Evidence map›Paper›PMID 28057755›Full record

ArticleThe Journal of biological chemistry2017

General Control Nonderepressible 2 (GCN2) Kinase Inhibits Target of Rapamycin Complex 1 in Response to Amino Acid Starvation in

Wenjie Yuan, Shuguang Guo, Jiaoqi Gao, Mingming Zhong, Gonghong Yan, Wangmeng Wu, Yapeng Chao, Yu Jiang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 61 citations in OpenAlex.

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  14. Review: Emerging roles of the signaling network of the protein kinase GCN2 in the plant stress response.Plant science : an international journal of experimental plant biology · 2022
    Review
  15. ThemBio · 2022
    Article
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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

8 authors at 4 institutions in 2 countries.

Wenjie YuanFrom the School of Life Science and Biotechnology, Dalian University of Technology, Dalian 116024, China.
Shuguang Guothe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.
Jiaoqi GaoFrom the School of Life Science and Biotechnology, Dalian University of Technology, Dalian 116024, China.
Mingming Zhongthe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.
Gonghong Yanthe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.
Wangmeng Wuthe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and.
Yapeng Chaothe State Key Laboratories of Transducer Technology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Yu Jiangthe Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, and yuj5@pitt.edu.
University of Pittsburgh · USDalian University · CNDalian University of Technology · CNInstitute of Microbiology · CN

Funding

The role of arachidonic acid in estrogen mediated mTOR activationR21CA169186 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JIANG, YU · 2013 to 2014
$361k
NCI NIH HHS R21 CA169186
6 · The paper itself

Abstract

In eukaryotic cells, two conserved protein kinases, Gcn2 and TOR complex 1 (TORC1), couple amino acid conditions to protein translation. Gcn2 functions as an amino acid sensor and is activated by uncharged tRNAs that accumulate when intracellular amino acids are limited. Activated Gcn2 phosphorylates and inhibits eukaryotic initiation factor-2α (eIF2α), resulting in repression of general protein synthesis. Like Gcn2, TORC1 is also involved in sensing amino acid conditions. However, the underlying mechanism remains unclear. In the present study, we show that TORC1 is a direct target of Gcn2 kinase in the yeast

Indexed as

Amino AcidsDown-RegulationMembrane ProteinsProtein BindingProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmino AcidsGCN2 protein, S cerevisiaeKog1 protein, S cerevisiaeMembrane ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteinsamino acidamino acid starvationautophagyGcn2histidineKog1TORC1TOR complex (TORC)uncharged tRNAyeast

Identifiers

PMID28057755
PMCPMC5314164
OpenAlexW2571385021

What OpenQuestion holds

Textmetadata
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.