Evidence map›Paper›PMID 32159929›Full record

ArticleChemMedChem2020

Synthesis and Biological Screening of New Lawson Derivatives as Selective Substrate-Based Inhibitors of Cytochrome bo

Isam Elamri, Melanie Radloff, Katharina F Hohmann, Vijaykumar D Nimbarte, Hamid R Nasiri, Michael Bolte, Schara Safarian, Hartmut Michel, Harald Schwalbe

Open access · hybridAbstract read
In one paragraph

Article in ChemMedChem, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 34% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Mechanistic and structural diversity between cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. 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

9 authors at 2 institutions in 1 country.

Isam ElamriCenter for Biomolecular Magnetic Resonance Institute of Organic Chemistry and Chemical Biology, Goethe-Universität Frankfurt am Main, Max-von Laue-Straße 7, 60438, Frankfurt am Main, Germany.
Melanie RadloffDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438, Frankfurt am Main, Germany.
Katharina F HohmannCenter for Biomolecular Magnetic Resonance Institute of Organic Chemistry and Chemical Biology, Goethe-Universität Frankfurt am Main, Max-von Laue-Straße 7, 60438, Frankfurt am Main, Germany.
Vijaykumar D NimbarteCenter for Biomolecular Magnetic Resonance Institute of Organic Chemistry and Chemical Biology, Goethe-Universität Frankfurt am Main, Max-von Laue-Straße 7, 60438, Frankfurt am Main, Germany.
Hamid R NasiriCenter for Biomolecular Magnetic Resonance Institute of Organic Chemistry and Chemical Biology, Goethe-Universität Frankfurt am Main, Max-von Laue-Straße 7, 60438, Frankfurt am Main, Germany.
Michael BolteInstitute for Inorganic Chemistry, Goethe-Universität, Frankfurt am Main, Germany.
Schara SafarianDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438, Frankfurt am Main, Germany.
Hartmut MichelDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438, Frankfurt am Main, Germany.
Harald SchwalbeCenter for Biomolecular Magnetic Resonance Institute of Organic Chemistry and Chemical Biology, Goethe-Universität Frankfurt am Main, Max-von Laue-Straße 7, 60438, Frankfurt am Main, Germany.ORCID 0000-0001-5693-7909
Goethe University Frankfurt · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The respiratory chain of Escherichia coli contains two different types of terminal oxidase that are differentially regulated as a response to changing environmental conditions. These oxidoreductases catalyze the reduction of molecular oxygen to water and contribute to the proton motive force. The cytochrome bo

Indexed as

AlkylationDose-Response Relationship, DrugDrug Evaluation, PreclinicalEnzyme InhibitorsEscherichia coliEscherichia coli ProteinsMolecular StructureNaphthoquinonesOxidoreductasesStructure-Activity RelationshipEnzyme InhibitorsEscherichia coli ProteinsNaphthoquinonesOxidoreductasesubiquinol oxidasealkylationcytochromeshydroxynaphthoquinoneinhibitor designoxidasesreductases

Identifiers

PMID32159929
PMCPMC7497249
OpenAlexW3010819122

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.