Evidence map›Paper›PMID 37497541›Full record

ArticleFrontiers in microbiology2023

Leader peptide removal in lasso peptide biosynthesis based on penultimate isoleucine residue.

Yuwei Duan, Weijing Niu, Linlin Pang, Da-Shuai Mu, Zong-Jun Du, Youming Zhang, Xiaoying Bian, Guannan Zhong

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2023. 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
1.7field-weighted citation impact, top 17% 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. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  2. Article
  3. Evolution-Guided Discovery of Antimycobacterial Triculamin-Like Lasso Peptides.Angewandte Chemie (International ed. in English) · 2025
    Article
  4. 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 3 institutions in 1 country.

Yuwei DuanHelmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Weijing NiuHelmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Linlin PangHelmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Da-Shuai MuHelmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Zong-Jun DuHelmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Youming ZhangHelmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Xiaoying BianHelmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Guannan ZhongHelmholtz International Laboratory for Anti-Infectives, State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.
Shandong University · CNState Key Laboratory of Microbial TechnologyShenzhen Institutes of Advanced Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lasso peptides are ribosomally synthesized peptides that undergo post-translational modifications including leader peptide removal by B (or the segregated B1 and B2) proteins and core peptide macrolactamization by C proteins to form a unique lariat topology. A conserved threonine residue at the penultimate position of leader peptide is hitherto found in lasso peptide precursors and shown to be a critical recognition element for effective enzymatic processing. We identified a lasso peptide biosynthetic gene cluster (

Indexed as

biosynthesislasso peptidepenultimate isoleucine residuepeptidasephosphorylationpost-translational modification

Identifiers

PMID37497541
PMCPMC10368454
OpenAlexW4383896443

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.