Evidence map›Paper›PMID 32250484›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2020

Zelkovamycin is an OXPHOS Inhibitory Member of the Argyrin Natural Product Family.

Daniel Krahn, Geronimo Heilmann, Felix C E Vogel, Chrisovalantis Papadopoulos, Susanne Zweerink, Farnusch Kaschani, Hemmo Meyer, Alexander Roesch, Markus Kaiser

Open access · hybridAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 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
0.3field-weighted citation impact, top 44% 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. Review
  2. Article
  3. Article
  4. Zelkovamycin is an OXPHOS Inhibitory Member of the Argyrin Natural Product Family.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    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 3 institutions in 1 country.

Daniel KrahnChemische Biologie, Universität Duisburg-Essen, ZMB, Fakultät für Biologie, Universitätsstr. 2, 45117, Essen, Germany.
Geronimo HeilmannChemische Biologie, Universität Duisburg-Essen, ZMB, Fakultät für Biologie, Universitätsstr. 2, 45117, Essen, Germany.
Felix C E VogelDepartment of Dermatology, University hospital Essen, West German Cancer Center, University Duisburg-Essen and the German Cancer Consortium (DKTK).
Chrisovalantis PapadopoulosMolekularbiologie I, Universität Duisburg-Essen, ZMB, Fakultät für Biologie, Universitätsstr. 2, 45117, Essen, Germany.
Susanne ZweerinkChemische Biologie, Universität Duisburg-Essen, ZMB, Fakultät für Biologie, Universitätsstr. 2, 45117, Essen, Germany.
Farnusch KaschaniChemische Biologie, Universität Duisburg-Essen, ZMB, Fakultät für Biologie, Universitätsstr. 2, 45117, Essen, Germany.
Hemmo MeyerMolekularbiologie I, Universität Duisburg-Essen, ZMB, Fakultät für Biologie, Universitätsstr. 2, 45117, Essen, Germany.
Alexander RoeschDepartment of Dermatology, University hospital Essen, West German Cancer Center, University Duisburg-Essen and the German Cancer Consortium (DKTK).
Markus KaiserChemische Biologie, Universität Duisburg-Essen, ZMB, Fakultät für Biologie, Universitätsstr. 2, 45117, Essen, Germany.ORCID http://orcid.org/0000-0002-6540-8520
University of Duisburg-Essen · DEGerman Cancer Research Center · DEUniversity of Cologne · DE

Funding

Deutsche Forschungsgemeinschaft CRC103Deutsche Forschungsgemeinschaft CRC1093
6 · The paper itself

Abstract

Natural products (NPs) are an important inspirational source for developing drugs and chemical probes. In 1999, the group of Ōmura reported the constitutional elucidation of zelkovamycin. Although largely unrecognized so far, this NP displays structural similarities as well as differences to the argyrin NP family, a class of peptidic NPs with promising anticancer activities and diverse mode-of-action at the molecular level. By a combination of structure elucidation experiments, the first total synthesis of zelkovamycin and bioassays, the zelkovamycin configuration was determined and its previously proposed molecular structure was revised. The full structure assignment proves zelkovamycin as an additional member of the argyrins with however unique OXPHOS inhibitory properties. Zelkovamycin may therefore not only serve as a new starting point for chemical inhibitors of the OXPHOS system, but also guide customized argyrin NP isolation and biosynthesis studies.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesBiological ProductsMolecular StructureAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBiological Productszelkovamycinargyrinbioactivitycyclopeptidesnatural productszelkovamycin

Identifiers

PMID32250484
PMCPMC7383741
OpenAlexW3014573085

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.