Evidence map›Paper›PMID 32605991›Full record

ArticlemBio2020

Isolated Heme A Synthase from Aquifex aeolicus Is a Trimer.

Hui Zeng, Guoliang Zhu, Shuangbo Zhang, Xinmei Li, Janosch Martin, Nina Morgner, Fei Sun, Guohong Peng, Hao Xie, Hartmut Michel

Open access · goldAbstract read
In one paragraph

Article in mBio, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 40% of its field
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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Biosynthesis and trafficking of hemeCritical reviews in biochemistry and molecular biology · 2021
    Review
  6. 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

10 authors at 3 institutions in 2 countries.

Hui ZengDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Guoliang ZhuNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Shuangbo ZhangNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Xinmei LiNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Janosch MartinInstitute of Physical and Theoretical Chemistry, Goethe University, Frankfurt am Main, Germany.
Nina MorgnerInstitute of Physical and Theoretical Chemistry, Goethe University, Frankfurt am Main, Germany.
Fei SunNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Guohong PengDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Hao XieDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany Hao.Xie@biophys.mpg.de Hartmut.Michel@biophys.mpg.de.ORCID 0000-0002-2422-2527
Hartmut MichelDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Frankfurt am Main, Germany Hao.Xie@biophys.mpg.de Hartmut.Michel@biophys.mpg.de.
Chinese Academy of Sciences · CNMax Planck Institute of Biophysics · DEGoethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The integral membrane protein heme A synthase (HAS) catalyzes the biosynthesis of heme A, which is a prerequisite for cellular respiration in a wide range of aerobic organisms. Previous studies have revealed that HAS can form homo-oligomeric complexes, and this oligomerization appears to be evolutionarily conserved among prokaryotes and eukaryotes and is shown to be essential for the biological function of eukaryotic HAS. Despite its importance, little is known about the detailed structural properties of HAS oligomers. Here, we aimed to address this critical issue by analyzing the oligomeric state of HAS from

Indexed as

AquifexBacterial ProteinsCytochrome b GroupHemeMembrane ProteinsModels, MolecularOxygenProtein MultimerizationBacterial ProteinsCtaA protein, bacteriaCytochrome b GroupHemeheme aMembrane ProteinsOxygenAquifex aeolicuscofactor biosynthesisheme A synthasehyperthermophilic bacteriummetalloproteinsprotein oligomerizationrespiratory chainstructural biology

Identifiers

PMID32605991
PMCPMC7327177
OpenAlexW3038352335

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.