Evidence map›Paper›PMID 30026518›Full record

ArticleNature communications2018

Enzymatic one-step ring contraction for quinolone biosynthesis.

Shinji Kishimoto, Kodai Hara, Hiroshi Hashimoto, Yuichiro Hirayama, Pier Alexandre Champagne, Kendall N Houk, Yi Tang, Kenji Watanabe

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Unravelling the Functional Diversity of Type III Polyketide Synthases in Fungi.Angewandte Chemie (International ed. in English) · 2025
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  14. Alkaloids from Marine Fungi: Promising Antimicrobials.Antibiotics (Basel, Switzerland) · 2020
    Review
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

8 authors at 2 institutions in 2 countries.

Shinji KishimotoDepartment of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan.
Kodai HaraDepartment of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan.
Hiroshi HashimotoDepartment of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan.
Yuichiro HirayamaDepartment of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan.
Pier Alexandre ChampagneDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California, 90095, USA.ORCID http://orcid.org/0000-0002-0546-7537
Kendall N HoukDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California, 90095, USA.
Yi TangDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California, 90095, USA.ORCID http://orcid.org/0000-0003-1597-0141
Kenji WatanabeDepartment of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, 422-8526, Japan. kenji55@u-shizuoka-ken.ac.jp.
University of Shizuoka · JPUniversity of California, Los Angeles · US

Funding

MIRA: Enzymology and Self-Resistance of Natural Product BiosynthesisR35GM118056 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Yi Tang · 2016 to 2026
$6.1M
Rediscovering Natural Chemical Diversity -1DP1GM106413DP1GM106413 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TANG, YI · 2012 to 2016
$3.9M
NIGMS NIH HHS DP1 GM106413NIGMS NIH HHS R35 GM118056
6 · The paper itself

Abstract

The 6,6-quinolone scaffolds on which viridicatin-type fungal alkaloids are built are frequently found in metabolites that display useful biological activities. Here we report in vitro and computational analyses leading to the discovery of a hemocyanin-like protein AsqI from the Aspergillus nidulans aspoquinolone biosynthetic pathway that forms viridicatins via a conversion of the cyclopenin-type 6,7-bicyclic system into the viridicatin-type 6,6-bicyclic core through elimination of carbon dioxide and methylamine through methyl isocyanate.

Indexed as

AlkaloidsAspergillus nidulansBinding SitesBiosynthetic PathwaysCarbon DioxideCloning, MolecularCrystallography, X-RayCyclizationEscherichia coliFungal ProteinsGene ExpressionGenetic VectorsHemocyaninsHydroxyquinolinesIsocyanatesKineticsAlkaloidsCarbon DioxideFungal ProteinsHemocyaninsHydroxyquinolinesIsocyanatesmethylamineMethylaminesmethyl isocyanateQuinolonesRecombinant ProteinsviridicatinZinc

Identifiers

PMID30026518
PMCPMC6053404
OpenAlexW2884860115

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.