Evidence map›Paper›PMID 26979951›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Biosynthetic investigation of phomopsins reveals a widespread pathway for ribosomal natural products in Ascomycetes.

Wei Ding, Wan-Qiu Liu, Youli Jia, Yongzhen Li, Wilfred A van der Donk, Qi Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
12.9field-weighted citation impact, top 1% 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

50 citing papers in PubMed, 105 citations in OpenAlex.

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  9. Decoding Pecan's Fungal Foe: A Genomic Insight intoJournal of fungi (Basel, Switzerland) · 2025
    Article
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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

6 authors at 2 institutions in 2 countries.

Wei DingDepartment of Chemistry, Fudan University, Shanghai 200433, China;
Wan-Qiu LiuDepartment of Chemistry, Fudan University, Shanghai 200433, China;
Youli JiaDepartment of Chemistry, Fudan University, Shanghai 200433, China;
Yongzhen LiDepartment of Chemistry, Fudan University, Shanghai 200433, China;
Wilfred A van der DonkDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801; Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL 61801 vddonk@illinois.edu qizhang@sioc.ac.cn.
Qi ZhangDepartment of Chemistry, Fudan University, Shanghai 200433, China; Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801; vddonk@illinois.edu qizhang@sioc.ac.cn.
Fudan University · CNUniversity of Illinois Urbana-Champaign · US

Funding

Posttranslational Modifications in Natural Product BiosynthesisR01GM058822 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 1999 to 2015
$3.8M
Posttranslational Modifications during Natural Product BiosynthesisR37GM058822 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI VAN DER DONK, WILFRED A. · 2016 to 2025
$2.9M
Howard Hughes Medical InstituteNIGMS NIH HHS GM R01 058822NIGMS NIH HHS R01 GM058822NIGMS NIH HHS R37 GM058822
6 · The paper itself

Abstract

Production of ribosomally synthesized and posttranslationally modified peptides (RiPPs) has rarely been reported in fungi, even though organisms of this kingdom have a long history as a prolific source of natural products. Here we report an investigation of the phomopsins, antimitotic mycotoxins. We show that phomopsin is a fungal RiPP and demonstrate the widespread presence of a pathway for the biosynthesis of a family of fungal cyclic RiPPs, which we term dikaritins. We characterize PhomM as an S-adenosylmethionine-dependent α-N-methyltransferase that converts phomopsin A to an N,N-dimethylated congener (phomopsin E), and show that the methyltransferases involved in dikaritin biosynthesis have evolved differently and likely have broad substrate specificities. Genome mining studies identified eight previously unknown dikaritins in different strains, highlighting the untapped capacity of RiPP biosynthesis in fungi and setting the stage for investigating the biological activities and unknown biosynthetic transformations of this family of fungal natural products.

Indexed as

Amino Acid SequenceAntimitotic AgentsAscomycotaBiological ProductsBiosynthetic PathwaysFungal ProteinsGenes, FungalMolecular Sequence DataMultigene FamilyMycotoxinsOligopeptidesProtein MethyltransferasesProtein Processing, Post-TranslationalRepetitive Sequences, Amino AcidRibosomesAntimitotic AgentsBiological ProductsFungal ProteinsMycotoxinsOligopeptidesphomopsinProtein Methyltransferasesbiosynthesismethyltransferasemycotoxinposttranslational modificationRiPP

Identifiers

PMID26979951
PMCPMC4822579
OpenAlexW2302372433

What OpenQuestion holds

Textmetadata
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.