Evidence map›Paper›PMID 39992511›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

Purification and Analysis of eIF2α Phosphorylation by Stress-Activated Protein Kinase Gcn2 from S. cerevisiae.

Ritu Gupta, Swati Gaikwad, Hongfang Qui, Charles Bou-Nader, Jinwei Zhang, Alan G Hinnebusch

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. 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. Substrate Binding Relieves Autoinhibition of the Mammalian GCN2 Kinase.bioRxiv : the preprint server for biology · 2026
    Article
  2. 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

6 authors.

Ritu GuptaDivision of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Swati GaikwadDivision of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Hongfang QuiDivision of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Charles Bou-NaderLaboratory of Molecular Biology, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
Jinwei ZhangLaboratory of Molecular Biology, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.
Alan G HinnebuschDivision of Molecular and Cellular Biology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA. alanh@mail.nih.gov.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gcn2 is the sole eIF2α kinase in budding yeast, responsible for inhibiting general translation while inducing translation of transcriptional activator Gcn4, a master regulator of amino acid biosynthesis, in nutrient-starved cells. Gcn2 is activated by interactions between multiple regulatory domains that overcome the inherent latency of its protein kinase domain, including a pseudokinase domain, one related to histidyl-tRNA synthetase, a ribosome-binding and dimerization domain, and a region that binds the trans-acting activators Gcn1/Gcn20, which respond to deacylated tRNAs engendered by amino acid starvation or other impediments to translation elongation that lead to ribosome stalling and collisions. Here, we describe methods for purifying Gcn2 from yeast cells and assaying its protein kinase activity against a recombinant segment of eIF2α.

Indexed as

Eukaryotic Initiation Factor-2Protein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsPhosphorylationEukaryotic Initiation Factor-2GCN2 protein, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinseIF2α phosphorylationGcn2 purificationKinase assayS. cerevisiaeYeast

Identifiers

PMID39992511

What OpenQuestion holds

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Registered trials

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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.