Evidence map›Paper›PMID 28968144›Full record

ArticlePrion2017

Spatial sequestration and oligomer remodeling during de novo [PSI

Douglas R Lyke, Anita L Manogaran

Abstract read
In one paragraph

Article in Prion, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. The three faces of Sup35.Yeast (Chichester, England) · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Douglas R Lykea Department of Biological Sciences , Marquette University , Milwaukee , WI , USA.
Anita L Manogarana Department of Biological Sciences , Marquette University , Milwaukee , WI , USA.

Funding

Investigation of cellular factors involved in yeast prion appearanceR15GM109336 · NIGMS · MARQUETTE UNIVERSITY · PI MANOGARAN, ANITA L. · 2014 to 2014
$343k
NIGMS NIH HHS R15 GM109336
6 · The paper itself

Abstract

Prions are misfolded, aggregated, infectious proteins found in a range of organisms from mammals to bacteria. In mammals, prion formation is difficult to study because misfolding and aggregation take place prior to symptom presentation. The study of the yeast prion [PSI

Indexed as

AmyloidCells, CulturedDenaturing Gradient Gel ElectrophoresisGreen Fluorescent ProteinsLuminescent AgentsMicroscopy, VideoPeptide Termination FactorsPrionsProtein AggregatesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTime FactorsAmyloidGreen Fluorescent ProteinsLuminescent AgentsPeptide Termination FactorsPrionsProtein AggregatesSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeamyloidinfectivityinheritanceoligomerprion[PSI+]spatial sequestrationSup35yeast

Identifiers

PMID28968144
PMCPMC5639836

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.