Evidence map›Paper›PMID 28522457›Full record

ArticlePlant physiology2017

Structure of eIF4E in Complex with an eIF4G Peptide Supports a Universal Bipartite Binding Mode for Protein Translation.

Manuel Miras, Verónica Truniger, Cristina Silva, Núria Verdaguer, Miguel A Aranda, Jordi Querol-Audí

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

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  18. Structural studies of the eIF4E-VPg complex reveal a direct competition for capped RNA: Implications for translation.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

6 authors at 2 institutions in 1 country.

Manuel MirasCentro de Edafología y Biología Aplicada del Segura (CEBAS), Consejo Superior de Investigaciones Científicas (CSIC), 30100 Espinardo, Murcia, Spain.
Verónica TrunigerCentro de Edafología y Biología Aplicada del Segura (CEBAS), Consejo Superior de Investigaciones Científicas (CSIC), 30100 Espinardo, Murcia, Spain.
Cristina SilvaInstitut de Biologia Molecular de Barcelona/CSIC, Parc Científic de Barcelona, 08028 Barcelona, Spain.
Núria VerdaguerInstitut de Biologia Molecular de Barcelona/CSIC, Parc Científic de Barcelona, 08028 Barcelona, Spain.
Miguel A ArandaCentro de Edafología y Biología Aplicada del Segura (CEBAS), Consejo Superior de Investigaciones Científicas (CSIC), 30100 Espinardo, Murcia, Spain jquerolaudi@gmail.com m.aranda@cebas.csic.es.ORCID http://orcid.org/0000-0002-0828-973X
Jordi Querol-AudíInstitut de Biologia Molecular de Barcelona/CSIC, Parc Científic de Barcelona, 08028 Barcelona, Spain jquerolaudi@gmail.com m.aranda@cebas.csic.es.
Consejo Superior de Investigaciones Científicas · ESInstitut de Biologia Molecular de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The association-dissociation of the cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) with eIF4G is a key control step in eukaryotic translation. The paradigm on the eIF4E-eIF4G interaction states that eIF4G binds to the dorsal surface of eIF4E through a single canonical alpha-helical motif, while metazoan eIF4E-binding proteins (m4E-BPs) advantageously compete against eIF4G via bimodal interactions involving this canonical motif and a second noncanonical motif of the eIF4E surface. Metazoan eIF4Gs share this extended binding interface with m4E-BPs, with significant implications on the understanding of translation regulation and the design of therapeutic molecules. Here we show the high-resolution structure of melon (

Indexed as

Protein BiosynthesisAmino Acid SequenceAmino Acid SubstitutionCrystallography, X-RayCucumis meloDisease ResistanceEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GHydrophobic and Hydrophilic InteractionsModels, MolecularMutationPeptidesProtein BindingProtein DomainsSequence AlignmentEukaryotic Initiation Factor-4EEukaryotic Initiation Factor-4GPeptides

Identifiers

PMID28522457
PMCPMC5490897
OpenAlexW2615698784

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.