Evidence map›Paper›PMID 41940658›Full record

ArticleMicrobiology spectrum2026

Structural characterization of the native oligomerization mode of MvaT proteins in

Delyana Vasileva, Chiho Suzuki-Minakuchi, Takatoshi Arakawa, Yoshitaka Moriwaki, Kento Yonezawa, Nobutaka Shimizu, Zui Fujimoto, Tohru Terada, Kazunori Okada, Hideaki Nojiri

Abstract read
In one paragraph

Article in Microbiology spectrum, 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

10 authors.

Delyana VasilevaAgro-Biotechnology Research Center, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-7919-7883
Chiho Suzuki-MinakuchiAgro-Biotechnology Research Center, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0001-6622-1955
Takatoshi ArakawaDepartment of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0001-6496-5440
Yoshitaka MoriwakiCollaborative Research Institute for Innovative Microbiology, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-0448-9790
Kento YonezawaInstitute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Ibaraki, Japan.ORCID 0000-0002-6656-0313
Nobutaka ShimizuInstitute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Ibaraki, Japan.ORCID 0000-0002-3636-1663
Zui FujimotoResearch Center for Advanced Analysis, National Agriculture and Food Research Organization (NARO), Ibaraki, Japan.ORCID 0000-0002-3551-6854
Tohru TeradaCollaborative Research Institute for Innovative Microbiology, The University of Tokyo, Tokyo, Japan.ORCID 0000-0002-7091-0646
Kazunori OkadaAgro-Biotechnology Research Center, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0001-7321-7911
Hideaki NojiriAgro-Biotechnology Research Center, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.ORCID 0000-0003-3091-8691

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone-like protein H1 (H-NS) proteins are key regulators of horizontally acquired genes in enterobacteria. Functional analogs of H-NS, collectively known as H-NS family proteins, have been discovered in diverse bacteria and on large transmissible plasmids. These proteins share the ability to form oligomers through their N-terminal oligomerization domain, a feature critical for their regulatory functions. The N-terminal domain of MvaT proteins, members of the H-NS family proteins in pseudomonads, consists of a central and a terminal dimerization site. We previously elucidated the structure of the central dimerization site of TurB, an MvaT homolog in

Indexed as

H-NSnucleoid-associated proteinsPseudomonassmall angle X-ray scatteringX-ray crystallography

Identifiers

PMID41940658
PMCPMC13141940

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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.