ArticleCurrent genetics2007
Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP.
Article in Current genetics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 52 citations in OpenAlex.
- Mapping of Prion Structures in the Yeast Rnq1.International journal of molecular sciences · 2024Article
- Intrinsically Disordered Compositional Bias in Proteins: Sequence Traits, Region Clustering, and Generation of Hypothetical Functional Associations.Bioinformatics and biology insights · 2024Article
- [PRIONPathogens (Basel, Switzerland) · 2022Article
- Article
- Article
- The actin cytoskeletal network plays a role in yeast prion transmission and contributes to prion stability.Molecular microbiology · 2020Article
- Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.Molecular and cellular biology · 2015Article
- Effect of domestication on the spread of the [PIN+] prion in Saccharomyces cerevisiae.Genetics · 2014Article
- Article
- Yeast prions and human prion-like proteins: sequence features and prediction methods.Cellular and molecular life sciences : CMLS · 2014Review
- Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.PLoS genetics · 2014Article
- Exploring the basis of [PIN(+)] variant differences in [PSI(+)] induction.Journal of molecular biology · 2013Article
- Diversity, biogenesis and function of microbial amyloids.Trends in microbiology · 2012Review
- Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.Molecular and cellular biology · 2012Article
- A small, glutamine-free domain propagates the [SWI(+)] prion in budding yeast.Molecular and cellular biology · 2011Article
- Amyloid in neurodegenerative diseases: friend or foe?Seminars in cell & developmental biology · 2011Review
- Use of yeast as a system to study amyloid toxicity.Methods (San Diego, Calif.) · 2011Article
- [PSI+] maintenance is dependent on the composition, not primary sequence, of the oligopeptide repeat domain.PloS one · 2011Article
- Analysis of the [RNQ+] prion reveals stability of amyloid fibers as the key determinant of yeast prion variant propagation.The Journal of biological chemistry · 2010Article
- Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.PLoS genetics · 2010Article
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
Prions are viewed as enigmatic infectious entities whose genetic properties are enciphered solely in an array of self-propagating protein aggregate conformations. Rnq1, a yeast protein with yet unknown function, forms a prion named [PIN+] for its ability to facilitate the de novo induction of another prion, [PSI+]. Here we investigate a set of RNQ1 truncations that were designed to cover major Rnq1 sequence elements similar to those important for the propagation of other yeast prions: a region rich in asparagines and glutamines and several types of oligopeptide repeats. Proteins encoded by these RNQ1 truncations were tested for their ability to (a) join (decorate) pre-existing [PIN+] aggregates made of wild-type Rnq1 and (b) maintain the heritable aggregated state in the absence of wild-type RNQ1. While the possible involvement of particular sequence elements in the propagation of [PIN+] is discussed, the major result is that the efficiency of transmission of [PIN+] from wild-type Rnq1 to a fragment decreased with the fragment's length.
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.