Evidence map›Paper›PMID 40028132›Full record

ArticleACS omega2025

Apoprotein Intermolecular Interactions and Heme Insertion for 3D Domain Swapping in Myoglobin.

Gissi Novientri, Koji Takeda, Lian Duan, Kowit Hengphasatporn, Yasuteru Shigeta, Cheng Xie, Tsuyoshi Mashima, Shun Hirota

Abstract read
In one paragraph

Article in ACS omega, 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. 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

8 authors.

Gissi NovientriDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.ORCID https://orcid.org/0000-0002-6376-8880
Koji TakedaDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.ORCID https://orcid.org/0009-0003-9008-3662
Lian DuanCenter for Computational Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan.
Kowit HengphasatpornCenter for Computational Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan.
Yasuteru ShigetaCenter for Computational Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan.ORCID https://orcid.org/0000-0002-3219-6007
Cheng XieDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
Tsuyoshi MashimaDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.ORCID https://orcid.org/0000-0002-2402-1573
Shun HirotaDivision of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.ORCID https://orcid.org/0000-0003-3227-8376

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many proteins, including heme proteins undergo three-dimensional domain swapping (3D-DS). The loop between E and F helices is converted to a helical structure in the myoglobin (Mb) 3D-DS dimer. However, the relationship between 3D-DS and heme insertion in Mb remains unclear. Here, we systematically investigated the 3D-DS propensity of wild-type (WT) Mb and its variant in which one to three Ala residues were introduced into the hinge region: G80A (K

Identifiers

PMID40028132
PMCPMC11865968

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.