds.Eukaryotic cell · 2014Article
- Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability.PLoS genetics · 2013Article
- A Discrete-Time Branching Process Model of Yeast Prion Curing Curves.Mathematical population studies · 2013Article
- Prions in yeast.Genetics · 2012Review
- Article
- [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
- The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.PloS one · 2009Article
- Hsp104 and prion propagation.Protein and peptide letters · 2009Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Guanidine hydrochloride (Gdn.HCl) blocks the propagation of yeast prions by inhibiting Hsp104, a molecular chaperone that is absolutely required for yeast prion propagation. We had previously proposed that ongoing cell division is required for Gdn.HCl-induced loss of the [PSI+] prion. Subsequently, Wu et al.[Wu Y, Greene LE, Masison DC, Eisenberg E (2005) Proc Natl Acad Sci USA 102:12789-12794] claimed to show that Gdn.HCl can eliminate the [PSI+] prion from alpha-factor-arrested cells leading them to propose that in Gdn.HCl-treated cells the prion aggregates are degraded by an Hsp104-independent mechanism. Here we demonstrate that the results of Wu et al. can be explained by an unusually high rate of alpha-factor-induced cell death in the [PSI+] strain (780-1D) used in their studies. What appeared to be no growth in their experiments was actually no increase in total cell number in a dividing culture through a counterbalancing level of cell death. Using media-exchange experiments, we provide further support for our original proposal that elimination of the [PSI+] prion by Gdn.HCl requires ongoing cell division and that prions are not destroyed during or after the evident curing phase.
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.