Evidence map›Paper›PMID 41671188›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation.

Sijia Guo, Suze Ma, Lulu Song, Jun Wang, Tonghai Liu, Wupeng Yan, Wei Zhang, Zixin Deng, Wei Ding, Qi Zhang

Erratum issuedAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Sijia GuoState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.ORCID 0009-0005-5073-2626
Suze MaNational Engineering Research Center for Carbohydrate Synthesis, College of Chemistry and Materials, Jiangxi Normal University, Nanchang 330022, China.ORCID 0000-0001-8030-2401
Lulu SongState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.
Jun WangState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.ORCID 0000-0003-2585-5614
Tonghai LiuState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.
Wupeng YanState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.
Wei ZhangKey Laboratory of Extreme Environmental Microbial Resources and Engineering of Gansu Province, Northwest Institute of Eco-Environment and Resources, Chinese Academy of Sciences, Lanzhou, Gansu 73000, China.
Zixin DengState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.
Wei DingState Key Laboratory of Microbial Metabolism, School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, China.ORCID 0000-0001-6036-5368
Qi ZhangNational Engineering Research Center for Carbohydrate Synthesis, College of Chemistry and Materials, Jiangxi Normal University, Nanchang 330022, China.ORCID 0000-0002-8135-2221

Funding

MOST | National Key Research and Development Program of China (NKPs) 2021YFA0910501MOST | National Natural Science Foundation of China (NSFC) 22477049MOST | National Natural Science Foundation of China (NSFC) 32270070MOST | National Natural Science Foundation of China (NSFC) U22A20451
6 · The paper itself

Abstract

Ribosomally synthesized and posttranslationally modified peptides (RiPPs) are a fertile ground for uncovering new enzymatic chemistry and structural complexity. Here, we describe minviopeptin, an unusual ADP-ribosylated triceptide accessed through heterologous expression of a cryptic biosynthetic gene cluster. Structural and functional analyses reveal a combination of crosslinking, ADP-ribosylation, and oxidative peptide cleavage, underscoring the capacity of RiPP pathways to generate densely functionalized molecular scaffolds. By revealing ADP-ribosylation as a previously unrecognized RiPP modification and exposing reactivity within radical SAM and nonheme iron enzymes, this work broadens the landscape of RiPP biosynthetic chemistries and offers opportunities for natural product diversification and peptide engineering.

Indexed as

ADP-RibosylationPeptidesProtein Processing, Post-TranslationalRibosomesAmino Acid SequenceMultigene FamilyPeptidesposttranslational modificationradical SAMRiPPtriceptideαKG-NHFe enzyme

Identifiers

PMID41671188
PMCPMC12912966

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Registered trials

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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.