Evidence map›Paper›PMID 41341041›Full record

ArticleACS central science2025

A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini.

Shravan R Dommaraju, Sanath K Kandy, Hengqian Ren, Dominic P Luciano, Shogo Fujiki, David Sarlah, Huimin Zhao, Jonathan R Chekan, Douglas A Mitchell

Abstract read
In one paragraph

Article in ACS central science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Repositioning the Leader Peptide in Graspetide Biosynthesis.Journal of the American Chemical Society · 2026
    Article
  7. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Shravan R DommarajuDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, United States.ORCID https://orcid.org/0000-0002-0565-1748
Sanath K KandyDepartment of Chemistry and Biochemistry, University of North Carolina at Greensboro, Greensboro, North Carolina 27402, United States.
Hengqian RenCarl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Dominic P LucianoDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Shogo FujikiDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
David SarlahDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Huimin ZhaoDepartment of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID https://orcid.org/0000-0002-9069-6739
Jonathan R ChekanDepartment of Chemistry and Biochemistry, University of North Carolina at Greensboro, Greensboro, North Carolina 27402, United States.ORCID https://orcid.org/0000-0003-4651-0594
Douglas A MitchellDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, United States.ORCID https://orcid.org/0000-0002-9564-0953

Funding

Enzyme Chemistry and Biological Function of RiPP-like Modifications.R01GM097142 · NIGMS · VANDERBILT UNIVERSITY · PI MITCHELL, DOUGLAS ALAN · 2012 to 2024
$4.1M
Bioinformatic Guided Discovery and Characterization of New RiPP Natural ProductsR35GM147439 · NIGMS · UNIVERSITY OF NORTH CAROLINA GREENSBORO · PI Jonathan Rodi Chekan · 2022 to 2026
$1.8M
Discovery and Engineering of RiPP Natural ProductsR35GM158411 · NIGMS · VANDERBILT UNIVERSITY · PI Douglas Alan Mitchell · 2025 to 2026
$1.2M
NIGMS NIH HHS R01 GM097142NIGMS NIH HHS R35 GM147439NIGMS NIH HHS R35 GM158411
6 · The paper itself

Abstract

Advances in bioinformatics have enabled the discovery of unique enzymatic reactions, particularly for ribosomally synthesized and post-translationally modified peptides (RiPPs). The recently discovered daptides, peptides with their C-terminus replaced by an amine, represent one such case, but the diversity, requirements, and engineering potential of daptide biosynthesis remain to be established. Using the daptide biosynthetic gene clusters from

Identifiers

PMID41341041
PMCPMC12670281

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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.