Evidence map›Paper›PMID 35347143›Full record

ArticleNature communications2022

Correlational networking guides the discovery of unclustered lanthipeptide protease-encoding genes.

Dan Xue, Ethan A Older, Zheng Zhong, Zhuo Shang, Nanzhu Chen, Nolan Dittenhauser, Lukuan Hou, Peiyan Cai, Michael D Walla, Shi-Hui Dong and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.6field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  5. Review
  6. Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025
    Review
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  8. Review
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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

16 authors at 4 institutions in 4 countries.

Dan Xue *Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Ethan A Older *Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Zheng Zhong *Department of Chemistry and The Swire Institute of Marine Science, The University of Hong Kong, Pokfulam Road, Hong Kong, China.ORCID http://orcid.org/0000-0002-1262-4115
Zhuo ShangDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Nanzhu ChenDepartment of Chemistry and The Swire Institute of Marine Science, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Nolan DittenhauserDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Lukuan HouDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Peiyan CaiDepartment of Chemistry and The Swire Institute of Marine Science, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Michael D WallaThe Mass Spectrometry Center, Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA.
Shi-Hui DongState Key Laboratory of Applied Organic Chemistry, College of Chemistry and Chemical Engineering, Lanzhou University, Lanzhou, China.ORCID http://orcid.org/0000-0002-1743-2163
Xiaoyu TangInstitute of Chemical Biology, Shenzhen Bay Laboratory, Shenzhen, China.ORCID http://orcid.org/0000-0002-6406-9870
Hexin ChenDepartment of Biological Sciences, University of South Carolina, Columbia, SC, USA.ORCID http://orcid.org/0000-0001-9300-0859
Prakash NagarkattiDepartment of Pathology, Microbiology and Immunology, School of Medicine, University of South Carolina, Columbia, SC, USA.
Mitzi NagarkattiDepartment of Pathology, Microbiology and Immunology, School of Medicine, University of South Carolina, Columbia, SC, USA.
Yong-Xin LiDepartment of Chemistry and The Swire Institute of Marine Science, The University of Hong Kong, Pokfulam Road, Hong Kong, China. yxpli@hku.hk.ORCID http://orcid.org/0000-0003-4422-2302
Jie LiDepartment of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, USA. li439@mailbox.sc.edu.ORCID http://orcid.org/0000-0001-7977-6749
University of South Carolina · USSouthern Marine Science and Engineering Guangdong Laboratory (Guangzhou) · CNLanzhou University · CNShenzhen Bay Laboratory · CN

Funding

Targeting NMDA Receptors and Brain Estradiol to Rescue Memory in Aging FemalesP20GM109091 · NIGMS · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI RONINSON, IGOR B · 2014 to 2024
$25.2M
Targeting early ceramide elevation in pre-symptomatic eczemaP20GM103641 · NIGMS · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI ENOS, REILLY, NAGARKATTI, PRAKASH S · 2012 to 2023
$20.7M
NIGMS NIH HHS P20 GM103641NIGMS NIH HHS P20 GM109091
6 · The paper itself

Abstract

Bacterial natural product biosynthetic genes, canonically clustered, have been increasingly found to rely on hidden enzymes encoded elsewhere in the genome for completion of biosynthesis. The study and application of lanthipeptides are frequently hindered by unclustered protease genes required for final maturation. Here, we establish a global correlation network bridging the gap between lanthipeptide precursors and hidden proteases. Applying our analysis to 161,954 bacterial genomes, we establish 5209 correlations between precursors and hidden proteases, with 91 prioritized. We use network predictions and co-expression analysis to reveal a previously missing protease for the maturation of class I lanthipeptide paenilan. We further discover widely distributed bacterial M16B metallopeptidases of previously unclear biological function as a new family of lanthipeptide proteases. We show the involvement of a pair of bifunctional M16B proteases in the production of previously unreported class III lanthipeptides with high substrate specificity. Together, these results demonstrate the strength of our correlational networking approach to the discovery of hidden lanthipeptide proteases and potentially other missing enzymes for natural products biosynthesis.

Indexed as

Genome, BacterialPeptide HydrolasesBacteriaEndopeptidasesSubstrate SpecificityEndopeptidasesPeptide Hydrolases

Identifiers

PMID35347143
PMCPMC8960859
OpenAlexW4221113615

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.