Evidence map›Paper›PMID 36213119›Full record

ArticleFrontiers in molecular biosciences2022

eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly.

Belén Chaves-Arquero, Santiago Martínez-Lumbreras, Nathalie Sibille, Sergio Camero, Pau Bernadó, M Ángeles Jiménez, Silvia Zorrilla, José Manuel Pérez-Cañadillas

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 48% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

8 authors at 2 institutions in 2 countries.

Belén Chaves-ArqueroDepartment of Biological Physical Chemistry, Institute of Physical-Chemistry "Rocasolano", CSIC, Madrid, Spain.
Santiago Martínez-LumbrerasDepartment of Biological Physical Chemistry, Institute of Physical-Chemistry "Rocasolano", CSIC, Madrid, Spain.
Nathalie SibilleCentre de Biochimie Structurale (CBS), CNRS, INSERM, Univ. Montpellier, Montpellier, France.
Sergio CameroDepartment of Biological Physical Chemistry, Institute of Physical-Chemistry "Rocasolano", CSIC, Madrid, Spain.
Pau BernadóCentre de Biochimie Structurale (CBS), CNRS, INSERM, Univ. Montpellier, Montpellier, France.
M Ángeles JiménezDepartment of Biological Physical Chemistry, Institute of Physical-Chemistry "Rocasolano", CSIC, Madrid, Spain.
Silvia ZorrillaDepartment of Cellular and Molecular Biology, Biological Research Center, CSIC, Madrid, Spain.
José Manuel Pérez-CañadillasDepartment of Biological Physical Chemistry, Institute of Physical-Chemistry "Rocasolano", CSIC, Madrid, Spain.
Instituto de Química Física Blas Cabrera · ESUniversité de Montpellier · FR

Funding

NIMHD NIH HHS L60 MD003770
6 · The paper itself

Abstract

Yeast eIF4G1 interacts with RNA binding proteins (RBPs) like Pab1 and Pub1 affecting its function in translation initiation and stress granules formation. We present an NMR and SAXS study of the N-terminal intrinsically disordered region of eIF4G1 (residues 1-249) and its interactions with Pub1, Pab1 and RNA. The conformational ensemble of eIF4G1

Indexed as

eIF4G1intrinsically disordered proteins (IDP)NMRPab1paramagnetic relaxation enhancement (PRE)Pub1SAXS (small-angle X-ray scattering)structural ensemble

Identifiers

PMID36213119
PMCPMC9537944
OpenAlexW4295364118

What OpenQuestion 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 OpenQuestion graph.