Evidence map›Paper›PMID 35269643›Full record

ArticleInternational journal of molecular sciences2022

Nst1, Densely Associated to P-Body in the Post-Exponential Phases of

Yoon-Jeong Choi, Kiwon Song

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
0.3field-weighted citation impact, top 50% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. The Multivalent Polyampholyte Domain of Nst1, a P-Body-AssociatedInternational journal of molecular sciences · 2022
    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

2 authors at 1 institution in 1 country.

Yoon-Jeong ChoiDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea.ORCID 0000-0002-8565-0103
Kiwon SongDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Korea.
Yonsei University · KR

Funding

National Research Foundation of Korea NRF-2017R1A2B4009785
6 · The paper itself

Abstract

Membrane-less biomolecular compartmentalization is a core phenomenon involved in many physiological activities that occur ubiquitously in cells. Condensates, such as promyelocytic leukemia (PML) bodies, stress granules, and P-bodies (PBs), have been investigated to understand the process of membrane-less cellular compartmentalization. In budding yeast, PBs dispersed in the cytoplasm of exponentially growing cells rapidly accumulate in response to various stresses such as osmotic stress, glucose deficiency, and heat stress. In addition, cells start to accumulate PBs chronically in post-exponential phases. Specific protein-protein interactions are involved in accelerating PB accumulation in each circumstance, and discovering the regulatory mechanism for each is the key to understanding cellular condensation. Here, we demonstrate that Nst1 of budding yeast

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCytoplasmDEAD-box RNA HelicasesGlucoseProcessing BodiesDEAD-box RNA HelicasesDHH1 protein, S cerevisiaeGlucoseNst1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinscondensationEdc3liquid–liquid phase separationmRNP granuleNst1P-bodypost-exponential growth phases

Identifiers

PMID35269643
PMCPMC8910029
OpenAlexW4214608946

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.