Evidence map›Paper›PMID 35953547›Full record

ArticleNature chemical biology2022

Bicyclostreptins are radical SAM enzyme-modified peptides with unique cyclization motifs.

Leah B Bushin, Brett C Covington, Kenzie A Clark, Alessio Caruso, Mohammad R Seyedsayamdost

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. The radical SAM enzyme EpeE exhibits distinct site reactivity during the biosynthesis of the RiPP natural product epipeptide.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  13. Discovering functional small molecules in the gut microbiome.Current opinion in chemical biology · 2023
    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

5 authors at 1 institution in 1 country.

Leah B BushinDepartment of Chemistry, Princeton University, Princeton, NJ, USA.ORCID http://orcid.org/0000-0003-0538-2469
Brett C CovingtonDepartment of Chemistry, Princeton University, Princeton, NJ, USA.
Kenzie A ClarkDepartment of Chemistry, Princeton University, Princeton, NJ, USA.ORCID http://orcid.org/0000-0003-0298-1124
Alessio CarusoDepartment of Chemistry, Princeton University, Princeton, NJ, USA.ORCID http://orcid.org/0000-0001-5612-8140
Mohammad R SeyedsayamdostDepartment of Chemistry, Princeton University, Princeton, NJ, USA. mrseyed@princeton.edu.ORCID http://orcid.org/0000-0003-2707-4854
Princeton University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial natural products comprise diverse architectures that are generated by equally diverse biosynthetic strategies. In peptide natural products, amino acid sidechains are frequently used as sites of modification to generate macrocyclic motifs. Backbone amide groups, among the most stable of biological moieties, are rarely used for this purpose. Here we report the discovery and biosynthesis of bicyclostreptins-peptide natural products from Streptococcus spp. with an unprecedented structural motif consisting of a macrocyclic β-ether and a heterocyclic sp

Indexed as

Biological ProductsMetalloproteinsAmidesBacterial ProteinsCarbonCyclizationEthersHumansNitrogenPeptidesS-AdenosylmethionineStreptococcusAmidesBacterial ProteinsBiological ProductsCarbonEthersMetalloproteinsNitrogenPeptidesS-Adenosylmethionine

Identifiers

PMID35953547
OpenAlexW4291022246

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.