Evidence map›Paper›PMID 36598500›Full record

ArticleIUCrJ2023

Analysis of the conformational heterogeneity of the Rieske iron-sulfur protein in complex III

Jan Philip Wieferig, Werner Kühlbrandt

Open access · goldAbstract read
In one paragraph

Article in IUCrJ, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.4field-weighted citation impact, top 48% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Distinct ubiquinone binding at the oxidation and reduction sites of cytochrome bcProceedings of the National Academy of Sciences of the United States of America · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Jan Philip WieferigDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany.ORCID 0000-0002-5552-3381
Werner KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany.
Max Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Movement of the Rieske domain of the iron-sulfur protein is essential for intramolecular electron transfer within complex III

Indexed as

Cytochromes bElectron Transport Complex IIICryoelectron MicroscopyCytochromes cCytochromes c1Protein ConformationCytochromes bCytochromes cCytochromes c1Electron Transport Complex IIIRieske iron-sulfur proteincomplex III2conformational heterogeneityiron–sulfur proteinsRieske domains

Identifiers

PMID36598500
PMCPMC9812224
OpenAlexW4310177718

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.