Evidence map›Paper›PMID 28893371›Full record

ArticleBMB reports2017

Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells.

Chan-Gi Pack, Yuji Inoue, Takashi Higurashi, Shigeko Kawai-Noma, Daigo Hayashi, Elizabeth Craig, Hideki Taguchi

Open access · goldAbstract readNews
PubMed Full text at PMC Publisher
In one paragraph

Article in BMB reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 33% of its field
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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
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

7 authors at 3 institutions in 3 countries.

Chan-Gi PackAsan Institute for Life Sciences, Asan Medical Center, University of Ulsan College of Medicine, Seoul 05505, Korea.
Yuji InoueDepartment of Biomolecular Engineering, Graduate School of Biosciences and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Takashi HigurashiDepartment of Biochemistry, University of Wisconsin, WI 53706, USA.
Shigeko Kawai-NomaDepartment of Biomolecular Engineering, Graduate School of Biosciences and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Daigo HayashiDepartment of Biomolecular Engineering, Graduate School of Biosciences and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Elizabeth CraigDepartment of Biochemistry, University of Wisconsin, WI 53706, USA.
Hideki TaguchiDepartment of Biomolecular Engineering, Graduate School of Biosciences and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Tokyo Institute of Technology · JPUniversity of Wisconsin–Madison · USUlsan College · KR

Funding

MRNA DEGRADATION AND TRANSLATION CONTROL IN YEASTR01GM053655 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI JOHNSON, ARLEN W · 1995 to 2017
$5.1M
NIGMS NIH HHS R01 GM053655
6 · The paper itself

Abstract

Budding yeast has dozens of prions, which are mutually dependent on each other for the de novo prion formation. In addition to the interactions among prions, transmissions of prions are strictly dependent on two chaperone systems: the Hsp104 and the Hsp70/Hsp40 (J-protein) systems, both of which cooperatively remodel the prion aggregates to ensure the multiplication of prion entities. Since it has been postulated that prions and the remodeling factors constitute complex networks in cells, a quantitative approach to describe the interactions in live cells would be required. Here, the researchers applied dual-color fluorescence cross-correlation spectroscopy to investigate the molecular network of interaction in single live cells. The findings demonstrate that yeast prions and remodeling factors constitute a network through heterogeneous protein-protein interactions. [BMB Reports 2017; 50(9): 478-483].

Indexed as

HSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsPrionsProtein BindingSpectrometry, FluorescenceHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsPrions

Identifiers

PMID28893371
PMCPMC5625696
OpenAlexW2756968658

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.