ReviewProtein and peptide letters2009
Application of GFP-labeling to study prions in yeast.
Review in Protein and peptide letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed, 17 citations in OpenAlex.
- Human J-Domain Protein DnaJB6 Protects Yeast from [Biology · 2022Article
- Article
- Biochemical Principles in Prion-Based Inheritance.Epigenomes · 2022Review
- Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020Review
- Osmolytes ameliorate the effects of stress in the absence of the heat shock protein Hsp104 in Saccharomyces cerevisiae.PloS one · 2019Article
- Curing of [PSIPrion · 2018Article
- Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells.BMB reports · 2017Article
- Heat shock protein 104 (Hsp104)-mediated curing of [The Journal of biological chemistry · 2017Article
- Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds.Eukaryotic cell · 2014Article
- Septin-containing barriers control the differential inheritance of cytoplasmic elements.Cell reports · 2013Article
- Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.Prion · 2012Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Fluorescent live cell imaging has recently been used in numerous studies to examine prions in yeast. These fluorescence studies take advantage of the fact that unlike the normally folded form, the misfolded amyloid form of the prion protein is aggregated. The studies have used fluorescence to identify new prions, to study the transmission of prion from mother to daughter, and to understand the role of molecular chaperones in this transmission. The use of fluorescence imaging complements the more standard methods used to study prion propagation. This review discusses the various studies that have taken advantage of fluorescence imaging technique particularly in regard to understanding the transmission and curing of the [PSI(+)], the prion form of the translation termination factor Sup35p.
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.