Evidence map›Paper›PMID 24811713›Full record

ArticleBiochemistry2014

Insights into the architecture of the eIF2Bα/β/δ regulatory subcomplex.

Andrew M Bogorad, Bing Xia, Dana G Sandor, Artem B Mamonov, Tanya R Cafarella, Stefan Jehle, Sandor Vajda, Dima Kozakov, Assen Marintchev

Open access · bronzeAbstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  7. Characterization and Mapping ofFrontiers in plant science · 2021
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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

9 authors at 1 institution in 1 country.

Andrew M BogoradDepartment of Physiology and Biophysics, Boston University School of Medicine , Boston, Massachusetts 02118, United States.
Bing Xia
Dana G Sandor
Artem B Mamonov
Tanya R Cafarella
Stefan Jehle
Sandor Vajda
Dima Kozakov
Assen Marintchev
Boston University · US

Funding

A MULTISTAGE APPROACH TO PROTEIN-PROTEIN DOCKINGR01GM061867 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI VAJDA, SANDOR · 2000 to 2016
$4.0M
Mechanisms of assembly and remodeling of human translation initiation complexesR01GM095720 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI MARINTCHEV, ASSEN G · 2011 to 2015
$1.5M
Refinement Methods for Protein Docking based on Exploring Multi-Dimensional EnergR01GM093147 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI KOZAKOV, DMYTRO, PASCHALIDIS, IOANNIS · 2011 to 2014
$1.2M
NIGMS NIH HHS GM61687NIGMS NIH HHS GM93147NIGMS NIH HHS R01 GM061867NIGMS NIH HHS R01 GM095720
6 · The paper itself

Abstract

Eukaryotic translation initiation factor 2B (eIF2B), the guanine nucleotide exchange factor for the G-protein eIF2, is one of the main targets for the regulation of protein synthesis. The eIF2B activity is inhibited in response to a wide range of stress factors and diseases, including viral infections, hypoxia, nutrient starvation, and heme deficiency, collectively known as the integrated stress response. eIF2B has five subunits (α-ε). The α, β, and δ subunits are homologous to each other and form the eIF2B regulatory subcomplex, which is believed to be a trimer consisting of monomeric α, β, and δ subunits. Here we use a combination of biophysical methods, site-directed mutagenesis, and bioinformatics to show that the human eIF2Bα subunit is in fact a homodimer, at odds with the current trimeric model for the eIF2Bα/β/δ regulatory complex. eIF2Bα dimerizes using the same interface that is found in the homodimeric archaeal eIF2Bα/β/δ homolog aIF2B and related metabolic enzymes. We also present evidence that the eIF2Bβ/δ binding interface is similar to that in the eIF2Bα2 homodimer. Mutations at the predicted eIF2Bβ/δ dimer interface cause genetic neurological disorders in humans. We propose that the eIF2B regulatory subcomplex is an α2β2δ2 hexamer, composed of one α2 homodimer and two βδ heterodimers. Our results offer novel insights into the architecture of eIF2B and its interactions with the G-protein eIF2.

Indexed as

Amino Acid SequenceArchaeal ProteinsEukaryotic Initiation Factor-2BHumansMolecular Docking SimulationMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein BindingProtein ConformationProtein MultimerizationProtein SubunitsArchaeal ProteinsEukaryotic Initiation Factor-2BProtein Subunits

Identifiers

PMID24811713
PMCPMC4045321
OpenAlexW2080448503

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.