Weakening the IF2-fMet-tRNA Interaction Suppresses the Lethal Phenotype Caused by GTPase Inactivation.

Jerneja Tomsic, Enrico Caserta, Cynthia L Pon, Claudio O Gualerzi

Open access · goldAbstract read

In one paragraph

Article in International journal of molecular sciences, 2021. 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

0.1field-weighted citation impact, top 54% 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, 1 citations in OpenAlex.

Compact IF2 allows initiator tRNA accommodation into the P site and gates the ribosome to elongation.Nature communications · 2022
Article

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

4 authors at 2 institutions in 2 countries.

Jerneja TomsicLaboratory of Genetics, Department of Bioscience and Biotechnology, University of Camerino, 62032 Camerino, Italy.

Enrico CasertaLaboratory of Genetics, Department of Bioscience and Biotechnology, University of Camerino, 62032 Camerino, Italy.

Cynthia L PonLaboratory of Genetics, Department of Bioscience and Biotechnology, University of Camerino, 62032 Camerino, Italy.

Claudio O GualerziLaboratory of Genetics, Department of Bioscience and Biotechnology, University of Camerino, 62032 Camerino, Italy.

Università di Camerino · ITCity of Hope · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Substitution of the conserved Histidine 448 present in one of the three consensus elements characterizing the guanosine nucleotide binding domain (IF2 G2) of

Indexed as

Genes, LethalEscherichia coliEscherichia coli ProteinsGTP PhosphohydrolasesGuanosine TriphosphateHydrolysisModels, MolecularPhenotypeProkaryotic Initiation Factor-2Protein ConformationProtein DomainsRibosomesRNA, Transfer, MetEscherichia coli ProteinsGTP PhosphohydrolasesGuanosine TriphosphateProkaryotic Initiation Factor-2RNA, Transfer, MettRNA, formylmethionine-bacterial translation initiationdominant lethal phenotypeGTP hydrolysisinitiation factor IF2lethality suppression

Identifiers

PMID34948034

DOI10.3390/ijms222413238

PMCPMC8709274

OpenAlexW4200357700

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.