Evidence map›Paper›PMID 39062472›Full record

ArticleBiomolecules2024

Structural and Thermodynamic Insights into Dimerization Interfaces of Drosophila Glutathione Transferases.

Mathieu Schwartz, Nicolas Petiot, Jeanne Chaloyard, Véronique Senty-Segault, Frédéric Lirussi, Patrick Senet, Adrien Nicolai, Jean-Marie Heydel, Francis Canon, Sanjiv Sonkaria and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomolecules, 2024. 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. Structural Analysis of theBiomolecules · 2024
    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

13 authors.

Mathieu SchwartzFlavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France.ORCID 0000-0002-2670-5274
Nicolas PetiotLaboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Université de Bourgogne Franche-Comté, 21078 Dijon, France.
Jeanne ChaloyardFlavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France.
Véronique Senty-SegaultFlavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France.
Frédéric LirussiUMR 1231, Lipides Nutrition Cancer, INSERM, 21000 Dijon, France.ORCID 0000-0002-0649-6719
Patrick SenetLaboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Université de Bourgogne Franche-Comté, 21078 Dijon, France.
Adrien NicolaiLaboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Université de Bourgogne Franche-Comté, 21078 Dijon, France.ORCID 0000-0001-7779-4652
Jean-Marie HeydelFlavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France.ORCID 0000-0002-6089-9922
Francis CanonIndependent Researcher, 21000 Dijon, France.ORCID 0000-0002-6140-5007
Sanjiv SonkariaSoft Foundry Institute, Seoul National University, Kwanak-gu, Seoul 39-131, Republic of Korea.
Varsha KhareSoft Foundry Institute, Seoul National University, Kwanak-gu, Seoul 39-131, Republic of Korea.
Claude DidierjeanCRM2 Laboratory, CNRS, Université de Lorraine, 54000 Nancy, France.ORCID 0000-0002-3176-8974
Fabrice NeiersFlavour Perception: Molecular Mechanisms (Flavours), INRAE, CNRS, Université de Bourgogne, 21000 Dijon, France.ORCID 0000-0002-8965-4929

Funding

Basic Research Program in Science and Engineering by the Ministry of Education, Korea 2022R1A2C1006090National Research Foundation of Korea 2022R1A2C1006090
6 · The paper itself

Abstract

This study presents a comprehensive analysis of the dimerization interfaces of fly GSTs through sequence alignment. Our investigation revealed GSTE1 as a particularly intriguing target, providing valuable insights into the variations within Delta and Epsilon GST interfaces. The X-ray structure of GSTE1 was determined, unveiling remarkable thermal stability and a distinctive dimerization interface. Utilizing circular dichroism, we assessed the thermal stability of GSTE1 and other Drosophila GSTs with resolved X-ray structures. The subsequent examination of GST dimer stability correlated with the dimerization interface supported by findings from X-ray structural analysis and thermal stability measurements. Our discussion extends to the broader context of GST dimer interfaces, offering a generalized perspective on their stability. This research enhances our understanding of the structural and thermodynamic aspects of GST dimerization, contributing valuable insights to the field.

Indexed as

Glutathione TransferaseProtein MultimerizationThermodynamicsAmino Acid SequenceAnimalsCrystallography, X-RayDrosophilaDrosophila melanogasterDrosophila ProteinsModels, MolecularDrosophila ProteinsGlutathione TransferaseDelta GSTdimerization interfaceDrosophila melanogasterEpsilon GSTglutathione transferasesGSTprotein stability

Identifiers

PMID39062472
PMCPMC11274453

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.