Evidence map›Paper›PMID 40107730›Full record

ArticleRNA (New York, N.Y.)2025

Deciphering the influence of the [4Fe-4S] cluster of tRNA thiolation enzymes on tRNA binding.

Sylvain Gervason, Sambuddha Sen, Jean-Luc Ravanat, Sylvain Caillat, Djemel Hamdane, Béatrice Golinelli-Pimpaneau

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 2025. 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
–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

1 citing paper in PubMed.

  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

6 authors.

Sylvain Gervason *Laboratoire de Chimie des Processus Biologiques, Collège de France, CNRS UMR 8829, Sorbonne Université, Paris cedex 05, France.
Sambuddha Sen *Laboratoire de Chimie des Processus Biologiques, Collège de France, CNRS UMR 8829, Sorbonne Université, Paris cedex 05, France.
Jean-Luc RavanatUniversity of Grenoble Alpes, CEA, CNRS, Grenoble INP, IRIG, SyMMES, F-38000 Grenoble, France.
Sylvain CaillatUniversity of Grenoble Alpes, CEA, CNRS, Grenoble INP, IRIG, SyMMES, F-38000 Grenoble, France.
Djemel HamdaneLaboratoire de Chimie des Processus Biologiques, Collège de France, CNRS UMR 8829, Sorbonne Université, Paris cedex 05, France djemel.hamdane@sorbonne-universite.fr beatrice.golinelli@college-de-france.fr.
Béatrice Golinelli-PimpaneauLaboratoire de Chimie des Processus Biologiques, Collège de France, CNRS UMR 8829, Sorbonne Université, Paris cedex 05, France djemel.hamdane@sorbonne-universite.fr beatrice.golinelli@college-de-france.fr.ORCID 0000-0001-8248-4704

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Iron-sulfur clusters [Fe-S] play crucial roles in diverse biological reactions, often serving as prosthetic groups for enzymes. Specifically, certain tRNA-modifying enzymes utilize these clusters to catalyze the thiolation of specific nucleosides. While the participation of [4Fe-4S] clusters in such catalytic processes is known, their potential influence on tRNA binding remains unexplored. In this study, we examine the impact of the cluster on the affinity for tRNA of TtuI from the archeon

Indexed as

Iron-Sulfur ProteinsMethanococcusRNA, TransferEscherichia coliProtein BindingThiouridineIron-Sulfur ProteinsRNA, TransferThiouridine[Fe–S] clusterfluorescencetRNA affinitytRNA modificationtRNA thiolation

Identifiers

PMID40107730
PMCPMC12084879

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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.