Evidence map›Paper›PMID 42353222›Full record

ArticleInternational journal of molecular sciences2026

Structural Basis of pppGpp Binding to the N-Terminal Domain of the Bifunctional RelA/SpoT Homolog Rel

Svetlana A Korban, Zoya A Spiridonova, Pavel S Kasatsky, Alexey V Shvetsov, Vladislav V Gurzhiy, Alena Paleskava, Anna A Kulminskaya, Andrey L Konevega, Daria S Vinogradova

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

9 authors.

Svetlana A KorbanPetersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre "Kurchatov Institute", Gatchina 188300, Russia.
Zoya A SpiridonovaPetersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre "Kurchatov Institute", Gatchina 188300, Russia.
Pavel S KasatskyPetersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre "Kurchatov Institute", Gatchina 188300, Russia.
Alexey V ShvetsovPetersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre "Kurchatov Institute", Gatchina 188300, Russia.ORCID 0000-0003-1140-5751
Vladislav V GurzhiyCrystallography Department, Institute of Earth Sciences, St. Petersburg State University, Saint Petersburg 199034, Russia.ORCID 0000-0003-2730-6264
Alena PaleskavaPetersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre "Kurchatov Institute", Gatchina 188300, Russia.ORCID 0000-0001-8623-8404
Anna A KulminskayaPetersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre "Kurchatov Institute", Gatchina 188300, Russia.ORCID 0000-0002-3481-0007
Andrey L KonevegaPetersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre "Kurchatov Institute", Gatchina 188300, Russia.ORCID 0000-0003-0125-7150
Daria S VinogradovaPetersburg Nuclear Physics Institute Named by B.P. Konstantinov of National Research Centre "Kurchatov Institute", Gatchina 188300, Russia.

Funding

Russian Science Foundation 23-74-10088Saint-Petersburg State University 126022017738-9
6 · The paper itself

Abstract

RelA/SpoT homologue family enzymes participate in controlling the cellular levels of the alarmone (p)ppGpp, thereby activating the stringent response and promoting survival under stress conditions. These proteins contain an N-terminal catalytic domain and a C-terminal regulatory domain. They catalyze both the synthesis of ppGpp/pppGpp from ATP and GDP/GTP and their hydrolysis to GDP/GTP and pyrophosphate. Here, we report the crystal structure of the N-terminal domain of Rel from

Indexed as

Bacterial ProteinsGuanosine PentaphosphateLigasesPyrophosphatasesStreptococcusBinding SitesCatalytic DomainCrystallography, X-RayMolecular Dynamics SimulationProtein BindingProtein ConformationProtein DomainsBacterial Proteinsguanosine 3',5'-polyphosphate synthetasesGuanosine PentaphosphateLigasesPyrophosphatasesalarmonebifunctional enzymecrystal structuremolecular dynamicsnanoDSFpppGppRelA/SpoT homologRelSeqstringent responseX-ray

Identifiers

PMID42353222
PMCPMC13299517

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.