Evidence map›Paper›PMID 34521887›Full record

ArticleScientific reports2021

Selective

Erik Schleicher, Stephan Rein, Boris Illarionov, Ariane Lehmann, Tarek Al Said, Sylwia Kacprzak, Robert Bittl, Adelbert Bacher, Markus Fischer, Stefan Weber

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 25% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Multiple quantumScience advances · 2026
    Article
  2. 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 4 institutions in 1 country.

Erik SchleicherInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Albertstr. 21, 79104, Freiburg, Germany. erik.schleicher@pc.uni-freiburg.de.ORCID http://orcid.org/0000-0003-3010-9528
Stephan ReinInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Albertstr. 21, 79104, Freiburg, Germany.
Boris IllarionovInstitut für Lebensmittelchemie, Universität Hamburg, Grindelallee 117, 20146, Hamburg, Germany.
Ariane LehmannInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Albertstr. 21, 79104, Freiburg, Germany.
Tarek Al SaidInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Albertstr. 21, 79104, Freiburg, Germany.ORCID http://orcid.org/0000-0002-9057-5451
Sylwia KacprzakInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Albertstr. 21, 79104, Freiburg, Germany.
Robert BittlFachbereich Physik, Freie Universität Berlin, Arnimallee 14, 14195, Berlin, Germany.ORCID http://orcid.org/0000-0003-4103-3768
Adelbert BacherDepartment Chemie, Technische Universität München, Lichtenbergstr. 4, 85748, Garching, Germany.ORCID http://orcid.org/0000-0001-5174-4139
Markus FischerInstitut für Lebensmittelchemie, Universität Hamburg, Grindelallee 117, 20146, Hamburg, Germany.ORCID http://orcid.org/0000-0001-7243-4199
Stefan WeberInstitut für Physikalische Chemie, Albert-Ludwigs-Universität Freiburg, Albertstr. 21, 79104, Freiburg, Germany. stefan.weber@pc.uni-freiburg.de.ORCID http://orcid.org/0000-0003-4090-7435
University of Freiburg · DEUniversität Hamburg · DEFreie Universität Berlin · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Flavocoenzymes are nearly ubiquitous cofactors that are involved in the catalysis and regulation of a wide range of biological processes including some light-induced ones, such as the photolyase-mediated DNA repair, magnetoreception of migratory birds, and the blue-light driven phototropism in plants. One of the factors that enable versatile flavin-coenzyme biochemistry and biophysics is the fine-tuning of the cofactor's frontier orbital by interactions with the protein environment. Probing the singly-occupied molecular orbital (SOMO) of the intermediate radical state of flavins is therefore a prerequisite for a thorough understanding of the diverse functions of the flavoprotein family. This may be ultimately achieved by unravelling the hyperfine structure of a flavin by electron paramagnetic resonance. In this contribution we present a rigorous approach to obtaining a hyperfine map of the flavin's chromophoric 7,8-dimethyl isoalloxazine unit at an as yet unprecedented level of resolution and accuracy. We combine powerful high-microwave-frequency/high-magnetic-field electron-nuclear double resonance (ENDOR) with

Identifiers

PMID34521887
PMCPMC8440535
OpenAlexW3201121350

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.